|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
1-401 |
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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 1 MNVFNPAQFRAQFPALQDAGVYLDSAATALKPEAVVEATRQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLNAPD 80
Cdd:PRK10874 1 MNVFNPAQFRAQFPALQDAGVYLDSAATALKPQAVIEATQQFYSLSAGNVHRSQFAAAQRLTARYEAAREQVAQLLNAPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 81 DKTIVWTRGTTESINMVAQCYARPRLQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPLNAQRLPDVDLLPELITPR 160
Cdd:PRK10874 81 AKNIVWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLVPWLMVAQQTGAKVVKLPLGADRLPDVDLLPELITPR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 161 SRILALGQMSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELLE 240
Cdd:PRK10874 161 TRILALGQMSNVTGGCPDLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKSELLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 241 AMSPWLGGGKMIHEVSFDGFTTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAEDALAKRPGFRS 320
Cdd:PRK10874 241 AMSPWQGGGKMLTEVSFDGFTPQSAPWRFEAGTPNVAGVIGLSAALEWLADIDINQAESWSRSLATLAEDALAKLPGFRS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 321 FRCQDSSLLAFDFAGVHHSDMVTLLAEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDVDALVNAVDRALELLV 400
Cdd:PRK10874 321 FRCQDSSLLAFDFAGVHHSDLVTLLAEYGIALRAGQHCAQPLLAALGVTGTLRASFAPYNTQSDVDALVNAVDRALELLV 400
|
.
gi 485654104 401 D 401
Cdd:PRK10874 401 D 401
|
|
| FeS_syn_CsdA |
TIGR03392 |
cysteine desulfurase, catalytic subunit CsdA; Members of this protein family are CsdS. This ... |
4-401 |
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: 792.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 4 FNPAQFRAQFPALQDAGVYLDSAATALKPEAVVEATRQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLNAPDDKT 83
Cdd:TIGR03392 1 FNPAQFRRQFPALQDATVYLDSAATALKPQAVIDATQQFYRLSSGTVHRSQHQEAQSLTARYEAAREQVAQLLNAPDAEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 84 IVWTRGTTESINMVAQCYARPRLQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPLNAQRLPDVDLLPELITPRSRI 163
Cdd:TIGR03392 81 IVWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLIPWLMVAQQTGAKVVKLPIGADLLPDIDQLPELLTPRTRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 164 LALGQMSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMS 243
Cdd:TIGR03392 161 LALGQMSNVTGGCPDLARAITLAHQYGCVVVVDGAQGVVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKTELLEAMP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 244 PWLGGGKMIHEVSFDGFTTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAEDALAKRPGFRSFRC 323
Cdd:TIGR03392 241 PWQGGGKMLSHVSFDGFTPQAVPWRFEAGTPNIAGVIGLSAALEWLADIDINAAESWSVSLATLAEEALAQLPGFRSFRC 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 485654104 324 QDSSLLAFDFAGVHHSDMVTLLAEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDVDALVNAVDRALELLVD 401
Cdd:TIGR03392 321 QGSSLLAFDFAGVHHSDLVTLLAEQGIALRAGQHCAQPLMAALGVSGTLRASFAPYNTQQDVDALVNAVGRALELLVD 398
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
5-398 |
0e+00 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 533.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 5 NPAQFRAQFPALQDAGVYLDSAATALKPEAVVEATRQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLNAPDDKTI 84
Cdd:COG0520 1 DVEAIRADFPVLGKPLVYLDNAATGQKPRPVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAASPDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 85 VWTRGTTESINMVAQCYarPRLQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPLNAQRLPDVDLLPELITPRSRIL 164
Cdd:COG0520 81 IFTRGTTEAINLVAYGL--GRLKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDGELDLEALEALLTPRTKLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 165 ALGQMSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMSP 244
Cdd:COG0520 159 AVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELLEALPP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 245 WLGGGKMIHEVSFDGFTTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAEDALAKRPGFRSFRCQ 324
Cdd:COG0520 239 FLGGGGMIEWVSFDGTTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAIPGVRILGPA 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 485654104 325 D----SSLLAFDFAGVHHSDMVTLLAEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDVDALVNAVDRALEL 398
Cdd:COG0520 319 DpedrSGIVSFNVDGVHPHDVAALLDDEGIAVRAGHHCAQPLMRRLGVPGTVRASFHLYNTEEEIDRLVEALKKLAEL 396
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
21-388 |
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: 523.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 21 VYLDSAATALKPEAVVEATRQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLNAPDDKTIVWTRGTTESINMVAQC 100
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 101 YARPrLQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPLNAQRLPDVDLLPELITPRSRILALGQMSNVTGGCPDLA 180
