|
Name |
Accession |
Description |
Interval |
E-value |
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
5-381 |
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: 569.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 5 KTIYLDHAATTPMHPQVIEAMTAIMQDTFGNPSSIHGFGRHAHEKLETARQIIADSLQAKPHEIIFNSGGTEGDNTAILE 84
Cdd:COG1104 2 MMIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSSLHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNLAIKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 85 TAFSRQKEGRHLITTAIEHPAVLNTMKYLETKGFDVTYLPVDEKGNLSIEEVKKALREDTILVSVMYGNNEIGNLMPIKE 164
Cdd:COG1104 82 AARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQPIAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 165 IGELLADHPAYFHTDAVQAYGNQTIHPEELGIDLLSISAHKINGPKGVGFLYKRDGVNIPALLLGGEQEEKRRAGTENLA 244
Cdd:COG1104 162 IAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRKGVRLEPLIHGGGQERGLRSGTENVP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 245 GIWGMAKAVELLSpEEREARNNKYKGLQQLILDTLEANEIPYQVNGDLTNKLPHVLNLRLIGEANDLLLMKLDLNGVAIS 324
Cdd:COG1104 242 GIVGLGKAAELAA-EELEEEAARLRALRDRLEEGLLAAIPGVVINGDPENRLPNTLNFSFPGVEGEALLLALDLAGIAVS 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 488220002 325 TGSACTAGNIEPSHVLEAMyGEDTPILKESIRISFGLGNTEDDIQYFLDQLVRAVKK 381
Cdd:COG1104 321 SGSACSSGSLEPSHVLLAM-GLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVAR 376
|
|
| FeS_nifS |
TIGR03402 |
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related ... |
7-381 |
1.73e-156 |
|
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: 445.13 E-value: 1.73e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 7 IYLDHAATTPMHPQVIEAMTAIMQDTFGNPSSIHGFGRHAHEKLETARQIIADSLQAKPHEIIFNSGGTEGDNTAILETA 86
Cdd:TIGR03402 1 IYLDNNATTRVDPEVLEAMLPYFTEYFGNPSSMHSFGGEVGKAVEEAREQVAKLLGAEPDEIIFTSGGTESDNTAIKSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 87 FSrQKEGRHLITTAIEHPAVLNTMKYLETKGFDVTYLPVDEKGNLSIEEVKKALREDTILVSVMYGNNEIGNLMPIKEIG 166
Cdd:TIGR03402 81 AA-QPEKRHIITTAVEHPAVLSLCQHLEKQGYKVTYLPVDEEGRLDLEELRAAITDDTALVSVMWANNETGTIFPIEEIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 167 ELLADHPAYFHTDAVQAYGNQTIHPEELGIDLLSISAHKINGPKGVGFLYKRDGVNIPALLLGGEQEEKRRAGTENLAGI 246
Cdd:TIGR03402 160 EIAKERGALFHTDAVQAVGKIPIDLKEMNIDMLSLSGHKLHGPKGVGALYIRKGTRFRPLLRGGHQERGRRAGTENVPGI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 247 WGMAKAVElLSPEEREARNNKYKGLQqlilDTLEA---NEIPY-QVNGDLTNKLPHVLNLRLI---GEAndlLLMKLDLN 319
Cdd:TIGR03402 240 VGLGKAAE-LATEHLEEENTRVRALR----DRLEAgllARIPDaRLNGDPTKRLPNTVNISFEyieGEA---ILLLLDME 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488220002 320 GVAISTGSACTAGNIEPSHVLEAMyGEDTPILKESIRISFGLGNTEDDIQYFLDQLVRAVKK 381
Cdd:TIGR03402 312 GICASSGSACTSGSLEPSHVLRAM-GVPHTAAHGSIRFSLSRYNTEEDIDYVLEVLPPIIAR 372
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
7-368 |
2.34e-122 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 357.81 E-value: 2.34e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 7 IYLDHAATTPMHPQVIEAMTAIMQDTFGNPSSI-HGFGRHAHEKLETARQIIADSLQAKPHEIIFNSGGTEGDNTAILET 85
Cdd:PLN02651 1 LYLDMQATTPIDPRVLDAMLPFLIEHFGNPHSRtHLYGWESEDAVEKARAQVAALIGADPKEIIFTSGATESNNLAIKGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 86 AFSRQKEGRHLITTAIEHPAVLNTMKYLETKGFDVTYLPVDEKGNLSIEEVKKALREDTILVSVMYGNNEIGNLMPIKEI 165
