|
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: 749.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 1 MKAFDSEKFRQQFPALQQSTTFLDSAATALKPACMIEATGHYYQNHSATVHRSQHTTAQAMTARYEQARSLVAELINAPL 80
Cdd:PRK10874 1 MNVFNPAQFRAQFPALQDAGVYLDSAATALKPQAVIEATQQFYSLSAGNVHRSQFAAAQRLTARYEAAREQVAQLLNAPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 81 PEDIVWTKGTTEAINLIAQSYFRPRLNAGDEIIVSEQEHHANLLPWLILAEQTKAKIVKWPIGKQHQPEITTLAELLNEK 160
Cdd:PRK10874 81 AKNIVWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLVPWLMVAQQTGAKVVKLPLGADRLPDVDLLPELITPR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 161 SRLVAISQMSNVTGATVDLAQVSALAHQYDCRVVVDGAQGIVHSPVDMQQLDIDFYAFSAHKLYGPNGVGVLYAKSELLN 240
Cdd:PRK10874 161 TRILALGQMSNVTGGCPDLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKSELLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 241 AMSPWHGGGKMLTQVSFEGFTPESVPYRFEAGTPNVAGVIGFAATLEWLKTVDIQLAESHAIDLTDYTEQQLSTLPGFIS 320
Cdd:PRK10874 241 AMSPWQGGGKMLTEVSFDGFTPQSAPWRFEAGTPNVAGVIGLSAALEWLADIDINQAESWSRSLATLAEDALAKLPGFRS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 321 YRATGSTLLAFNIAGIHHHDLATLLAEQNISLRSGQHCAQPLLDALGINGCLRVSFMPYNNYQDADKLVSAVKFALSLLN 400
Cdd:PRK10874 321 FRCQDSSLLAFDFAGVHHSDLVTLLAEYGIALRAGQHCAQPLLAALGVTGTLRASFAPYNTQSDVDALVNAVDRALELLV 400
|
.
gi 498913418 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: 688.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 4 FDSEKFRQQFPALQQSTTFLDSAATALKPACMIEATGHYYQNHSATVHRSQHTTAQAMTARYEQARSLVAELINAPLPED 83
Cdd:TIGR03392 1 FNPAQFRRQFPALQDATVYLDSAATALKPQAVIDATQQFYRLSSGTVHRSQHQEAQSLTARYEAAREQVAQLLNAPDAEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 84 IVWTKGTTEAINLIAQSYFRPRLNAGDEIIVSEQEHHANLLPWLILAEQTKAKIVKWPIGKQHQPEITTLAELLNEKSRL 163
Cdd:TIGR03392 81 IVWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLIPWLMVAQQTGAKVVKLPIGADLLPDIDQLPELLTPRTRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 164 VAISQMSNVTGATVDLAQVSALAHQYDCRVVVDGAQGIVHSPVDMQQLDIDFYAFSAHKLYGPNGVGVLYAKSELLNAMS 243
Cdd:TIGR03392 161 LALGQMSNVTGGCPDLARAITLAHQYGCVVVVDGAQGVVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKTELLEAMP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 244 PWHGGGKMLTQVSFEGFTPESVPYRFEAGTPNVAGVIGFAATLEWLKTVDIQLAESHAIDLTDYTEQQLSTLPGFISYRA 323
Cdd:TIGR03392 241 PWQGGGKMLSHVSFDGFTPQAVPWRFEAGTPNIAGVIGLSAALEWLADIDINAAESWSVSLATLAEEALAQLPGFRSFRC 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498913418 324 TGSTLLAFNIAGIHHHDLATLLAEQNISLRSGQHCAQPLLDALGINGCLRVSFMPYNNYQDADKLVSAVKFALSLLND 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: 538.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 5 DSEKFRQQFPALQQSTTFLDSAATALKPACMIEATGHYYQNHSATVHRSQHTTAQAMTARYEQARSLVAELINAPLPEDI 84
Cdd:COG0520 1 DVEAIRADFPVLGKPLVYLDNAATGQKPRPVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAASPDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 85 VWTKGTTEAINLIAQSYfrPRLNAGDEIIVSEQEHHANLLPWLILAEQTKAKIVKWPIGKQHQPEITTLAELLNEKSRLV 164
Cdd:COG0520 81 IFTRGTTEAINLVAYGL--GRLKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDGELDLEALEALLTPRTKLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 165 AISQMSNVTGATVDLAQVSALAHQYDCRVVVDGAQGIVHSPVDMQQLDIDFYAFSAHKLYGPNGVGVLYAKSELLNAMSP 244
Cdd:COG0520 159 AVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELLEALPP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 245 WHGGGKMLTQVSFEGFTPESVPYRFEAGTPNVAGVIGFAATLEWLKTVDIQLAESHAIDLTDYTEQQLSTLPGFISYRAT 324
Cdd:COG0520 239 FLGGGGMIEWVSFDGTTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAIPGVRILGPA 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498913418 325 GST----LLAFNIAGIHHHDLATLLAEQNISLRSGQHCAQPLLDALGINGCLRVSFMPYNNYQDADKLVSAVKFALSL 398
Cdd:COG0520 319 DPEdrsgIVSFNVDGVHPHDVAALLDDEGIAVRAGHHCAQPLMRRLGVPGTVRASFHLYNTEEEIDRLVEALKKLAEL 396
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
22-388 |
5.76e-164 |
|
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: 464.41 E-value: 5.76e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 22 FLDSAATALKPACMIEATGHYYQNHSATVHRSQHTTAQAMTARYEQARSLVAELINAPLPEDIVWTKGTTEAINLIAQSY 101
Cdd:pfam00266 2 YLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAINLVALSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 102 FRPrLNAGDEIIVSEQEHHANLLPWLILAEQTKAKIVKWPIGKQHQPEITTLAELLNEKSRLVAISQMSNVTGATVDLAQ 181
Cdd:pfam00266 82 GRS-LKPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 182 VSALAHQYDCRVVVDGAQGIVHSPVDMQQLDIDFYAFSAHKLYGPNGVGVLYAKSELLNAMSPWHGGGKMLTQVSFEGFT 261
