|
Name |
Accession |
Description |
Interval |
E-value |
| sufS |
TIGR01979 |
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine ... |
7-406 |
0e+00 |
|
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: 602.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 7 ARLRGQFPALAQEVNGHPLVYLDNAATTQKPQAVLDAINHYYRADNANVHRAAHALSGRATRAFEDARETVARFINASRS 86
Cdd:TIGR01979 1 KNIRADFPILKRKINGKPLVYLDSAATSQKPQQVIDAVAEYYRNSNANVHRGIHTLSVRATEAYEAVREKVAKFINAASD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 87 HEVIWTRGTTEAINLVAQSWGMSELRAGDEIVLSTLEHHANIVPWQLVAQRTGAVIRVIPLDERGDLDLAAYHAMLGPRT 166
Cdd:TIGR01979 81 EEIVFTRGTTESINLVAYSWGDSNLKAGDEIVISEMEHHANIVPWQLLAERTGATLKFIPLDDDGTLDLDDLEKLLTEKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 167 RLVSVAHVSNALGTVTPVKEMVAAAKAVGSLSLIDGAQAVAHLEVDVQAIGCDFYAFSGHKLYGPTGIGVLWGRTELLER 246
Cdd:TIGR01979 161 KLVAITHVSNVLGTVNPVEEIAKLAHQVGAKVLVDGAQAVPHMPVDVQALDCDFYVFSGHKMYGPTGIGVLYGKEELLEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 247 MPPWQAGGEMIDRVSFAGTTFNTLPFKFEAGTPHIAGAIGLAAAIDFVMKQDRDSLASHEAALTDYLVAGLQQVPGLRLV 326
Cdd:TIGR01979 241 MPPFLGGGEMIAEVSFEETTYNEAPHKFEAGTPNIAGVIGLGAAIDYLEAIGLENIEAHEHELTAYALERLGEIPGLRIY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 327 G--EPGQRAGAVSFLLEDIHPQDAATLLDMQGIALRVGHHCAMPLMESLGVGGTMRASLACYNNRDDVDALLAALHKLRD 404
Cdd:TIGR01979 321 GprDAEDRGGIISFNVEGVHPHDVGTILDEEGIAVRSGHHCAQPLMRRFGVPATCRASFYIYNTEEDIDALVEALKKVRK 400
|
..
gi 2067391329 405 FF 406
Cdd:TIGR01979 401 FF 402
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
7-405 |
0e+00 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 602.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 7 ARLRGQFPalaqeVNGHPLVYLDNAATTQKPQAVLDAINHYYRADNANVHRAAHALSGRATRAFEDARETVARFINASRS 86
Cdd:COG0520 3 EAIRADFP-----VLGKPLVYLDNAATGQKPRPVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAASP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 87 HEVIWTRGTTEAINLVAQSWGMseLRAGDEIVLSTLEHHANIVPWQLVAQRTGAVIRVIPLDERGDLDLAAYHAMLGPRT 166
Cdd:COG0520 78 DEIIFTRGTTEAINLVAYGLGR--LKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDGELDLEALEALLTPRT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 167 RLVSVAHVSNALGTVTPVKEMVAAAKAVGSLSLIDGAQAVAHLEVDVQAIGCDFYAFSGHKLYGPTGIGVLWGRTELLER 246
Cdd:COG0520 156 KLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELLEA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 247 MPPWQAGGEMIDRVSFAGTTFNTLPFKFEAGTPHIAGAIGLAAAIDFVMKQDRDSLASHEAALTDYLVAGLQQVPGLRLV 326
Cdd:COG0520 236 LPPFLGGGGMIEWVSFDGTTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAIPGVRIL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 327 G--EPGQRAGAVSFLLEDIHPQDAATLLDMQGIALRVGHHCAMPLMESLGVGGTMRASLACYNNRDDVDALLAALHKLRD 404
Cdd:COG0520 316 GpaDPEDRSGIVSFNVDGVHPHDVAALLDDEGIAVRAGHHCAQPLMRRLGVPGTVRASFHLYNTEEEIDRLVEALKKLAE 395
|
.
