|
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: 892.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 1 MKLPIYLDYSATTPVDPRVAQKMSECLLMDGNFGNPASRSHVFGWKAEEAVENARRQVAELVNADPREIVWTSGATESDN 80
Cdd:PRK14012 1 MKLPIYLDYSATTPVDPRVAEKMMPYLTMDGTFGNPASRSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 81 LAIKGVAHFYSGKGKHIITSKIEHKAVLDTCRQLEREGFEVTYLEPGEDGLITPALVEAALRDDTILVSVMHVNNEIGTV 160
Cdd:PRK14012 81 LAIKGAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 161 NDIAAIGELTRSRGVLFHVDAAQSTGKVEIDLDKLKVDLMSFSAHKTYGPKGIGALYVRRKPRVRIEGQMHGGGHERGMR 240
Cdd:PRK14012 161 QDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRLEAQMHGGGHERGMR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 241 SGTLATHQIVGMGEAFRIAKEEMAQENARVLALRDRFFAQIDGLEELYINGSMTSRVPHNLNVSFNYVEGESLIMALKDL 320
Cdd:PRK14012 241 SGTLPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGIKDIEEVYLNGDLEQRVPGNLNVSFNYVEGESLIMALKDL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 321 AVSSGSACTSASLEPSYVLRALGRNDELAHSSIRFTFGRFTTEEEIDYAAKKVVEAVSKLRELSPLWDMYKEGVDLSQVE 400
Cdd:PRK14012 321 AVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGKLRELSPLWEMFKEGVDLNSIE 400
|
....
gi 15599009 401 WQAH 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: 804.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 1 MKLPIYLDYSATTPVDPRVAQKMSECLLMDgnFGNPASRSHVFGWKAEEAVENARRQVAELVNADPREIVWTSGATESDN 80
Cdd:TIGR02006 1 MKLPIYLDYAATTPVDPRVAEKMMPYLTEK--FGNPASRSHSFGWEAEEAVENARNQVAELIGADSREIVFTSGATESNN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 81 LAIKGVAHFYSGKGKHIITSKIEHKAVLDTCRQLEREGFEVTYLEPGEDGLITPALVEAALRDDTILVSVMHVNNEIGTV 160
Cdd:TIGR02006 79 LAIKGIAHFYKSKGNHIITSKTEHKAVLDTCRYLEREGFEVTYLPPKSNGLIDLEELKAAIRDDTILVSIMHVNNEIGVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 161 NDIAAIGELTRSRGVLFHVDAAQSTGKVEIDLDKLKVDLMSFSAHKTYGPKGIGALYVRRKPRVRIEGQMHGGGHERGMR 240
Cdd:TIGR02006 159 QDIAAIGEICRERKVFFHVDAAQSVGKIPINVNELKVDLMSISGHKIYGPKGIGALYVRRKPRVRLEALIHGGGHERGMR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 241 SGTLATHQIVGMGEAFRIAKEEMAQENARVLALRDRFFAQIDGLEELYINGSMTSRVPHNLNVSFNYVEGESLIMALKDL 320
Cdd:TIGR02006 239 SGTLPTHQIVGMGEAFRIAKEEMAQDTAHVLALRDRLLNGIKSIEEVYLNGDLEHRVPGNLNVSFNYVEGESLIMALKDL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 321 AVSSGSACTSASLEPSYVLRALGRNDELAHSSIRFTFGRFTTEEEIDYAAKKVVEAVSKLRELSPLWDMYKEGVDLSQVE 400
Cdd:TIGR02006 319 AVSSGSACTSASLEPSYVLRALGINDELAHSSIRFTIGRFTTEEEIDYAVKLVKSAIDKLRELSPLWEMFKEGVDLNSIE 398
|
....
gi 15599009 401 WQAH 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: 649.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 2 KLPIYLDYSATTPVDPRVAQKMSECllMDGNFGNPASrSHVFGWKAEEAVENARRQVAELVNADPREIVWTSGATESDNL 81
Cdd:COG1104 1 MMMIYLDNAATTPVDPEVLEAMLPY--LTEYFGNPSS-LHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 82 AIKGVAHFYSGKGKHIITSKIEHKAVLDTCRQLEREGFEVTYLEPGEDGLITPALVEAALRDDTILVSVMHVNNEIGTVN 161
Cdd:COG1104 78 AIKGAARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 162 DIAAIGELTRSRGVLFHVDAAQSTGKVEIDLDKLKVDLMSFSAHKTYGPKGIGALYVRRkpRVRIEGQMHGGGHERGMRS 241
Cdd:COG1104 158 PIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRK--GVRLEPLIHGGGQERGLRS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 242 GTLATHQIVGMGEAFRIAKEEMAQENARVLALRDRFFAQI-DGLEELYINGSMTSRVPHNLNVSFNYVEGESLIMAL--K 318
Cdd:COG1104 236 GTENVPGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLlAAIPGVVINGDPENRLPNTLNFSFPGVEGEALLLALdlA 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599009 319 DLAVSSGSACTSASLEPSYVLRALGRNDELAHSSIRFTFGRFTTEEEIDYAAKKVVEAVSKLRELS 384
Cdd:COG1104 316 GIAVSSGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARLRKLS 381
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
5-368 |
1.88e-101 |
|
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: 305.71 E-value: 1.88e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 5 IYLDYSATTPVDPRVAQKMSEcLLMDGNfGNPASRSHVFGWKAEEAVENARRQVAELVNA-DPREIVWTSGATESDNLAI 83
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQE-YYTDYN-GNVHRGVHTLGKEATQAYEEAREKVAEFINApSNDEIIFTSGTTEAINLVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 84 KGVAHFYsGKGKHIITSKIEHKAVLDTCRQL-EREGFEVTYLEPGEDGLITPALVEAALRDDTILVSVMHVNNEIGTVND 162
Cdd:pfam00266 79 LSLGRSL-KPGDEIVITEMEHHANLVPWQELaKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 163 IAAIGELTRSRGVLFHVDAAQSTGKVEIDLDKLKVDLMSFSAHKTYGPKGIGALYVRRKPRVRIEGQMHGGG-------H 235
Cdd:pfam00266 158 VPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGmietvslQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 236 ERGM-------RSGTLATHQIVGMGEAFR-IAKEEMAQENARVLALRDRFFAQIDGLEELYINGSmtSRVPHNLNVSFNY 307
Cdd:pfam00266 238 ESTFadapwkfEAGTPNIAGIIGLGAALEyLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGP--ERRASIISFNFKG 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599009 308 VEGESLIMALKD--LAVSSGSACTsaslEPSYVLRALgrndelaHSSIRFTFGRFTTEEEIDY 368
