|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
4-404 |
0e+00 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 860.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 4 MNVFNPAQFRAQFPALQDAGVYLDSAATALKPEAVVEATQQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLNAPD 83
Cdd:PRK10874 1 MNVFNPAQFRAQFPALQDAGVYLDSAATALKPQAVIEATQQFYSLSAGNVHRSQFAAAQRLTARYEAAREQVAQLLNAPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 84 DKTIVWTRGTTESINMVAQCYARPRLQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPLNAQRLPDVDLLPELITPR 163
Cdd:PRK10874 81 AKNIVWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLVPWLMVAQQTGAKVVKLPLGADRLPDVDLLPELITPR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 164 SRILALGQMSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELLE 243
Cdd:PRK10874 161 TRILALGQMSNVTGGCPDLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKSELLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 244 AMSPWLGGGKMVHEVSFDGFTTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAEDALAKRPGFRS 323
Cdd:PRK10874 241 AMSPWQGGGKMLTEVSFDGFTPQSAPWRFEAGTPNVAGVIGLSAALEWLADIDINQAESWSRSLATLAEDALAKLPGFRS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 324 FRCQDSSLLAFDFAGVHHSDMVTLLAEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDVDALVNAVDRALELLV 403
Cdd:PRK10874 321 FRCQDSSLLAFDFAGVHHSDLVTLLAEYGIALRAGQHCAQPLLAALGVTGTLRASFAPYNTQSDVDALVNAVDRALELLV 400
|
.
4LW2_C 404 D 404
Cdd:PRK10874 401 D 401
|
|
| FeS_syn_CsdA |
TIGR03392 |
cysteine desulfurase, catalytic subunit CsdA; Members of this protein family are CsdS. This ... |
7-404 |
0e+00 |
|
cysteine desulfurase, catalytic subunit CsdA; Members of this protein family are CsdS. This protein, found Escherichia coli, Yersinia pestis, Photorhabdus luminescens, and related species, and related to SufS, works together with and physically interacts with CsdE (a paralog of SufE). CsdA has cysteine desulfurase activity that is enhanced by CsdE, a sulfur acceptor protein. This gene pair, although involved in FeS cluster biosynthesis, is not found next to other such genes as are its paralogs from the Suf or Isc systems. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 274558 [Multi-domain] Cd Length: 398 Bit Score: 793.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 7 FNPAQFRAQFPALQDAGVYLDSAATALKPEAVVEATQQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLNAPDDKT 86
Cdd:TIGR03392 1 FNPAQFRRQFPALQDATVYLDSAATALKPQAVIDATQQFYRLSSGTVHRSQHQEAQSLTARYEAAREQVAQLLNAPDAEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 87 IVWTRGTTESINMVAQCYARPRLQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPLNAQRLPDVDLLPELITPRSRI 166
Cdd:TIGR03392 81 IVWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLIPWLMVAQQTGAKVVKLPIGADLLPDIDQLPELLTPRTRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 167 LALGQMSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMS 246
Cdd:TIGR03392 161 LALGQMSNVTGGCPDLARAITLAHQYGCVVVVDGAQGVVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKTELLEAMP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 247 PWLGGGKMVHEVSFDGFTTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAEDALAKRPGFRSFRC 326
Cdd:TIGR03392 241 PWQGGGKMLSHVSFDGFTPQAVPWRFEAGTPNIAGVIGLSAALEWLADIDINAAESWSVSLATLAEEALAQLPGFRSFRC 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
4LW2_C 327 QDSSLLAFDFAGVHHSDMVTLLAEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDVDALVNAVDRALELLVD 404
Cdd:TIGR03392 321 QGSSLLAFDFAGVHHSDLVTLLAEQGIALRAGQHCAQPLMAALGVSGTLRASFAPYNTQQDVDALVNAVGRALELLVD 398
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
8-401 |
0e+00 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 533.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 8 NPAQFRAQFPALQDAGVYLDSAATALKPEAVVEATQQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLNAPDDKTI 87
Cdd:COG0520 1 DVEAIRADFPVLGKPLVYLDNAATGQKPRPVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAASPDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 88 VWTRGTTESINMVAQCYarPRLQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPLNAQRLPDVDLLPELITPRSRIL 167
Cdd:COG0520 81 IFTRGTTEAINLVAYGL--GRLKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDGELDLEALEALLTPRTKLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 168 ALGQMSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMSP 247
Cdd:COG0520 159 AVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELLEALPP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 248 WLGGGKMVHEVSFDGFTTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAEDALAKRPGFRSFRCQ 327
Cdd:COG0520 239 FLGGGGMIEWVSFDGTTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAIPGVRILGPA 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
4LW2_C 328 D----SSLLAFDFAGVHHSDMVTLLAEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDVDALVNAVDRALEL 401
Cdd:COG0520 319 DpedrSGIVSFNVDGVHPHDVAALLDDEGIAVRAGHHCAQPLMRRLGVPGTVRASFHLYNTEEEIDRLVEALKKLAEL 396
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
24-391 |
0e+00 |
|
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: 523.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 24 VYLDSAATALKPEAVVEATQQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLNAPDDKTIVWTRGTTESINMVAQC 103