Cdd:pfam00266 81 LGRS-LKPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 181 RAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMSPWLGGGKMIHEVSFDGF 260
Cdd:pfam00266 160 EIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGMIETVSLQES 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 261 TTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAEDALAKRPGFRSFR-CQDSSLLAFDFAGVHHS 339
Cdd:pfam00266 240 TFADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGpERRASIISFNFKGVHPH 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 485654104 340 DMVTLLAEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDVDAL 388
Cdd:pfam00266 320 DVATLLDESGIAVRSGHHCAQPLMVRLGLGGTVRASFYIYNTQEDVDRL 368
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
21-392 |
7.29e-172 |
|
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: 484.66 E-value: 7.29e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 21 VYLDSAATALKPEAVVEATRQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLNAPDDKTIVWTRGTTESINMVAQC 100
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINAPSPDEIIFTRNTTEAINLVAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 101 YARPRlQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPLNAQRLPDVDLLPELITPRSRILALGQMSNVTGGCPDLA 180
Cdd:cd06453 81 LGRAN-KPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 181 RAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMSPWLGGGKMIHEVSFDGF 260
Cdd:cd06453 160 EIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMIEEVSFEET 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 261 TTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAEDALAKRPGFRSFRCQDS--SLLAFDFAGVHH 338
Cdd:cd06453 240 TYADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEIPGVRVYGDAEDraGVVSFNLEGIHP 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 485654104 339 SDMVTLLAEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDVDALVNAV 392
Cdd:cd06453 320 HDVATILDQYGIAVRAGHHCAQPLMRRLGVPGTVRASFGLYNTEEEIDALVEAL 373
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
3-394 |
3.33e-123 |
|
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: 369.57 E-value: 3.33e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 3 VFNPAQFRAQFPALQDA--G---VYLDSAATALKPEAVVEATRQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLN 77
Cdd:NF041166 224 PFDVNAVRRDFPILQERvnGkplVWFDNAATTQKPQAVIDRLSYFYEHENSNIHRAAHELAARATDAYEGAREKVRRFIG 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 78 APDDKTIVWTRGTTESINMVAQCYARPRLQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPlnaqrlpdVD-----L 152
Cdd:NF041166 304 APSVDEIIFVRGTTEAINLVAKSWGRQNIGAGDEIIVSHLEHHANIVPWQQLAQETGAKLRVIP--------VDdsgqiL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 153 LPE---LITPRSRILALGQMSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGI 229
Cdd:NF041166 376 LDEyakLLNPRTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGI 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 230 GVLYGKSELLEAMSPWLGGGKMIHEVSFDGFTTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAE 309
Cdd:NF041166 456 GVVYGKRDLLEAMPPWQGGGNMIADVTFEKTVYQPAPNRFEAGTGNIADAVGLGAALDYVERIGIENIARYEHDLLEYAT 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 310 DALAKRPGFR---SFRcQDSSLLAFDFAGvHHSDMV-TLLAEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDV 385
Cdd:NF041166 536 AGLAEVPGLRligTAA-DKASVLSFVLDG-YSTEEVgKALNQEGIAVRSGHHCAQPILRRFGVEATVRPSLAFYNTCEEV 613
|
....*....
gi 485654104 386 DALVNAVDR 394
Cdd:NF041166 614 DALVAVLRR 622
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
1-401 |
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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 1 MNVFNPAQFRAQFPALQDAGVYLDSAATALKPEAVVEATRQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLNAPD 80
Cdd:PRK10874 1 MNVFNPAQFRAQFPALQDAGVYLDSAATALKPQAVIEATQQFYSLSAGNVHRSQFAAAQRLTARYEAAREQVAQLLNAPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 81 DKTIVWTRGTTESINMVAQCYARPRLQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPLNAQRLPDVDLLPELITPR 160
Cdd:PRK10874 81 AKNIVWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLVPWLMVAQQTGAKVVKLPLGADRLPDVDLLPELITPR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 161 SRILALGQMSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELLE 240
Cdd:PRK10874 161 TRILALGQMSNVTGGCPDLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKSELLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 241 AMSPWLGGGKMIHEVSFDGFTTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAEDALAKRPGFRS 320
Cdd:PRK10874 241 AMSPWQGGGKMLTEVSFDGFTPQSAPWRFEAGTPNVAGVIGLSAALEWLADIDINQAESWSRSLATLAEDALAKLPGFRS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 321 FRCQDSSLLAFDFAGVHHSDMVTLLAEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDVDALVNAVDRALELLV 400
Cdd:PRK10874 321 FRCQDSSLLAFDFAGVHHSDLVTLLAEYGIALRAGQHCAQPLLAALGVTGTLRASFAPYNTQSDVDALVNAVDRALELLV 400
|
.