Cdd:PLN02651 81 MHFYKDKKKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVEEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 166 GELLADHPAYFHTDAVQAYGNQTIHPEELGIDLLSISAHKINGPKGVGFLY--KRDGVNIPALLLGGEQEEKRRAGTENL 243
Cdd:PLN02651 161 GELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYvrRRPRVRLEPLMSGGGQERGRRSGTENT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 244 AGIWGMAKAVELLSpEEREARNNKYKGLQQLILDTLEANEIPYQVNG--DLTNKLPHVLNLRLIGEANDLLLMKldLNGV 321
Cdd:PLN02651 241 PLVVGLGAACELAM-KEMDYDEKHMKALRERLLNGLRAKLGGVRVNGprDPEKRYPGTLNLSFAYVEGESLLMG--LKEV 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 488220002 322 AISTGSACTAGNIEPSHVLEAMyGEDTPILKESIRISFGLGNTEDDI 368
Cdd:PLN02651 318 AVSSGSACTSASLEPSYVLRAL-GVPEEMAHGSLRLGVGRFTTEEEV 363
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
7-371 |
7.40e-88 |
|
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: 269.89 E-value: 7.40e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 7 IYLDHAATTPMHPQVIEAMTAIMQDTFGNP-SSIHGFGRHAHEKLETARQIIADSLQAK-PHEIIFNSGGTEGDNTAILe 84
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVhRGVHTLGKEATQAYEEAREKVAEFINAPsNDEIIFTSGTTEAINLVAL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 85 TAFSRQKEGRHLITTAIEHPAVLNTMKYL-ETKGFDVTYLPVDEKGNLSIEEVKKALREDTILVSVMYGNNEIGNLMPIK 163
Cdd:pfam00266 80 SLGRSLKPGDEIVITEMEHHANLVPWQELaKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 164 EIGELLADHPAYFHTDAVQAYGNQTIHPEELGIDLLSISAHKINGPKGVGFLYKRD--GVNIPALLLGG----------- 230
Cdd:pfam00266 160 EIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRdlLEKMPPLLGGGgmietvslqes 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 231 ---EQEEKRRAGTENLAGIWGMAKAVELLSPEEREARNNKYKGLQQLILDTLEANEIpYQVNGDLtnKLPHVLNLRLIGE 307
Cdd:pfam00266 240 tfaDAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPG-IRLYGPE--RRASIISFNFKGV 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488220002 308 ANDLLLMKLDLNGVAISTGSACTagniEPSHVLEAMYGedtpilkeSIRISFGLGNTEDDIQYF 371
Cdd:pfam00266 317 HPHDVATLLDESGIAVRSGHHCA----QPLMVRLGLGG--------TVRASFYIYNTQEDVDRL 368
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
7-379 |
2.60e-56 |
|
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: 188.44 E-value: 2.60e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 7 IYLDHAATTPMHPQVIEAMTAIMQDTFGNPS-SIHGFGRHAHEKLETARQIIADSLQAK-PHEIIFNSGGTEGDNTAILe 84
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHrGVHELSARATDAYEAAREKVARFINAPsPDEIIFTRNTTEAINLVAY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 85 tAFSRQ-KEGRHLITTAIEHPAVLNTMKYL-ETKGFDVTYLPVDEKGNLSIEEVKKALREDTILVSVMYGNNEIGNLMPI 162
Cdd:cd06453 80 -GLGRAnKPGDEIVTSVMEHHSNIVPWQQLaERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 163 KEIGELLADHPAYFHTDAVQAYGNQTIHPEELGIDLLSISAHKINGPKGVGFLYKRDGV--NIPALLLGGEQEE------ 234
Cdd:cd06453 159 KEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELleEMPPYGGGGEMIEevsfee 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 235 --------KRRAGTENLAGIWGMAKAVELLSPEEREARNNKYKGLQQLILDTLEanEIPY-QVNGDLTNKLPhVLNLRLI 305
Cdd:cd06453 239 ttyadlphKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLS--EIPGvRVYGDAEDRAG-VVSFNLE 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488220002 306 GEANDLLLMKLDLNGVAISTGSACTagniEPSHvlEAMYgedtpiLKESIRISFGLGNTEDDIqyflDQLVRAV 379
Cdd:cd06453 316 GIHPHDVATILDQYGIAVRAGHHCA----QPLM--RRLG------VPGTVRASFGLYNTEEEI----DALVEAL 373