gi 2067391329 405 F 405
Cdd:COG0520 396 L 396
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
26-399 |
0e+00 |
|
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: 599.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 26 VYLDNAATTQKPQAVLDAINHYYRADNANVHRAAHALSGRATRAFEDARETVARFINASRSHEVIWTRGTTEAINLVAQS 105
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINAPSPDEIIFTRNTTEAINLVAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 106 WGMSeLRAGDEIVLSTLEHHANIVPWQLVAQRTGAVIRVIPLDERGDLDLAAYHAMLGPRTRLVSVAHVSNALGTVTPVK 185
Cdd:cd06453 81 LGRA-NKPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 186 EMVAAAKAVGSLSLIDGAQAVAHLEVDVQAIGCDFYAFSGHKLYGPTGIGVLWGRTELLERMPPWQAGGEMIDRVSFAGT 265
Cdd:cd06453 160 EIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMIEEVSFEET 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 266 TFNTLPFKFEAGTPHIAGAIGLAAAIDFVMKQDRDSLASHEAALTDYLVAGLQQVPGLRLVGEPGQRAGAVSFLLEDIHP 345
Cdd:cd06453 240 TYADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEIPGVRVYGDAEDRAGVVSFNLEGIHP 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2067391329 346 QDAATLLDMQGIALRVGHHCAMPLMESLGVGGTMRASLACYNNRDDVDALLAAL 399
Cdd:cd06453 320 HDVATILDQYGIAVRAGHHCAQPLMRRLGVPGTVRASFGLYNTEEEIDALVEAL 373
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
13-402 |
0e+00 |
|
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: 567.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 13 FPALAQEVNGHPLVYLDNAATTQKPQAVLDAINHYYRADNANVHRAAHALSGRATRAFEDARETVARFINASRSHEVIWT 92
Cdd:NF041166 234 FPILQERVNGKPLVWFDNAATTQKPQAVIDRLSYFYEHENSNIHRAAHELAARATDAYEGAREKVRRFIGAPSVDEIIFV 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 93 RGTTEAINLVAQSWGMSELRAGDEIVLSTLEHHANIVPWQLVAQRTGAVIRVIPLDERGDLDLAAYHAMLGPRTRLVSVA 172
Cdd:NF041166 314 RGTTEAINLVAKSWGRQNIGAGDEIIVSHLEHHANIVPWQQLAQETGAKLRVIPVDDSGQILLDEYAKLLNPRTKLVSVT 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 173 HVSNALGTVTPVKEMVAAAKAVGSLSLIDGAQAVAHLEVDVQAIGCDFYAFSGHKLYGPTGIGVLWGRTELLERMPPWQA 252
Cdd:NF041166 394 QVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGIGVVYGKRDLLEAMPPWQG 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 253 GGEMIDRVSFAGTTFNTLPFKFEAGTPHIAGAIGLAAAIDFVMKQDRDSLASHEAALTDYLVAGLQQVPGLRLVGEPGQR 332
Cdd:NF041166 474 GGNMIADVTFEKTVYQPAPNRFEAGTGNIADAVGLGAALDYVERIGIENIARYEHDLLEYATAGLAEVPGLRLIGTAADK 553
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 333 AGAVSFLLEDIHPQDAATLLDMQGIALRVGHHCAMPLMESLGVGGTMRASLACYNNRDDVDALLAALHKL 402
Cdd:NF041166 554 ASVLSFVLDGYSTEEVGKALNQEGIAVRSGHHCAQPILRRFGVEATVRPSLAFYNTCEEVDALVAVLRRL 623
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
26-395 |
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: 508.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 26 VYLDNAATTQKPQAVLDAINHYYRADNANVHRAAHALSGRATRAFEDARETVARFINASRSHEVIWTRGTTEAINLVAQS 105
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 106 WGMSeLRAGDEIVLSTLEHHANIVPWQLVAQRTGAVIRVIPLDERGDLDLAAYHAMLGPRTRLVSVAHVSNALGTVTPVK 185
Cdd:pfam00266 81 LGRS-LKPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 186 EMVAAAKAVGSLSLIDGAQAVAHLEVDVQAIGCDFYAFSGHKLYGPTGIGVLWGRTELLERMPPWQAGGEMIDRVSFAGT 265
Cdd:pfam00266 160 EIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGMIETVSLQES 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 266 TFNTLPFKFEAGTPHIAGAIGLAAAIDFVMKQDRDSLASHEAALTDYLVAGLQQVPGLRLVGePGQRAGAVSFLLEDIHP 345
Cdd:pfam00266 240 TFADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYG-PERRASIISFNFKGVHP 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2067391329 346 QDAATLLDMQGIALRVGHHCAMPLMESLGVGGTMRASLACYNNRDDVDAL 395
Cdd:pfam00266 319 HDVATLLDESGIAVRSGHHCAQPLMVRLGLGGTVRASFYIYNTQEDVDRL 368
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
7-406 |
1.26e-179 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 506.59 E-value: 1.26e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 7 ARLRGQFPALAQEVNGHPLVYLDNAATTQKPQAVLDAINHYYRADNANVHRAAHALSGRATRAFEDARETVARFINASRS 86