gi 485654104 401 D 401
Cdd:PRK10874 401 D 401
|
|
| FeS_syn_CsdA |
TIGR03392 |
cysteine desulfurase, catalytic subunit CsdA; Members of this protein family are CsdS. This ... |
4-401 |
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: 792.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 4 FNPAQFRAQFPALQDAGVYLDSAATALKPEAVVEATRQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLNAPDDKT 83
Cdd:TIGR03392 1 FNPAQFRRQFPALQDATVYLDSAATALKPQAVIDATQQFYRLSSGTVHRSQHQEAQSLTARYEAAREQVAQLLNAPDAEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 84 IVWTRGTTESINMVAQCYARPRLQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPLNAQRLPDVDLLPELITPRSRI 163
Cdd:TIGR03392 81 IVWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLIPWLMVAQQTGAKVVKLPIGADLLPDIDQLPELLTPRTRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 164 LALGQMSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMS 243
Cdd:TIGR03392 161 LALGQMSNVTGGCPDLARAITLAHQYGCVVVVDGAQGVVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKTELLEAMP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 244 PWLGGGKMIHEVSFDGFTTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAEDALAKRPGFRSFRC 323
Cdd:TIGR03392 241 PWQGGGKMLSHVSFDGFTPQAVPWRFEAGTPNIAGVIGLSAALEWLADIDINAAESWSVSLATLAEEALAQLPGFRSFRC 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 485654104 324 QDSSLLAFDFAGVHHSDMVTLLAEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDVDALVNAVDRALELLVD 401
Cdd:TIGR03392 321 QGSSLLAFDFAGVHHSDLVTLLAEQGIALRAGQHCAQPLMAALGVSGTLRASFAPYNTQQDVDALVNAVGRALELLVD 398
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
5-398 |
0e+00 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 533.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 5 NPAQFRAQFPALQDAGVYLDSAATALKPEAVVEATRQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLNAPDDKTI 84
Cdd:COG0520 1 DVEAIRADFPVLGKPLVYLDNAATGQKPRPVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAASPDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 85 VWTRGTTESINMVAQCYarPRLQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPLNAQRLPDVDLLPELITPRSRIL 164
Cdd:COG0520 81 IFTRGTTEAINLVAYGL--GRLKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDGELDLEALEALLTPRTKLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 165 ALGQMSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMSP 244
Cdd:COG0520 159 AVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELLEALPP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 245 WLGGGKMIHEVSFDGFTTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAEDALAKRPGFRSFRCQ 324
Cdd:COG0520 239 FLGGGGMIEWVSFDGTTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAIPGVRILGPA 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 485654104 325 D----SSLLAFDFAGVHHSDMVTLLAEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDVDALVNAVDRALEL 398
Cdd:COG0520 319 DpedrSGIVSFNVDGVHPHDVAALLDDEGIAVRAGHHCAQPLMRRLGVPGTVRASFHLYNTEEEIDRLVEALKKLAEL 396
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
21-388 |
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: 523.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 21 VYLDSAATALKPEAVVEATRQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLNAPDDKTIVWTRGTTESINMVAQC 100
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 101 YARPrLQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPLNAQRLPDVDLLPELITPRSRILALGQMSNVTGGCPDLA 180
Cdd:pfam00266 81 LGRS-LKPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 181 RAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMSPWLGGGKMIHEVSFDGF 260
Cdd:pfam00266 160 EIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGMIETVSLQES 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 261 TTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAEDALAKRPGFRSFR-CQDSSLLAFDFAGVHHS 339
Cdd:pfam00266 240 TFADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGpERRASIISFNFKGVHPH 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 485654104 340 DMVTLLAEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDVDAL 388
Cdd:pfam00266 320 DVATLLDESGIAVRSGHHCAQPLMVRLGLGGTVRASFYIYNTQEDVDRL 368
|
|
| sufS |
TIGR01979 |
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine ... |
10-399 |
3.01e-172 |
|
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: 486.78 E-value: 3.01e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 10 RAQFPALQ-----DAGVYLDSAATALKPEAVVEATRQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLNAPDDKTI 84
Cdd:TIGR01979 4 RADFPILKrkingKPLVYLDSAATSQKPQQVIDAVAEYYRNSNANVHRGIHTLSVRATEAYEAVREKVAKFINAASDEEI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 85 VWTRGTTESINMVAQCYARPRLQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPLNAQRLPDVDLLPELITPRSRIL 164
Cdd:TIGR01979 84 VFTRGTTESINLVAYSWGDSNLKAGDEIVISEMEHHANIVPWQLLAERTGATLKFIPLDDDGTLDLDDLEKLLTEKTKLV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 165 ALGQMSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMSP 244
Cdd:TIGR01979 164 AITHVSNVLGTVNPVEEIAKLAHQVGAKVLVDGAQAVPHMPVDVQALDCDFYVFSGHKMYGPTGIGVLYGKEELLEQMPP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 245 WLGGGKMIHEVSFDGFTTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAEDALAKRPGFRSFRCQ 324
Cdd:TIGR01979 244 FLGGGEMIAEVSFEETTYNEAPHKFEAGTPNIAGVIGLGAAIDYLEAIGLENIEAHEHELTAYALERLGEIPGLRIYGPR 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 485654104 325 DS----SLLAFDFAGVHHSDMVTLLAEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDVDALVNAVDRALELL 399
Cdd:TIGR01979 324 DAedrgGIISFNVEGVHPHDVGTILDEEGIAVRSGHHCAQPLMRRFGVPATCRASFYIYNTEEDIDALVEALKKVRKFF 402