Cdd:pfam00266 316 VHPHDVATLLDEsgIAVRSGHHCA----QPLMVRLGL-------GGTVRASFYIYNTQEDVDR 367
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
5-377 |
6.34e-70 |
|
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: 224.65 E-value: 6.34e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 5 IYLDYSATTPVDPRVAQKMSECLLMDGnfGNPASRSHVFGWKAEEAVENARRQVAELVNA-DPREIVWTSGATESDNLAI 83
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYN--ANVHRGVHELSARATDAYEAAREKVARFINApSPDEIIFTRNTTEAINLVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 84 KGVAhFYSGKGKHIITSKIEHKAVLDTCRQL-EREGFEVTYLEPGEDGLITPALVEAALRDDTILVSVMHVNNEIGTVND 162
Cdd:cd06453 79 YGLG-RANKPGDEIVTSVMEHHSNIVPWQQLaERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 163 IAAIGELTRSRGVLFHVDAAQSTGKVEIDLDKLKVDLMSFSAHKTYGPKGIGALYVRRKPRVRIEgQMHGGG-------- 234
Cdd:cd06453 158 VKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMP-PYGGGGemieevsf 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 235 -----HERGMR--SGTLATHQIVGMGEAFR----IAKEEMAQENARVLA-LRDRfFAQIDGLeELYinGSMTSRVPhnlN 302
Cdd:cd06453 237 eettyADLPHKfeAGTPNIAGAIGLGAAIDylekIGMEAIAAHEHELTAyALER-LSEIPGV-RVY--GDAEDRAG---V 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 303 VSFNyVEG---ESLIMAL--KDLAVSSGSACTsaslEPsyVLRALGRNdelahSSIRFTFGRFTTEEEIDyaakKVVEAV 377
Cdd:cd06453 310 VSFN-LEGihpHDVATILdqYGIAVRAGHHCA----QP--LMRRLGVP-----GTVRASFGLYNTEEEID----ALVEAL 373
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
47-220 |
3.82e-18 |
|
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: 86.45 E-value: 3.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 47 AEEAVENARRQVAELVNA-DPREIVWTSGATESDNLAIK--GVAHFysGKGKHIITSKIEHKAVldtcrqleregfevty 123
Cdd:NF041166 287 ATDAYEGAREKVRRFIGApSVDEIIFVRGTTEAINLVAKswGRQNI--GAGDEIIVSHLEHHAN---------------- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 124 lepgedglITP-----ALVEAALR----DD----------------TILVSVMHVNNEIGTVNDIAAIGELTRSRGVLFH 178
Cdd:NF041166 349 --------IVPwqqlaQETGAKLRvipvDDsgqilldeyakllnprTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVL 420
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15599009 179 VDAAQSTGKVEIDLDKLKVDLMSFSAHKTYGPKGIGALYVRR 220
Cdd:NF041166 421 VDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGIGVVYGKR 462
|
|
| |
|
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: 892.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 1 MKLPIYLDYSATTPVDPRVAQKMSECLLMDGNFGNPASRSHVFGWKAEEAVENARRQVAELVNADPREIVWTSGATESDN 80
Cdd:PRK14012 1 MKLPIYLDYSATTPVDPRVAEKMMPYLTMDGTFGNPASRSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 81 LAIKGVAHFYSGKGKHIITSKIEHKAVLDTCRQLEREGFEVTYLEPGEDGLITPALVEAALRDDTILVSVMHVNNEIGTV 160
Cdd:PRK14012 81 LAIKGAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 161 NDIAAIGELTRSRGVLFHVDAAQSTGKVEIDLDKLKVDLMSFSAHKTYGPKGIGALYVRRKPRVRIEGQMHGGGHERGMR 240
Cdd:PRK14012 161 QDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRLEAQMHGGGHERGMR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 241 SGTLATHQIVGMGEAFRIAKEEMAQENARVLALRDRFFAQIDGLEELYINGSMTSRVPHNLNVSFNYVEGESLIMALKDL 320
Cdd:PRK14012 241 SGTLPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGIKDIEEVYLNGDLEQRVPGNLNVSFNYVEGESLIMALKDL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 321 AVSSGSACTSASLEPSYVLRALGRNDELAHSSIRFTFGRFTTEEEIDYAAKKVVEAVSKLRELSPLWDMYKEGVDLSQVE 400
Cdd:PRK14012 321 AVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGKLRELSPLWEMFKEGVDLNSIE 400
|
....
gi 15599009 401 WQAH 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: 804.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 1 MKLPIYLDYSATTPVDPRVAQKMSECLLMDgnFGNPASRSHVFGWKAEEAVENARRQVAELVNADPREIVWTSGATESDN 80
Cdd:TIGR02006 1 MKLPIYLDYAATTPVDPRVAEKMMPYLTEK--FGNPASRSHSFGWEAEEAVENARNQVAELIGADSREIVFTSGATESNN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 81 LAIKGVAHFYSGKGKHIITSKIEHKAVLDTCRQLEREGFEVTYLEPGEDGLITPALVEAALRDDTILVSVMHVNNEIGTV 160
Cdd:TIGR02006 79 LAIKGIAHFYKSKGNHIITSKTEHKAVLDTCRYLEREGFEVTYLPPKSNGLIDLEELKAAIRDDTILVSIMHVNNEIGVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 161 NDIAAIGELTRSRGVLFHVDAAQSTGKVEIDLDKLKVDLMSFSAHKTYGPKGIGALYVRRKPRVRIEGQMHGGGHERGMR 240
Cdd:TIGR02006 159 QDIAAIGEICRERKVFFHVDAAQSVGKIPINVNELKVDLMSISGHKIYGPKGIGALYVRRKPRVRLEALIHGGGHERGMR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 241 SGTLATHQIVGMGEAFRIAKEEMAQENARVLALRDRFFAQIDGLEELYINGSMTSRVPHNLNVSFNYVEGESLIMALKDL 320
Cdd:TIGR02006 239 SGTLPTHQIVGMGEAFRIAKEEMAQDTAHVLALRDRLLNGIKSIEEVYLNGDLEHRVPGNLNVSFNYVEGESLIMALKDL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 321 AVSSGSACTSASLEPSYVLRALGRNDELAHSSIRFTFGRFTTEEEIDYAAKKVVEAVSKLRELSPLWDMYKEGVDLSQVE 400
Cdd:TIGR02006 319 AVSSGSACTSASLEPSYVLRALGINDELAHSSIRFTIGRFTTEEEIDYAVKLVKSAIDKLRELSPLWEMFKEGVDLNSIE 398
|
....