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 104 YARPrLQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPLNAQRLPDVDLLPELITPRSRILALGQMSNVTGGCPDLA 183
Cdd:pfam00266 81 LGRS-LKPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 184 RAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMSPWLGGGKMVHEVSFDGF 263
Cdd:pfam00266 160 EIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGMIETVSLQES 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 264 TTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAEDALAKRPGFRSFR-CQDSSLLAFDFAGVHHS 342
Cdd:pfam00266 240 TFADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGpERRASIISFNFKGVHPH 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
4LW2_C 343 DMVTLLAEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDVDAL 391
Cdd:pfam00266 320 DVATLLDESGIAVRSGHHCAQPLMVRLGLGGTVRASFYIYNTQEDVDRL 368
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
24-395 |
8.47e-171 |
|
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: 481.97 E-value: 8.47e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 24 VYLDSAATALKPEAVVEATQQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLNAPDDKTIVWTRGTTESINMVAQC 103
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINAPSPDEIIFTRNTTEAINLVAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 104 YARPRlQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPLNAQRLPDVDLLPELITPRSRILALGQMSNVTGGCPDLA 183
Cdd:cd06453 81 LGRAN-KPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 184 RAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMSPWLGGGKMVHEVSFDGF 263
Cdd:cd06453 160 EIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMIEEVSFEET 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 264 TTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAEDALAKRPGFRSFRCQDS--SLLAFDFAGVHH 341
Cdd:cd06453 240 TYADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEIPGVRVYGDAEDraGVVSFNLEGIHP 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
4LW2_C 342 SDMVTLLAEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDVDALVNAV 395
Cdd:cd06453 320 HDVATILDQYGIAVRAGHHCAQPLMRRLGVPGTVRASFGLYNTEEEIDALVEAL 373
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
6-397 |
1.90e-121 |
|
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: 365.33 E-value: 1.90e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 6 VFNPAQFRAQFPALQDA--G---VYLDSAATALKPEAVVEATQQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLN 80
Cdd:NF041166 224 PFDVNAVRRDFPILQERvnGkplVWFDNAATTQKPQAVIDRLSYFYEHENSNIHRAAHELAARATDAYEGAREKVRRFIG 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 81 APDDKTIVWTRGTTESINMVAQCYARPRLQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPlnaqrlpdVD-----L 155
Cdd:NF041166 304 APSVDEIIFVRGTTEAINLVAKSWGRQNIGAGDEIIVSHLEHHANIVPWQQLAQETGAKLRVIP--------VDdsgqiL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 156 LPE---LITPRSRILALGQMSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGI 232
Cdd:NF041166 376 LDEyakLLNPRTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGI 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 233 GVLYGKSELLEAMSPWLGGGKMVHEVSFDGFTTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAE 312
Cdd:NF041166 456 GVVYGKRDLLEAMPPWQGGGNMIADVTFEKTVYQPAPNRFEAGTGNIADAVGLGAALDYVERIGIENIARYEHDLLEYAT 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 313 DALAKRPGFR---SFRcQDSSLLAFDFAGvHHSDMV-TLLAEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDV 388
Cdd:NF041166 536 AGLAEVPGLRligTAA-DKASVLSFVLDG-YSTEEVgKALNQEGIAVRSGHHCAQPILRRFGVEATVRPSLAFYNTCEEV 613
|
....*....
4LW2_C 389 DALVNAVDR 397
Cdd:NF041166 614 DALVAVLRR 622
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
4-404 |
0e+00 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 860.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 4 MNVFNPAQFRAQFPALQDAGVYLDSAATALKPEAVVEATQQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLNAPD 83
Cdd:PRK10874 1 MNVFNPAQFRAQFPALQDAGVYLDSAATALKPQAVIEATQQFYSLSAGNVHRSQFAAAQRLTARYEAAREQVAQLLNAPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 84 DKTIVWTRGTTESINMVAQCYARPRLQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPLNAQRLPDVDLLPELITPR 163
Cdd:PRK10874 81 AKNIVWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLVPWLMVAQQTGAKVVKLPLGADRLPDVDLLPELITPR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 164 SRILALGQMSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELLE 243
Cdd:PRK10874 161 TRILALGQMSNVTGGCPDLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKSELLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 244 AMSPWLGGGKMVHEVSFDGFTTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAEDALAKRPGFRS 323
Cdd:PRK10874 241 AMSPWQGGGKMLTEVSFDGFTPQSAPWRFEAGTPNVAGVIGLSAALEWLADIDINQAESWSRSLATLAEDALAKLPGFRS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 324 FRCQDSSLLAFDFAGVHHSDMVTLLAEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDVDALVNAVDRALELLV 403
Cdd:PRK10874 321 FRCQDSSLLAFDFAGVHHSDLVTLLAEYGIALRAGQHCAQPLLAALGVTGTLRASFAPYNTQSDVDALVNAVDRALELLV 400
|
.