Cdd:pfam00266 161 IGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGMIETVSLQEST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 262 PESVPYRFEAGTPNVAGVIGFAATLEWLKTVDIQLAESHAIDLTDYTEQQLSTLPGFISYRATG-STLLAFNIAGIHHHD 340
Cdd:pfam00266 241 FADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPERrASIISFNFKGVHPHD 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 498913418 341 LATLLAEQNISLRSGQHCAQPLLDALGINGCLRVSFMPYNNYQDADKL 388
Cdd:pfam00266 321 VATLLDESGIAVRSGHHCAQPLMVRLGLGGTVRASFYIYNTQEDVDRL 368
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
21-392 |
8.41e-164 |
|
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: 464.25 E-value: 8.41e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 21 TFLDSAATALKPACMIEATGHYYQNHSATVHRSQHTTAQAMTARYEQARSLVAELINAPLPEDIVWTKGTTEAINLIAQS 100
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINAPSPDEIIFTRNTTEAINLVAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 101 YFRPRlNAGDEIIVSEQEHHANLLPWLILAEQTKAKIVKWPIGKQHQPEITTLAELLNEKSRLVAISQMSNVTGATVDLA 180
Cdd:cd06453 81 LGRAN-KPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 181 QVSALAHQYDCRVVVDGAQGIVHSPVDMQQLDIDFYAFSAHKLYGPNGVGVLYAKSELLNAMSPWHGGGKMLTQVSFEGF 260
Cdd:cd06453 160 EIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMIEEVSFEET 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 261 TPESVPYRFEAGTPNVAGVIGFAATLEWLKTVDIQLAESHAIDLTDYTEQQLSTLPGFISYR-ATGST-LLAFNIAGIHH 338
Cdd:cd06453 240 TYADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEIPGVRVYGdAEDRAgVVSFNLEGIHP 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 498913418 339 HDLATLLAEQNISLRSGQHCAQPLLDALGINGCLRVSFMPYNNYQDADKLVSAV 392
Cdd:cd06453 320 HDVATILDQYGIAVRAGHHCAQPLMRRLGVPGTVRASFGLYNTEEEIDALVEAL 373
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
3-392 |
2.44e-115 |
|
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: 349.54 E-value: 2.44e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 3 AFDSEKFRQQFPALQQSTT-----FLDSAATALKPACMIEATGHYYQNHSATVHRSQHTTAqamtAR----YEQARSLVA 73
Cdd:NF041166 224 PFDVNAVRRDFPILQERVNgkplvWFDNAATTQKPQAVIDRLSYFYEHENSNIHRAAHELA----ARatdaYEGAREKVR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 74 ELINAPLPEDIVWTKGTTEAINLIAQSYFRPRLNAGDEIIVSEQEHHANLLPWLILAEQTKAKIVKWPIGKQHQPEITTL 153
Cdd:NF041166 300 RFIGAPSVDEIIFVRGTTEAINLVAKSWGRQNIGAGDEIIVSHLEHHANIVPWQQLAQETGAKLRVIPVDDSGQILLDEY 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 154 AELLNEKSRLVAISQMSNVTGATVDLAQVSALAHQYDCRVVVDGAQGIVHSPVDMQQLDIDFYAFSAHKLYGPNGVGVLY 233
Cdd:NF041166 380 AKLLNPRTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGIGVVY 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 234 AKSELLNAMSPWHGGGKMLTQVSFEgftpESV----PYRFEAGTPNVAGVIGFAATLEWLKTVDIQLAESHAIDLTDYTE 309
Cdd:NF041166 460 GKRDLLEAMPPWQGGGNMIADVTFE----KTVyqpaPNRFEAGTGNIADAVGLGAALDYVERIGIENIARYEHDLLEYAT 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 310 QQLSTLPG--FISYRATGSTLLAFNIAGIHHHDLATLLAEQNISLRSGQHCAQPLLDALGINGCLRVSFMPYNNYQDADK 387
Cdd:NF041166 536 AGLAEVPGlrLIGTAADKASVLSFVLDGYSTEEVGKALNQEGIAVRSGHHCAQPILRRFGVEATVRPSLAFYNTCEEVDA 615
|
....*
gi 498913418 388 LVSAV 392
Cdd:NF041166 616 LVAVL 620
|
|
| |
|
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: 749.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 1 MKAFDSEKFRQQFPALQQSTTFLDSAATALKPACMIEATGHYYQNHSATVHRSQHTTAQAMTARYEQARSLVAELINAPL 80
Cdd:PRK10874 1 MNVFNPAQFRAQFPALQDAGVYLDSAATALKPQAVIEATQQFYSLSAGNVHRSQFAAAQRLTARYEAAREQVAQLLNAPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 81 PEDIVWTKGTTEAINLIAQSYFRPRLNAGDEIIVSEQEHHANLLPWLILAEQTKAKIVKWPIGKQHQPEITTLAELLNEK 160
Cdd:PRK10874 81 AKNIVWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLVPWLMVAQQTGAKVVKLPLGADRLPDVDLLPELITPR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 161 SRLVAISQMSNVTGATVDLAQVSALAHQYDCRVVVDGAQGIVHSPVDMQQLDIDFYAFSAHKLYGPNGVGVLYAKSELLN 240
Cdd:PRK10874 161 TRILALGQMSNVTGGCPDLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKSELLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 241 AMSPWHGGGKMLTQVSFEGFTPESVPYRFEAGTPNVAGVIGFAATLEWLKTVDIQLAESHAIDLTDYTEQQLSTLPGFIS 320
Cdd:PRK10874 241 AMSPWQGGGKMLTEVSFDGFTPQSAPWRFEAGTPNVAGVIGLSAALEWLADIDINQAESWSRSLATLAEDALAKLPGFRS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 321 YRATGSTLLAFNIAGIHHHDLATLLAEQNISLRSGQHCAQPLLDALGINGCLRVSFMPYNNYQDADKLVSAVKFALSLLN 400
Cdd:PRK10874 321 FRCQDSSLLAFDFAGVHHSDLVTLLAEYGIALRAGQHCAQPLLAALGVTGTLRASFAPYNTQSDVDALVNAVDRALELLV 400
|
.