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
21-392 |
7.29e-172 |
|
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: 484.66 E-value: 7.29e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 21 VYLDSAATALKPEAVVEATRQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLNAPDDKTIVWTRGTTESINMVAQC 100
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINAPSPDEIIFTRNTTEAINLVAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 101 YARPRlQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPLNAQRLPDVDLLPELITPRSRILALGQMSNVTGGCPDLA 180
Cdd:cd06453 81 LGRAN-KPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 181 RAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMSPWLGGGKMIHEVSFDGF 260
Cdd:cd06453 160 EIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMIEEVSFEET 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 261 TTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAEDALAKRPGFRSFRCQDS--SLLAFDFAGVHH 338
Cdd:cd06453 240 TYADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEIPGVRVYGDAEDraGVVSFNLEGIHP 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 485654104 339 SDMVTLLAEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDVDALVNAV 392
Cdd:cd06453 320 HDVATILDQYGIAVRAGHHCAQPLMRRLGVPGTVRASFGLYNTEEEIDALVEAL 373
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
10-391 |
8.62e-139 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 402.59 E-value: 8.62e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 10 RAQFPAL-QDAG----VYLDSAATALKPEAVVEATRQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLNAPDDKTI 84
Cdd:PLN02855 18 RPDFPILdQTVNgsklVYLDNAATSQKPAAVLDALQDYYEEYNSNVHRGIHALSAKATDAYELARKKVAAFINASTSREI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 85 VWTRGTTESINMVAQCYARPRLQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPLNAQRLPDVDLLPELITPRSRIL 164
Cdd:PLN02855 98 VFTRNATEAINLVAYTWGLANLKPGDEVILSVAEHHSNIVPWQLVAQKTGAVLKFVGLTPDEVLDVEQLKELLSEKTKLV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 165 ALGQMSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMSP 244
Cdd:PLN02855 178 ATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLWGKSDLLESMPP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 245 WLGGGKMIHEVSFDGFTTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAEDALAKRPGFRSFRCQ 324
Cdd:PLN02855 258 FLGGGEMISDVFLDHSTYAPPPSRFEAGTPAIGEAIGLGAAIDYLSEIGMDRIHEYEVELGTYLYEKLSSVPGVRIYGPK 337
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 485654104 325 DS------SLLAFDFAGVHHSDMVTLL-AEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDVDALVNA 391
Cdd:PLN02855 338 PSegvgraALCAFNVEGIHPTDLSTFLdQQHGVAIRSGHHCAQPLHRYLGVNASARASLYFYNTKEEVDAFIHA 411
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
4-399 |
4.67e-132 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 384.87 E-value: 4.67e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 4 FNPAQFRAQFPAL--QDAG---VYLDSAATALKPEAVVEATRQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLNA 78
Cdd:PRK09295 3 FSVEKVRADFPVLsrEVNGlplAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKQAALFINA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 79 PDDKTIVWTRGTTESINMVAQCYARPRLQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPLNAQRLPDVDLLPELIT 158
Cdd:PRK09295 83 RSAEELVFVRGTTEGINLVANSWGNSNVRAGDNIIISEMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPALFD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 159 PRSRILALGQMSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSEL 238
Cdd:PRK09295 163 ERTRLLAITHVSNVLGTENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKEAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 239 LEAMSPWLGGGKMIHEVSF-DGFTTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAEDALAKRPG 317
Cdd:PRK09295 243 LQEMPPWEGGGSMIATVSLtEGTTWAKAPWRFEAGTPNTGGIIGLGAALDYVSALGLNNIAEYEQNLMHYALSQLESVPD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 318 FRSF-RCQDSSLLAFDFaGVHHS-DMVTLLAEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDVDALVNAVDRA 395
Cdd:PRK09295 323 LTLYgPQNRLGVIAFNL-GKHHAyDVGSFLDNYGIAVRTGHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVAGLQRI 401
|
....
gi 485654104 396 LELL 399
Cdd:PRK09295 402 HRLL 405
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
3-394 |
3.33e-123 |
|
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: 369.57 E-value: 3.33e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 3 VFNPAQFRAQFPALQDA--G---VYLDSAATALKPEAVVEATRQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLN 77
Cdd:NF041166 224 PFDVNAVRRDFPILQERvnGkplVWFDNAATTQKPQAVIDRLSYFYEHENSNIHRAAHELAARATDAYEGAREKVRRFIG 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 78 APDDKTIVWTRGTTESINMVAQCYARPRLQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPlnaqrlpdVD-----L 152
Cdd:NF041166 304 APSVDEIIFVRGTTEAINLVAKSWGRQNIGAGDEIIVSHLEHHANIVPWQQLAQETGAKLRVIP--------VDdsgqiL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 153 LPE---LITPRSRILALGQMSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGI 229
Cdd:NF041166 376 LDEyakLLNPRTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGI 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 230 GVLYGKSELLEAMSPWLGGGKMIHEVSFDGFTTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESWSRSLATLAE 309
Cdd:NF041166 456 GVVYGKRDLLEAMPPWQGGGNMIADVTFEKTVYQPAPNRFEAGTGNIADAVGLGAALDYVERIGIENIARYEHDLLEYAT 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 310 DALAKRPGFR---SFRcQDSSLLAFDFAGvHHSDMV-TLLAEYGIALRAGQHCAQPLLAELGVTGTLRASFAPYNTKSDV 385
Cdd:NF041166 536 AGLAEVPGLRligTAA-DKASVLSFVLDG-YSTEEVgKALNQEGIAVRSGHHCAQPILRRFGVEATVRPSLAFYNTCEEV 613
|
....*....