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
5-381 |
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: 569.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 5 KTIYLDHAATTPMHPQVIEAMTAIMQDTFGNPSSIHGFGRHAHEKLETARQIIADSLQAKPHEIIFNSGGTEGDNTAILE 84
Cdd:COG1104 2 MMIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSSLHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNLAIKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 85 TAFSRQKEGRHLITTAIEHPAVLNTMKYLETKGFDVTYLPVDEKGNLSIEEVKKALREDTILVSVMYGNNEIGNLMPIKE 164
Cdd:COG1104 82 AARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQPIAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 165 IGELLADHPAYFHTDAVQAYGNQTIHPEELGIDLLSISAHKINGPKGVGFLYKRDGVNIPALLLGGEQEEKRRAGTENLA 244
Cdd:COG1104 162 IAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRKGVRLEPLIHGGGQERGLRSGTENVP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 245 GIWGMAKAVELLSpEEREARNNKYKGLQQLILDTLEANEIPYQVNGDLTNKLPHVLNLRLIGEANDLLLMKLDLNGVAIS 324
Cdd:COG1104 242 GIVGLGKAAELAA-EELEEEAARLRALRDRLEEGLLAAIPGVVINGDPENRLPNTLNFSFPGVEGEALLLALDLAGIAVS 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 488220002 325 TGSACTAGNIEPSHVLEAMyGEDTPILKESIRISFGLGNTEDDIQYFLDQLVRAVKK 381
Cdd:COG1104 321 SGSACSSGSLEPSHVLLAM-GLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVAR 376
|
|
| FeS_nifS |
TIGR03402 |
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related ... |
7-381 |
1.73e-156 |
|
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: 445.13 E-value: 1.73e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 7 IYLDHAATTPMHPQVIEAMTAIMQDTFGNPSSIHGFGRHAHEKLETARQIIADSLQAKPHEIIFNSGGTEGDNTAILETA 86
Cdd:TIGR03402 1 IYLDNNATTRVDPEVLEAMLPYFTEYFGNPSSMHSFGGEVGKAVEEAREQVAKLLGAEPDEIIFTSGGTESDNTAIKSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 87 FSrQKEGRHLITTAIEHPAVLNTMKYLETKGFDVTYLPVDEKGNLSIEEVKKALREDTILVSVMYGNNEIGNLMPIKEIG 166
Cdd:TIGR03402 81 AA-QPEKRHIITTAVEHPAVLSLCQHLEKQGYKVTYLPVDEEGRLDLEELRAAITDDTALVSVMWANNETGTIFPIEEIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 167 ELLADHPAYFHTDAVQAYGNQTIHPEELGIDLLSISAHKINGPKGVGFLYKRDGVNIPALLLGGEQEEKRRAGTENLAGI 246
Cdd:TIGR03402 160 EIAKERGALFHTDAVQAVGKIPIDLKEMNIDMLSLSGHKLHGPKGVGALYIRKGTRFRPLLRGGHQERGRRAGTENVPGI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 247 WGMAKAVElLSPEEREARNNKYKGLQqlilDTLEA---NEIPY-QVNGDLTNKLPHVLNLRLI---GEAndlLLMKLDLN 319
Cdd:TIGR03402 240 VGLGKAAE-LATEHLEEENTRVRALR----DRLEAgllARIPDaRLNGDPTKRLPNTVNISFEyieGEA---ILLLLDME 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488220002 320 GVAISTGSACTAGNIEPSHVLEAMyGEDTPILKESIRISFGLGNTEDDIQYFLDQLVRAVKK 381
Cdd:TIGR03402 312 GICASSGSACTSGSLEPSHVLRAM-GVPHTAAHGSIRFSLSRYNTEEDIDYVLEVLPPIIAR 372
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
7-368 |
2.34e-122 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 357.81 E-value: 2.34e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 7 IYLDHAATTPMHPQVIEAMTAIMQDTFGNPSSI-HGFGRHAHEKLETARQIIADSLQAKPHEIIFNSGGTEGDNTAILET 85
Cdd:PLN02651 1 LYLDMQATTPIDPRVLDAMLPFLIEHFGNPHSRtHLYGWESEDAVEKARAQVAALIGADPKEIIFTSGATESNNLAIKGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 86 AFSRQKEGRHLITTAIEHPAVLNTMKYLETKGFDVTYLPVDEKGNLSIEEVKKALREDTILVSVMYGNNEIGNLMPIKEI 165
