|
Name |
Accession |
Description |
Interval |
E-value |
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
1-383 |
0e+00 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 762.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 1 MIYLDYAATTPICEEALTVYQKLSMDMYGNASSLHDAGGKAKHILEYCREKIANIIGGEASGIYFTSGGTESNFLAIQSL 80
Cdd:PRK02948 1 MIYLDYAATTPMSKEALQTYQKAASQYFGNESSLHDIGGTASSLLQVCRKTFAEMIGGEEQGIYFTSGGTESNYLAIQSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 81 LNGLPKTKRHFITTAMEHQSIHNCAAFLEQQGYDVTVIEPNEYGLITEEILLTHIRPETGLVSIQHANSETGIIQPIQHL 160
Cdd:PRK02948 81 LNALPQNKKHIITTPMEHASIHSYFQSLESQGYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQPIAEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 161 SSYLHNKGILLHCDAVQTFGKIPINTKNLGVDALSMSSHKIHGPKGVGAVYIRPDVPWKPVYPLTTHEYGFRAGTVNVPG 240
Cdd:PRK02948 161 GALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYINPQVRWKPVFPGTTHEKGFRPGTVNVPG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 241 IGAFTAAAELIVSEMEKQISRNEALRTYFLDQIRIRSLPVTlaADTSKAECLPHIIGCFFHSFEGQYVMLECNRSNICIS 320
Cdd:PRK02948 241 IAAFLTAAENILKNMQEESLRFKELRSYFLEQIQTLPLPIE--VEGHSTSCLPHIIGVTIKGIEGQYTMLECNRRGIAIS 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 585557 321 TGSACSAGYHGPSETMKALRKTEQEALQFIRISFGRHTTAEQLEQLLHTFTVLWEQKKGEFDI 383
Cdd:PRK02948 319 TGSACQVGKQEPSKTMLAIGKTYEEAKQFVRFSFGQQTTKDQIDTTIHALETIGNQFYRGVKI 381
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
1-370 |
6.00e-163 |
|
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: 462.21 E-value: 6.00e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 1 MIYLDYAATTPICEEALTVYQKLSMDMYGNASSLHDAGGKAKHILEYCREKIANIIGGEASGIYFTSGGTESNFLAIQSL 80
Cdd:COG1104 3 MIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSSLHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNLAIKGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 81 LNGLPKTKRHFITTAMEHQSIHNCAAFLEQQGYDVTVIEPNEYGLITEEILLTHIRPETGLVSIQHANSETGIIQPIQHL 160
Cdd:COG1104 83 ARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQPIAEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 161 SSYLHNKGILLHCDAVQTFGKIPINTKNLGVDALSMSSHKIHGPKGVGAVYIRPDVPWKPVYPLTTHEYGFRAGTVNVPG 240
Cdd:COG1104 163 AEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRKGVRLEPLIHGGGQERGLRSGTENVPG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 241 IGAFTAAAELIVSEMEKQISRNEALRTYFLDQIRiRSLP-VTLAADtsKAECLPHIIGCFFHSFEGQYVMLECNRSNICI 319
Cdd:COG1104 243 IVGLGKAAELAAEELEEEAARLRALRDRLEEGLL-AAIPgVVINGD--PENRLPNTLNFSFPGVEGEALLLALDLAGIAV 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 585557 320 STGSACSAGYHGPSETMKALRKTEQEALQFIRISFGRHTTAEQLEQLLHTF 370
Cdd:COG1104 320 SSGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEAL 370
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
2-366 |
7.15e-119 |
|
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: 349.62 E-value: 7.15e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 2 IYLDYAATTPICEEALTVYQKLSMDMYGNA-SSLHDAGGKAKHILEYCREKIANIIGGE-ASGIYFTSGGTESNFLAIQS 79
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVhRGVHTLGKEATQAYEEAREKVAEFINAPsNDEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 80 LLNGLpKTKRHFITTAMEHQSIHNCAAFLEQQ-GYDVTVIEPNEYGLITEEILLTHIRPETGLVSIQHANSETGIIQPIQ 158