4LW2_C 404 D 404
Cdd:PRK10874 401 D 401
|
|
| FeS_syn_CsdA |
TIGR03392 |
cysteine desulfurase, catalytic subunit CsdA; Members of this protein family are CsdS. This ... |
7-404 |
0e+00 |
|
cysteine desulfurase, catalytic subunit CsdA; Members of this protein family are CsdS. This protein, found Escherichia coli, Yersinia pestis, Photorhabdus luminescens, and related species, and related to SufS, works together with and physically interacts with CsdE (a paralog of SufE). CsdA has cysteine desulfurase activity that is enhanced by CsdE, a sulfur acceptor protein. This gene pair, although involved in FeS cluster biosynthesis, is not found next to other such genes as are its paralogs from the Suf or Isc systems. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 274558 [Multi-domain] Cd Length: 398 Bit Score: 793.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 7 FNPAQFRAQFPALQDAGVYLDSAATALKPEAVVEATQQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLNAPDDKT 86
Cdd:TIGR03392 1 FNPAQFRRQFPALQDATVYLDSAATALKPQAVIDATQQFYRLSSGTVHRSQHQEAQSLTARYEAAREQVAQLLNAPDAEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 87 IVWTRGTTESINMVAQCYARPRLQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPLNAQRLPDVDLLPELITPRSRI 166
Cdd:TIGR03392 81 IVWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLIPWLMVAQQTGAKVVKLPIGADLLPDIDQLPELLTPRTRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 167 LALGQMSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMS 246
Cdd:TIGR03392 161 LALGQMSNVTGGCPDLARAITLAHQYGCVVVVDGAQGVVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKTELLEAMP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 247 PWLGGGKMVHEVSFDGFTTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAEDALAKRPGFRSFRC 326
Cdd:TIGR03392 241 PWQGGGKMLSHVSFDGFTPQAVPWRFEAGTPNIAGVIGLSAALEWLADIDINAAESWSVSLATLAEEALAQLPGFRSFRC 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
4LW2_C 327 QDSSLLAFDFAGVHHSDMVTLLAEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDVDALVNAVDRALELLVD 404
Cdd:TIGR03392 321 QGSSLLAFDFAGVHHSDLVTLLAEQGIALRAGQHCAQPLMAALGVSGTLRASFAPYNTQQDVDALVNAVGRALELLVD 398
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
8-401 |
0e+00 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 533.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 8 NPAQFRAQFPALQDAGVYLDSAATALKPEAVVEATQQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLNAPDDKTI 87
Cdd:COG0520 1 DVEAIRADFPVLGKPLVYLDNAATGQKPRPVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAASPDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 88 VWTRGTTESINMVAQCYarPRLQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPLNAQRLPDVDLLPELITPRSRIL 167
Cdd:COG0520 81 IFTRGTTEAINLVAYGL--GRLKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDGELDLEALEALLTPRTKLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 168 ALGQMSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMSP 247
Cdd:COG0520 159 AVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELLEALPP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 248 WLGGGKMVHEVSFDGFTTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAEDALAKRPGFRSFRCQ 327
Cdd:COG0520 239 FLGGGGMIEWVSFDGTTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAIPGVRILGPA 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
4LW2_C 328 D----SSLLAFDFAGVHHSDMVTLLAEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDVDALVNAVDRALEL 401
Cdd:COG0520 319 DpedrSGIVSFNVDGVHPHDVAALLDDEGIAVRAGHHCAQPLMRRLGVPGTVRASFHLYNTEEEIDRLVEALKKLAEL 396
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
24-391 |
0e+00 |
|
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: 523.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 24 VYLDSAATALKPEAVVEATQQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLNAPDDKTIVWTRGTTESINMVAQC 103
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 104 YARPrLQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPLNAQRLPDVDLLPELITPRSRILALGQMSNVTGGCPDLA 183
Cdd:pfam00266 81 LGRS-LKPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 184 RAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMSPWLGGGKMVHEVSFDGF 263
Cdd:pfam00266 160 EIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGMIETVSLQES 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 264 TTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAEDALAKRPGFRSFR-CQDSSLLAFDFAGVHHS 342
Cdd:pfam00266 240 TFADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGpERRASIISFNFKGVHPH 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
4LW2_C 343 DMVTLLAEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDVDAL 391
Cdd:pfam00266 320 DVATLLDESGIAVRSGHHCAQPLMVRLGLGGTVRASFYIYNTQEDVDRL 368
|
|
| sufS |
TIGR01979 |
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine ... |
13-402 |
2.21e-171 |
|
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine desulfurases involved in FeS cluster formation needed for nitrogen fixation among other vital functions. Many cysteine desulfurases are also active as selenocysteine lyase and/or cysteine sulfinate desulfinase. This subfamily is associated with the six-gene SUF system described in E. coli and Erwinia as an FeS cluster formation system during oxidative stress. The active site Cys is this subfamily resembles GHHC with one or both His conserved. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 131034 [Multi-domain] Cd Length: 403 Bit Score: 484.85 E-value: 2.21e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 13 RAQFPALQ-----DAGVYLDSAATALKPEAVVEATQQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLNAPDDKTI 87
Cdd:TIGR01979 4 RADFPILKrkingKPLVYLDSAATSQKPQQVIDAVAEYYRNSNANVHRGIHTLSVRATEAYEAVREKVAKFINAASDEEI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 88 VWTRGTTESINMVAQCYARPRLQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPLNAQRLPDVDLLPELITPRSRIL 167
Cdd:TIGR01979 84 VFTRGTTESINLVAYSWGDSNLKAGDEIVISEMEHHANIVPWQLLAERTGATLKFIPLDDDGTLDLDDLEKLLTEKTKLV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 168 ALGQMSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMSP 247