gi 485654104 386 DALVNAVDR 394
Cdd:NF041166 614 DALVAVLRR 622
|
|
| am_tr_V_VC1184 |
TIGR01976 |
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of ... |
4-392 |
1.20e-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: 201.13 E-value: 1.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 4 FNPAQFRAQFPALQDAG-VYLDSAATALKPE----AVVEATRQFYSLSAGNVHRSQfaEAQRLTARyeaAREKVAQLLNA 78
Cdd:TIGR01976 1 FDVEAVRGQFPALADGDrVFFDNPAGTQIPQsvadAVSAALTRSNANRGGAYESSR--RADQVVDD---AREAVADLLNA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 79 pDDKTIVWTRGTTESINMVAQCYARpRLQPGDEIIVSVAEHHANLVPWLMVAQQTGAKVVKLPLNAQ--RLPDVDLLPeL 156
Cdd:TIGR01976 76 -DPPEVVFGANATSLTFLLSRAISR-RWGPGDEVIVTRLDHEANISPWLQAAERAGAKVKWARVDEAtgELHPDDLAS-L 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 157 ITPRSRILALGQMSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTgIGVLYGKS 236
Cdd:TIGR01976 153 LSPRTRLVAVTAASNTLGSIVDLAAITELVHAAGALVVVDAVHYAPHGLIDVQATGADFLTCSAYKFFGPH-MGILWGRP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 237 ELLEAMSPwlgggkmihevSFDGFTTQSAPWKLEAGTPNVAGVIGLSAALEWLADYD--------------INQAESWSR 302
Cdd:TIGR01976 232 ELLMNLPP-----------YKLTFSYDTGPERFELGTPQYELLAGVVAAVDYLAGLGesangsrrerlvasFQAIDAYEN 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 303 SLATLAEDALAKRPGFRSFRCQDSS----LLAFDFAGVHHSDMVTLLAEYGIALRAGQHCAQPLLAELGVT---GTLRAS 375
Cdd:TIGR01976 301 RLAEYLLVGLSDLPGVTLYGVARLAarvpTVSFTVHGLPPQRVVRRLADQGIDAWAGHFYAVRLLRRLGLNdegGVVRVG 380
|
410
....*....|....*..
gi 485654104 376 FAPYNTKSDVDALVNAV 392
Cdd:TIGR01976 381 LAHYNTAEEVDRLLEAL 397
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
21-397 |
1.41e-60 |
|
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: 200.66 E-value: 1.41e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 21 VYLDSAATA-LKPEaVVEATRQFYSLSAGN---VHRsqfaEAQRLTARYEAAREKVAQLLNApDDKTIVWTRGTTESINM 96
Cdd:COG1104 4 IYLDNAATTpVDPE-VLEAMLPYLTEYFGNpssLHS----FGREARAALEEAREQVAALLGA-DPEEIIFTSGGTEANNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 97 VAQCYARPRLQPGDEIIVSVAEHHA--NLVPWLmvaQQTGAKVVKLPLNAQRLPDVDLLPELITPRSRILALGQMSNVTG 174
Cdd:COG1104 78 AIKGAARAYRKKGKHIITSAIEHPAvlETARFL---EKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 175 GCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELleAMSPWL-GGGkmiH 253
Cdd:COG1104 155 TIQPIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRKGV--RLEPLIhGGG---Q 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 254 EvsfdgfttqsapWKLEAGTPNVAGVIGLSAALEWLADydiNQAESWSR--SLATLAEDALAKR-PGFRSFRCQDSSL-- 328
Cdd:COG1104 230 E------------RGLRSGTENVPGIVGLGKAAELAAE---ELEEEAARlrALRDRLEEGLLAAiPGVVINGDPENRLpn 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 329 -LAFDFAGVHHSDMVTLLAEYGIALRAGQHCAQ------PLLAELGVT-----GTLRASFAPYNTKSDVDALVNAVDRAL 396
Cdd:COG1104 295 tLNFSFPGVEGEALLLALDLAGIAVSSGSACSSgslepsHVLLAMGLDeelahGSIRFSLGRFTTEEEIDRAIEALKEIV 374
|
.
gi 485654104 397 E 397
Cdd:COG1104 375 A 375
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
21-386 |
1.22e-30 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 120.53 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 21 VYLD-SAATALKPEaVVEATRQFYSLSAGNVHRSQFAEAQRLTARYEAAREKVAQLLNApDDKTIVWTRGTTESINMVAQ 99
Cdd:PLN02651 1 LYLDmQATTPIDPR-VLDAMLPFLIEHFGNPHSRTHLYGWESEDAVEKARAQVAALIGA-DPKEIIFTSGATESNNLAIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 100 CYARPRLQPGDEIIVSVAEHHANL--VPWLmvaQQTGAKVVKLPLNAQRLPDVDLLPELITPRSRILALGQMSNVTGGCP 177
Cdd:PLN02651 79 GVMHFYKDKKKHVITTQTEHKCVLdsCRHL---QQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 178 DLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMSPWLGGGKMIHevsf 257
Cdd:PLN02651 156 PVEEIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRLEPLMSGGGQER---- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 258 dgfttqsapwKLEAGTPNVAGVIGLSAALEwLADYDINQAESWSRSLATLAEDAL-AKRPGFR--SFRCQDSSL---LAF 331
Cdd:PLN02651 232 ----------GRRSGTENTPLVVGLGAACE-LAMKEMDYDEKHMKALRERLLNGLrAKLGGVRvnGPRDPEKRYpgtLNL 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 485654104 332 DFAGVHHSdmVTLLAEYGIALRAGQHC----AQP--LLAELGV-----TGTLRASFAPYNTKSDVD 386
Cdd:PLN02651 301 SFAYVEGE--SLLMGLKEVAVSSGSACtsasLEPsyVLRALGVpeemaHGSLRLGVGRFTTEEEVD 364
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
21-233 |
4.94e-28 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 113.88 E-value: 4.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 21 VYLDSAATALKPEAVVEATRQFYSLSA--GNVH-RS-----QFAEAqrltarYEAAREKVAQLLNApDDKTIVWTRGTTE 92