Cdd:pfam00266 81 LGRSL-KPGDEIVITEMEHHANLVPWQELAKRtGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 159 HLSSYLHNKGILLHCDAVQTFGKIPINTKNLGVDALSMSSHKIHGPKGVGAVYIRPD--VPWKPVYPLTT-------HEY 229
Cdd:pfam00266 160 EIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDllEKMPPLLGGGGmietvslQES 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 230 G-------FRAGTVNVPGIGAFTAAAELIvSEMEKQISRNEALRTYFLDQIRIRSLPVTLAADTskaECLPHIIGCFFHS 302
Cdd:pfam00266 240 TfadapwkFEAGTPNIAGIIGLGAALEYL-SEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGP---ERRASIISFNFKG 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 585557 303 FEGQYVMLECNRSNICISTGSACSagyhGPSETMKALRKTeqealqfIRISFGRHTTAEQLEQL 366
Cdd:pfam00266 316 VHPHDVATLLDESGIAVRSGHHCA----QPLMVRLGLGGT-------VRASFYIYNTQEDVDRL 368
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
2-367 |
6.51e-42 |
|
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: 151.08 E-value: 6.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 2 IYLDYAATT--PICE-EALTVYQKlsmDMYGNAS-SLHDAGGKAKHILEYCREKIANIIGGE-ASGIYFTSGGTEsnflA 76
Cdd:cd06453 1 VYLDNAATSqkPQPViDAIVDYYR---HYNANVHrGVHELSARATDAYEAAREKVARFINAPsPDEIIFTRNTTE----A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 77 IQSLLNGLPKTKR---HFITTAMEHQSIHNCAAFL-EQQGYDVTVIEPNEYGLITEEILLTHIRPETGLVSIQHANSETG 152
Cdd:cd06453 74 INLVAYGLGRANKpgdEIVTSVMEHHSNIVPWQQLaERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 153 IIQPIQHLSSYLHNKGILLHCDAVQTFGKIPINTKNLGVDALSMSSHKIHGPKGVGAVYIRPDV-----PWK-------- 219
Cdd:cd06453 154 TINPVKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELleempPYGgggemiee 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 220 -PVYPLTTHE--YGFRAGTVNVPGIGAFTAAAELIVSE-MEKqISRNEA-LRTYFLDqiRIRSLP-VTLAADTskaeclP 293
Cdd:cd06453 234 vSFEETTYADlpHKFEAGTPNIAGAIGLGAAIDYLEKIgMEA-IAAHEHeLTAYALE--RLSEIPgVRVYGDA------E 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 585557 294 HIIGCFFHSFEG---QYVMLECNRSNICISTGSACSagyhgpsetMKALRKTEQEALqfIRISFGRHTTAEQLEQLL 367
Cdd:cd06453 305 DRAGVVSFNLEGihpHDVATILDQYGIAVRAGHHCA---------QPLMRRLGVPGT--VRASFGLYNTEEEIDALV 370
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
1-383 |
0e+00 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 762.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 1 MIYLDYAATTPICEEALTVYQKLSMDMYGNASSLHDAGGKAKHILEYCREKIANIIGGEASGIYFTSGGTESNFLAIQSL 80
Cdd:PRK02948 1 MIYLDYAATTPMSKEALQTYQKAASQYFGNESSLHDIGGTASSLLQVCRKTFAEMIGGEEQGIYFTSGGTESNYLAIQSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 81 LNGLPKTKRHFITTAMEHQSIHNCAAFLEQQGYDVTVIEPNEYGLITEEILLTHIRPETGLVSIQHANSETGIIQPIQHL 160
Cdd:PRK02948 81 LNALPQNKKHIITTPMEHASIHSYFQSLESQGYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQPIAEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 161 SSYLHNKGILLHCDAVQTFGKIPINTKNLGVDALSMSSHKIHGPKGVGAVYIRPDVPWKPVYPLTTHEYGFRAGTVNVPG 240
Cdd:PRK02948 161 GALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYINPQVRWKPVFPGTTHEKGFRPGTVNVPG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 241 IGAFTAAAELIVSEMEKQISRNEALRTYFLDQIRIRSLPVTlaADTSKAECLPHIIGCFFHSFEGQYVMLECNRSNICIS 320
Cdd:PRK02948 241 IAAFLTAAENILKNMQEESLRFKELRSYFLEQIQTLPLPIE--VEGHSTSCLPHIIGVTIKGIEGQYTMLECNRRGIAIS 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 585557 321 TGSACSAGYHGPSETMKALRKTEQEALQFIRISFGRHTTAEQLEQLLHTFTVLWEQKKGEFDI 383