Cdd:PLN02855 15 AETRPDFPILDQTVNGSKLVYLDNAATSQKPAAVLDALQDYYEEYNSNVHRGIHALSAKATDAYELARKKVAAFINASTS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 87 HEVIWTRGTTEAINLVAQSWGMSELRAGDEIVLSTLEHHANIVPWQLVAQRTGAVIRVIPLDERGDLDLAAYHAMLGPRT 166
Cdd:PLN02855 95 REIVFTRNATEAINLVAYTWGLANLKPGDEVILSVAEHHSNIVPWQLVAQKTGAVLKFVGLTPDEVLDVEQLKELLSEKT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 167 RLVSVAHVSNALGTVTPVKEMVAAAKAVGSLSLIDGAQAVAHLEVDVQAIGCDFYAFSGHKLYGPTGIGVLWGRTELLER 246
Cdd:PLN02855 175 KLVATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLWGKSDLLES 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 247 MPPWQAGGEMIDRVSFAGTTFNTLPFKFEAGTPHIAGAIGLAAAIDFVMKQDRDSLASHEAALTDYLVAGLQQVPGLRLV 326
Cdd:PLN02855 255 MPPFLGGGEMISDVFLDHSTYAPPPSRFEAGTPAIGEAIGLGAAIDYLSEIGMDRIHEYEVELGTYLYEKLSSVPGVRIY 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 327 G-EPGQ---RAGAVSFLLEDIHPQDAATLLDMQ-GIALRVGHHCAMPLMESLGVGGTMRASLACYNNRDDVDALLAALHK 401
Cdd:PLN02855 335 GpKPSEgvgRAALCAFNVEGIHPTDLSTFLDQQhGVAIRSGHHCAQPLHRYLGVNASARASLYFYNTKEEVDAFIHALKD 414
|
....*
gi 2067391329 402 LRDFF 406
Cdd:PLN02855 415 TIAFF 419
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| sufS |
TIGR01979 |
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine ... |
7-406 |
0e+00 |
|
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: 602.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 7 ARLRGQFPALAQEVNGHPLVYLDNAATTQKPQAVLDAINHYYRADNANVHRAAHALSGRATRAFEDARETVARFINASRS 86
Cdd:TIGR01979 1 KNIRADFPILKRKINGKPLVYLDSAATSQKPQQVIDAVAEYYRNSNANVHRGIHTLSVRATEAYEAVREKVAKFINAASD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 87 HEVIWTRGTTEAINLVAQSWGMSELRAGDEIVLSTLEHHANIVPWQLVAQRTGAVIRVIPLDERGDLDLAAYHAMLGPRT 166
Cdd:TIGR01979 81 EEIVFTRGTTESINLVAYSWGDSNLKAGDEIVISEMEHHANIVPWQLLAERTGATLKFIPLDDDGTLDLDDLEKLLTEKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 167 RLVSVAHVSNALGTVTPVKEMVAAAKAVGSLSLIDGAQAVAHLEVDVQAIGCDFYAFSGHKLYGPTGIGVLWGRTELLER 246
Cdd:TIGR01979 161 KLVAITHVSNVLGTVNPVEEIAKLAHQVGAKVLVDGAQAVPHMPVDVQALDCDFYVFSGHKMYGPTGIGVLYGKEELLEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 247 MPPWQAGGEMIDRVSFAGTTFNTLPFKFEAGTPHIAGAIGLAAAIDFVMKQDRDSLASHEAALTDYLVAGLQQVPGLRLV 326
Cdd:TIGR01979 241 MPPFLGGGEMIAEVSFEETTYNEAPHKFEAGTPNIAGVIGLGAAIDYLEAIGLENIEAHEHELTAYALERLGEIPGLRIY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 327 G--EPGQRAGAVSFLLEDIHPQDAATLLDMQGIALRVGHHCAMPLMESLGVGGTMRASLACYNNRDDVDALLAALHKLRD 404
Cdd:TIGR01979 321 GprDAEDRGGIISFNVEGVHPHDVGTILDEEGIAVRSGHHCAQPLMRRFGVPATCRASFYIYNTEEDIDALVEALKKVRK 400
|
..
gi 2067391329 405 FF 406
Cdd:TIGR01979 401 FF 402
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
7-405 |
0e+00 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 602.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 7 ARLRGQFPalaqeVNGHPLVYLDNAATTQKPQAVLDAINHYYRADNANVHRAAHALSGRATRAFEDARETVARFINASRS 86
Cdd:COG0520 3 EAIRADFP-----VLGKPLVYLDNAATGQKPRPVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAASP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 87 HEVIWTRGTTEAINLVAQSWGMseLRAGDEIVLSTLEHHANIVPWQLVAQRTGAVIRVIPLDERGDLDLAAYHAMLGPRT 166
Cdd:COG0520 78 DEIIFTRGTTEAINLVAYGLGR--LKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDGELDLEALEALLTPRT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 167 RLVSVAHVSNALGTVTPVKEMVAAAKAVGSLSLIDGAQAVAHLEVDVQAIGCDFYAFSGHKLYGPTGIGVLWGRTELLER 246
Cdd:COG0520 156 KLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELLEA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 247 MPPWQAGGEMIDRVSFAGTTFNTLPFKFEAGTPHIAGAIGLAAAIDFVMKQDRDSLASHEAALTDYLVAGLQQVPGLRLV 326
Cdd:COG0520 236 LPPFLGGGGMIEWVSFDGTTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAIPGVRIL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 327 G--EPGQRAGAVSFLLEDIHPQDAATLLDMQGIALRVGHHCAMPLMESLGVGGTMRASLACYNNRDDVDALLAALHKLRD 404
Cdd:COG0520 316 GpaDPEDRSGIVSFNVDGVHPHDVAALLDDEGIAVRAGHHCAQPLMRRLGVPGTVRASFHLYNTEEEIDRLVEALKKLAE 395
|
.