gi 498913418 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: 688.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 4 FDSEKFRQQFPALQQSTTFLDSAATALKPACMIEATGHYYQNHSATVHRSQHTTAQAMTARYEQARSLVAELINAPLPED 83
Cdd:TIGR03392 1 FNPAQFRRQFPALQDATVYLDSAATALKPQAVIDATQQFYRLSSGTVHRSQHQEAQSLTARYEAAREQVAQLLNAPDAEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 84 IVWTKGTTEAINLIAQSYFRPRLNAGDEIIVSEQEHHANLLPWLILAEQTKAKIVKWPIGKQHQPEITTLAELLNEKSRL 163
Cdd:TIGR03392 81 IVWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLIPWLMVAQQTGAKVVKLPIGADLLPDIDQLPELLTPRTRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 164 VAISQMSNVTGATVDLAQVSALAHQYDCRVVVDGAQGIVHSPVDMQQLDIDFYAFSAHKLYGPNGVGVLYAKSELLNAMS 243
Cdd:TIGR03392 161 LALGQMSNVTGGCPDLARAITLAHQYGCVVVVDGAQGVVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKTELLEAMP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 244 PWHGGGKMLTQVSFEGFTPESVPYRFEAGTPNVAGVIGFAATLEWLKTVDIQLAESHAIDLTDYTEQQLSTLPGFISYRA 323
Cdd:TIGR03392 241 PWQGGGKMLSHVSFDGFTPQAVPWRFEAGTPNIAGVIGLSAALEWLADIDINAAESWSVSLATLAEEALAQLPGFRSFRC 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498913418 324 TGSTLLAFNIAGIHHHDLATLLAEQNISLRSGQHCAQPLLDALGINGCLRVSFMPYNNYQDADKLVSAVKFALSLLND 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: 538.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 5 DSEKFRQQFPALQQSTTFLDSAATALKPACMIEATGHYYQNHSATVHRSQHTTAQAMTARYEQARSLVAELINAPLPEDI 84
Cdd:COG0520 1 DVEAIRADFPVLGKPLVYLDNAATGQKPRPVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAASPDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 85 VWTKGTTEAINLIAQSYfrPRLNAGDEIIVSEQEHHANLLPWLILAEQTKAKIVKWPIGKQHQPEITTLAELLNEKSRLV 164
Cdd:COG0520 81 IFTRGTTEAINLVAYGL--GRLKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDGELDLEALEALLTPRTKLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 165 AISQMSNVTGATVDLAQVSALAHQYDCRVVVDGAQGIVHSPVDMQQLDIDFYAFSAHKLYGPNGVGVLYAKSELLNAMSP 244
Cdd:COG0520 159 AVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELLEALPP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 245 WHGGGKMLTQVSFEGFTPESVPYRFEAGTPNVAGVIGFAATLEWLKTVDIQLAESHAIDLTDYTEQQLSTLPGFISYRAT 324
Cdd:COG0520 239 FLGGGGMIEWVSFDGTTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAIPGVRILGPA 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498913418 325 GST----LLAFNIAGIHHHDLATLLAEQNISLRSGQHCAQPLLDALGINGCLRVSFMPYNNYQDADKLVSAVKFALSL 398
Cdd:COG0520 319 DPEdrsgIVSFNVDGVHPHDVAALLDDEGIAVRAGHHCAQPLMRRLGVPGTVRASFHLYNTEEEIDRLVEALKKLAEL 396
|
|
| sufS |
TIGR01979 |
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine ... |
7-393 |
1.99e-165 |
|
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: 469.44 E-value: 1.99e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 7 EKFRQQFPALQQST-----TFLDSAATALKPACMIEATGHYYQNHSATVHRSQHTTAQAMTARYEQARSLVAELINAPLP 81
Cdd:TIGR01979 1 KNIRADFPILKRKIngkplVYLDSAATSQKPQQVIDAVAEYYRNSNANVHRGIHTLSVRATEAYEAVREKVAKFINAASD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 82 EDIVWTKGTTEAINLIAQSYFRPRLNAGDEIIVSEQEHHANLLPWLILAEQTKAKIVKWPIGKQHQPEITTLAELLNEKS 161
Cdd:TIGR01979 81 EEIVFTRGTTESINLVAYSWGDSNLKAGDEIVISEMEHHANIVPWQLLAERTGATLKFIPLDDDGTLDLDDLEKLLTEKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 162 RLVAISQMSNVTGATVDLAQVSALAHQYDCRVVVDGAQGIVHSPVDMQQLDIDFYAFSAHKLYGPNGVGVLYAKSELLNA 241
Cdd:TIGR01979 161 KLVAITHVSNVLGTVNPVEEIAKLAHQVGAKVLVDGAQAVPHMPVDVQALDCDFYVFSGHKMYGPTGIGVLYGKEELLEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 242 MSPWHGGGKMLTQVSFEGFTPESVPYRFEAGTPNVAGVIGFAATLEWLKTVDIQLAESHAIDLTDYTEQQLSTLPGFISY 321
Cdd:TIGR01979 241 MPPFLGGGEMIAEVSFEETTYNEAPHKFEAGTPNIAGVIGLGAAIDYLEAIGLENIEAHEHELTAYALERLGEIPGLRIY 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498913418 322 RATGST----LLAFNIAGIHHHDLATLLAEQNISLRSGQHCAQPLLDALGINGCLRVSFMPYNNYQDADKLVSAVK 393
Cdd:TIGR01979 321 GPRDAEdrggIISFNVEGVHPHDVGTILDEEGIAVRSGHHCAQPLMRRFGVPATCRASFYIYNTEEDIDALVEALK 396
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
22-388 |
5.76e-164 |
|
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: 464.41 E-value: 5.76e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 22 FLDSAATALKPACMIEATGHYYQNHSATVHRSQHTTAQAMTARYEQARSLVAELINAPLPEDIVWTKGTTEAINLIAQSY 101
Cdd:pfam00266 2 YLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAINLVALSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 102 FRPrLNAGDEIIVSEQEHHANLLPWLILAEQTKAKIVKWPIGKQHQPEITTLAELLNEKSRLVAISQMSNVTGATVDLAQ 181
Cdd:pfam00266 82 GRS-LKPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 182 VSALAHQYDCRVVVDGAQGIVHSPVDMQQLDIDFYAFSAHKLYGPNGVGVLYAKSELLNAMSPWHGGGKMLTQVSFEGFT 261