Cdd:PRK02948 319 TGSACQVGKQEPSKTMLAIGKTYEEAKQFVRFSFGQQTTKDQIDTTIHALETIGNQFYRGVKI 381
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
1-370 |
6.00e-163 |
|
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: 462.21 E-value: 6.00e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 1 MIYLDYAATTPICEEALTVYQKLSMDMYGNASSLHDAGGKAKHILEYCREKIANIIGGEASGIYFTSGGTESNFLAIQSL 80
Cdd:COG1104 3 MIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSSLHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNLAIKGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 81 LNGLPKTKRHFITTAMEHQSIHNCAAFLEQQGYDVTVIEPNEYGLITEEILLTHIRPETGLVSIQHANSETGIIQPIQHL 160
Cdd:COG1104 83 ARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQPIAEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 161 SSYLHNKGILLHCDAVQTFGKIPINTKNLGVDALSMSSHKIHGPKGVGAVYIRPDVPWKPVYPLTTHEYGFRAGTVNVPG 240
Cdd:COG1104 163 AEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRKGVRLEPLIHGGGQERGLRSGTENVPG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 241 IGAFTAAAELIVSEMEKQISRNEALRTYFLDQIRiRSLP-VTLAADtsKAECLPHIIGCFFHSFEGQYVMLECNRSNICI 319
Cdd:COG1104 243 IVGLGKAAELAAEELEEEAARLRALRDRLEEGLL-AAIPgVVINGD--PENRLPNTLNFSFPGVEGEALLLALDLAGIAV 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 585557 320 STGSACSAGYHGPSETMKALRKTEQEALQFIRISFGRHTTAEQLEQLLHTF 370
Cdd:COG1104 320 SSGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEAL 370
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
2-366 |
7.15e-119 |
|
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: 349.62 E-value: 7.15e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 2 IYLDYAATTPICEEALTVYQKLSMDMYGNA-SSLHDAGGKAKHILEYCREKIANIIGGE-ASGIYFTSGGTESNFLAIQS 79
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVhRGVHTLGKEATQAYEEAREKVAEFINAPsNDEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 80 LLNGLpKTKRHFITTAMEHQSIHNCAAFLEQQ-GYDVTVIEPNEYGLITEEILLTHIRPETGLVSIQHANSETGIIQPIQ 158
Cdd:pfam00266 81 LGRSL-KPGDEIVITEMEHHANLVPWQELAKRtGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 159 HLSSYLHNKGILLHCDAVQTFGKIPINTKNLGVDALSMSSHKIHGPKGVGAVYIRPD--VPWKPVYPLTT-------HEY 229
Cdd:pfam00266 160 EIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDllEKMPPLLGGGGmietvslQES 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 230 G-------FRAGTVNVPGIGAFTAAAELIvSEMEKQISRNEALRTYFLDQIRIRSLPVTLAADTskaECLPHIIGCFFHS 302
Cdd:pfam00266 240 TfadapwkFEAGTPNIAGIIGLGAALEYL-SEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGP---ERRASIISFNFKG 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 585557 303 FEGQYVMLECNRSNICISTGSACSagyhGPSETMKALRKTeqealqfIRISFGRHTTAEQLEQL 366
Cdd:pfam00266 316 VHPHDVATLLDESGIAVRSGHHCA----QPLMVRLGLGGT-------VRASFYIYNTQEDVDRL 368
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
2-364 |
1.16e-93 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 285.01 E-value: 1.16e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 2 IYLDYAATTPICEEALTVYQKLSMDMYGNASSL-HDAGGKAKHILEYCREKIANIIGGEASGIYFTSGGTESNFLAIQSL 80
Cdd:PLN02651 1 LYLDMQATTPIDPRVLDAMLPFLIEHFGNPHSRtHLYGWESEDAVEKARAQVAALIGADPKEIIFTSGATESNNLAIKGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 81 LNGLPKTKRHFITTAMEHQSIHNCAAFLEQQGYDVTVIEPNEYGLITEEILLTHIRPETGLVSIQHANSETGIIQPIQHL 160