Cdd:PLN02651 81 MHFYKDKKKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVEEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 166 GELLADHPAYFHTDAVQAYGNQTIHPEELGIDLLSISAHKINGPKGVGFLY--KRDGVNIPALLLGGEQEEKRRAGTENL 243
Cdd:PLN02651 161 GELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYvrRRPRVRLEPLMSGGGQERGRRSGTENT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 244 AGIWGMAKAVELLSpEEREARNNKYKGLQQLILDTLEANEIPYQVNG--DLTNKLPHVLNLRLIGEANDLLLMKldLNGV 321
Cdd:PLN02651 241 PLVVGLGAACELAM-KEMDYDEKHMKALRERLLNGLRAKLGGVRVNGprDPEKRYPGTLNLSFAYVEGESLLMG--LKEV 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 488220002 322 AISTGSACTAGNIEPSHVLEAMyGEDTPILKESIRISFGLGNTEDDI 368
Cdd:PLN02651 318 AVSSGSACTSASLEPSYVLRAL-GVPEEMAHGSLRLGVGRFTTEEEV 363
|
|
| DNA_S_dndA |
TIGR03235 |
cysteine desulfurase DndA; This model describes DndA, a protein related to IscS and part of a ... |
8-358 |
5.32e-118 |
|
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: 346.40 E-value: 5.32e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 8 YLDHAATTPMHPQVIEAMTAIMQDTFGNPSSI-HGFGRHAHEKLETARQIIADSLQAKPHEIIFNSGGTEGDNTAILETA 86
Cdd:TIGR03235 1 YLDHNATTPIDPAVAEAMLPWLLEEFGNPSSRtHEFGHNAKKAVERARKQVAEALGADTEEVIFTSGATESNNLAILGLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 87 -FSRQKEGRHLITTAIEHPAVLNTMKYLETKGFDVTYLPVDEKGNLSIEEVKKALREDTILVSVMYGNNEIGNLMPIKEI 165
Cdd:TIGR03235 81 rAGEQKGKKHIITSAIEHPAVLEPIRALERNGFTVTYLPVDESGRIDVDELADAIRPDTLLVSIMHVNNETGSIQPIREI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 166 GELLADHPAYFHTDAVQAYGNQTIHPEELGIDLLSISAHKINGPKGVGFLY--KRDGVNIP--ALLLGGEQEEKRRAGTE 241
Cdd:TIGR03235 161 AEVLEAHEAFFHVDAAQVVGKITVDLSADRIDLISCSGHKIYGPKGIGALVirKRGKPKAPlkPIMFGGGQERGLRPGTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 242 NLAGIWGMAKAVElLSPEEREARNNKYKGLQQLILDTLEANeiPYQVNGDLTNKLPHVLNLRLIGeANDLLLMKLDLNGV 321
Cdd:TIGR03235 241 PVHLIVGMGEAAE-IARRNAQAWEVKLRAMRNQLRDALQTL--GVKLNGDPAETIPHILNFSIDG-VNSEALIVNLRADA 316
|
330 340 350
....*....|....*....|....*....|....*..
gi 488220002 322 AISTGSACTAGNIEPSHVLEAMyGEDTPILKESIRIS 358
Cdd:TIGR03235 317 AVSTGSACSSSKYEPSHVLQAM-GLDTDRARGAIRFS 352
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
7-381 |
1.69e-117 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 346.93 E-value: 1.69e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 7 IYLDHAATTPMHPQVIEAMTAIMQ--DTFGNPSS-IHGFGRHAHEKLETARQIIADSLQAKPHEIIFNSGGTEGDNTAIL 83
Cdd:PRK14012 5 IYLDYSATTPVDPRVAEKMMPYLTmdGTFGNPASrSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDNLAIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 84 ETAFSRQKEGRHLITTAIEHPAVLNTMKYLETKGFDVTYLPVDEKGNLSIEEVKKALREDTILVSVMYGNNEIGNLMPIK 163
Cdd:PRK14012 85 GAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVIQDIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 164 EIGELLADHPAYFHTDAVQAYGNQTIHPEELGIDLLSISAHKINGPKGVGFLY--KRDGVNIPALLLGGEQEEKRRAGTE 241
Cdd:PRK14012 165 AIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYvrRKPRVRLEAQMHGGGHERGMRSGTL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 242 NLAGIWGMAKAVElLSPEEREARNNKYKGLQQLILDTLEANEIPYqVNGDLTNKLPHVLNLRLIGEANDLLLMKldLNGV 321
Cdd:PRK14012 245 PTHQIVGMGEAAR-IAKEEMATENERIRALRDRLWNGIKDIEEVY-LNGDLEQRVPGNLNVSFNYVEGESLIMA--LKDL 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 322 AISTGSACTAGNIEPSHVLEAMyGEDTPILKESIRISFGLGNTEDDIQYFLDQLVRAVKK 381
Cdd:PRK14012 321 AVSSGSACTSASLEPSYVLRAL-GLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGK 379