Cdd:pfam00266 161 IGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGMIETVSLQEST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 262 PESVPYRFEAGTPNVAGVIGFAATLEWLKTVDIQLAESHAIDLTDYTEQQLSTLPGFISYRATG-STLLAFNIAGIHHHD 340
Cdd:pfam00266 241 FADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPERrASIISFNFKGVHPHD 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 498913418 341 LATLLAEQNISLRSGQHCAQPLLDALGINGCLRVSFMPYNNYQDADKL 388
Cdd:pfam00266 321 VATLLDESGIAVRSGHHCAQPLMVRLGLGGTVRASFYIYNTQEDVDRL 368
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
21-392 |
8.41e-164 |
|
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: 464.25 E-value: 8.41e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 21 TFLDSAATALKPACMIEATGHYYQNHSATVHRSQHTTAQAMTARYEQARSLVAELINAPLPEDIVWTKGTTEAINLIAQS 100
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINAPSPDEIIFTRNTTEAINLVAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 101 YFRPRlNAGDEIIVSEQEHHANLLPWLILAEQTKAKIVKWPIGKQHQPEITTLAELLNEKSRLVAISQMSNVTGATVDLA 180
Cdd:cd06453 81 LGRAN-KPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 181 QVSALAHQYDCRVVVDGAQGIVHSPVDMQQLDIDFYAFSAHKLYGPNGVGVLYAKSELLNAMSPWHGGGKMLTQVSFEGF 260
Cdd:cd06453 160 EIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMIEEVSFEET 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 261 TPESVPYRFEAGTPNVAGVIGFAATLEWLKTVDIQLAESHAIDLTDYTEQQLSTLPGFISYR-ATGST-LLAFNIAGIHH 338
Cdd:cd06453 240 TYADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEIPGVRVYGdAEDRAgVVSFNLEGIHP 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 498913418 339 HDLATLLAEQNISLRSGQHCAQPLLDALGINGCLRVSFMPYNNYQDADKLVSAV 392
Cdd:cd06453 320 HDVATILDQYGIAVRAGHHCAQPLMRRLGVPGTVRASFGLYNTEEEIDALVEAL 373
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
4-393 |
1.65e-128 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 376.01 E-value: 1.65e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 4 FDSEKFRQQFPALQQST-----TFLDSAATALKPACMIEATGHYYQNHSATVHRSQHTTAQAMTARYEQARSLVAELINA 78
Cdd:PRK09295 3 FSVEKVRADFPVLSREVnglplAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKQAALFINA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 79 PLPEDIVWTKGTTEAINLIAQSYFRPRLNAGDEIIVSEQEHHANLLPWLILAEQTKAKIVKWPIGKQHQPEITTLAELLN 158
Cdd:PRK09295 83 RSAEELVFVRGTTEGINLVANSWGNSNVRAGDNIIISEMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPALFD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 159 EKSRLVAISQMSNVTGATVDLAQVSALAHQYDCRVVVDGAQGIVHSPVDMQQLDIDFYAFSAHKLYGPNGVGVLYAKSEL 238
Cdd:PRK09295 163 ERTRLLAITHVSNVLGTENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKEAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 239 LNAMSPWHGGGKMLTQVSF-EGFTPESVPYRFEAGTPNVAGVIGFAATLEWLKTVDIQLAESHAIDLTDYTEQQLSTLPG 317
Cdd:PRK09295 243 LQEMPPWEGGGSMIATVSLtEGTTWAKAPWRFEAGTPNTGGIIGLGAALDYVSALGLNNIAEYEQNLMHYALSQLESVPD 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498913418 318 FISYRATGST-LLAFNIAGIHHHDLATLLAEQNISLRSGQHCAQPLLDALGINGCLRVSFMPYNNYQDADKLVSAVK 393
Cdd:PRK09295 323 LTLYGPQNRLgVIAFNLGKHHAYDVGSFLDNYGIAVRTGHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVAGLQ 399
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
10-401 |
4.32e-124 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 365.22 E-value: 4.32e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 10 RQQFPALQQSTT-----FLDSAATALKPACMIEATGHYYQNHSATVHRSQHTTAQAMTARYEQARSLVAELINAPLPEDI 84
Cdd:PLN02855 18 RPDFPILDQTVNgsklvYLDNAATSQKPAAVLDALQDYYEEYNSNVHRGIHALSAKATDAYELARKKVAAFINASTSREI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 85 VWTKGTTEAINLIAQSYFRPRLNAGDEIIVSEQEHHANLLPWLILAEQTKAKIVKWPIGKQHQPEITTLAELLNEKSRLV 164
Cdd:PLN02855 98 VFTRNATEAINLVAYTWGLANLKPGDEVILSVAEHHSNIVPWQLVAQKTGAVLKFVGLTPDEVLDVEQLKELLSEKTKLV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 165 AISQMSNVTGATVDLAQVSALAHQYDCRVVVDGAQGIVHSPVDMQQLDIDFYAFSAHKLYGPNGVGVLYAKSELLNAMSP 244
Cdd:PLN02855 178 ATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLWGKSDLLESMPP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 245 WHGGGKMLTQVSFEGFTPESVPYRFEAGTPNVAGVIGFAATLEWLKTVDIQLAESHAIDLTDYTEQQLSTLPGFISYRAT 324
Cdd:PLN02855 258 FLGGGEMISDVFLDHSTYAPPPSRFEAGTPAIGEAIGLGAAIDYLSEIGMDRIHEYEVELGTYLYEKLSSVPGVRIYGPK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 325 GS------TLLAFNIAGIHHHDLATLLAEQN-ISLRSGQHCAQPLLDALGINGCLRVSFMPYNNYQDADKLVSAVKFALS 397
Cdd:PLN02855 338 PSegvgraALCAFNVEGIHPTDLSTFLDQQHgVAIRSGHHCAQPLHRYLGVNASARASLYFYNTKEEVDAFIHALKDTIA 417
|
....