gi 2067391329 405 F 405
Cdd:COG0520 396 L 396
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
26-399 |
0e+00 |
|
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: 599.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 26 VYLDNAATTQKPQAVLDAINHYYRADNANVHRAAHALSGRATRAFEDARETVARFINASRSHEVIWTRGTTEAINLVAQS 105
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINAPSPDEIIFTRNTTEAINLVAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 106 WGMSeLRAGDEIVLSTLEHHANIVPWQLVAQRTGAVIRVIPLDERGDLDLAAYHAMLGPRTRLVSVAHVSNALGTVTPVK 185
Cdd:cd06453 81 LGRA-NKPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 186 EMVAAAKAVGSLSLIDGAQAVAHLEVDVQAIGCDFYAFSGHKLYGPTGIGVLWGRTELLERMPPWQAGGEMIDRVSFAGT 265
Cdd:cd06453 160 EIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMIEEVSFEET 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 266 TFNTLPFKFEAGTPHIAGAIGLAAAIDFVMKQDRDSLASHEAALTDYLVAGLQQVPGLRLVGEPGQRAGAVSFLLEDIHP 345
Cdd:cd06453 240 TYADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEIPGVRVYGDAEDRAGVVSFNLEGIHP 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2067391329 346 QDAATLLDMQGIALRVGHHCAMPLMESLGVGGTMRASLACYNNRDDVDALLAAL 399
Cdd:cd06453 320 HDVATILDQYGIAVRAGHHCAQPLMRRLGVPGTVRASFGLYNTEEEIDALVEAL 373
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
13-402 |
0e+00 |
|
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: 567.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 13 FPALAQEVNGHPLVYLDNAATTQKPQAVLDAINHYYRADNANVHRAAHALSGRATRAFEDARETVARFINASRSHEVIWT 92
Cdd:NF041166 234 FPILQERVNGKPLVWFDNAATTQKPQAVIDRLSYFYEHENSNIHRAAHELAARATDAYEGAREKVRRFIGAPSVDEIIFV 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 93 RGTTEAINLVAQSWGMSELRAGDEIVLSTLEHHANIVPWQLVAQRTGAVIRVIPLDERGDLDLAAYHAMLGPRTRLVSVA 172
Cdd:NF041166 314 RGTTEAINLVAKSWGRQNIGAGDEIIVSHLEHHANIVPWQQLAQETGAKLRVIPVDDSGQILLDEYAKLLNPRTKLVSVT 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 173 HVSNALGTVTPVKEMVAAAKAVGSLSLIDGAQAVAHLEVDVQAIGCDFYAFSGHKLYGPTGIGVLWGRTELLERMPPWQA 252
Cdd:NF041166 394 QVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGIGVVYGKRDLLEAMPPWQG 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 253 GGEMIDRVSFAGTTFNTLPFKFEAGTPHIAGAIGLAAAIDFVMKQDRDSLASHEAALTDYLVAGLQQVPGLRLVGEPGQR 332
Cdd:NF041166 474 GGNMIADVTFEKTVYQPAPNRFEAGTGNIADAVGLGAALDYVERIGIENIARYEHDLLEYATAGLAEVPGLRLIGTAADK 553
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 333 AGAVSFLLEDIHPQDAATLLDMQGIALRVGHHCAMPLMESLGVGGTMRASLACYNNRDDVDALLAALHKL 402
Cdd:NF041166 554 ASVLSFVLDGYSTEEVGKALNQEGIAVRSGHHCAQPILRRFGVEATVRPSLAFYNTCEEVDALVAVLRRL 623
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
26-395 |
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: 508.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 26 VYLDNAATTQKPQAVLDAINHYYRADNANVHRAAHALSGRATRAFEDARETVARFINASRSHEVIWTRGTTEAINLVAQS 105
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 106 WGMSeLRAGDEIVLSTLEHHANIVPWQLVAQRTGAVIRVIPLDERGDLDLAAYHAMLGPRTRLVSVAHVSNALGTVTPVK 185