Cdd:PLN02651 81 MHFYKDKKKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVEEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 161 SSYLHNKGILLHCDAVQTFGKIPINTKNLGVDALSMSSHKIHGPKGVGAVYIR--PDVPWKPVYPLTTHEYGFRAGTVNV 238
Cdd:PLN02651 161 GELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRrrPRVRLEPLMSGGGQERGRRSGTENT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 239 PGIGAFTAAAELIVSEMEKQISRNEALRTYFLDQIRIRSLPVTLAADTSKAECLPHIIGCFFHSFEGQYVMLecNRSNIC 318
Cdd:PLN02651 241 PLVVGLGAACELAMKEMDYDEKHMKALRERLLNGLRAKLGGVRVNGPRDPEKRYPGTLNLSFAYVEGESLLM--GLKEVA 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 585557 319 ISTGSACSAGYHGPSETMKALRKTEQEALQFIRISFGRHTTAEQLE 364
Cdd:PLN02651 319 VSSGSACTSASLEPSYVLRALGVPEEMAHGSLRLGVGRFTTEEEVD 364
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
2-364 |
7.72e-90 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 276.82 E-value: 7.72e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 2 IYLDYAATTPICEEALTVY-QKLSMD-MYGN-ASSLHDAGGKAKHILEYCREKIANIIGGEASGIYFTSGGTESNFLAIQ 78
Cdd:PRK14012 5 IYLDYSATTPVDPRVAEKMmPYLTMDgTFGNpASRSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDNLAIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 79 SLLNGLPKTKRHFITTAMEHQSIHNCAAFLEQQGYDVTVIEPNEYGLITEEILLTHIRPETGLVSIQHANSETGIIQPIQ 158
Cdd:PRK14012 85 GAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVIQDIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 159 HLSSYLHNKGILLHCDAVQTFGKIPINTKNLGVDALSMSSHKIHGPKGVGAVYIR--PDVPWKPVYPLTTHEYGFRAGTV 236
Cdd:PRK14012 165 AIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRrkPRVRLEAQMHGGGHERGMRSGTL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 237 NVPGIGAFTAAAELIVSEMEKQISRNEALRTYFLDQirIRSLP-VTLAADTSKAecLPHIIGCFFHSFEGQYVMLECNrs 315
Cdd:PRK14012 245 PTHQIVGMGEAARIAKEEMATENERIRALRDRLWNG--IKDIEeVYLNGDLEQR--VPGNLNVSFNYVEGESLIMALK-- 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 585557 316 NICISTGSACSAGYHGPSETMKALRKTEQEALQFIRISFGRHTTAEQLE 364
Cdd:PRK14012 319 DLAVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEID 367
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
2-368 |
5.00e-47 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 165.31 E-value: 5.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 2 IYLDYAATTPICEEALTVYQKLSMDMYGNAS-SLHDAGGKAKHILEYCREKIANIIGGEASG-IYFTSGGTEsnflAIQS 79
Cdd:COG0520 17 VYLDNAATGQKPRPVIDAIRDYYEPYNANVHrGAHELSAEATDAYEAAREKVARFIGAASPDeIIFTRGTTE----AINL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 80 LLNGLPKTKR--HFITTAMEHQSihNCAAFLE---QQGYDVTVIEPNEYGLITEEILLTHIRPETGLVSIQHANSETGII 154
Cdd:COG0520 93 VAYGLGRLKPgdEILITEMEHHS--NIVPWQElaeRTGAEVRVIPLDEDGELDLEALEALLTPRTKLVAVTHVSNVTGTV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 155 QPIQHLSSYLHNKGILLHCDAVQTFGKIPINTKNLGVDALSMSSHKIHGPKGVGAVYIRPDV-----PWKP-------VY 222
Cdd:COG0520 171 NPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELlealpPFLGgggmiewVS 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 223 PLTTH----EYGFRAGTVNVPGIGAFTAAAELI----VSEMEKqisRNEALRTYFLDqiRIRSLP-VTLAADTSKAECLP 293
Cdd:COG0520 251 FDGTTyadlPRRFEAGTPNIAGAIGLGAAIDYLeaigMEAIEA---RERELTAYALE--GLAAIPgVRILGPADPEDRSG 325
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 585557 294 hiIGCFfhSFEG---QYVMLECNRSNICISTGSACSAGYhgpsetMKALRKTEqealqFIRISFGRHTTAEQLEQLLH 368
Cdd:COG0520 326 --IVSF--NVDGvhpHDVAALLDDEGIAVRAGHHCAQPL------MRRLGVPG-----TVRASFHLYNTEEEIDRLVE 388