gi 498913418 398 LLND 401
Cdd:PLN02855 418 FFSS 421
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
3-392 |
2.44e-115 |
|
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: 349.54 E-value: 2.44e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 3 AFDSEKFRQQFPALQQSTT-----FLDSAATALKPACMIEATGHYYQNHSATVHRSQHTTAqamtAR----YEQARSLVA 73
Cdd:NF041166 224 PFDVNAVRRDFPILQERVNgkplvWFDNAATTQKPQAVIDRLSYFYEHENSNIHRAAHELA----ARatdaYEGAREKVR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 74 ELINAPLPEDIVWTKGTTEAINLIAQSYFRPRLNAGDEIIVSEQEHHANLLPWLILAEQTKAKIVKWPIGKQHQPEITTL 153
Cdd:NF041166 300 RFIGAPSVDEIIFVRGTTEAINLVAKSWGRQNIGAGDEIIVSHLEHHANIVPWQQLAQETGAKLRVIPVDDSGQILLDEY 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 154 AELLNEKSRLVAISQMSNVTGATVDLAQVSALAHQYDCRVVVDGAQGIVHSPVDMQQLDIDFYAFSAHKLYGPNGVGVLY 233
Cdd:NF041166 380 AKLLNPRTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGIGVVY 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 234 AKSELLNAMSPWHGGGKMLTQVSFEgftpESV----PYRFEAGTPNVAGVIGFAATLEWLKTVDIQLAESHAIDLTDYTE 309
Cdd:NF041166 460 GKRDLLEAMPPWQGGGNMIADVTFE----KTVyqpaPNRFEAGTGNIADAVGLGAALDYVERIGIENIARYEHDLLEYAT 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 310 QQLSTLPG--FISYRATGSTLLAFNIAGIHHHDLATLLAEQNISLRSGQHCAQPLLDALGINGCLRVSFMPYNNYQDADK 387
Cdd:NF041166 536 AGLAEVPGlrLIGTAADKASVLSFVLDGYSTEEVGKALNQEGIAVRSGHHCAQPILRRFGVEATVRPSLAFYNTCEEVDA 615
|
....*
gi 498913418 388 LVSAV 392
Cdd:NF041166 616 LVAVL 620
|
|
| am_tr_V_VC1184 |
TIGR01976 |
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of ... |
4-392 |
3.94e-66 |
|
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: 215.77 E-value: 3.94e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 4 FDSEKFRQQFPALQQ-STTFLDSAATALKPACMIEATGHYYQNHSATVHRSQHTTAQAmTARYEQARSLVAELINAPLPE 82
Cdd:TIGR01976 1 FDVEAVRGQFPALADgDRVFFDNPAGTQIPQSVADAVSAALTRSNANRGGAYESSRRA-DQVVDDAREAVADLLNADPPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 83 dIVWTKGTTEAINLIAQSYFRpRLNAGDEIIVSEQEHHANLLPWLILAEQTKAKiVKW-----PIGKQHQPEittLAELL 157
Cdd:TIGR01976 80 -VVFGANATSLTFLLSRAISR-RWGPGDEVIVTRLDHEANISPWLQAAERAGAK-VKWarvdeATGELHPDD---LASLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 158 NEKSRLVAISQMSNVTGATVDLAQVSALAHQYDCRVVVDGAQGIVHSPVDMQQLDIDFYAFSAHKLYGPNgVGVLYAKSE 237
Cdd:TIGR01976 154 SPRTRLVAVTAASNTLGSIVDLAAITELVHAAGALVVVDAVHYAPHGLIDVQATGADFLTCSAYKFFGPH-MGILWGRPE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 238 LLNAMSPwhgggkmltqvSFEGFTPESVPYRFEAGTPNVAGVIGFAATLEWLKTVD--------------IQLAESHAID 303
Cdd:TIGR01976 233 LLMNLPP-----------YKLTFSYDTGPERFELGTPQYELLAGVVAAVDYLAGLGesangsrrerlvasFQAIDAYENR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 304 LTDYTEQQLSTLPGFISY---RATGST-LLAFNIAGIHHHDLATLLAEQNISLRSGQHCAQPLLDALGIN---GCLRVSF 376
Cdd:TIGR01976 302 LAEYLLVGLSDLPGVTLYgvaRLAARVpTVSFTVHGLPPQRVVRRLADQGIDAWAGHFYAVRLLRRLGLNdegGVVRVGL 381
|
410
....*....|....*.
gi 498913418 377 MPYNNYQDADKLVSAV 392
Cdd:TIGR01976 382 AHYNTAEEVDRLLEAL 397
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
23-393 |
2.73e-55 |
|
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: 186.79 E-value: 2.73e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 23 LDSAATA-LKP---ACMIEATGHYYQNHSatvhrSQHTTAQAMTARYEQARSLVAELINAPlPEDIVWTKGTTEAINLIA 98
Cdd:COG1104 6 LDNAATTpVDPevlEAMLPYLTEYFGNPS-----SLHSFGREARAALEEAREQVAALLGAD-PEEIIFTSGGTEANNLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 99 QSYFRPRLNAGDEIIVSEQEHHA--NLLPWLilaEQTKAKIVKWPIGKQHQPEITTLAELLNEKSRLVAISQMSNVTGAT 176
Cdd:COG1104 80 KGAARAYRKKGKHIITSAIEHPAvlETARFL---EKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 177 VDLAQVSALAHQYDCRVVVDGAQGIVHSPVDMQQLDIDFYAFSAHKLYGPNGVGVLYAKSELlnAMSP-WHGGGkmltQv 255
Cdd:COG1104 157 QPIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRKGV--RLEPlIHGGG----Q- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 256 sfEgftpesvpYRFEAGTPNVAGVIGFAATLEWLKTvDIQLAESHAIDLTDYTEQQL-STLPGFI-----SYRAtgSTLL 329
Cdd:COG1104 230 --E--------RGLRSGTENVPGIVGLGKAAELAAE-ELEEEAARLRALRDRLEEGLlAAIPGVVingdpENRL--PNTL 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498913418 330 AFNIAGIHHHDLATLLAEQNISLRSGQHCAQ------PLLDALGIN-----GCLRVSFMPYNNYQDADKLVSAVK 393
Cdd:COG1104 297 NFSFPGVEGEALLLALDLAGIAVSSGSACSSgslepsHVLLAMGLDeelahGSIRFSLGRFTTEEEIDRAIEALK 371
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
66-249 |
4.72e-23 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 99.63 E-value: 4.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 66 EQARSLVAELINAPlPEDIVWTKGTTEAINL----IAQSYfrprLNAGDEIIVSEQEHHANLLPWLILaEQTKAKIVKWP 141
Cdd:PRK14012 52 DIARNQIADLIGAD-PREIVFTSGATESDNLaikgAAHFY----QKKGKHIITSKTEHKAVLDTCRQL-EREGFEVTYLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 142 IGKQHQPEITTLAELLNEKSRLVAISQMSNVTGATVDLAQVSALAHQYDCRVVVDGAQGIVHSPVDMQQLDIDFYAFSAH 221
Cdd:PRK14012 126 PQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVIQDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAH 205
|
170 180 190
....*....|....*....|....*....|..