Cdd:TIGR01979 164 AITHVSNVLGTVNPVEEIAKLAHQVGAKVLVDGAQAVPHMPVDVQALDCDFYVFSGHKMYGPTGIGVLYGKEELLEQMPP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 248 WLGGGKMVHEVSFDGFTTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAEDALAKRPGFRSFRCQ 327
Cdd:TIGR01979 244 FLGGGEMIAEVSFEETTYNEAPHKFEAGTPNIAGVIGLGAAIDYLEAIGLENIEAHEHELTAYALERLGEIPGLRIYGPR 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
4LW2_C 328 DS----SLLAFDFAGVHHSDMVTLLAEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDVDALVNAVDRALELL 402
Cdd:TIGR01979 324 DAedrgGIISFNVEGVHPHDVGTILDEEGIAVRSGHHCAQPLMRRFGVPATCRASFYIYNTEEDIDALVEALKKVRKFF 402
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
24-395 |
8.47e-171 |
|
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: 481.97 E-value: 8.47e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 24 VYLDSAATALKPEAVVEATQQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLNAPDDKTIVWTRGTTESINMVAQC 103
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINAPSPDEIIFTRNTTEAINLVAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 104 YARPRlQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPLNAQRLPDVDLLPELITPRSRILALGQMSNVTGGCPDLA 183
Cdd:cd06453 81 LGRAN-KPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 184 RAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMSPWLGGGKMVHEVSFDGF 263
Cdd:cd06453 160 EIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMIEEVSFEET 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 264 TTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAEDALAKRPGFRSFRCQDS--SLLAFDFAGVHH 341
Cdd:cd06453 240 TYADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEIPGVRVYGDAEDraGVVSFNLEGIHP 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
4LW2_C 342 SDMVTLLAEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDVDALVNAV 395
Cdd:cd06453 320 HDVATILDQYGIAVRAGHHCAQPLMRRLGVPGTVRASFGLYNTEEEIDALVEAL 373
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
13-394 |
7.53e-138 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 400.28 E-value: 7.53e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 13 RAQFPAL-QDAG----VYLDSAATALKPEAVVEATQQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLNAPDDKTI 87
Cdd:PLN02855 18 RPDFPILdQTVNgsklVYLDNAATSQKPAAVLDALQDYYEEYNSNVHRGIHALSAKATDAYELARKKVAAFINASTSREI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 88 VWTRGTTESINMVAQCYARPRLQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPLNAQRLPDVDLLPELITPRSRIL 167
Cdd:PLN02855 98 VFTRNATEAINLVAYTWGLANLKPGDEVILSVAEHHSNIVPWQLVAQKTGAVLKFVGLTPDEVLDVEQLKELLSEKTKLV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 168 ALGQMSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMSP 247
Cdd:PLN02855 178 ATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLWGKSDLLESMPP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 248 WLGGGKMVHEVSFDGFTTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAEDALAKRPGFRSFRCQ 327
Cdd:PLN02855 258 FLGGGEMISDVFLDHSTYAPPPSRFEAGTPAIGEAIGLGAAIDYLSEIGMDRIHEYEVELGTYLYEKLSSVPGVRIYGPK 337
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
4LW2_C 328 DS------SLLAFDFAGVHHSDMVTLL-AEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDVDALVNA 394
Cdd:PLN02855 338 PSegvgraALCAFNVEGIHPTDLSTFLdQQHGVAIRSGHHCAQPLHRYLGVNASARASLYFYNTKEEVDAFIHA 411
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
7-402 |
3.24e-131 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 382.95 E-value: 3.24e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 7 FNPAQFRAQFPAL--QDAG---VYLDSAATALKPEAVVEATQQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLNA 81
Cdd:PRK09295 3 FSVEKVRADFPVLsrEVNGlplAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKQAALFINA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 82 PDDKTIVWTRGTTESINMVAQCYARPRLQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPLNAQRLPDVDLLPELIT 161
Cdd:PRK09295 83 RSAEELVFVRGTTEGINLVANSWGNSNVRAGDNIIISEMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPALFD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 162 PRSRILALGQMSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSEL 241
Cdd:PRK09295 163 ERTRLLAITHVSNVLGTENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKEAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 242 LEAMSPWLGGGKMVHEVSF-DGFTTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAEDALAKRPG 320
Cdd:PRK09295 243 LQEMPPWEGGGSMIATVSLtEGTTWAKAPWRFEAGTPNTGGIIGLGAALDYVSALGLNNIAEYEQNLMHYALSQLESVPD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 321 FRSF-RCQDSSLLAFDFaGVHHS-DMVTLLAEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDVDALVNAVDRA 398
Cdd:PRK09295 323 LTLYgPQNRLGVIAFNL-GKHHAyDVGSFLDNYGIAVRTGHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVAGLQRI 401
|
....
4LW2_C 399 LELL 402
Cdd:PRK09295 402 HRLL 405
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
6-397 |
1.90e-121 |
|
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: 365.33 E-value: 1.90e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 6 VFNPAQFRAQFPALQDA--G---VYLDSAATALKPEAVVEATQQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLN 80
Cdd:NF041166 224 PFDVNAVRRDFPILQERvnGkplVWFDNAATTQKPQAVIDRLSYFYEHENSNIHRAAHELAARATDAYEGAREKVRRFIG 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 81 APDDKTIVWTRGTTESINMVAQCYARPRLQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPlnaqrlpdVD-----L 155
Cdd:NF041166 304 APSVDEIIFVRGTTEAINLVAKSWGRQNIGAGDEIIVSHLEHHANIVPWQQLAQETGAKLRVIP--------VDdsgqiL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 156 LPE---LITPRSRILALGQMSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGI 232
Cdd:NF041166 376 LDEyakLLNPRTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGI 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 233 GVLYGKSELLEAMSPWLGGGKMVHEVSFDGFTTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAE 312
Cdd:NF041166 456 GVVYGKRDLLEAMPPWQGGGNMIADVTFEKTVYQPAPNRFEAGTGNIADAVGLGAALDYVERIGIENIARYEHDLLEYAT 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 313 DALAKRPGFR---SFRcQDSSLLAFDFAGvHHSDMV-TLLAEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDV 388
Cdd:NF041166 536 AGLAEVPGLRligTAA-DKASVLSFVLDG-YSTEEVgKALNQEGIAVRSGHHCAQPILRRFGVEATVRPSLAFYNTCEEV 613
|
....*....