gi 15599009 401 WQAH 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: 649.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 2 KLPIYLDYSATTPVDPRVAQKMSECllMDGNFGNPASrSHVFGWKAEEAVENARRQVAELVNADPREIVWTSGATESDNL 81
Cdd:COG1104 1 MMMIYLDNAATTPVDPEVLEAMLPY--LTEYFGNPSS-LHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 82 AIKGVAHFYSGKGKHIITSKIEHKAVLDTCRQLEREGFEVTYLEPGEDGLITPALVEAALRDDTILVSVMHVNNEIGTVN 161
Cdd:COG1104 78 AIKGAARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 162 DIAAIGELTRSRGVLFHVDAAQSTGKVEIDLDKLKVDLMSFSAHKTYGPKGIGALYVRRkpRVRIEGQMHGGGHERGMRS 241
Cdd:COG1104 158 PIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRK--GVRLEPLIHGGGQERGLRS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 242 GTLATHQIVGMGEAFRIAKEEMAQENARVLALRDRFFAQI-DGLEELYINGSMTSRVPHNLNVSFNYVEGESLIMAL--K 318
Cdd:COG1104 236 GTENVPGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLlAAIPGVVINGDPENRLPNTLNFSFPGVEGEALLLALdlA 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599009 319 DLAVSSGSACTSASLEPSYVLRALGRNDELAHSSIRFTFGRFTTEEEIDYAAKKVVEAVSKLRELS 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: 555.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 5 IYLDYSATTPVDPRVAQKMSECLLmdGNFGNPASRSHVFGWKAEEAVENARRQVAELVNADPREIVWTSGATESDNLAIK 84
Cdd:PLN02651 1 LYLDMQATTPIDPRVLDAMLPFLI--EHFGNPHSRTHLYGWESEDAVEKARAQVAALIGADPKEIIFTSGATESNNLAIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 85 GVAHFYSGKGKHIITSKIEHKAVLDTCRQLEREGFEVTYLEPGEDGLITPALVEAALRDDTILVSVMHVNNEIGTVNDIA 164
Cdd:PLN02651 79 GVMHFYKDKKKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 165 AIGELTRSRGVLFHVDAAQSTGKVEIDLDKLKVDLMSFSAHKTYGPKGIGALYVRRKPRVRIEGQMHGGGHERGMRSGTL 244
Cdd:PLN02651 159 EIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRLEPLMSGGGQERGRRSGTE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 245 ATHQIVGMGEAFRIAKEEMAQENARVLALRDRFFAQI-DGLEELYING--SMTSRVPHNLNVSFNYVEGESLIMALKDLA 321
Cdd:PLN02651 239 NTPLVVGLGAACELAMKEMDYDEKHMKALRERLLNGLrAKLGGVRVNGprDPEKRYPGTLNLSFAYVEGESLLMGLKEVA 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 15599009 322 VSSGSACTSASLEPSYVLRALGRNDELAHSSIRFTFGRFTTEEEID 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 |
3.09e-169 |
|
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: 478.26 E-value: 3.09e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 5 IYLDYSATTPVDPRVAQKMSECLlmDGNFGNPASrSHVFGWKAEEAVENARRQVAELVNADPREIVWTSGATESDNLAIK 84
Cdd:TIGR03402 1 IYLDNNATTRVDPEVLEAMLPYF--TEYFGNPSS-MHSFGGEVGKAVEEAREQVAKLLGAEPDEIIFTSGGTESDNTAIK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 85 GVAHFYSGKgKHIITSKIEHKAVLDTCRQLEREGFEVTYLEPGEDGLITPALVEAALRDDTILVSVMHVNNEIGTVNDIA 164
Cdd:TIGR03402 78 SALAAQPEK-RHIITTAVEHPAVLSLCQHLEKQGYKVTYLPVDEEGRLDLEELRAAITDDTALVSVMWANNETGTIFPIE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 165 AIGELTRSRGVLFHVDAAQSTGKVEIDLDKLKVDLMSFSAHKTYGPKGIGALYVRRKprVRIEGQMHGGGHERGMRSGTL 244
Cdd:TIGR03402 157 EIGEIAKERGALFHTDAVQAVGKIPIDLKEMNIDMLSLSGHKLHGPKGVGALYIRKG--TRFRPLLRGGHQERGRRAGTE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 245 ATHQIVGMGEAFRIAKEEMAQENARVLALRDRFfaqIDGLEEL----YINGSMTSRVPHNLNVSFNYVEGESLIMAL--K 318
Cdd:TIGR03402 235 NVPGIVGLGKAAELATEHLEEENTRVRALRDRL---EAGLLARipdaRLNGDPTKRLPNTVNISFEYIEGEAILLLLdmE 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599009 319 DLAVSSGSACTSASLEPSYVLRALGRNDELAHSSIRFTFGRFTTEEEIDYAAKKVVEAVSKLRELSPL 386
Cdd:TIGR03402 312 GICASSGSACTSGSLEPSHVLRAMGVPHTAAHGSIRFSLSRYNTEEDIDYVLEVLPPIIARLRAMSPF 379
|
|
| DNA_S_dndA |
TIGR03235 |
cysteine desulfurase DndA; This model describes DndA, a protein related to IscS and part of a ... |
6-356 |
3.84e-152 |
|
cysteine desulfurase DndA; This model describes DndA, a protein related to IscS and part of a larger family of cysteine desulfurases. It is encoded, typically, divergently from a conserved, sparsely distributed operon for sulfur modification of DNA. This modification system is designated dnd, after the phenotype of DNA degradation during electrophoresis. The system is sporadically distributed in bacteria, much like some restriction enzyme operons. DndB is described as a putative ATPase. [DNA metabolism, Restriction/modification]
Pssm-ID: 163191 [Multi-domain] Cd Length: 353 Bit Score: 434.22 E-value: 3.84e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 6 YLDYSATTPVDPRVAQKMSECLLMDgnFGNPASRSHVFGWKAEEAVENARRQVAELVNADPREIVWTSGATESDNLAIKG 85
Cdd:TIGR03235 1 YLDHNATTPIDPAVAEAMLPWLLEE--FGNPSSRTHEFGHNAKKAVERARKQVAEALGADTEEVIFTSGATESNNLAILG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 86 VAHFYSGKG-KHIITSKIEHKAVLDTCRQLEREGFEVTYLEPGEDGLITPALVEAALRDDTILVSVMHVNNEIGTVNDIA 164