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
7-375 |
3.81e-98 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 296.64 E-value: 3.81e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 7 IYLDHAATTPMHPQVIEAMTAIMQDTFGNPSSIHGFGRHAHEKLETARQIIADSLQAKPHEIIFNSGGTEGDNTAILETA 86
Cdd:PRK02948 2 IYLDYAATTPMSKEALQTYQKAASQYFGNESSLHDIGGTASSLLQVCRKTFAEMIGGEEQGIYFTSGGTESNYLAIQSLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 87 FSRQKEGRHLITTAIEHPAVLNTMKYLETKGFDVTYLPVDEKGNLSIEEVKKALREDTILVSVMYGNNEIGNLMPIKEIG 166
Cdd:PRK02948 82 NALPQNKKHIITTPMEHASIHSYFQSLESQGYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQPIAEIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 167 ELLADHPAYFHTDAVQAYGNQTIHPEELGIDLLSISAHKINGPKGVGFLYKRDGVNIPALLLGGEQEEKRRAGTENLAGI 246
Cdd:PRK02948 162 ALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYINPQVRWKPVFPGTTHEKGFRPGTVNVPGI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 247 WGMAKAVELLSpEEREARNNKYKGLQQLILDTLEANEIPYQVNGDLTNKLPHVLNLRLIGEANDLLLMKLDLNGVAISTG 326
Cdd:PRK02948 242 AAFLTAAENIL-KNMQEESLRFKELRSYFLEQIQTLPLPIEVEGHSTSCLPHIIGVTIKGIEGQYTMLECNRRGIAISTG 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 488220002 327 SACTAGNIEPSHVLEAMyGEDTPILKESIRISFGLGNTEDDIQYFLDQL 375
Cdd:PRK02948 321 SACQVGKQEPSKTMLAI-GKTYEEAKQFVRFSFGQQTTKDQIDTTIHAL 368
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
7-371 |
7.40e-88 |
|
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: 269.89 E-value: 7.40e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 7 IYLDHAATTPMHPQVIEAMTAIMQDTFGNP-SSIHGFGRHAHEKLETARQIIADSLQAK-PHEIIFNSGGTEGDNTAILe 84
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVhRGVHTLGKEATQAYEEAREKVAEFINAPsNDEIIFTSGTTEAINLVAL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 85 TAFSRQKEGRHLITTAIEHPAVLNTMKYL-ETKGFDVTYLPVDEKGNLSIEEVKKALREDTILVSVMYGNNEIGNLMPIK 163
Cdd:pfam00266 80 SLGRSLKPGDEIVITEMEHHANLVPWQELaKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 164 EIGELLADHPAYFHTDAVQAYGNQTIHPEELGIDLLSISAHKINGPKGVGFLYKRD--GVNIPALLLGG----------- 230
Cdd:pfam00266 160 EIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRdlLEKMPPLLGGGgmietvslqes 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 231 ---EQEEKRRAGTENLAGIWGMAKAVELLSPEEREARNNKYKGLQQLILDTLEANEIpYQVNGDLtnKLPHVLNLRLIGE 307
Cdd:pfam00266 240 tfaDAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPG-IRLYGPE--RRASIISFNFKGV 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488220002 308 ANDLLLMKLDLNGVAISTGSACTagniEPSHVLEAMYGedtpilkeSIRISFGLGNTEDDIQYF 371
Cdd:pfam00266 317 HPHDVATLLDESGIAVRSGHHCA----QPLMVRLGLGG--------TVRASFYIYNTQEDVDRL 368
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
7-381 |
7.75e-67 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 216.54 E-value: 7.75e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 7 IYLDHAATTPMHPQVIEAMTAIMQDTFGNPS-SIHGFGRHAHEKLETARQIIADSLQAK-PHEIIFNSGGTEGDNTAILe 84
Cdd:COG0520 17 VYLDNAATGQKPRPVIDAIRDYYEPYNANVHrGAHELSAEATDAYEAAREKVARFIGAAsPDEIIFTRGTTEAINLVAY- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 85 tAFSRQKEGRHLITTAIEHPAVLNTMKYL-ETKGFDVTYLPVDEKGNLSIEEVKKALREDTILVSVMYGNNEIGNLMPIK 163
Cdd:COG0520 96 -GLGRLKPGDEILITEMEHHSNIVPWQELaERTGAEVRVIPLDEDGELDLEALEALLTPRTKLVAVTHVSNVTGTVNPVK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 164 EIGELLADHPAYFHTDAVQAYGNQTIHPEELGIDLLSISAHKINGPKGVGFLYKRDGV--NIPALLLGGEQEEK------ 235