Cdd:pfam00266 81 LGRS-LKPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 186 EMVAAAKAVGSLSLIDGAQAVAHLEVDVQAIGCDFYAFSGHKLYGPTGIGVLWGRTELLERMPPWQAGGEMIDRVSFAGT 265
Cdd:pfam00266 160 EIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGMIETVSLQES 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 266 TFNTLPFKFEAGTPHIAGAIGLAAAIDFVMKQDRDSLASHEAALTDYLVAGLQQVPGLRLVGePGQRAGAVSFLLEDIHP 345
Cdd:pfam00266 240 TFADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYG-PERRASIISFNFKGVHP 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2067391329 346 QDAATLLDMQGIALRVGHHCAMPLMESLGVGGTMRASLACYNNRDDVDAL 395
Cdd:pfam00266 319 HDVATLLDESGIAVRSGHHCAQPLMVRLGLGGTVRASFYIYNTQEDVDRL 368
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
7-406 |
1.26e-179 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 506.59 E-value: 1.26e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 7 ARLRGQFPALAQEVNGHPLVYLDNAATTQKPQAVLDAINHYYRADNANVHRAAHALSGRATRAFEDARETVARFINASRS 86
Cdd:PLN02855 15 AETRPDFPILDQTVNGSKLVYLDNAATSQKPAAVLDALQDYYEEYNSNVHRGIHALSAKATDAYELARKKVAAFINASTS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 87 HEVIWTRGTTEAINLVAQSWGMSELRAGDEIVLSTLEHHANIVPWQLVAQRTGAVIRVIPLDERGDLDLAAYHAMLGPRT 166
Cdd:PLN02855 95 REIVFTRNATEAINLVAYTWGLANLKPGDEVILSVAEHHSNIVPWQLVAQKTGAVLKFVGLTPDEVLDVEQLKELLSEKT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 167 RLVSVAHVSNALGTVTPVKEMVAAAKAVGSLSLIDGAQAVAHLEVDVQAIGCDFYAFSGHKLYGPTGIGVLWGRTELLER 246
Cdd:PLN02855 175 KLVATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLWGKSDLLES 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 247 MPPWQAGGEMIDRVSFAGTTFNTLPFKFEAGTPHIAGAIGLAAAIDFVMKQDRDSLASHEAALTDYLVAGLQQVPGLRLV 326
Cdd:PLN02855 255 MPPFLGGGEMISDVFLDHSTYAPPPSRFEAGTPAIGEAIGLGAAIDYLSEIGMDRIHEYEVELGTYLYEKLSSVPGVRIY 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 327 G-EPGQ---RAGAVSFLLEDIHPQDAATLLDMQ-GIALRVGHHCAMPLMESLGVGGTMRASLACYNNRDDVDALLAALHK 401
Cdd:PLN02855 335 GpKPSEgvgRAALCAFNVEGIHPTDLSTFLDQQhGVAIRSGHHCAQPLHRYLGVNASARASLYFYNTKEEVDAFIHALKD 414
|
....*
gi 2067391329 402 LRDFF 406
Cdd:PLN02855 415 TIAFF 419
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
8-402 |
1.41e-166 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 472.70 E-value: 1.41e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 8 RLRGQFPALAQEVNGHPLVYLDNAATTQKPQAVLDAINHYYRADNANVHRAAHALSGRATRAFEDARETVARFINASRSH 87
Cdd:PRK09295 7 KVRADFPVLSREVNGLPLAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKQAALFINARSAE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 88 EVIWTRGTTEAINLVAQSWGMSELRAGDEIVLSTLEHHANIVPWQLVAQRTGAVIRVIPLDERGDLDLAAYHAMLGPRTR 167
Cdd:PRK09295 87 ELVFVRGTTEGINLVANSWGNSNVRAGDNIIISEMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPALFDERTR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 168 LVSVAHVSNALGTVTPVKEMVAAAKAVGSLSLIDGAQAVAHLEVDVQAIGCDFYAFSGHKLYGPTGIGVLWGRTELLERM 247
Cdd:PRK09295 167 LLAITHVSNVLGTENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKEALLQEM 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 248 PPWQAGGEMIDRVSFA-GTTFNTLPFKFEAGTPHIAGAIGLAAAIDFVMKQDRDSLASHEAALTDYLVAGLQQVPGLRLV 326