Cdd:PRK14012 5 IYLDYSATTPVDPRVAEKMMPYLTMDGtfGNPAsRShrfgwQAEEA------VDIARNQIADLIGA-DPREIVFTSGATE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 93 SINM----VAQCYARPrlqpGDEIIVSVAEHHANLVPWLMVAQQtGAKVVKLPLNAQRLPDVDLLPELITPRSRILALGQ 168
Cdd:PRK14012 78 SDNLaikgAAHFYQKK----GKHIITSKTEHKAVLDTCRQLERE-GFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMH 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 485654104 169 MSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLY 233
Cdd:PRK14012 153 VNNEIGVIQDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALY 217
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
21-287 |
3.91e-16 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 79.39 E-value: 3.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 21 VYLDSAATA-LKPEAV---VEATRQFYSlSAGNVHRSQFAEAQRLtaryEAAREKVAQLLNApDDKTIVWTRGTTESiNM 96
Cdd:PRK02948 2 IYLDYAATTpMSKEALqtyQKAASQYFG-NESSLHDIGGTASSLL----QVCRKTFAEMIGG-EEQGIYFTSGGTES-NY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 97 VA-QCYARPRLQPGDEIIVSVAEHHA--NLVPWLmvaQQTGAKVVKLPLNAQRLPDVDLLPELITPRSrILALGQMSNV- 172
Cdd:PRK02948 75 LAiQSLLNALPQNKKHIITTPMEHASihSYFQSL---ESQGYTVTEIPVDKSGLIRLVDLERAITPDT-VLASIQHANSe 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 173 TGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELleamsPWlgggKMI 252
Cdd:PRK02948 151 IGTIQPIAEIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYINPQV-----RW----KPV 221
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 485654104 253 -----HEvsfDGFttqsapwklEAGTPNVAGVIGLSAALE 287
Cdd:PRK02948 222 fpgttHE---KGF---------RPGTVNVPGIAAFLTAAE 249
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
65-235 |
4.73e-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: 4.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 65 YEAAREKVAQLLNAPDDKTIVwTRGTTESINMVAQCYarprLQPGDEIIVSVAEHHANLvpWLMVAQQtGAKVVKLPLN- 143
Cdd:cd01494 2 LEELEEKLARLLQPGNDKAVF-VPSGTGANEAALLAL----LGPGDEVIVDANGHGSRY--WVAAELA-GAKPVPVPVDd 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 144 --AQRLPDVDLLPELITPRSRILALGQMSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAVHFPADVQQLD---IDFYAF 218
Cdd:cd01494 74 agYGGLDVAILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPeggADVVTF 153
|
170
....*....|....*..
gi 485654104 219 SGHKLYGPTGIGVLYGK 235
Cdd:cd01494 154 SLHKNLGGEGGGVVIVK 170
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
21-391 |
4.54e-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: 63.51 E-value: 4.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 21 VYLDSAATALKPEAVVEATRQFYSLSAGNVHRSQFAEAQRLtarYEAAREKVAQLLNAPDDKT-IVWTRGTTESINMVAQ 99
Cdd:cd00609 1 IDLSIGEPDFPPPPEVLEALAAAALRAGLLGYYPDPGLPEL---REAIAEWLGRRGGVDVPPEeIVVTNGAQEALSLLLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 100 CYarprLQPGDEIIVSVaehhanlvP----WLMVAQQTGAKVVKLPLNAQ--RLPDVDLLPELITPRSRILALGQMSNVT 173
Cdd:cd00609 78 AL----LNPGDEVLVPD--------PtypgYEAAARLAGAEVVPVPLDEEggFLLDLELLEAAKTPKTKLLYLNNPNNPT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 174 GGCPD---LARAITFAHSAGMVVMVDGA------QGAVHFPAD-VQQLDIDFYAFSGHKLYGPTG--IGVLYGKSELLEA 241
Cdd:cd00609 146 GAVLSeeeLEELAELAKKHGILIISDEAyaelvyDGEPPPALAlLDAYERVIVLRSFSKTFGLPGlrIGYLIAPPEELLE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 242 MSpwlgggKMIHEVSFdgfttqsapwkleaGTPNVAGVIGLSAALEWLADYdINQAESWSRSLATLAEDALAKRPGFRSF 321
Cdd:cd00609 226 RL------KKLLPYTT--------------SGPSTLSQAAAAAALDDGEEH-LEELRERYRRRRDALLEALKELGPLVVV 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 485654104 322 RCQDSSLLAFDFAGVHHSDMVT-LLAEYGIALRAGQHCAQPLlaelgvTGTLRASFApyNTKSDVDALVNA 391
Cdd:cd00609 285 KPSGGFFLWLDLPEGDDEEFLErLLLEAGVVVRPGSAFGEGG------EGFVRLSFA--TPEEELEEALER 347
|
|
| AspB |
COG0436 |
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ... |
32-242 |
4.23e-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: 4.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 32 PEAVVEATRQ-------FYSLSAGnvhrsqfaeaqrltarYEAAREKVAQLLNA-------PDDktIVWTRGTTESINMV 97
Cdd:COG0436 45 PDHIREAAIEalddgvtGYTPSAG----------------IPELREAIAAYYKRrygvdldPDE--ILVTNGAKEALALA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 98 AQCYarprLQPGDEIIVsvaehhanLVP----WLMVAQQTGAKVVKLPLNAQR--LPDVDLLPELITPRSRILALGQMSN 171
Cdd:COG0436 107 LLAL----LNPGDEVLV--------PDPgypsYRAAVRLAGGKPVPVPLDEENgfLPDPEALEAAITPRTKAIVLNSPNN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 172 VTGGC---PDLARAITFAHSAGMVVMVD--------GAQGAVHFpADVQQLD---IDFYAFSghKLYGPTG--IGVLYGK 235
Cdd:COG0436 175 PTGAVysrEELEALAELAREHDLLVISDeiyeelvyDGAEHVSI-LSLPGLKdrtIVINSFS--KSYAMTGwrIGYAVGP 251
|
....*..