Cdd:COG0520 175 EIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELleALPPFLGGGGMIEWvsfdgt 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 236 ------RR--AGTENLAGIWGMAKAVELLS---PEEREARNnkyKGLQQLILDTLEanEIP-YQVNG--DLTNKLPhVLN 301
Cdd:COG0520 255 tyadlpRRfeAGTPNIAGAIGLGAAIDYLEaigMEAIEARE---RELTAYALEGLA--AIPgVRILGpaDPEDRSG-IVS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 302 LRLIGEANDLLLMKLDLNGVAISTGSACTagniepsHVLEAMYGedtpiLKESIRISFGLGNTEDDIqyflDQLVRAVKK 381
Cdd:COG0520 329 FNVDGVHPHDVAALLDDEGIAVRAGHHCA-------QPLMRRLG-----VPGTVRASFHLYNTEEEI----DRLVEALKK 392
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
7-379 |
2.60e-56 |
|
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: 188.44 E-value: 2.60e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 7 IYLDHAATTPMHPQVIEAMTAIMQDTFGNPS-SIHGFGRHAHEKLETARQIIADSLQAK-PHEIIFNSGGTEGDNTAILe 84
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHrGVHELSARATDAYEAAREKVARFINAPsPDEIIFTRNTTEAINLVAY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 85 tAFSRQ-KEGRHLITTAIEHPAVLNTMKYL-ETKGFDVTYLPVDEKGNLSIEEVKKALREDTILVSVMYGNNEIGNLMPI 162
Cdd:cd06453 80 -GLGRAnKPGDEIVTSVMEHHSNIVPWQQLaERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 163 KEIGELLADHPAYFHTDAVQAYGNQTIHPEELGIDLLSISAHKINGPKGVGFLYKRDGV--NIPALLLGGEQEE------ 234
Cdd:cd06453 159 KEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELleEMPPYGGGGEMIEevsfee 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 235 --------KRRAGTENLAGIWGMAKAVELLSPEEREARNNKYKGLQQLILDTLEanEIPY-QVNGDLTNKLPhVLNLRLI 305
Cdd:cd06453 239 ttyadlphKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLS--EIPGvRVYGDAEDRAG-VVSFNLE 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488220002 306 GEANDLLLMKLDLNGVAISTGSACTagniEPSHvlEAMYgedtpiLKESIRISFGLGNTEDDIqyflDQLVRAV 379
Cdd:cd06453 316 GIHPHDVATILDQYGIAVRAGHHCA----QPLM--RRLG------VPGTVRASFGLYNTEEEI----DALVEAL 373
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
2-375 |
1.75e-29 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 117.93 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 2 NEVKTIYLDHAATTPMHPQVIEAMTAIMQDTFGN-PSSIHGFGRHAHEKLETARQIIADSLQAK-PHEIIFNSGGTEGDN 79
Cdd:PLN02855 29 NGSKLVYLDNAATSQKPAAVLDALQDYYEEYNSNvHRGIHALSAKATDAYELARKKVAAFINAStSREIVFTRNATEAIN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 80 TAILETAFSRQKEGRHLITTAIEHPAVLNTMKYL-ETKGFDVTYLPVDEKGNLSIEEVKKALREDTILVSVMYGNNEIGN 158
Cdd:PLN02855 109 LVAYTWGLANLKPGDEVILSVAEHHSNIVPWQLVaQKTGAVLKFVGLTPDEVLDVEQLKELLSEKTKLVATHHVSNVLGS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 159 LMPIKEIGELLADHPAYFHTDAVQAYGNQTIHPEELGIDLLSISAHKINGPKGVGFLYKRDGV--NIPALLLGGE----- 231
Cdd:PLN02855 189 ILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLWGKSDLleSMPPFLGGGEmisdv 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 232 -------QEEKRR--AGTENLAGIWGMAKAVELLSpeerearnnkykglqQLILDTLEANEIpyQVNGDLTNKLPHVLNL 302
Cdd:PLN02855 269 fldhstyAPPPSRfeAGTPAIGEAIGLGAAIDYLS---------------EIGMDRIHEYEV--ELGTYLYEKLSSVPGV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 303 RLIG--------------------EANDLLLMkLDL-NGVAISTGSACTagniEPSHvleAMYGedtpiLKESIRISFGL 361
Cdd:PLN02855 332 RIYGpkpsegvgraalcafnvegiHPTDLSTF-LDQqHGVAIRSGHHCA----QPLH---RYLG-----VNASARASLYF 398
|
410
....*....|....