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
2-367 |
6.51e-42 |
|
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: 151.08 E-value: 6.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 2 IYLDYAATT--PICE-EALTVYQKlsmDMYGNAS-SLHDAGGKAKHILEYCREKIANIIGGE-ASGIYFTSGGTEsnflA 76
Cdd:cd06453 1 VYLDNAATSqkPQPViDAIVDYYR---HYNANVHrGVHELSARATDAYEAAREKVARFINAPsPDEIIFTRNTTE----A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 77 IQSLLNGLPKTKR---HFITTAMEHQSIHNCAAFL-EQQGYDVTVIEPNEYGLITEEILLTHIRPETGLVSIQHANSETG 152
Cdd:cd06453 74 INLVAYGLGRANKpgdEIVTSVMEHHSNIVPWQQLaERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 153 IIQPIQHLSSYLHNKGILLHCDAVQTFGKIPINTKNLGVDALSMSSHKIHGPKGVGAVYIRPDV-----PWK-------- 219
Cdd:cd06453 154 TINPVKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELleempPYGgggemiee 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 220 -PVYPLTTHE--YGFRAGTVNVPGIGAFTAAAELIVSE-MEKqISRNEA-LRTYFLDqiRIRSLP-VTLAADTskaeclP 293
Cdd:cd06453 234 vSFEETTYADlpHKFEAGTPNIAGAIGLGAAIDYLEKIgMEA-IAAHEHeLTAYALE--RLSEIPgVRVYGDA------E 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 585557 294 HIIGCFFHSFEG---QYVMLECNRSNICISTGSACSagyhgpsetMKALRKTEQEALqfIRISFGRHTTAEQLEQLL 367
Cdd:cd06453 305 DRAGVVSFNLEGihpHDVATILDQYGIAVRAGHHCA---------QPLMRRLGVPGT--VRASFGLYNTEEEIDALV 370
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
1-279 |
1.15e-19 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 90.19 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 1 MIYLDYAATTpicEEALTVYQKLsMDMYGNASS-----LHDAGGKAKHILEYCREKIANIIGGEASG-IYFTSGGTES-N 73
Cdd:PLN02855 33 LVYLDNAATS---QKPAAVLDAL-QDYYEEYNSnvhrgIHALSAKATDAYELARKKVAAFINASTSReIVFTRNATEAiN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 74 FLAIQSLLNGLpKTKRHFITTAMEHQS-IHNCAAFLEQQGYDVTVIEPNEYGLITEEILLTHIRPETGLVSIQHANSETG 152
Cdd:PLN02855 109 LVAYTWGLANL-KPGDEVILSVAEHHSnIVPWQLVAQKTGAVLKFVGLTPDEVLDVEQLKELLSEKTKLVATHHVSNVLG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 153 IIQPIQHLSSYLHNKGILLHCDAVQTFGKIPINTKNLGVDALSMSSHKIHGPKGVGAVYIRPDV-----PWK-------P 220
Cdd:PLN02855 188 SILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLWGKSDLlesmpPFLgggemisD 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 585557 221 VYpLTTHEYG-----FRAGTvnvPGIG---AFTAAAELI-------VSEMEKQISrnealrTYFLDqiRIRSLP 279
Cdd:PLN02855 268 VF-LDHSTYApppsrFEAGT---PAIGeaiGLGAAIDYLseigmdrIHEYEVELG------TYLYE--KLSSVP 329
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
1-274 |
5.82e-16 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 79.02 E-value: 5.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 1 MIYLDYAATT--PICeealTVYQKLSMDMYGNAS---SLHDAGGKAKHILEYCREKIANIIG-GEASGIYFTSGGTESNF 74
Cdd:PRK09295 24 LAYLDSAASAqkPSQ----VIDAEAEFYRHGYAAvhrGIHTLSAQATEKMENVRKQAALFINaRSAEELVFVRGTTEGIN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 75 LAIQSLLNGLPKTKRHFITTAMEHQS-IHNCAAFLEQQGYDVTVIEPNEYGLITEEILLTHIRPETGLVSIQHANSETGI 153
Cdd:PRK09295 100 LVANSWGNSNVRAGDNIIISEMEHHAnIVPWQMLCARVGAELRVIPLNPDGTLQLETLPALFDERTRLLAITHVSNVLGT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 154 IQPIQHLSSYLHNKGILLHCDAVQTFGKIPINTKNLGVDALSMSSHKIHGPKGVGAVYIRPDV-----PW-------KPV 221
Cdd:PRK09295 180 ENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKEALlqempPWegggsmiATV 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 585557 222 YPLTTHEYG-----FRAGTVNVPGIGAFTAAAELIVSEMEKQISRNE-ALRTYFLDQIR 274