gi 498913418 222 KLYGPNGVGVLYAKSE----LLNAMspwHGGG 249
Cdd:PRK14012 206 KIYGPKGIGALYVRRKprvrLEAQM---HGGG 234
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
22-339 |
3.68e-21 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 94.03 E-value: 3.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 22 FLDSAATAlkPAC------MIEATGHYYQNHSatvhrSQHTTAQAMTARYEQARSLVAELINAPlPEDIVWTKGTTEAIN 95
Cdd:PRK02948 3 YLDYAATT--PMSkealqtYQKAASQYFGNES-----SLHDIGGTASSLLQVCRKTFAEMIGGE-EQGIYFTSGGTESNY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 96 LIAQSYFRPRLNAGDEIIVSEQEHHA--NLLPWLilaEQTKAKIVKWPIGKQHQPEITTLAELLNEKSRLVAISQMSNVT 173
Cdd:PRK02948 75 LAIQSLLNALPQNKKHIITTPMEHASihSYFQSL---ESQGYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 174 GATVDLAQVSALAHQYDCRVVVDGAQGIVHSPVDMQQLDIDFYAFSAHKLYGPNGVGVLYakselLNAMSPWHgggkmlt 253
Cdd:PRK02948 152 GTIQPIAEIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVY-----INPQVRWK------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 254 qVSFEGFTPEsvpYRFEAGTPNVAGVIGF-AATLEWLKTVDIQlaESHAIDLTDYTEQQLSTLPGFISYRATGSTLLAfN 332
Cdd:PRK02948 220 -PVFPGTTHE---KGFRPGTVNVPGIAAFlTAAENILKNMQEE--SLRFKELRSYFLEQIQTLPLPIEVEGHSTSCLP-H 292
|
....*..
gi 498913418 333 IAGIHHH 339
Cdd:PRK02948 293 IIGVTIK 299
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
22-306 |
5.13e-19 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 87.79 E-value: 5.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 22 FLD-SAATALKPAcMIEATGHYYQNHSATVHRSQHTTAQAMTARYEQARSLVAELINAPLPEdIVWTKGTTEAINLIAQS 100
Cdd:PLN02651 2 YLDmQATTPIDPR-VLDAMLPFLIEHFGNPHSRTHLYGWESEDAVEKARAQVAALIGADPKE-IIFTSGATESNNLAIKG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 101 YFRPRLNAGDEIIVSEQEHHANL--LPWLilaEQTKAKIVKWPIGKQHQPEITTLAELLNEKSRLVAISQMSNVTGATVD 178
Cdd:PLN02651 80 VMHFYKDKKKHVITTQTEHKCVLdsCRHL---QQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 179 LAQVSALAHQYDCRVVVDGAQGIVHSPVDMQQLDIDFYAFSAHKLYGPNGVGVLYAKSELLNAMSP-WHGGGKmltqvsf 257
Cdd:PLN02651 157 VEEIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRLEPlMSGGGQ------- 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 498913418 258 EGftpesvpyRFEAGTPNVAGVIGFAATLEwLKTVDIQLAESHAIDLTD 306
Cdd:PLN02651 230 ER--------GRRSGTENTPLVVGLGAACE-LAMKEMDYDEKHMKALRE 269
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
65-235 |
6.13e-14 |
|
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).
Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 69.33 E-value: 6.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 65 YEQARSLVAELINaPLPEDIVWTKGTTEAINLIAQSYFRPrlnaGDEIIVSEQEHHANLLpwlILAEQTKAKIVKWPIGK 144
Cdd:cd01494 2 LEELEEKLARLLQ-PGNDKAVFVPSGTGANEAALLALLGP----GDEVIVDANGHGSRYW---VAAELAGAKPVPVPVDD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 145 QHQPEIT--TLAELLN-EKSRLVAISQMSNVTGATVDLAQVSALAHQYDCRVVVDGAQGIVHSPVDMQQLD---IDFYAF 218
Cdd:cd01494 74 AGYGGLDvaILEELKAkPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPeggADVVTF 153
|
170
....*....|....*..