gi 488220002 362 GNTEDDIQYFLDQL 375
Cdd:PLN02855 399 YNTKEEVDAFIHAL 412
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
2-381 |
2.71e-24 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 102.91 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 2 NEVKTIYLDHAATTPMHPQVIEAMTAIMQDTFGN-PSSIHGFGRHAHEKLETARQIIADSLQAK-PHEIIFNSGGTEGDN 79
Cdd:PRK09295 20 NGLPLAYLDSAASAQKPSQVIDAEAEFYRHGYAAvHRGIHTLSAQATEKMENVRKQAALFINARsAEELVFVRGTTEGIN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 80 TAILETAFSRQKEGRHLITTAIEHPAVLNTMKYL-ETKGFDVTYLPVDEKGNLSIEEVKKALREDTILVSVMYGNNEIGN 158
Cdd:PRK09295 100 LVANSWGNSNVRAGDNIIISEMEHHANIVPWQMLcARVGAELRVIPLNPDGTLQLETLPALFDERTRLLAITHVSNVLGT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 159 LMPIKEIGELLADHPAYFHTDAVQAYGNQTIHPEELGIDLLSISAHKINGPKGVGFLYKRDGV--NIPALLLGG------ 230
Cdd:PRK09295 180 ENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKEALlqEMPPWEGGGsmiatv 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 231 ---------EQEEKRRAGTENLAGIWGMAKAVELLSPEEREARNNKYKGLQQLILDTLEAneipyqvngdltnklphVLN 301
Cdd:PRK09295 260 sltegttwaKAPWRFEAGTPNTGGIIGLGAALDYVSALGLNNIAEYEQNLMHYALSQLES-----------------VPD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 302 LRLIGEANDLLLMK--------------LDLNGVAISTGSACTAGNIEPSHVlEAMygedtpilkesIRISFGLGNTEDD 367
Cdd:PRK09295 323 LTLYGPQNRLGVIAfnlgkhhaydvgsfLDNYGIAVRTGHHCAMPLMAYYNV-PAM-----------CRASLAMYNTHEE 390
|
410
....*....|....
gi 488220002 368 IqyflDQLVRAVKK 381
Cdd:PRK09295 391 V----DRLVAGLQR 400
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
6-381 |
2.20e-17 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 82.78 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 6 TIYLDHAATTpMHPQ-VIEAMTAIMQDTFGN-PSSIHGFGRHAHEKLETARQIIADSLQA-KPHEIIFNSGGTEGDNTAI 82
Cdd:PRK10874 20 GVYLDSAATA-LKPQaVIEATQQFYSLSAGNvHRSQFAAAQRLTARYEAAREQVAQLLNApDAKNIVWTRGTTESINLVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 83 LETAFSRQKEGRHLITTAIEHPAvlNTMKYL---ETKGFDVTYLPVDEKGNLSIEEVKKALREDTILVSVMYGNNEIGNL 159
Cdd:PRK10874 99 QSYARPRLQPGDEIIVSEAEHHA--NLVPWLmvaQQTGAKVVKLPLGADRLPDVDLLPELITPRTRILALGQMSNVTGGC 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 160 MPIKEIGELLADHPAYFHTDAVQAYGNQTIHPEELGIDLLSISAHKINGPKGVGFLY-KRDGVN-IPALLLGG------- 230
Cdd:PRK10874 177 PDLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYgKSELLEaMSPWQGGGkmltevs 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 231 -----EQEEKRR--AGTENLAGIWGMAKAVELLSPEEREARNNKYKGLQQLILDTLEaneipyQVNGDLTNKLPH--VLN 301
Cdd:PRK10874 257 fdgftPQSAPWRfeAGTPNVAGVIGLSAALEWLADIDINQAESWSRSLATLAEDALA------KLPGFRSFRCQDssLLA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 302 LRLIGEANDLLLMKLDLNGVAISTGSACTagniEPshvLEAMYGedtpiLKESIRISFGLGNTEDDIqyflDQLVRAVKK 381
Cdd:PRK10874 331 FDFAGVHHSDLVTLLAEYGIALRAGQHCA----QP---LLAALG-----VTGTLRASFAPYNTQSDV----DALVNAVDR 394
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
117-215 |
8.30e-11 |
|
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.
Pssm-ID: 99744 [Multi-domain] Cd Length: 356 Bit Score: 62.69 E-value: 8.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 117 GFDVTYLPVDEKGNLSIEEVKKALREDTI-LVSVMYGNNEIGNLMPIKEIGELLADHPAYFHTDAVQAYGNQTIHPEELG 195
Cdd:cd06451 97 GADVDVVEKPWGEAVSPEEIAEALEQHDIkAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVDAVSSLGGEPFRMDEWG 176
|
90 100
....*....|....*....|.
gi 488220002 196 IDLLSISAHK-INGPKGVGFL 215
Cdd:cd06451 177 VDVAYTGSQKaLGAPPGLGPI 197
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
49-218 |
2.23e-10 |
|
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: 58.93 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 49 KLETARQIIADSLQAKPHEIIFNSGGTEGDNTAiLETAFSRqkeGRHLITTAIEHPAVLNTMkyLETKGFDVTYLPVDE- 127
Cdd:cd01494 1 KLEELEEKLARLLQPGNDKAVFVPSGTGANEAA-LLALLGP---GDEVIVDANGHGSRYWVA--AELAGAKPVPVPVDDa 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 128 -KGNLSIEEVKKALREDTI-LVSVMYGNNEIGNLMPIKEIGELLADHPAYFHTDAVQAYGNQT---IHPEELGIDLLSIS 202
Cdd:cd01494 75 gYGGLDVAILEELKAKPNVaLIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPapgVLIPEGGADVVTFS 154
|
170
....*....|....*.