4LW2_C 389 DALVNAVDR 397
Cdd:NF041166 614 DALVAVLRR 622
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
24-400 |
6.35e-61 |
|
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: 201.43 E-value: 6.35e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 24 VYLDSAATA-LKPEaVVEATQQFYSLSAGN---VHRsqfaEAQRLTARYEAAREKVAQLLNApDDKTIVWTRGTTESINM 99
Cdd:COG1104 4 IYLDNAATTpVDPE-VLEAMLPYLTEYFGNpssLHS----FGREARAALEEAREQVAALLGA-DPEEIIFTSGGTEANNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 100 VAQCYARPRLQPGDEIIVSVAEHHA--NLVPWLmvaQQTGAKVVKLPLNAQRLPDVDLLPELITPRSRILALGQMSNVTG 177
Cdd:COG1104 78 AIKGAARAYRKKGKHIITSAIEHPAvlETARFL---EKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 178 GCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELleAMSPWL-GGGkmvH 256
Cdd:COG1104 155 TIQPIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRKGV--RLEPLIhGGG---Q 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 257 EvsfdgfttqsapWKLEAGTPNVAGVIGLSAALEWLADydiNQAESWSR--SLATLAEDALAKR-PGFRSFRCQDSSL-- 331
Cdd:COG1104 230 E------------RGLRSGTENVPGIVGLGKAAELAAE---ELEEEAARlrALRDRLEEGLLAAiPGVVINGDPENRLpn 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 332 -LAFDFAGVHHSDMVTLLAEYGIALRAGQHCAQ------PLLAELGVT-----GTLRASFAPYNTKSDVDALVNAVDRAL 399
Cdd:COG1104 295 tLNFSFPGVEGEALLLALDLAGIAVSSGSACSSgslepsHVLLAMGLDeelahGSIRFSLGRFTTEEEIDRAIEALKEIV 374
|
.
4LW2_C 400 E 400
Cdd:COG1104 375 A 375
|
|
| am_tr_V_VC1184 |
TIGR01976 |
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of ... |
7-395 |
2.87e-60 |
|
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of probable pyridoxal phosphate-dependent enzymes in the aminotransferase class V family (pfam00266). The most closely related characterized proteins are active as cysteine desulfurases, selenocysteine lyases, or both; some are involved in FeS cofactor biosynthesis and are designated NifS. An active site Cys residue present in those sequences, in motifs resembling GHHC or GSAC, is not found in this family. The function of members of this family is unknown, but seems unlike to be as an aminotransferase. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 273906 [Multi-domain] Cd Length: 397 Bit Score: 200.36 E-value: 2.87e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 7 FNPAQFRAQFPALQDAG-VYLDSAATALKPEAVVEATQQfySLSAGNVHRSQFAEAQRLTARY-EAAREKVAQLLNApDD 84
Cdd:TIGR01976 1 FDVEAVRGQFPALADGDrVFFDNPAGTQIPQSVADAVSA--ALTRSNANRGGAYESSRRADQVvDDAREAVADLLNA-DP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 85 KTIVWTRGTTESINMVAQCYARpRLQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPLNAQ--RLPDVDLLPeLITP 162
Cdd:TIGR01976 78 PEVVFGANATSLTFLLSRAISR-RWGPGDEVIVTRLDHEANISPWLQAAERAGAKVKWARVDEAtgELHPDDLAS-LLSP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 163 RSRILALGQMSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTgIGVLYGKSELL 242
Cdd:TIGR01976 156 RTRLVAVTAASNTLGSIVDLAAITELVHAAGALVVVDAVHYAPHGLIDVQATGADFLTCSAYKFFGPH-MGILWGRPELL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 243 EAMSPwlgggkmvhevSFDGFTTQSAPWKLEAGTPNVAGVIGLSAALEWLADYD--------------INQAESWSRSLA 308
Cdd:TIGR01976 235 MNLPP-----------YKLTFSYDTGPERFELGTPQYELLAGVVAAVDYLAGLGesangsrrerlvasFQAIDAYENRLA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 309 TLAEDALAKRPGFRSFRCQDSS----LLAFDFAGVHHSDMVTLLAEYGIALRAGQHCAQPLLAELGVT---GTLRASFAP 381
Cdd:TIGR01976 304 EYLLVGLSDLPGVTLYGVARLAarvpTVSFTVHGLPPQRVVRRLADQGIDAWAGHFYAVRLLRRLGLNdegGVVRVGLAH 383
|
410
....*....|....