Cdd:PRK09295 247 PPWEGGGSMIATVSLTeGTTWAKAPWRFEAGTPNTGGIIGLGAALDYVSALGLNNIAEYEQNLMHYALSQLESVPDLTLY 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2067391329 327 GePGQRAGAVSFLLEDIHPQDAATLLDMQGIALRVGHHCAMPLMESLGVGGTMRASLACYNNRDDVDALLAAL---HKL 402
Cdd:PRK09295 327 G-PQNRLGVIAFNLGKHHAYDVGSFLDNYGIAVRTGHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVAGLqriHRL 404
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
1-401 |
1.92e-153 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 439.09 E-value: 1.92e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 1 MNQQQHARLRGQFPALAqevngHPLVYLDNAATTQKPQAVLDAINHYYRADNANVHRAAHALSGRATRAFEDARETVARF 80
Cdd:PRK10874 1 MNVFNPAQFRAQFPALQ-----DAGVYLDSAATALKPQAVIEATQQFYSLSAGNVHRSQFAAAQRLTARYEAAREQVAQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 81 INASRSHEVIWTRGTTEAINLVAQSWGMSELRAGDEIVLSTLEHHANIVPWQLVAQRTGAVIRVIPLDERGDLDLAAYHA 160
Cdd:PRK10874 76 LNAPDAKNIVWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLVPWLMVAQQTGAKVVKLPLGADRLPDVDLLPE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 161 MLGPRTRLVSVAHVSNALGTVTPVKEMVAAAKAVGSLSLIDGAQAVAHLEVDVQAIGCDFYAFSGHKLYGPTGIGVLWGR 240
Cdd:PRK10874 156 LITPRTRILALGQMSNVTGGCPDLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 241 TELLERMPPWQAGGEMIDRVSFAGTTFNTLPFKFEAGTPHIAGAIGLAAAIDFVMKQDRDSLASHEAALTDYLVAGLQQV 320
Cdd:PRK10874 236 SELLEAMSPWQGGGKMLTEVSFDGFTPQSAPWRFEAGTPNVAGVIGLSAALEWLADIDINQAESWSRSLATLAEDALAKL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 321 PGLRLVGEPGqrAGAVSFLLEDIHPQDAATLLDMQGIALRVGHHCAMPLMESLGVGGTMRASLACYNNRDDVDALLAALH 400
Cdd:PRK10874 316 PGFRSFRCQD--SSLLAFDFAGVHHSDLVTLLAEYGIALRAGQHCAQPLLAALGVTGTLRASFAPYNTQSDVDALVNAVD 393
|
.
gi 2067391329 401 K 401
Cdd:PRK10874 394 R 394
|
|
| FeS_syn_CsdA |
TIGR03392 |
cysteine desulfurase, catalytic subunit CsdA; Members of this protein family are CsdS. This ... |
7-399 |
1.22e-138 |
|
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: 401.52 E-value: 1.22e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 7 ARLRGQFPALAQEvnghpLVYLDNAATTQKPQAVLDAINHYYRADNANVHRAAHALSGRATRAFEDARETVARFINASRS 86
Cdd:TIGR03392 4 AQFRRQFPALQDA-----TVYLDSAATALKPQAVIDATQQFYRLSSGTVHRSQHQEAQSLTARYEAAREQVAQLLNAPDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 87 HEVIWTRGTTEAINLVAQSWGMSELRAGDEIVLSTLEHHANIVPWQLVAQRTGAVIRVIPLDERGDLDLAAYHAMLGPRT 166
Cdd:TIGR03392 79 ENIVWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLIPWLMVAQQTGAKVVKLPIGADLLPDIDQLPELLTPRT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 167 RLVSVAHVSNALGTVTPVKEMVAAAKAVGSLSLIDGAQAVAHLEVDVQAIGCDFYAFSGHKLYGPTGIGVLWGRTELLER 246
Cdd:TIGR03392 159 RILALGQMSNVTGGCPDLARAITLAHQYGCVVVVDGAQGVVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKTELLEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 247 MPPWQAGGEMIDRVSFAGTTFNTLPFKFEAGTPHIAGAIGLAAAIDFVMKQDRDSLASHEAALTDYLVAGLQQVPGLRLV 326