Cdd:TIGR03235 79 LARAGEQKGkKHIITSAIEHPAVLEPIRALERNGFTVTYLPVDESGRIDVDELADAIRPDTLLVSIMHVNNETGSIQPIR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 165 AIGELTRSRGVLFHVDAAQSTGKVEIDLDKLKVDLMSFSAHKTYGPKGIGALYVRR--KPRVRIEGQMHGGGHERGMRSG 242
Cdd:TIGR03235 159 EIAEVLEAHEAFFHVDAAQVVGKITVDLSADRIDLISCSGHKIYGPKGIGALVIRKrgKPKAPLKPIMFGGGQERGLRPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 243 TLATHQIVGMGEAFRIAKEEMAQENARVLALRDRFFAQIDGLeELYINGSMTSRVPHNLNVSFNYVEGESLIMALK-DLA 321
Cdd:TIGR03235 239 TLPVHLIVGMGEAAEIARRNAQAWEVKLRAMRNQLRDALQTL-GVKLNGDPAETIPHILNFSIDGVNSEALIVNLRaDAA 317
|
330 340 350
....*....|....*....|....*....|....*
gi 15599009 322 VSSGSACTSASLEPSYVLRALGRNDELAHSSIRFT 356
Cdd:TIGR03235 318 VSTGSACSSSKYEPSHVLQAMGLDTDRARGAIRFS 352
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
5-395 |
1.19e-104 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 314.36 E-value: 1.19e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 5 IYLDYSATTPVDPRVAQKMSEclLMDGNFGNpASRSHVFGWKAEEAVENARRQVAELVNADPREIVWTSGATESDNLAIK 84
Cdd:PRK02948 2 IYLDYAATTPMSKEALQTYQK--AASQYFGN-ESSLHDIGGTASSLLQVCRKTFAEMIGGEEQGIYFTSGGTESNYLAIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 85 GVAHFYSGKGKHIITSKIEHKAVLDTCRQLEREGFEVTYLEPGEDGLITPALVEAALRDDTILVSVMHVNNEIGTVNDIA 164
Cdd:PRK02948 79 SLLNALPQNKKHIITTPMEHASIHSYFQSLESQGYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQPIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 165 AIGELTRSRGVLFHVDAAQSTGKVEIDLDKLKVDLMSFSAHKTYGPKGIGALYVRrkPRVRIEGQMHGGGHERGMRSGTL 244
Cdd:PRK02948 159 EIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYIN--PQVRWKPVFPGTTHEKGFRPGTV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 245 ATHQIVGMGEAFRIAKEEMAQENARVLALRDRFFAQIDGLE-ELYINGSMTSRVPHNLNVSFNYVEGEsLIMA---LKDL 320
Cdd:PRK02948 237 NVPGIAAFLTAAENILKNMQEESLRFKELRSYFLEQIQTLPlPIEVEGHSTSCLPHIIGVTIKGIEGQ-YTMLecnRRGI 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599009 321 AVSSGSACTSASLEPSYVLRALGRNDELAHSSIRFTFGRFTTEEEIDyaakKVVEAvsklreLSPLWDMYKEGVD 395
Cdd:PRK02948 316 AISTGSACQVGKQEPSKTMLAIGKTYEEAKQFVRFSFGQQTTKDQID----TTIHA------LETIGNQFYRGVK 380
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
5-368 |
1.88e-101 |
|
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: 305.71 E-value: 1.88e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 5 IYLDYSATTPVDPRVAQKMSEcLLMDGNfGNPASRSHVFGWKAEEAVENARRQVAELVNA-DPREIVWTSGATESDNLAI 83
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQE-YYTDYN-GNVHRGVHTLGKEATQAYEEAREKVAEFINApSNDEIIFTSGTTEAINLVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 84 KGVAHFYsGKGKHIITSKIEHKAVLDTCRQL-EREGFEVTYLEPGEDGLITPALVEAALRDDTILVSVMHVNNEIGTVND 162
Cdd:pfam00266 79 LSLGRSL-KPGDEIVITEMEHHANLVPWQELaKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 163 IAAIGELTRSRGVLFHVDAAQSTGKVEIDLDKLKVDLMSFSAHKTYGPKGIGALYVRRKPRVRIEGQMHGGG-------H 235
Cdd:pfam00266 158 VPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGmietvslQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 236 ERGM-------RSGTLATHQIVGMGEAFR-IAKEEMAQENARVLALRDRFFAQIDGLEELYINGSmtSRVPHNLNVSFNY 307
Cdd:pfam00266 238 ESTFadapwkfEAGTPNIAGIIGLGAALEyLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGP--ERRASIISFNFKG 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599009 308 VEGESLIMALKD--LAVSSGSACTsaslEPSYVLRALgrndelaHSSIRFTFGRFTTEEEIDY 368
Cdd:pfam00266 316 VHPHDVATLLDEsgIAVRSGHHCA----QPLMVRLGL-------GGTVRASFYIYNTQEDVDR 367
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
5-383 |
2.33e-75 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 239.27 E-value: 2.33e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 5 IYLDYSATTPVdPR-VAQKMSECLLMDGnfGNPASRSHVFGWKAEEAVENARRQVAELVNA-DPREIVWTSGATESDNLA 82
Cdd:COG0520 17 VYLDNAATGQK-PRpVIDAIRDYYEPYN--ANVHRGAHELSAEATDAYEAAREKVARFIGAaSPDEIIFTRGTTEAINLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 83 IKGVAHFysGKGKHIITSKIEHKAVLDTCRQL-EREGFEVTYLEPGEDGLITPALVEAALRDDTILVSVMHVNNEIGTVN 161
Cdd:COG0520 94 AYGLGRL--KPGDEILITEMEHHSNIVPWQELaERTGAEVRVIPLDEDGELDLEALEALLTPRTKLVAVTHVSNVTGTVN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 162 DIAAIGELTRSRGVLFHVDAAQSTGKVEIDLDKLKVDLMSFSAHKTYGPKGIGALYVRRK---------------PRVRI 226
Cdd:COG0520 172 PVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKREllealppflggggmiEWVSF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 227 EGQMHGGGHERgMRSGTLATHQIVGMGEAFRIaKEEMAQEN--ARVLALRDRFF---AQIDGLeELYINGSMTSRVPhnl 301
Cdd:COG0520 252 DGTTYADLPRR-FEAGTPNIAGAIGLGAAIDY-LEAIGMEAieARERELTAYALeglAAIPGV-RILGPADPEDRSG--- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 302 NVSFNyVEG---ESLIMALKDL--AVSSGSACTsaslEPsyVLRALGrndelAHSSIRFTFGRFTTEEEIDYaakkVVEA 376
Cdd:COG0520 326 IVSFN-VDGvhpHDVAALLDDEgiAVRAGHHCA----QP--LMRRLG-----VPGTVRASFHLYNTEEEIDR----LVEA 389
|
....*..