4LW2_C 382 YNTKSDVDALVNAV 395
Cdd:TIGR01976 384 YNTAEEVDRLLEAL 397
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
24-389 |
9.30e-31 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 120.91 E-value: 9.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 24 VYLD-SAATALKPEaVVEATQQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLNApDDKTIVWTRGTTESINMVAQ 102
Cdd:PLN02651 1 LYLDmQATTPIDPR-VLDAMLPFLIEHFGNPHSRTHLYGWESEDAVEKARAQVAALIGA-DPKEIIFTSGATESNNLAIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 103 CYARPRLQPGDEIIVSVAEHHANL--VPWLmvaQQTGAKVVKLPLNAQRLPDVDLLPELITPRSRILALGQMSNVTGGCP 180
Cdd:PLN02651 79 GVMHFYKDKKKHVITTQTEHKCVLdsCRHL---QQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 181 DLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMSPWLGGGKMVHevsf 260
Cdd:PLN02651 156 PVEEIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRLEPLMSGGGQER---- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 261 dgfttqsapwKLEAGTPNVAGVIGLSAALEwLADYDINQAESWSRSLATLAEDAL-AKRPGFR--SFRCQDSSL---LAF 334
Cdd:PLN02651 232 ----------GRRSGTENTPLVVGLGAACE-LAMKEMDYDEKHMKALRERLLNGLrAKLGGVRvnGPRDPEKRYpgtLNL 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
4LW2_C 335 DFAGVHHSdmVTLLAEYGIALRAGQHC----AQP--LLAELGV-----TGTLRASFAPYNTKSDVD 389
Cdd:PLN02651 301 SFAYVEGE--SLLMGLKEVAVSSGSACtsasLEPsyVLRALGVpeemaHGSLRLGVGRFTTEEEVD 364
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
24-236 |
4.21e-28 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 114.27 E-value: 4.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 24 VYLDSAATALKPEAVVEATQQFYSLSA--GNVH-RS-----QFAEAqrltarYEAAREKVAQLLNApDDKTIVWTRGTTE 95
Cdd:PRK14012 5 IYLDYSATTPVDPRVAEKMMPYLTMDGtfGNPAsRShrfgwQAEEA------VDIARNQIADLIGA-DPREIVFTSGATE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 96 SINM----VAQCYARPrlqpGDEIIVSVAEHHANLVPWLMVAQQtGAKVVKLPLNAQRLPDVDLLPELITPRSRILALGQ 171
Cdd:PRK14012 78 SDNLaikgAAHFYQKK----GKHIITSKTEHKAVLDTCRQLERE-GFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMH 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
4LW2_C 172 MSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLY 236
Cdd:PRK14012 153 VNNEIGVIQDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALY 217
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
24-290 |
1.03e-16 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 80.93 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 24 VYLDSAATA-LKPEAV---VEATQQFYSlSAGNVHRSQFAEAQRLtaryEAAREKVAQLLNApDDKTIVWTRGTTESiNM 99
Cdd:PRK02948 2 IYLDYAATTpMSKEALqtyQKAASQYFG-NESSLHDIGGTASSLL----QVCRKTFAEMIGG-EEQGIYFTSGGTES-NY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 100 VA-QCYARPRLQPGDEIIVSVAEHHA--NLVPWLmvaQQTGAKVVKLPLNAQRLPDVDLLPELITPRSrILALGQMSNV- 175
Cdd:PRK02948 75 LAiQSLLNALPQNKKHIITTPMEHASihSYFQSL---ESQGYTVTEIPVDKSGLIRLVDLERAITPDT-VLASIQHANSe 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 176 TGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELleamsPWlgggKMV 255
Cdd:PRK02948 151 IGTIQPIAEIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYINPQV-----RW----KPV 221
|
250 260 270 280
....*....|....*....|....*....|....*....|
4LW2_C 256 -----HEvsfDGFttqsapwklEAGTPNVAGVIGLSAALE 290
Cdd:PRK02948 222 fpgttHE---KGF---------RPGTVNVPGIAAFLTAAE 249
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
68-238 |
5.24e-15 |
|
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: 72.42 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 68 YEAAREKVAQLLNAPDDKTIVwTRGTTESINMVAQCYarprLQPGDEIIVSVAEHHANLvpWLMVAQQtGAKVVKLPLN- 146
Cdd:cd01494 2 LEELEEKLARLLQPGNDKAVF-VPSGTGANEAALLAL----LGPGDEVIVDANGHGSRY--WVAAELA-GAKPVPVPVDd 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 147 --AQRLPDVDLLPELITPRSRILALGQMSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLD---IDFYAF 221
Cdd:cd01494 74 agYGGLDVAILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPeggADVVTF 153
|
170
....*....|....*..
4LW2_C 222 SGHKLYGPTGIGVLYGK 238
Cdd:cd01494 154 SLHKNLGGEGGGVVIVK 170
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
24-394 |
7.60e-11 |
|
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: 63.13 E-value: 7.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 24 VYLDSAATALKPEAVVEATQQFYSLSAGNVHRSQFAEAQRLtarYEAAREKVAQLLNAPDDKT-IVWTRGTTESINMVAQ 102
Cdd:cd00609 1 IDLSIGEPDFPPPPEVLEALAAAALRAGLLGYYPDPGLPEL---REAIAEWLGRRGGVDVPPEeIVVTNGAQEALSLLLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 103 CYarprLQPGDEIIVSVaehhanlvP----WLMVAQQTGAKVVKLPLNAQ--RLPDVDLLPELITPRSRILALGQMSNVT 176
Cdd:cd00609 78 AL----LNPGDEVLVPD--------PtypgYEAAARLAGAEVVPVPLDEEggFLLDLELLEAAKTPKTKLLYLNNPNNPT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 177 GGCPD---LARAITFAHSAGMVVMVDGA------QGAVH-FPADVQQLDIDFYAFSGHKLYGPTG--IGVLYGKSELLEA 244
Cdd:cd00609 146 GAVLSeeeLEELAELAKKHGILIISDEAyaelvyDGEPPpALALLDAYERVIVLRSFSKTFGLPGlrIGYLIAPPEELLE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 245 MSpwlgggKMVHEVSFdgfttqsapwkleaGTPNVAGVIGLSAALEWLADYdINQAESWSRSLATLAEDALAKRPGFRSF 324
Cdd:cd00609 226 RL------KKLLPYTT--------------SGPSTLSQAAAAAALDDGEEH-LEELRERYRRRRDALLEALKELGPLVVV 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
4LW2_C 325 RCQDSSLLAFDFAGVHHSDMVT-LLAEYGIALRAGQHCAQPLlaelgvTGTLRASFApyNTKSDVDALVNA 394
Cdd:cd00609 285 KPSGGFFLWLDLPEGDDEEFLErLLLEAGVVVRPGSAFGEGG------EGFVRLSFA--TPEEELEEALER 347
|
|
| AspB |
COG0436 |
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ... |
35-245 |
4.22e-10 |
|
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; Aspartate/methionine/tyrosine aminotransferase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 440205 [Multi-domain] Cd Length: 387 Bit Score: 60.91 E-value: 4.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 35 PEAVVEATQQ-------FYSLSAGnvhrsqfaeaqrltarYEAAREKVAQLLNA-------PDDktIVWTRGTTESINMV 100
Cdd:COG0436 45 PDHIREAAIEalddgvtGYTPSAG----------------IPELREAIAAYYKRrygvdldPDE--ILVTNGAKEALALA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 101 AQCYarprLQPGDEIIVsvaehhanLVP----WLMVAQQTGAKVVKLPLNAQR--LPDVDLLPELITPRSRILALGQMSN 174
Cdd:COG0436 107 LLAL----LNPGDEVLV--------PDPgypsYRAAVRLAGGKPVPVPLDEENgfLPDPEALEAAITPRTKAIVLNSPNN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 175 VTGGC---PDLARAITFAHSAGMVVMVD--------GAQGAVHFpADVQQLD---IDFYAFSghKLYGPTG--IGVLYGK 238
Cdd:COG0436 175 PTGAVysrEELEALAELAREHDLLVISDeiyeelvyDGAEHVSI-LSLPGLKdrtIVINSFS--KSYAMTGwrIGYAVGP 251
|
....*..