gi 485654104 236 SELLEAM 242
Cdd:COG0436 252 PELIAAL 258
|
|
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
11-232 |
1.88e-08 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 56.41 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 11 AQFPALqDAGVYLDSAATALKPEAVVEAT-RQFYSLSAGNVHrSQFAEAQRLTARYEAAREKVAQLLNAP-DDKTIVWTR 88
Cdd:PLN02724 27 TEFARL-KGVVYLDHAGATLYSESQLEAAlADFSSNVYGNPH-SQSDSSMRSSDTIESARQQVLEYFNAPpSDYACVFTS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 89 GTTESINMVAQCYArprLQPGDEIIVSVAEHHANL-VPWLMVAQQTGAKVVKLPLNAQRL----PDVDLLPELITPRSR- 162
Cdd:PLN02724 105 GATAALKLVGETFP---WSSESHFCYTLENHNSVLgIREYALEKGAAAIAVDIEEAANQPtnsqGSVVVKSRGLQRRNTs 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 163 -------------ILALGQMSNVTGGCPDL--------ARAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGH 221
Cdd:PLN02724 182 klqkreddgeaynLFAFPSECNFSGAKFPLdlvklikdNQHSNFSKSGRWMVLLDAAKGCGTSPPDLSRYPADFVVVSFY 261
|
250
....*....|..
gi 485654104 222 KLYG-PTGIGVL 232
Cdd:PLN02724 262 KIFGyPTGLGAL 273
|
|
| PRK08361 |
PRK08361 |
aspartate aminotransferase; Provisional |
106-242 |
1.09e-04 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 236248 [Multi-domain] Cd Length: 391 Bit Score: 44.10 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 106 LQPGDEIIVSvaehHANLVPWLMVAQQTGAKVVKLPLNAQR--LPDVDLLPELITPRSRILALGQMSNVTGGCPD--LAR 181
Cdd:PRK08361 114 LEEGDEVIIP----DPAFVCYVEDAKIAEAKPIRIPLREENefQPDPDELLELITKRTRMIVINYPNNPTGATLDkeVAK 189
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 182 AIT-FAHSAGMVVMVDGA------QGAVHFPADVQQLDIDFYAFSGHKLYGPTG--IGVLYGKSELLEAM 242
Cdd:PRK08361 190 AIAdIAEDYNIYILSDEPyehflyEGAKHYPMIKYAPDNTILANSFSKTFAMTGwrLGFVIAPEQVIKDM 259
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
51-207 |
1.17e-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: 43.78 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 51 HRSQFAEAQRLTARYEAArekvaqllnapdDKTIVWTRGTTESINMVAQCYarprLQPGDEIIVSVAEH--HANLvpwLM 128
Cdd:cd00615 57 PTGPIKEAQELAARAFGA------------KHTFFLVNGTSSSNKAVILAV----CGPGDKILIDRNCHksVING---LV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 129 VAQQTgAKVVKLPLNAQR-----LPDVDLLPELITPRSRILALGQMSNVTGGCPDLARAITFAHSAGMVVMVDGAQGAvH 203
Cdd:cd00615 118 LSGAV-PVYLKPERNPYYgiaggIPPETFKKALIEHPDAKAAVITNPTYYGICYNLRKIVEEAHHRGLPVLVDEAHGA-H 195
|
....