gi 15599009 377 VSKLREL 383
Cdd:COG0520 390 LKKLAEL 396
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
5-377 |
6.34e-70 |
|
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: 224.65 E-value: 6.34e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 5 IYLDYSATTPVDPRVAQKMSECLLMDGnfGNPASRSHVFGWKAEEAVENARRQVAELVNA-DPREIVWTSGATESDNLAI 83
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYN--ANVHRGVHELSARATDAYEAAREKVARFINApSPDEIIFTRNTTEAINLVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 84 KGVAhFYSGKGKHIITSKIEHKAVLDTCRQL-EREGFEVTYLEPGEDGLITPALVEAALRDDTILVSVMHVNNEIGTVND 162
Cdd:cd06453 79 YGLG-RANKPGDEIVTSVMEHHSNIVPWQQLaERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 163 IAAIGELTRSRGVLFHVDAAQSTGKVEIDLDKLKVDLMSFSAHKTYGPKGIGALYVRRKPRVRIEgQMHGGG-------- 234
Cdd:cd06453 158 VKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMP-PYGGGGemieevsf 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 235 -----HERGMR--SGTLATHQIVGMGEAFR----IAKEEMAQENARVLA-LRDRfFAQIDGLeELYinGSMTSRVPhnlN 302
Cdd:cd06453 237 eettyADLPHKfeAGTPNIAGAIGLGAAIDylekIGMEAIAAHEHELTAyALER-LSEIPGV-RVY--GDAEDRAG---V 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 303 VSFNyVEG---ESLIMAL--KDLAVSSGSACTsaslEPsyVLRALGRNdelahSSIRFTFGRFTTEEEIDyaakKVVEAV 377
Cdd:cd06453 310 VSFN-LEGihpHDVATILdqYGIAVRAGHHCA----QP--LMRRLGVP-----GTVRASFGLYNTEEEID----ALVEAL 373
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
5-383 |
1.76e-28 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 115.61 E-value: 1.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 5 IYLDYSATTPVDPRVAQKMSECLlMDGNfGNPASRSHVFGWKAEEAVENARRQVAELVNA-DPREIVWTSGATESDNLAI 83
Cdd:PLN02855 34 VYLDNAATSQKPAAVLDALQDYY-EEYN-SNVHRGIHALSAKATDAYELARKKVAAFINAsTSREIVFTRNATEAINLVA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 84 K--GVAHFysGKGKHIITSKIEHKAVLdTCRQL--EREGFEVTYLEPGEDGLITPALVEAALRDDTILVSVMHVNNEIGT 159
Cdd:PLN02855 112 YtwGLANL--KPGDEVILSVAEHHSNI-VPWQLvaQKTGAVLKFVGLTPDEVLDVEQLKELLSEKTKLVATHHVSNVLGS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 160 VNDIAAIGELTRSRGVLFHVDAAQSTGKVEIDLDKLKVDLMSFSAHKTYGPKGIGALYVRRKPRVRIEGQMhGGGH---- 235
Cdd:PLN02855 189 ILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLWGKSDLLESMPPFL-GGGEmisd 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 236 ---------ERGMR--SGTLATHQIVGMGEAFR-IAKEEMAQENARVLALRDRFFAQIDGLEELYINGSMTSRVPHNLN- 302
Cdd:PLN02855 268 vfldhstyaPPPSRfeAGTPAIGEAIGLGAAIDyLSEIGMDRIHEYEVELGTYLYEKLSSVPGVRIYGPKPSEGVGRAAl 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 303 VSFNyVEG------ESLIMALKDLAVSSGSACTsaslEPSYvlRALGRNDElAHSSIRFtfgrFTTEEEIDYAAKKVVEA 376
Cdd:PLN02855 348 CAFN-VEGihptdlSTFLDQQHGVAIRSGHHCA----QPLH--RYLGVNAS-ARASLYF----YNTKEEVDAFIHALKDT 415
|
....*..
gi 15599009 377 VSKLREL 383
Cdd:PLN02855 416 IAFFSSF 422
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
41-220 |
3.16e-28 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 114.46 E-value: 3.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 41 HVFGWKAEEAVENARRQVAELVNA-DPREIVWTSGATESDNLAIKGVAHFYSGKGKHIITSKIEHKAVLDTCRQL-EREG 118
Cdd:PRK09295 59 HTLSAQATEKMENVRKQAALFINArSAEELVFVRGTTEGINLVANSWGNSNVRAGDNIIISEMEHHANIVPWQMLcARVG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 119 FEVTYLEPGEDGLITPALVEAALRDDTILVSVMHVNNEIGTVNDIAAIGELTRSRGVLFHVDAAQSTGKVEIDLDKLKVD 198
Cdd:PRK09295 139 AELRVIPLNPDGTLQLETLPALFDERTRLLAITHVSNVLGTENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCD 218
|
170 180
....*....|....*....|..
gi 15599009 199 LMSFSAHKTYGPKGIGALYVRR 220
Cdd:PRK09295 219 FYVFSGHKLYGPTGIGILYVKE 240
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
5-217 |
1.14e-27 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 112.82 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 5 IYLDySATTPVDPR-VAQKMSECLLMDGnfGNPASRSHVFGWKAEEAVENARRQVAELVNA-DPREIVWTSGATESDNLA 82
Cdd:PRK10874 21 VYLD-SAATALKPQaVIEATQQFYSLSA--GNVHRSQFAAAQRLTARYEAAREQVAQLLNApDAKNIVWTRGTTESINLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 83 IKGVAHFYSGKGKHIITSKIEHKAVLDTCRQL-EREGFEVTYLEPGEDGLITPALVEAALRDDTILVSVMHVNNEIGTVN 161
Cdd:PRK10874 98 AQSYARPRLQPGDEIIVSEAEHHANLVPWLMVaQQTGAKVVKLPLGADRLPDVDLLPELITPRTRILALGQMSNVTGGCP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15599009 162 DIAAIGELTRSRGVLFHVDAAQSTGKVEIDLDKLKVDLMSFSAHKTYGPKGIGALY 217
Cdd:PRK10874 178 DLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLY 233
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
47-220 |
3.82e-18 |
|
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: 86.45 E-value: 3.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 47 AEEAVENARRQVAELVNA-DPREIVWTSGATESDNLAIK--GVAHFysGKGKHIITSKIEHKAVldtcrqleregfevty 123
Cdd:NF041166 287 ATDAYEGAREKVRRFIGApSVDEIIFVRGTTEAINLVAKswGRQNI--GAGDEIIVSHLEHHAN---------------- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 124 lepgedglITP-----ALVEAALR----DD----------------TILVSVMHVNNEIGTVNDIAAIGELTRSRGVLFH 178
Cdd:NF041166 349 --------IVPwqqlaQETGAKLRvipvDDsgqilldeyakllnprTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVL 420
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15599009 179 VDAAQSTGKVEIDLDKLKVDLMSFSAHKTYGPKGIGALYVRR 220
Cdd:NF041166 421 VDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGIGVVYGKR 462
|
|
| PucG |
COG0075 |
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ... |
115-287 |
1.00e-15 |
|
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: 77.82 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 115 EREGFEVTYLEPGEDGLITPALVEAALRDDTILVSVMHVNNE--IGTVNDIAAIGELTRSRGVLFHVDAAQSTGKVEIDL 192
Cdd:COG0075 94 ERYGAEVVVLEVPWGEAVDPEEVEEALAADPDIKAVAVVHNEtsTGVLNPLEEIGALAKEHGALLIVDAVSSLGGVPLDM 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 193 DKLKVDLMSFSAHKTY-GPKGIGALYVRRKPRVRIEG----------QMHGGGHERGMRSGTLATHQIVGMGEAFRIAKE 261
Cdd:COG0075 174 DEWGIDVVVSGSQKCLmLPPGLAFVAVSERALEAIEArklpsyyldlKLWLKYWEKGQTPYTPPVSLLYALREALDLILE 253
|
170 180
....*....|....*....|....*..