4LW2_C 239 SELLEAM 245
Cdd:COG0436 252 PELIAAL 258
|
|
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
14-235 |
1.86e-08 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 56.41 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 14 AQFPALqDAGVYLDSAATALKPEAVVEAT-QQFYSLSAGNVHrSQFAEAQRLTARYEAAREKVAQLLNAP-DDKTIVWTR 91
Cdd:PLN02724 27 TEFARL-KGVVYLDHAGATLYSESQLEAAlADFSSNVYGNPH-SQSDSSMRSSDTIESARQQVLEYFNAPpSDYACVFTS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 92 GTTESINMVAQCYArprLQPGDEIIVSVAEHHANL-VPWLMVAQQTGAKVVKLPLNAQRL----PDVDLLPELITPRSR- 165
Cdd:PLN02724 105 GATAALKLVGETFP---WSSESHFCYTLENHNSVLgIREYALEKGAAAIAVDIEEAANQPtnsqGSVVVKSRGLQRRNTs 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 166 -------------ILALGQMSNVTGGCPDL--------ARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGH 224
Cdd:PLN02724 182 klqkreddgeaynLFAFPSECNFSGAKFPLdlvklikdNQHSNFSKSGRWMVLLDAAKGCGTSPPDLSRYPADFVVVSFY 261
|
250
....*....|..
4LW2_C 225 KLYG-PTGIGVL 235
Cdd:PLN02724 262 KIFGyPTGLGAL 273
|
|
| PRK08361 |
PRK08361 |
aspartate aminotransferase; Provisional |
109-245 |
1.11e-04 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 236248 [Multi-domain] Cd Length: 391 Bit Score: 44.10 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 109 LQPGDEIIVSvaehHANLVPWLMVAQQTGAKVVKLPLNAQR--LPDVDLLPELITPRSRILALGQMSNVTGGCPD--LAR 184
Cdd:PRK08361 114 LEEGDEVIIP----DPAFVCYVEDAKIAEAKPIRIPLREENefQPDPDELLELITKRTRMIVINYPNNPTGATLDkeVAK 189
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 185 AIT-FAHSAGMVVMVDGA------QGAVHFPADVQQLDIDFYAFSGHKLYGPTG--IGVLYGKSELLEAM 245
Cdd:PRK08361 190 AIAdIAEDYNIYILSDEPyehflyEGAKHYPMIKYAPDNTILANSFSKTFAMTGwrLGFVIAPEQVIKDM 259
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
54-210 |
1.26e-04 |
|
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.
Pssm-ID: 99739 [Multi-domain] Cd Length: 294 Bit Score: 43.39 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 54 HRSQFAEAQRLTARYEAArekvaqllnapdDKTIVWTRGTTESINMVAQCYarprLQPGDEIIVSVAEH--HANLvpwLM 131
Cdd:cd00615 57 PTGPIKEAQELAARAFGA------------KHTFFLVNGTSSSNKAVILAV----CGPGDKILIDRNCHksVING---LV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 132 VAQQTgAKVVKLPLNAQR-----LPDVDLLPELITPRSRILALGQMSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAvH 206
Cdd:cd00615 118 LSGAV-PVYLKPERNPYYgiaggIPPETFKKALIEHPDAKAAVITNPTYYGICYNLRKIVEEAHHRGLPVLVDEAHGA-H 195
|
....