gi 498913418 219 SAHKLYGPNGVGVLYAK 235
Cdd:cd01494 154 SLHKNLGGEGGGVVIVK 170
|
|
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
12-392 |
3.18e-10 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 62.19 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 12 QFPALQQsTTFLDSAATALKPACMIEATGHYYQNHSATVHRSQHTTAQAMTARYEQARSLVAELINAPlPED--IVWTKG 89
Cdd:PLN02724 28 EFARLKG-VVYLDHAGATLYSESQLEAALADFSSNVYGNPHSQSDSSMRSSDTIESARQQVLEYFNAP-PSDyaCVFTSG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 90 TTEAINLIAQSYfrPrLNAGDEIIVSEQEHHANL-------------LPWLILAEQTKAKIVKWPIGKQHQP-EITTLAE 155
Cdd:PLN02724 106 ATAALKLVGETF--P-WSSESHFCYTLENHNSVLgireyalekgaaaIAVDIEEAANQPTNSQGSVVVKSRGlQRRNTSK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 156 LLNEKSR-----LVAISQMSNVTGATVDL--------AQVSALAHQYDCRVVVDGAQGIVHSPVDMQQLDIDFYAFSAHK 222
Cdd:PLN02724 183 LQKREDDgeaynLFAFPSECNFSGAKFPLdlvklikdNQHSNFSKSGRWMVLLDAAKGCGTSPPDLSRYPADFVVVSFYK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 223 LYG-PNGVGVLYAKSEllnamspwhgGGKMLTQVSFEGFT-------------PESVPYRFEAGTPNVAGVIGFAATLEW 288
Cdd:PLN02724 263 IFGyPTGLGALLVRRD----------AAKLLKKKYFGGGTvaasiadidfvkrRERVEQRFEDGTISFLSIAALRHGFKL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 289 LKTVDIQLAESHAIDLTDYTEQQLSTLP--------------GF-ISYRATGSTlLAFNI-----AGIHHHDLATLLAEQ 348
Cdd:PLN02724 333 LNRLTISAIAMHTWALTHYVANSLRNLKhgngapvcvlygnhTFkLEFHIQGPI-VTFNLkradgSWVGHREVEKLASLS 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498913418 349 NISLRSG-----QHCAQPL----LDALG--------------IN----GCLRVSFMPYNNYQDADKLVSAV 392
Cdd:PLN02724 412 GIQLRTGcfcnpGACAKYLglshKDLQAnfeaghvcwddqdvIHgrptGAVRVSFGYMSTFEDCQKFIDFI 482
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
62-239 |
4.77e-09 |
|
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: 57.35 E-value: 4.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 62 TARYEQARSLVAELINAPL-----PEDIVWTKGTTEAINLIAQSYfrprLNAGDEIIVSEqehhanllP----WLILAEQ 132
Cdd:cd00609 35 DPGLPELREAIAEWLGRRGgvdvpPEEIVVTNGAQEALSLLLRAL----LNPGDEVLVPD--------PtypgYEAAARL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 133 TKAKIVKWPIGKQ--HQPEITTLAELLNEKSRLVAISQMSNVTGATVD---LAQVSALAHQYDCRVVVDGA-QGIVHSPV 206
Cdd:cd00609 103 AGAEVVPVPLDEEggFLLDLELLEAAKTPKTKLLYLNNPNNPTGAVLSeeeLEELAELAKKHGILIISDEAyAELVYDGE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 498913418 207 DMQQLDID------FYAFSAHKLYGPNG--VGVLYAKSELL 239
Cdd:cd00609 183 PPPALALLdayervIVLRSFSKTFGLPGlrIGYLIAPPEEL 223
|
|
| AspB |
COG0436 |
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ... |
81-196 |
3.28e-07 |
|
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: 52.05 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 81 PEDIVWTKGTTEAINLIAQSYfrprLNAGDEIIVSEqehhanllP-WLILAEQTK---AKIVKWPIGKQH--QPEITTLA 154
Cdd:COG0436 90 PDEILVTNGAKEALALALLAL----LNPGDEVLVPD--------PgYPSYRAAVRlagGKPVPVPLDEENgfLPDPEALE 157
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 498913418 155 ELLNEKSRLVAISQMSNVTGATV---DLAQVSALAHQYDCRVVVD 196
Cdd:COG0436 158 AAITPRTKAIVLNSPNNPTGAVYsreELEALAELAREHDLLVISD 202
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
134-242 |
2.17e-06 |
|
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.
Pssm-ID: 99744 [Multi-domain] Cd Length: 356 Bit Score: 49.21 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 134 KAKIVKWPIGKQHQPEitTLAELLNEKS-RLVAISQMSNVTGATVDLAQVSALAHQYDCRVVVDGAQGIVHSPVDMQQLD 212
Cdd:cd06451 99 DVDVVEKPWGEAVSPE--EIAEALEQHDiKAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVDAVSSLGGEPFRMDEWG 176
|
90 100 110
....*....|....*....|....*....|..
gi 498913418 213 IDfYAFSAHK--LYGPNGVGVLYAKSELLNAM 242
Cdd:cd06451 177 VD-VAYTGSQkaLGAPPGLGPIAFSERALERI 207
|
|
| PRK07568 |
PRK07568 |
pyridoxal phosphate-dependent aminotransferase; |
81-196 |
1.28e-05 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 181036 Cd Length: 397 Bit Score: 46.77 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 81 PEDIVWTKGTTEAINLIAQSYFrprlNAGDEIIVSEqEHHANLLPWLILAEqtkAKIVkwPIGKQ-----HQPEITTLAE 155
Cdd:PRK07568 88 PDEILITNGGSEAILFAMMAIC----DPGDEILVPE-PFYANYNGFATSAG---VKIV--PVTTKieegfHLPSKEEIEK 157
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 498913418 156 LLNEKSRLVAISQMSNVTGaTV----DLAQVSALAHQYDCRVVVD 196
Cdd:PRK07568 158 LITPKTKAILISNPGNPTG-VVytkeELEMLAEIAKKHDLFLISD 201
|
|
| SepCysS |
cd06452 |
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ... |
87-237 |
1.61e-05 |
|
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Cys-tRNA(Cys) is produced by O-phosphoseryl-tRNA synthetase which ligates O-phosphoserine (Sep) to tRNA(Cys), and Sep-tRNA:Cys-tRNA synthase (SepCysS) converts Sep-tRNA(Cys) to Cys-tRNA(Cys), in methanogenic archaea. SepCysS forms a dimer, each monomer is composed of a large and small domain; the larger, a typical pyridoxal 5'-phosphate (PLP)-dependent-like enzyme fold. In the active site of each monomer, PLP is covalently bound to a conserved Lys residue near the dimer interface.