gi 485654104 204 FPAD 207
Cdd:cd00615 196 FRFH 199
|
|
| PLN02409 |
PLN02409 |
serine--glyoxylate aminotransaminase |
106-242 |
1.83e-04 |
|
serine--glyoxylate aminotransaminase
Pssm-ID: 178031 [Multi-domain] Cd Length: 401 Bit Score: 43.21 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 106 LQPGDEIIVSVAEHHANLvpWLMVAQQTGAKVVKLPLNAQRLPDVDLLPELITP----RSRILALGQMSNVTGGCPDLA- 180
Cdd:PLN02409 81 LSPGDKVVSFRIGQFSLL--WIDQMQRLNFDVDVVESPWGQGADLDILKSKLRQdtnhKIKAVCVVHNETSTGVTNDLAg 158
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 485654104 181 -RAITFAHSAGMVVMVDGAQ--GAVHFPADVQQLDIdfyAFSGHK--LYGPTGIGVLYGKSELLEAM 242
Cdd:PLN02409 159 vRKLLDCAQHPALLLVDGVSsiGALDFRMDEWGVDV---ALTGSQkaLSLPTGLGIVCASPKALEAS 222
|
|
| PRK07568 |
PRK07568 |
pyridoxal phosphate-dependent aminotransferase; |
32-174 |
2.28e-04 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 181036 Cd Length: 397 Bit Score: 42.92 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 32 PEAVVEATRQF------YSLSAGnvhrsqfaeaqrltarYEAAREKVA---QLLN---APDDktIVWTRGTTESIN--MV 97
Cdd:PRK07568 45 PEVFFEAIKNYdeevlaYSHSQG----------------IPELREAFAkyyKKWGidvEPDE--ILITNGGSEAILfaMM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 98 AQCyarprlQPGDEIIVsvAE-HHANlvpWLMVAQQTGAKVVKLPLNAQ---RLPDVDLLPELITPRSRILALGQMSNVT 173
Cdd:PRK07568 107 AIC------DPGDEILV--PEpFYAN---YNGFATSAGVKIVPVTTKIEegfHLPSKEEIEKLITPKTKAILISNPGNPT 175
|
.
gi 485654104 174 G 174
Cdd:PRK07568 176 G 176
|
|
| PRK06836 |
PRK06836 |
pyridoxal phosphate-dependent aminotransferase; |
32-174 |
2.43e-04 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180720 Cd Length: 394 Bit Score: 42.87 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 32 PEAVVEATRQFYSLSAGNVHRSQFAeaqrltARYEAAREKVAQLLNA-------PDDktIVWTRGTTESINMVaqcyARP 104
Cdd:PRK06836 48 PAAVKEALRELAEEEDPGLHGYMPN------AGYPEVREAIAESLNRrfgtpltADH--IVMTCGAAGALNVA----LKA 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 485654104 105 RLQPGDEIIVsVAEHHANLVPWlmvAQQTGAKVVKLPLNAQR-LPDVDLLPELITPRSRILALGQMSNVTG 174
Cdd:PRK06836 116 ILNPGDEVIV-FAPYFVEYRFY---VDNHGGKLVVVPTDTDTfQPDLDALEAAITPKTKAVIINSPNNPTG 182
|
|
| PRK06290 |
PRK06290 |
LL-diaminopimelate aminotransferase; |
89-204 |
3.53e-04 |
|
LL-diaminopimelate aminotransferase;
Pssm-ID: 235772 Cd Length: 410 Bit Score: 42.33 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 89 GTTESINMVAQCYarprLQPGDEIIVS-----VAEHHANlvpWLmvaqqtGAKVVKLPLNAQR--LPDVDLLPELITPRS 161
Cdd:PRK06290 114 GSKPALAMLPSCF----INPGDVTLMTvpgypVTGTHTK---YY------GGEVYNLPLLEENnfLPDLDSIPKDIKEKA 180
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 485654104 162 RILALGQMSNVTGGCPDL---ARAITFAHSAGMVVMVDGAQGAVHF 204
Cdd:PRK06290 181 KLLYLNYPNNPTGAVATKefyEEVVDFAKENNIIVVQDAAYAALTF 226
|
|
| PRK05957 |
PRK05957 |
pyridoxal phosphate-dependent aminotransferase; |
32-162 |
1.64e-03 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235654 Cd Length: 389 Bit Score: 40.44 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 32 PEAVVEATRQFYSlsagNVHRSQFAEAQRLTARYEAAREKVAQL--LNAPDDKTIVWTRGTtesiNMVAQCYARPRLQPG 109
Cdd:PRK05957 42 PPEAIEALNNFLA----NPENHKYQAVQGIPPLLEAITQKLQQDngIELNNEQAIVVTAGS----NMAFMNAILAITDPG 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 485654104 110 DEIIVsvaehhanLVPWL----MVAQQTGAKVVKLPLNAQRLPDVDLLPELITPRSR 162
Cdd:PRK05957 114 DEIIL--------NTPYYfnheMAITMAGCQPILVPTDDNYQLQPEAIEQAITPKTR 162
|
|
| PRK09082 |
PRK09082 |
methionine aminotransferase; Validated |
32-174 |
4.83e-03 |
|
methionine aminotransferase; Validated
Pssm-ID: 181642 [Multi-domain] Cd Length: 386 Bit Score: 38.74 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485654104 32 PEAVVEATRqfYSLSAGnvhRSQFAEAQRLTARYEAAREKVAQLLNA-PDDKT-IVWTRGTTESINMVAQCYARPrlqpG 109
Cdd:PRK09082 45 PPYLVEALA--YAMAAG---HNQYPPMTGVAALREAIAAKTARLYGRqYDADSeITVTAGATEALFAAILALVRP----G 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 485654104 110 DEIIVsVAEHHANLVPWLMVAqqtGAKVVKLPLNAQRL-PDVDLLPELITPRSRILALGQMSNVTG 174
Cdd:PRK09082 116 DEVIV-FDPSYDSYAPAIELA---GGRAVRVALQPPDFrVDWQRFAAAISPRTRLIILNTPHNPSG 177
|
|
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