4LW2_C 207 FPAD 210
Cdd:cd00615 196 FRFH 199
|
|
| PLN02409 |
PLN02409 |
serine--glyoxylate aminotransaminase |
109-245 |
1.87e-04 |
|
serine--glyoxylate aminotransaminase
Pssm-ID: 178031 [Multi-domain] Cd Length: 401 Bit Score: 43.21 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 109 LQPGDEIIVSVAEHHANLvpWLMVAQQTGAKVVKLPLNAQRLPDVDLLPELITP----RSRILALGQMSNVTGGCPDLA- 183
Cdd:PLN02409 81 LSPGDKVVSFRIGQFSLL--WIDQMQRLNFDVDVVESPWGQGADLDILKSKLRQdtnhKIKAVCVVHNETSTGVTNDLAg 158
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
4LW2_C 184 -RAITFAHSAGMVVMVDGAQ--GAVHFPADVQQLDIdfyAFSGHK--LYGPTGIGVLYGKSELLEAM 245
Cdd:PLN02409 159 vRKLLDCAQHPALLLVDGVSsiGALDFRMDEWGVDV---ALTGSQkaLSLPTGLGIVCASPKALEAS 222
|
|
| PRK06290 |
PRK06290 |
LL-diaminopimelate aminotransferase; |
92-207 |
3.57e-04 |
|
LL-diaminopimelate aminotransferase;
Pssm-ID: 235772 Cd Length: 410 Bit Score: 42.33 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 92 GTTESINMVAQCYarprLQPGDEIIVS-----VAEHHANlvpWLmvaqqtGAKVVKLPLNAQR--LPDVDLLPELITPRS 164
Cdd:PRK06290 114 GSKPALAMLPSCF----INPGDVTLMTvpgypVTGTHTK---YY------GGEVYNLPLLEENnfLPDLDSIPKDIKEKA 180
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
4LW2_C 165 RILALGQMSNVTGGCPDL---ARAITFAHSAGMVVMVDGAQGAVHF 207
Cdd:PRK06290 181 KLLYLNYPNNPTGAVATKefyEEVVDFAKENNIIVVQDAAYAALTF 226
|
|
| PRK06836 |
PRK06836 |
pyridoxal phosphate-dependent aminotransferase; |
35-177 |
6.52e-04 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180720 Cd Length: 394 Bit Score: 41.72 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 35 PEAVVEATQQFYSLSAGNVHRSQFAeaqrltARYEAAREKVAQLLNA-------PDDktIVWTRGTTESINMVaqcyARP 107
Cdd:PRK06836 48 PAAVKEALRELAEEEDPGLHGYMPN------AGYPEVREAIAESLNRrfgtpltADH--IVMTCGAAGALNVA----LKA 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
4LW2_C 108 RLQPGDEIIVsVAEHHANLVPWlmvAQQTGAKVVKLPLNAQR-LPDVDLLPELITPRSRILALGQMSNVTG 177
Cdd:PRK06836 116 ILNPGDEVIV-FAPYFVEYRFY---VDNHGGKLVVVPTDTDTfQPDLDALEAAITPKTKAVIINSPNNPTG 182
|
|
| PRK07568 |
PRK07568 |
pyridoxal phosphate-dependent aminotransferase; |
35-177 |
7.71e-04 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 181036 Cd Length: 397 Bit Score: 41.38 E-value: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 35 PEAVVEATQQF------YSLSAGnvhrsqfaeaqrltarYEAAREKVA---QLLN---APDDktIVWTRGTTESIN--MV 100
Cdd:PRK07568 45 PEVFFEAIKNYdeevlaYSHSQG----------------IPELREAFAkyyKKWGidvEPDE--ILITNGGSEAILfaMM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 101 AQCyarprlQPGDEIIVsvAE-HHANlvpWLMVAQQTGAKVVKLPLNAQ---RLPDVDLLPELITPRSRILALGQMSNVT 176
Cdd:PRK07568 107 AIC------DPGDEILV--PEpFYAN---YNGFATSAGVKIVPVTTKIEegfHLPSKEEIEKLITPKTKAILISNPGNPT 175
|
.
4LW2_C 177 G 177
Cdd:PRK07568 176 G 176
|
|
| PRK05957 |
PRK05957 |
pyridoxal phosphate-dependent aminotransferase; |
35-165 |
3.47e-03 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235654 Cd Length: 389 Bit Score: 39.28 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 35 PEAVVEATQQFYSlsagNVHRSQFAEAQRLTARYEAAREKVAQL--LNAPDDKTIVWTRGTtesiNMVAQCYARPRLQPG 112
Cdd:PRK05957 42 PPEAIEALNNFLA----NPENHKYQAVQGIPPLLEAITQKLQQDngIELNNEQAIVVTAGS----NMAFMNAILAITDPG 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
4LW2_C 113 DEIIVsvaehhanLVPWL----MVAQQTGAKVVKLPLNAQRLPDVDLLPELITPRSR 165
Cdd:PRK05957 114 DEIIL--------NTPYYfnheMAITMAGCQPILVPTDDNYQLQPEAIEQAITPKTR 162
|
|
| PRK09082 |
PRK09082 |
methionine aminotransferase; Validated |
35-177 |
4.06e-03 |
|
methionine aminotransferase; Validated
Pssm-ID: 181642 [Multi-domain] Cd Length: 386 Bit Score: 39.13 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4LW2_C 35 PEAVVEATQqfYSLSAGnvhRSQFAEAQRLTARYEAAREKVAQLLNA-PDDKT-IVWTRGTTESINMVAQCYARPrlqpG 112
Cdd:PRK09082 45 PPYLVEALA--YAMAAG---HNQYPPMTGVAALREAIAAKTARLYGRqYDADSeITVTAGATEALFAAILALVRP----G 115
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90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
4LW2_C 113 DEIIVsVAEHHANLVPWLMVAqqtGAKVVKLPLNAQRL-PDVDLLPELITPRSRILALGQMSNVTG 177
Cdd:PRK09082 116 DEVIV-FDPSYDSYAPAIELA---GGRAVRVALQPPDFrVDWQRFAAAISPRTRLIILNTPHNPSG 177
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