Cdd:TIGR03392 239 MPPWQGGGKMLSHVSFDGFTPQAVPWRFEAGTPNIAGVIGLSAALEWLADIDINAAESWSVSLATLAEEALAQLPGFRSF 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2067391329 327 GEPGqrAGAVSFLLEDIHPQDAATLLDMQGIALRVGHHCAMPLMESLGVGGTMRASLACYNNRDDVDALLAAL 399
Cdd:TIGR03392 319 RCQG--SSLLAFDFAGVHHSDLVTLLAEQGIALRAGQHCAQPLMAALGVSGTLRASFAPYNTQQDVDALVNAV 389
|
|
| am_tr_V_VC1184 |
TIGR01976 |
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of ... |
7-399 |
4.54e-84 |
|
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: 262.00 E-value: 4.54e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 7 ARLRGQFPALAQEVnghpLVYLDNAATTQKPQAVLDAINHYYRADNANVHRAAHAlSGRATRAFEDARETVARFINASrS 86
Cdd:TIGR01976 4 EAVRGQFPALADGD----RVFFDNPAGTQIPQSVADAVSAALTRSNANRGGAYES-SRRADQVVDDAREAVADLLNAD-P 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 87 HEVIWTRGTTEAINLVAQSWGmSELRAGDEIVLSTLEHHANIVPWQLVAQRTGAVIRVIPLDER-GDLDLAAYHAMLGPR 165
Cdd:TIGR01976 78 PEVVFGANATSLTFLLSRAIS-RRWGPGDEVIVTRLDHEANISPWLQAAERAGAKVKWARVDEAtGELHPDDLASLLSPR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 166 TRLVSVAHVSNALGTVTPVKEMVAAAKAVGSLSLIDGAQAVAHLEVDVQAIGCDFYAFSGHKLYGPTgIGVLWGRTELLE 245
Cdd:TIGR01976 157 TRLVAVTAASNTLGSIVDLAAITELVHAAGALVVVDAVHYAPHGLIDVQATGADFLTCSAYKFFGPH-MGILWGRPELLM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 246 RMPPwqaggemiDRVSFAgttFNTLPFKFEAGTPHIAGAIGLAAAIDFVMKQDRD--------------SLASHEAALTD 311
Cdd:TIGR01976 236 NLPP--------YKLTFS---YDTGPERFELGTPQYELLAGVVAAVDYLAGLGESangsrrerlvasfqAIDAYENRLAE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 312 YLVAGLQQVPGLRLVG--EPGQRAGAVSFLLEDIHPQDAATLLDMQGIALRVGHHCAMPLMESLGV---GGTMRASLACY 386
Cdd:TIGR01976 305 YLLVGLSDLPGVTLYGvaRLAARVPTVSFTVHGLPPQRVVRRLADQGIDAWAGHFYAVRLLRRLGLndeGGVVRVGLAHY 384
|
410
....*....|...
gi 2067391329 387 NNRDDVDALLAAL 399
Cdd:TIGR01976 385 NTAEEVDRLLEAL 397
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
26-402 |
1.39e-66 |
|
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: 216.45 E-value: 1.39e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 26 VYLDNAATTQKPQAVLDAINHYYRADNANVHrAAHALSGRATRAFEDARETVARFINAsRSHEVIWTRGTTEAINLVAQS 105
Cdd:COG1104 4 IYLDNAATTPVDPEVLEAMLPYLTEYFGNPS-SLHSFGREARAALEEAREQVAALLGA-DPEEIIFTSGGTEANNLAIKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 106 WGMSELRAGDEIVLSTLEHHA--NIVPWqlvAQRTGAVIRVIPLDERGDLDLAAYHAMLGPRTRLVSVAHVSNALGTVTP 183
Cdd:COG1104 82 AARAYRKKGKHIITSAIEHPAvlETARF---LEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 184 VKEMVAAAKAVGSLSLIDGAQAVAHLEVDVQAIGCDFYAFSGHKLYGPTGIGVLWGRTELleRMPPWQAGG--EMIDRvs 261
Cdd:COG1104 159 IAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRKGV--RLEPLIHGGgqERGLR-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 262 fAGTtfntlpfkfE-----AGtphiagaiglaaaidF-----VMKQDRDSLASHEAALTDYLVAGLQQ-VPGLRLVGEPG 330
Cdd:COG1104 235 -SGT---------EnvpgiVG---------------LgkaaeLAAEELEEEAARLRALRDRLEEGLLAaIPGVVINGDPE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 331 QR-AGAVSFLLEDIHPQDAATLLDMQGIALRVGHHCA------MPLMESLGVG-----GTMRASLACYNNRDDVDALLAA 398
Cdd:COG1104 290 NRlPNTLNFSFPGVEGEALLLALDLAGIAVSSGSACSsgslepSHVLLAMGLDeelahGSIRFSLGRFTTEEEIDRAIEA 369
|
....