Cdd:PRK09295 260 SLTEGTTWAkapwrFEAGTPNTGGIIGLGAALDYVSALGLNNIAEYEqNLMHYALSQLE 318
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
45-213 |
7.21e-16 |
|
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: 74.73 E-value: 7.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 45 LEYCREKIANIIGGEASGIYFTSGGTESNFLAIQSLLnglpKTKRHFITTAMEHQSIHncAAFLEQQGYDVTVI--EPNE 122
Cdd:cd01494 2 LEELEEKLARLLQPGNDKAVFVPSGTGANEAALLALL----GPGDEVIVDANGHGSRY--WVAAELAGAKPVPVpvDDAG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 123 YGLITEEILL-THIRPETGLVSIQHANSETGIIQPIQHLSSYLHNKGILLHCDAVQTFGKIPINT---KNLGVDALSMSS 198
Cdd:cd01494 76 YGGLDVAILEeLKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGvliPEGGADVVTFSL 155
|
170
....*....|....*
gi 585557 199 HKIHGPKGVGAVYIR 213
Cdd:cd01494 156 HKNLGGEGGGVVIVK 170
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
2-249 |
1.76e-11 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 65.06 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 2 IYLDYAATtpiceeAL--TVYQKLSMDMYGNAS-----SLHDAGGKAKHILEYCREKIANIIGGE-ASGIYFTSGGTESN 73
Cdd:PRK10874 21 VYLDSAAT------ALkpQAVIEATQQFYSLSAgnvhrSQFAAAQRLTARYEAAREQVAQLLNAPdAKNIVWTRGTTESI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 74 FLAIQSLLNGLPKTKRHFITTAMEHQSihNCAAFL---EQQGYDVTVIEPNEYGLITEEILLTHIRPETGLVSIQHANSE 150
Cdd:PRK10874 95 NLVAQSYARPRLQPGDEIIVSEAEHHA--NLVPWLmvaQQTGAKVVKLPLGADRLPDVDLLPELITPRTRILALGQMSNV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 151 TGIIQPIQHLSSYLHNKGILLHCDAVQTFGKIPINTKNLGVDALSMSSHKIHGPKGVGAVYIRPDV-----PWKPVYPLT 225
Cdd:PRK10874 173 TGGCPDLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKSELleamsPWQGGGKML 252
|
250 260 270
....*....|....*....|....*....|....*
gi 585557 226 TH-----------EYGFRAGTVNVPGIGAFTAAAE 249
Cdd:PRK10874 253 TEvsfdgftpqsaPWRFEAGTPNVAGVIGLSAALE 287
|
|
| PucG |
COG0075 |
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ... |
105-285 |
2.37e-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: 58.56 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 105 AAFLEQQGYDVTVIE--------PNEYglitEEILLTHirPETGLVSIQHANSETGIIQPIQHLSSYLHNKGILLHCDAV 176
Cdd:COG0075 90 AEIAERYGAEVVVLEvpwgeavdPEEV----EEALAAD--PDIKAVAVVHNETSTGVLNPLEEIGALAKEHGALLIVDAV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 177 QTFGKIPINTKNLGVDALSMSSHK-IHGPKGVGAVYIRPD---------VP-----WKPVYPltTHEYGFRAGTVNVPGI 241
Cdd:COG0075 164 SSLGGVPLDMDEWGIDVVVSGSQKcLMLPPGLAFVAVSERaleaiearkLPsyyldLKLWLK--YWEKGQTPYTPPVSLL 241
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 585557 242 GAFTAAAELIVSE-MEKQISRNEALRTYFLDqiRIRSLPVTLAAD 285
Cdd:COG0075 242 YALREALDLILEEgLENRFARHRRLAEALRA--GLEALGLELFAE 284
|
|
| PRK13479 |
PRK13479 |
2-aminoethylphosphonate--pyruvate transaminase; Provisional |
108-216 |
4.59e-07 |
|
2-aminoethylphosphonate--pyruvate transaminase; Provisional
Pssm-ID: 184076 [Multi-domain] Cd Length: 368 Bit Score: 51.45 E-value: 4.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 108 LEQQGYDVTVIEPNEYGLIT----EEILLTHirPETGLVSIQHANSETGIIQPIQHLSS--YLHNKGILLhcDAVQTFGK 181
Cdd:PRK13479 99 AEYLGIAHVVLDTGEDEPPDaaevEAALAAD--PRITHVALVHCETTTGILNPLDEIAAvaKRHGKRLIV--DAMSSFGA 174
|
90 100 110
....*....|....*....|....*....|....*.