gi 488220002 203 AHKINGPKGVGFLYKR 218
Cdd:cd01494 155 LHKNLGGEGGGVVIVK 170
|
|
| PucG |
COG0075 |
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ... |
117-281 |
4.12e-09 |
|
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: 57.79 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 117 GFDVTYLPVDEKGNLSIEEVKKALREDTI--LVSVMYgnNE--IGNLMPIKEIGELLADHPAYFHTDAVQAYGNQTIHPE 192
Cdd:COG0075 97 GAEVVVLEVPWGEAVDPEEVEEALAADPDikAVAVVH--NEtsTGVLNPLEEIGALAKEHGALLIVDAVSSLGGVPLDMD 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 193 ELGIDLLSISAHK-INGPKGVGFLY-------KRDGVNIPAL-----LLGGEQEEKRRAGTENLAGIWGMAKAVELLSPE 259
Cdd:COG0075 175 EWGIDVVVSGSQKcLMLPPGLAFVAvseraleAIEARKLPSYyldlkLWLKYWEKGQTPYTPPVSLLYALREALDLILEE 254
|
170 180
....*....|....*....|..
gi 488220002 260 EREARNNKYKGLQQLILDTLEA 281
Cdd:COG0075 255 GLENRFARHRRLAEALRAGLEA 276
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
69-217 |
1.51e-06 |
|
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: 49.51 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 69 IFNSGGTEGDNTAIL---ETAFSRQKEGRHLITTAIE-------HPAVLNTMKYLETKgfdVTYLPVDEKGNLSIEEVKK 138
Cdd:cd06450 61 VFTSGGSESNLLALLaarDRARKRLKAGGGRGIDKLVivcsdqaHVSVEKAAAYLDVK---VRLVPVDEDGRMDPEALEA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 139 ALRED------TILVSVMYGNNEIGNLMPIKEIGELLADHPAYFHTDAvqAYGNQTI---HPEEL--GI---DLLSISAH 204
Cdd:cd06450 138 AIDEDkaeglnPIMVVATAGTTDTGAIDPLEEIADLAEKYDLWLHVDA--AYGGFLLpfpEPRHLdfGIervDSISVDPH 215
|
170
....*....|....*
gi 488220002 205 KING-PKGVG-FLYK 217
Cdd:cd06450 216 KYGLvPLGCSaVLVR 230
|
|
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
5-149 |
1.57e-06 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 50.25 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 5 KTIYLDHA-ATTPMHPQVIEAMTAIMQDTFGNPSSIHGFGRHAHEKLETARQIIADSLQAKPHE--IIFNSGGTEGdnTA 81
Cdd:PLN02724 34 GVVYLDHAgATLYSESQLEAALADFSSNVYGNPHSQSDSSMRSSDTIESARQQVLEYFNAPPSDyaCVFTSGATAA--LK 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488220002 82 ILETAFSRQKEGRHLITTAiEHPAVLNTMKYLETKGfdVTYLPVDekgnlsIEEVKKALREDTILVSV 149
Cdd:PLN02724 112 LVGETFPWSSESHFCYTLE-NHNSVLGIREYALEKG--AAAIAVD------IEEAANQPTNSQGSVVV 170
|
|
| PRK06225 |
PRK06225 |
pyridoxal phosphate-dependent aminotransferase; |
16-175 |
3.90e-03 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235749 [Multi-domain] Cd Length: 380 Bit Score: 38.97 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 16 PMHPQVIEAM-TAIMQDTFGNPSSIHGFgrhaheklETARQIIADSLQAKPHEIIFNSGGTEGDNTAILETAfsrqKEGR 94
Cdd:PRK06225 41 GPHEEVREAMiRCIEEGEYCKYPPPEGF--------PELRELILKDLGLDDDEALITAGATESLYLVMRAFL----SPGD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220002 95 HLITTaieHPAVLNTMKYLETKGFDVTYLPV-DEKGN--LSIEEVKKALREDTILVSVMYGNNEIGNLMP---IKEIGEL 168
Cdd:PRK06225 109 NAVTP---DPGYLIIDNFASRFGAEVIEVPIySEECNykLTPELVKENMDENTRLIYLIDPLNPLGSSYTeeeIKEFAEI 185
|
....*..
gi 488220002 169 LADHPAY 175
Cdd:PRK06225 186 ARDNDAF 192
|
|
| |