gi 15599009 262 E-MAQENARVLALRDRFFAqidGLEEL 287
Cdd:COG0075 254 EgLENRFARHRRLAEALRA---GLEAL 277
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
51-219 |
5.67e-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: 5.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 51 VENARRQVAELVNADPREIVWTSGATESDNLAIKGVAhfysGKGKHIITSKIEHKAVldTCRQLEREGFE---VTYLEPG 127
Cdd:cd01494 2 LEELEEKLARLLQPGNDKAVFVPSGTGANEAALLALL----GPGDEVIVDANGHGSR--YWVAAELAGAKpvpVPVDDAG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 128 EDGLITPALVEAALRDDTILVSVMHVNNEIGTVNDIAAIGELTRSRGVLFHVDAAQSTG---KVEIDLDKLKVDLMSFSA 204
Cdd:cd01494 76 YGGLDVAILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGaspAPGVLIPEGGADVVTFSL 155
|
170
....*....|....*
gi 15599009 205 HKTYGPKGIGALYVR 219
Cdd:cd01494 156 HKNLGGEGGGVVIVK 170
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
113-299 |
4.80e-11 |
|
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.
Pssm-ID: 99744 [Multi-domain] Cd Length: 356 Bit Score: 63.46 E-value: 4.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 113 QLEREGFEVTYLEPGEDGLITPALVEAALRDDTI-LVSVMHVNNEIGTVNDIAAIGELTRSRGVLFHVDAAQSTGKVEID 191
Cdd:cd06451 92 MAERYGADVDVVEKPWGEAVSPEEIAEALEQHDIkAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVDAVSSLGGEPFR 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 192 LDKLKVDLMSFSAHKTYG-PKGIGALYVRRKPRVRIE--GQMHGG----------GHERGMRSGTLATHQIVGMGEAFRI 258
Cdd:cd06451 172 MDEWGVDVAYTGSQKALGaPPGLGPIAFSERALERIKkkTKPKGFyfdlllllkyWGEGYSYPHTPPVNLLYALREALDL 251
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15599009 259 AKEE-------MAQENARVL--ALRDRFFaQIDGLEELYINGSMTSRVPH 299
Cdd:cd06451 252 ILEEglenrwaRHRRLAKALreGLEALGL-KLLAKPELRSPTVTAVLVPE 300
|
|
| PRK13479 |
PRK13479 |
2-aminoethylphosphonate--pyruvate transaminase; Provisional |
114-231 |
6.34e-10 |
|
2-aminoethylphosphonate--pyruvate transaminase; Provisional
Pssm-ID: 184076 [Multi-domain] Cd Length: 368 Bit Score: 60.31 E-value: 6.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 114 LEREGFEVTYLEPGEDGLITPALVEAAL-RDDTIL-VSVMHVNNEIGTVNDIAAIGELTRSRGVLFHVDAAQSTGKVEID 191
Cdd:PRK13479 99 AEYLGIAHVVLDTGEDEPPDAAEVEAALaADPRIThVALVHCETTTGILNPLDEIAAVAKRHGKRLIVDAMSSFGAIPID 178
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15599009 192 LDKLKVDLMSFSAHKTY-GPKGIGALYVRRKPRVRIEGQMH 231
Cdd:PRK13479 179 IAELGIDALISSANKCIeGVPGFGFVIARRSELEACKGNSR 219
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
56-377 |
8.61e-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: 57.15 E-value: 8.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 56 RQVAELVNADPREI-VWTSGATES---------DNLAIKGVAH--FYSGKGKHIITSKIEH----KA--VLDtcrqLERE 117
Cdd:COG0076 114 RWLADLLGLPEGAGgVFTSGGTEAnllallaarDRALARRVRAegLPGAPRPRIVVSEEAHssvdKAarLLG----LGRD 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 118 GfeVTYLEPGEDGLITPALVEAALRDD------TILV-----SVMHvnneiGTVNDIAAIGELTRSRGVLFHVDAA---- 182
Cdd:COG0076 190 A--LRKVPVDEDGRMDPDALEAAIDEDraaglnPIAVvatagTTNT-----GAIDPLAEIADIAREHGLWLHVDAAyggf 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 183 ---QSTGKVeiDLDKL-KVDLMSFSAHKT-YGPKGIGALYVRRKPRVRIEGQMHG---GGHERGmrSGTLATHQIVGmGE 254
Cdd:COG0076 263 alpSPELRH--LLDGIeRADSITVDPHKWlYVPYGCGAVLVRDPELLREAFSFHAsylGPADDG--VPNLGDYTLEL-SR 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 255 AFRIAK-------------EEMAQenaRVLALRDRFFAQIDGLEELYIngsmtsRVPHNLN-VSFNYVEGES-----LIM 315
Cdd:COG0076 338 RFRALKlwatlralgregyRELIE---RCIDLARYLAEGIAALPGFEL------LAPPELNiVCFRYKPAGLdeedaLNY 408
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599009 316 ALKDLAVSSGSA-CTSASLEPSYVLRALGRNDelahssirftfgrFTTEEEIDYAAKKVVEAV 377
Cdd:COG0076 409 ALRDRLRARGRAfLSPTKLDGRVVLRLVVLNP-------------RTTEDDVDALLDDLREAA 458
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
58-219 |
2.86e-07 |
|
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: 51.82 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 58 VAELVNADPREI--VWTSGATESDNLAIKGVAHFYSGKGKH----------IITSKIEHKAVLDTCRQLEREgfeVTYLE 125
Cdd:cd06450 47 LAKLFGLPSEDAdgVFTSGGSESNLLALLAARDRARKRLKAgggrgidklvIVCSDQAHVSVEKAAAYLDVK---VRLVP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 126 PGEDGLITPALVEAALRDD------TILVSVMHVNNEIGTVNDIAAIGELTRSRGVLFHVDAAqSTGKVEIDLD---KLK 196
Cdd:cd06450 124 VDEDGRMDPEALEAAIDEDkaeglnPIMVVATAGTTDTGAIDPLEEIADLAEKYDLWLHVDAA-YGGFLLPFPEprhLDF 202
|
170 180
....*....|....*....|....*....