Pssm-ID: 99745 Cd Length: 361 Bit Score: 46.62 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 87 TKGTTEAINLIAQSYFRPrlnaGDEIIVSEQEHHANLLPwlilAEQTKAKIVKWPIGKQHQPEIT------TLAELLNEK 160
Cdd:cd06452 65 TPGAREGKFAVMHSLCEK----GDWVVVDGLAHYTSYVA----AERAGLNVREVPNTGHPEYHITpegyaeVIEEVKDEF 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 161 SRLVAISQMSNVT---GATVDLAQVSALAHQYDCRVVVDGAQGIVHSPVDMQQLDIDFYAFSAHK-LYGPNGVGVLYAKS 236
Cdd:cd06452 137 GKPPALALLTHVDgnyGNLHDAKKIAKVCHEYGVPLLLNGAYTVGRMPVSGKELGADFIVGSGHKsMAASAPIGVLATTE 216
|
.
gi 498913418 237 E 237
Cdd:cd06452 217 E 217
|
|
| PRK08363 |
PRK08363 |
alanine aminotransferase; Validated |
81-196 |
3.46e-05 |
|
alanine aminotransferase; Validated
Pssm-ID: 181402 Cd Length: 398 Bit Score: 45.57 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 81 PEDIVWTKGTTEAINLIaqsyFRPRLNAGDEIIVSEQEHHanllPWLILAEQTKAKIVKWPIGKQH--QPEITTLAELLN 158
Cdd:PRK08363 93 PDDVRVTAAVTEALQLI----FGALLDPGDEILIPGPSYP----PYTGLVKFYGGVPVEYRTIEEEgwQPDIDDIRKKIT 164
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 498913418 159 EKSRLVAISQMSNVTGATVD---LAQVSALAHQYDCRVVVD 196
Cdd:PRK08363 165 EKTKAIAVINPNNPTGALYEkktLKEILDIAGEHDLPVISD 205
|
|
| PRK09331 |
PRK09331 |
Sep-tRNA:Cys-tRNA synthetase; Provisional |
107-237 |
3.93e-05 |
|
Sep-tRNA:Cys-tRNA synthetase; Provisional
Pssm-ID: 236469 Cd Length: 387 Bit Score: 45.31 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 107 NAGDEIIVSEQEHHANLLPwlilAEQTKAKIVKWPIGKQHQPEIT------TLAELLNEKSRLVAISQMSNVT---GATV 177
Cdd:PRK09331 100 KKGDYVVLDGLAHYTSYVA----AERAGLNVREVPKTGYPEYKITpeayaeKIEEVKEETGKPPALALLTHVDgnyGNLA 175
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498913418 178 DLAQVSALAHQYDCRVVVDGAQGIVHSPVDMQQLDIDFYAFSAHK-LYGPNGVGVLYAKSE 237
Cdd:PRK09331 176 DAKKVAKVAHEYGIPFLLNGAYTVGRMPVDGKKLGADFIVGSGHKsMAASAPSGVLATTEE 236
|
|
| PRK07324 |
PRK07324 |
transaminase; Validated |
69-196 |
3.19e-04 |
|
transaminase; Validated
Pssm-ID: 235989 Cd Length: 373 Bit Score: 42.62 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 69 RSLVAELINAPLPEDIVWTKGTTEAINLIAQSYFRPrlnaGDEIIV---SEQEHHAnlLPwlilaEQTKAKIVKWPIGKQ 145
Cdd:PRK07324 68 KEAVASLYQNVKPENILQTNGATGANFLVLYALVEP----GDHVISvypTYQQLYD--IP-----ESLGAEVDYWQLKEE 136
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 498913418 146 HQ--PEITTLAELLNEKSRLVAISQMSNVTGATVD---LAQVSALAHQYDCRVVVD 196
Cdd:PRK07324 137 NGwlPDLDELRRLVRPNTKLICINNANNPTGALMDrayLEEIVEIARSVDAYVLSD 192
|
|
| PLN02409 |
PLN02409 |
serine--glyoxylate aminotransaminase |
59-276 |
4.75e-04 |
|
serine--glyoxylate aminotransaminase
Pssm-ID: 178031 [Multi-domain] Cd Length: 401 Bit Score: 42.05 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 59 QAMTARYEQARSLVAELINAPLPEDIVWTKGTTEAINLIA--------QSYFRPRLNAGDEIIVSEQEHHANLlpWLILA 130
Cdd:PLN02409 26 RAMNRPNEDHRSPAFPALTKELLEDVKYIFKTKSGTPFIFpttgtgawESALTNTLSPGDKVVSFRIGQFSLL--WIDQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 131 EQTKAKI--VKWPIGKQHQPEI--TTLAELLNEKSRLVAISQMSNVTGATVDLAQVSAL--AHQYDCRVVVDGAQGIVHS 204
Cdd:PLN02409 104 QRLNFDVdvVESPWGQGADLDIlkSKLRQDTNHKIKAVCVVHNETSTGVTNDLAGVRKLldCAQHPALLLVDGVSSIGAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 205 PVDMQQLDIDF-YAFSAHKLYGPNGVGVLYAKSELLNAM----SP-----WHGGGKMLTQVSFEGFTP---------ESV 265
Cdd:PLN02409 184 DFRMDEWGVDVaLTGSQKALSLPTGLGIVCASPKALEASktakSPrvffdWADYLKFYKLGTYWPYTPsiqllyglrAAL 263
|
250
....*....|.
gi 498913418 266 PYRFEAGTPNV 276
Cdd:PLN02409 264 DLIFEEGLENV 274
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
148-204 |
3.28e-03 |
|
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.
Pssm-ID: 99738 [Multi-domain] Cd Length: 369 Bit Score: 39.49 E-value: 3.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498913418 148 PEITTLAELLNEKSRLVAISQMSNVTGATVDLAQVSALAHQYDCRVVVD--------------GAQGIVHS 204
Cdd:cd00614 113 DDPEALEAAIKPETKLVYVESPTNPTLKVVDIEAIAELAHEHGALLVVDntfatpylqrplelGADIVVHS 183
|
|
| PRK07503 |
PRK07503 |
methionine gamma-lyase; Provisional |
106-204 |
6.95e-03 |
|
methionine gamma-lyase; Provisional
Pssm-ID: 181005 [Multi-domain] Cd Length: 403 Bit Score: 38.24 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498913418 106 LNAGDEIIVSEQ--------EHHAnllpwlilaeqtkakIVKWPIgKQHQPEITTLAEL---LNEKSRLVAISQMSNVTG 174
Cdd:PRK07503 101 LRPGDEVIVDQTlygctfafLHHG---------------LGEFGV-TVRHVDLTDPAALkaaISDKTRMVYFETPANPNM 164
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 498913418 175 ATVDLAQVSALAHQYDCRVVVD--------------GAQGIVHS 204
Cdd:PRK07503 165 RLVDIAAVAEIAHGAGAKVVVDntyctpylqrplelGADLVVHS 208
|
|
| |