gi 585557 182 IPINTKNLGVDALSMSSHK-IHGPKGVGAVYIRPDV 216
Cdd:PRK13479 175 IPIDIAELGIDALISSANKcIEGVPGFGFVIARRSE 210
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
108-281 |
9.52e-06 |
|
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: 47.29 E-value: 9.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 108 LEQQGYDVTVIEPNEYGLITEEILLTHIR-PETGLVSIQHANSETGIIQPIQHLSSYLHNKGILLHCDAVQTFGKIPINT 186
Cdd:cd06451 93 AERYGADVDVVEKPWGEAVSPEEIAEALEqHDIKAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVDAVSSLGGEPFRM 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 187 KNLGVDALSMSSHK-IHGPKGVGAVYIRPDVpWKPVYPLTTH---------------EYGFRAGTVNVPGIGAFTAAAEL 250
Cdd:cd06451 173 DEWGVDVAYTGSQKaLGAPPGLGPIAFSERA-LERIKKKTKPkgfyfdlllllkywgEGYSYPHTPPVNLLYALREALDL 251
|
170 180 190
....*....|....*....|....*....|..
gi 585557 251 IVSE-MEKQISRNEALRTYFLDQIRIRSLPVT 281
Cdd:cd06451 252 ILEEgLENRWARHRRLAKALREGLEALGLKLL 283
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
52-196 |
1.84e-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: 46.17 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 52 IANIIGGEAsgIYFTSGGTESNFLAIQSLlnglpkTKRH--FITTAMEHQSIHNCAAfLEQQGYDVTVIEPNEYGLITEE 129
Cdd:cd06502 41 AAELFGKEA--ALFVPSGTAANQLALAAH------TQPGgsVICHETAHIYTDEAGA-PEFLSGVKLLPVPGENGKLTPE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 130 ILLTHIR-------PETGLVSIQHAnSETGIIQPIQHL---SSYLHNKGILLHCD------AVqTFGKIPINTKNLGVDA 193
Cdd:cd06502 112 DLEAAIRprddihfPPPSLVSLENT-TEGGTVYPLDELkaiSALAKENGLPLHLDgarlanAA-AALGVALKTYKSGVDS 189
|
...
gi 585557 194 LSM 196
Cdd:cd06502 190 VSF 192
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
52-213 |
1.05e-04 |
|
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: 44.05 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 52 IANIIGG--EASGIyFTSGGTESNFLAI----------QSLLNGLPKTKR-HFITTAMEHQSIHNCAAFL--EQQGydVT 116
Cdd:COG0076 116 LADLLGLpeGAGGV-FTSGGTEANLLALlaardralarRVRAEGLPGAPRpRIVVSEEAHSSVDKAARLLglGRDA--LR 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 117 VIEPNEYGLITEEILLTHIRPET-------GLVSIqhA-NSETGIIQPIQHLSSYLHNKGILLHCDA------------V 176
Cdd:COG0076 193 KVPVDEDGRMDPDALEAAIDEDRaaglnpiAVVAT--AgTTNTGAIDPLAEIADIAREHGLWLHVDAayggfalpspelR 270
|
170 180 190
....*....|....*....|....*....|....*....
gi 585557 177 QTFGKIPintknlGVDALSMSSHKiHG--PKGVGAVYIR 213
Cdd:COG0076 271 HLLDGIE------RADSITVDPHK-WLyvPYGCGAVLVR 302
|
|
| SepCysS |
cd06452 |
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ... |
112-210 |
7.69e-03 |
|
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: 38.14 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585557 112 GYDVTVIEPNEYGLITEEILL-THIRPetGLVSIQHANSETGIIQPIQHLSSYLHNKGILLHCDAVQTFGKIPINTKNLG 190
Cdd:cd06452 114 GHPEYHITPEGYAEVIEEVKDeFGKPP--ALALLTHVDGNYGNLHDAKKIAKVCHEYGVPLLLNGAYTVGRMPVSGKELG 191
|
90 100
....*....|....*....|...
gi 585557 191 VDALSMSSHK---IHGPKGVGAV 210
Cdd:cd06452 192 ADFIVGSGHKsmaASAPIGVLAT 214
|
|
| |