gi 15599009 197 ----VDLMSFSAHKtYG--PKGIGALYVR 219
Cdd:cd06450 203 gierVDSISVDPHK-YGlvPLGCSAVLVR 230
|
|
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
5-234 |
7.29e-07 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 51.41 E-value: 7.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 5 IYLDYSATTpvdpRVAQKMSECLLMDGN---FGNPASRSHVfGWKAEEAVENARRQVAELVNADPRE--IVWTSGATESd 79
Cdd:PLN02724 36 VYLDHAGAT----LYSESQLEAALADFSsnvYGNPHSQSDS-SMRSSDTIESARQQVLEYFNAPPSDyaCVFTSGATAA- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 80 nLAIKGVAHFYSGKGKHIITSKiEHKAVLdtcrqlereGFEVTYLEPGedGLITPALVEAAL---RDDTILVSVMHV--- 153
Cdd:PLN02724 110 -LKLVGETFPWSSESHFCYTLE-NHNSVL---------GIREYALEKG--AAAIAVDIEEAAnqpTNSQGSVVVKSRglq 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 154 ----------NNEIGTVNDIAAIGELTRS---------------RGVLFH--------VDAAQSTGKVEIDLDKLKVDLM 200
Cdd:PLN02724 177 rrntsklqkrEDDGEAYNLFAFPSECNFSgakfpldlvklikdnQHSNFSksgrwmvlLDAAKGCGTSPPDLSRYPADFV 256
|
250 260 270
....*....|....*....|....*....|....*
gi 15599009 201 SFSAHKTYG-PKGIGALYVRRKPRVRIEGQMHGGG 234
Cdd:PLN02724 257 VVSFYKIFGyPTGLGALLVRRDAAKLLKKKYFGGG 291
|
|
| PRK09331 |
PRK09331 |
Sep-tRNA:Cys-tRNA synthetase; Provisional |
56-213 |
8.37e-07 |
|
Sep-tRNA:Cys-tRNA synthetase; Provisional
Pssm-ID: 236469 Cd Length: 387 Bit Score: 50.70 E-value: 8.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 56 RQVAELVNADprEIVWTSGATESdnlaIKGVAHFYSGKGKHIITSKIEHK----AVldtcrqlEREGFEVTY--LEPGED 129
Cdd:PRK09331 70 EDLAEFLGMD--EARVTHGAREG----KFAVMHSLCKKGDYVVLDGLAHYtsyvAA-------ERAGLNVREvpKTGYPE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 130 GLITP----ALVEAALRDDTILVSVM---HVNNEIGTVNDIAAIGELTRSRGVLFHVDAAQSTGKVEIDLDKLKVDLMSF 202
Cdd:PRK09331 137 YKITPeayaEKIEEVKEETGKPPALAlltHVDGNYGNLADAKKVAKVAHEYGIPFLLNGAYTVGRMPVDGKKLGADFIVG 216
|
170
....*....|....
gi 15599009 203 SAHKTY---GPKGI 213
Cdd:PRK09331 217 SGHKSMaasAPSGV 230
|
|
| SepCysS |
cd06452 |
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ... |
58-287 |
1.32e-06 |
|
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Cys-tRNA(Cys) is produced by O-phosphoseryl-tRNA synthetase which ligates O-phosphoserine (Sep) to tRNA(Cys), and Sep-tRNA:Cys-tRNA synthase (SepCysS) converts Sep-tRNA(Cys) to Cys-tRNA(Cys), in methanogenic archaea. SepCysS forms a dimer, each monomer is composed of a large and small domain; the larger, a typical pyridoxal 5'-phosphate (PLP)-dependent-like enzyme fold. In the active site of each monomer, PLP is covalently bound to a conserved Lys residue near the dimer interface.
Pssm-ID: 99745 Cd Length: 361 Bit Score: 50.08 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 58 VAELVNADPREIvwTSGATEsdnlAIKGVAHFYSGKGKHIITSKIEHKAvldTCRQLEREGFEVTYLEPGE--DGLITPA 135
Cdd:cd06452 53 LAEFLGMDEARV--TPGARE----GKFAVMHSLCEKGDWVVVDGLAHYT---SYVAAERAGLNVREVPNTGhpEYHITPE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 136 LVEAALRDDT-------ILVSVMHVNNEIGTVNDIAAIGELTRSRGVLFHVDAAQSTGKVEIDLDKLKVDLMSFSAHKTY 208
Cdd:cd06452 124 GYAEVIEEVKdefgkppALALLTHVDGNYGNLHDAKKIAKVCHEYGVPLLLNGAYTVGRMPVSGKELGADFIVGSGHKSM 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 209 ---GPKGIGALYVRRKPRVRIEGQMHgGGHERGMRSGTLATHQIVGMGEAF-----RIA--KEEMAQENARVLALRDrff 278
Cdd:cd06452 204 aasAPIGVLATTEEWADIVFRTSQMF-KIKEVELLGCTLRGAPLVTLMASFphvkeRVKrwDEEVEKARWFVAELEK--- 279
|
....*....
gi 15599009 279 aqIDGLEEL 287
Cdd:cd06452 280 --IEGIKQL 286
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
49-383 |
2.96e-05 |
|
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: 45.79 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 49 EAVENARRQVAELVNADprEIVWTSGATESDNLAIKGVAHFYSG----KGKHIITskiehkavlDTCRQLEREGFEVTYL 124
Cdd:cd06502 32 PTTAKLEARAAELFGKE--AALFVPSGTAANQLALAAHTQPGGSvichETAHIYT---------DEAGAPEFLSGVKLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 125 EPGEDGLITPALVEAALR--DD-----TILVSvMHVNNEIGTV---NDIAAIGELTRSRGVLFHVDAAQ-----STGKVE 189
Cdd:cd06502 101 VPGENGKLTPEDLEAAIRprDDihfppPSLVS-LENTTEGGTVyplDELKAISALAKENGLPLHLDGARlanaaAALGVA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 190 IDLDKLKVDLMSFSahktyGPKGIGAL----------YVRRKPRVRiegQMHGGgherGMRSGTLATHQIVGM---GEAF 256
Cdd:cd06502 180 LKTYKSGVDSVSFC-----LSKGGGAPvgavvvgnrdFIARARRRR---KQAGG----GMRQSGFLAAAGLAAlenDLWL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 257 RIAKEemAQENARVLAlrdrffaqidglEELYINGSMTSRVPHnlNVSFNYVEGESLIMALKDLAVSSGsactsasLEPS 336
Cdd:cd06502 248 RRLRH--DHEMARRLA------------EALEELGGLESEVQT--NIVLLDPVEANAVFVELSKEAIER-------RGEG 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15599009 337 YVLRALGrndelaHSSIRFTFGRFTTEEEIDyaakkvvEAVSKLREL 383
Cdd:cd06502 305 VLFYAWG------EGGVRFVTHWDTTEEDVD-------ELLSALKAV 338
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
108-273 |
3.32e-05 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 45.28 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 108 LDTCRQL-EREGFEVTYLEPGEDGLITPALVEAALRDDTI-------LVSVMHVNNEIG----TVNDIAAIGELTRSRGV 175
Cdd:pfam01212 84 FDETGGHaELGGVQPRPLDGDEAGNMDLEDLEAAIREVGAdifpptgLISLENTHNSAGgqvvSLENLREIAALAREHGI 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 176 LFHVD------AAQSTGkveIDLDKLK--VDLMSFSAHKTYGpKGIGAL------YVRRKPRVRiegQMHGGgherGMR- 240
Cdd:pfam01212 164 PVHLDgarfanAAVALG---VIVKEITsyADSVTMCLSKGLG-APVGSVlagsddFIAKAIRQR---KYLGG----GLRq 232
|
170 180 190
....*....|....*....|....*....|....*
gi 15599009 241 SGTLATHQIVGMGEAFRIAKE--EMAQENARVLAL 273
Cdd:pfam01212 233 AGVLAAAGLRALEEGVARLARdhATARRLAEGLEL 267
|
|
| PLN02409 |
PLN02409 |
serine--glyoxylate aminotransaminase |
113-224 |
8.39e-05 |
|
serine--glyoxylate aminotransaminase
Pssm-ID: 178031 [Multi-domain] Cd Length: 401 Bit Score: 44.36 E-value: 8.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 113 QLEREGFEVTYLEPGEDGLITPALVEAALRDDTI----LVSVMHVNNEIGTVNDIAAIGELTRSR--GVLFHVDAAQSTG 186
Cdd:PLN02409 102 QMQRLNFDVDVVESPWGQGADLDILKSKLRQDTNhkikAVCVVHNETSTGVTNDLAGVRKLLDCAqhPALLLVDGVSSIG 181
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 15599009 187 KVEIDLDKLKVDLMSFSAHKTYG-----------PKGIGALYVRRKPRV 224
Cdd:PLN02409 182 ALDFRMDEWGVDVALTGSQKALSlptglgivcasPKALEASKTAKSPRV 230
|
|
| PRK06225 |
PRK06225 |
pyridoxal phosphate-dependent aminotransferase; |
65-216 |
1.61e-04 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235749 [Multi-domain] Cd Length: 380 Bit Score: 43.59 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 65 DPREIVWTSGATESDNLAIKGVAhfysGKGKHIITSKIEHKAVLDTCRQLEREGFEVTYLEPGEDGLITPALVEAALRDD 144
Cdd:PRK06225 82 DDDEALITAGATESLYLVMRAFL----SPGDNAVTPDPGYLIIDNFASRFGAEVIEVPIYSEECNYKLTPELVKENMDEN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 145 TILVSVMHVNNEIG---TVNDIAAIGELTRSRGVLFHVD------AAQSTGKVEIDLDKlKVDLMSFSahKTYGPKG--I 213
Cdd:PRK06225 158 TRLIYLIDPLNPLGssyTEEEIKEFAEIARDNDAFLLHDctyrdfAREHTLAAEYAPEH-TVTSYSFS--KIFGMAGlrI 234
|
...
gi 15599009 214 GAL 216
Cdd:PRK06225 235 GAV 237
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
55-375 |
2.06e-04 |
|
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: 43.10 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 55 RRQVAEL------VNADPREIVWTSGATEsdnlAIKGVAHFYSGKGKHIITSKIEHKAVLDTCRQLEREGFEVTYLEPGE 128
Cdd:cd00609 42 REAIAEWlgrrggVDVPPEEIVVTNGAQE----ALSLLLRALLNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 129 DgLITPALVEAALRDDTILVSVMHVNNEIGTV---NDIAAIGELTRSRGVLFHVDAA----QSTGKVEIDLDKLKVD--- 198
Cdd:cd00609 118 F-LLDLELLEAAKTPKTKLLYLNNPNNPTGAVlseEELEELAELAKKHGILIISDEAyaelVYDGEPPPALALLDAYerv 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 199 --LMSFSahKTYGPKG--IGALYVRRKPRVRIEGQMHgggherGMRSGTLATHQIVGMGEAFRIAKEEMAQENARVLALR 274
Cdd:cd00609 197 ivLRSFS--KTFGLPGlrIGYLIAPPEELLERLKKLL------PYTTSGPSTLSQAAAAAALDDGEEHLEELRERYRRRR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 275 DRF---FAQIDGLEELYINGSM--TSRVPHNLNVSFnyvegesLIMALKDLAVssgsactsaslepsyVLRALGRNDELA 349
Cdd:cd00609 269 DALleaLKELGPLVVVKPSGGFflWLDLPEGDDEEF-------LERLLLEAGV---------------VVRPGSAFGEGG 326
|
330 340
....*....|....*....|....*.
gi 15599009 350 HSSIRFTFGrfTTEEEIDYAAKKVVE 375
Cdd:cd00609 327 EGFVRLSFA--TPEEELEEALERLAE 350
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
1-180 |
2.95e-03 |
|
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: 39.49 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 1 MKLPIYLdysATTPVDPRVAQKMSECLLMDGNF-----GNPASrshvfgwkaeEAVEnarRQVAELVNADPrEIVWTSGA 75
Cdd:cd00614 3 VAPPIYQ---TSTFVFPSPAEAADLFALREGGYiysriGNPTV----------DALE---KKLAALEGGEA-ALAFSSGM 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599009 76 TesdnlAIKGVAHFYSGKGKHIITSKIEHKAVLDTCRQLERE-GFEVTYLEPGEdglitPALVEAALRDDTILVSVMHVN 154
Cdd:cd00614 66 A-----AISTVLLALLKAGDHVVASDDLYGGTYRLFERLLPKlGIEVTFVDPDD-----PEALEAAIKPETKLVYVESPT 135
|
170 180
....*....|....*....|....*.
gi 15599009 155 NEIGTVNDIAAIGELTRSRGVLFHVD 180
Cdd:cd00614 136 NPTLKVVDIEAIAELAHEHGALLVVD 161
|
|
| |