gi 2067391329 399 LHKL 402
Cdd:COG1104 370 LKEI 373
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
26-393 |
9.71e-35 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 131.70 E-value: 9.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 26 VYLDNAATTQKPQAVLDAINHYYRADNANVHRAAHALSGRATRAFEDARETVARFINASrSHEVIWTRGTTEAINLVAQS 105
Cdd:PLN02651 1 LYLDMQATTPIDPRVLDAMLPFLIEHFGNPHSRTHLYGWESEDAVEKARAQVAALIGAD-PKEIIFTSGATESNNLAIKG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 106 WGMSELRAGDEIVLSTLEHHANIVPWQLVAQRTGAVIRViPLDERGDLDLAAYHAMLGPRTRLVSVAHVSNALGTVTPVK 185
Cdd:PLN02651 80 VMHFYKDKKKHVITTQTEHKCVLDSCRHLQQEGFEVTYL-PVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 186 EMVAAAKAVGSLSLIDGAQAVAHLEVDVQAIGCDFYAFSGHKLYGPTGIGVLWGRTELLERMPPWQAGGEMiDRVSFAGT 265
Cdd:PLN02651 159 EIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRLEPLMSGGGQ-ERGRRSGT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 266 TFNTLPFKFEAGTPhiagaiglaaaidfVMKQDRDSLASHEAALTDYLVAGLQ-QVPGLRLVG--EPGQR-AGAVSFLLE 341
Cdd:PLN02651 238 ENTPLVVGLGAACE--------------LAMKEMDYDEKHMKALRERLLNGLRaKLGGVRVNGprDPEKRyPGTLNLSFA 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2067391329 342 DIHpqDAATLLDMQGIALRVGHHC------------AMPLMESLGVgGTMRASLACYNNRDDVD 393
Cdd:PLN02651 304 YVE--GESLLMGLKEVAVSSGSACtsaslepsyvlrALGVPEEMAH-GSLRLGVGRFTTEEEVD 364
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
26-254 |
9.61e-34 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 130.06 E-value: 9.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 26 VYLDNAATTQKPQAVLDAINHYYRADN--ANVHRAAHALSGRATRAFEDARETVARFINASrSHEVIWTRGTTEAINL-- 101
Cdd:PRK14012 5 IYLDYSATTPVDPRVAEKMMPYLTMDGtfGNPASRSHRFGWQAEEAVDIARNQIADLIGAD-PREIVFTSGATESDNLai 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 102 --VAQSWGmselRAGDEIVLSTLEHHANIVPW-QLvaQRTGAVIRVIPLDERGDLDLAAYHAMLGPRTRLVSVAHVSNAL 178
Cdd:PRK14012 84 kgAAHFYQ----KKGKHIITSKTEHKAVLDTCrQL--EREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2067391329 179 GTVTPVKEMVAAAKAVGSLSLIDGAQAVAHLEVDVQAIGCDFYAFSGHKLYGPTGIGVLWGRTELLERMPPWQAGG 254
Cdd:PRK14012 158 GVIQDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRLEAQMHGG 233
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
25-402 |
5.38e-25 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 105.20 E-value: 5.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 25 LVYLDNAATTQKPQAVLDAINH----YYraDNANvhrAAHALSGRATRAFEDARETVARFINASRSHeVIWTRGTTEAIN 100
Cdd:PRK02948 1 MIYLDYAATTPMSKEALQTYQKaasqYF--GNES---SLHDIGGTASSLLQVCRKTFAEMIGGEEQG-IYFTSGGTESNY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 101 LVAQSWGMSELRAGDEIVLSTLEHHANIVPWQLVAQRtGAVIRVIPLDERGDLDLAAYHAMLGPRTRLVSVAHVSNALGT 180
Cdd:PRK02948 75 LAIQSLLNALPQNKKHIITTPMEHASIHSYFQSLESQ-GYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 181 VTPVKEMVAAAKAVGSLSLIDGAQAVAHLEVDVQAIGCDFYAFSGHKLYGPTGIGVLWGRTELlermpPWQAggemidrv 260
Cdd:PRK02948 154 IQPIAEIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYINPQV-----RWKP-------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 261 SFAGTTFNTlpfKFEAGTPHIAGAIGLAAAIDFVMKQdRDSLASHEAALTDYLVAGLQQVP-GLRLVGEPGQR-AGAVSF 338
Cdd:PRK02948 221 VFPGTTHEK---GFRPGTVNVPGIAAFLTAAENILKN-MQEESLRFKELRSYFLEQIQTLPlPIEVEGHSTSClPHIIGV 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2067391329 339 LLEDIHPQDAATLLDMQGIALRVGHHCAM----PLMESLGVGGT-------MRASLACYNNRDDVDALLAALHKL 402
Cdd:PRK02948 297 TIKGIEGQYTMLECNRRGIAISTGSACQVgkqePSKTMLAIGKTyeeakqfVRFSFGQQTTKDQIDTTIHALETI 371
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
70-240 |
2.25e-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: 70.49 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 70 FEDARETVARFINASRSHEVIwTRGTTEAINLVAQSWGMselrAGDEIVLSTLEHHANIVpwqLVAQRTGAVIRVIPLDE 149
Cdd:cd01494 2 LEELEEKLARLLQPGNDKAVF-VPSGTGANEAALLALLG----PGDEVIVDANGHGSRYW---VAAELAGAKPVPVPVDD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 150 RGDLDLAAYH---AMLGPRTRLVSVAHVSNALGTVTPVKEMVAAAKAVGSLSLIDGAQAVAH---LEVDVQAIGCDFYAF 223
Cdd:cd01494 74 AGYGGLDVAIleeLKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGAspaPGVLIPEGGADVVTF 153
|
170
....*....|....*..
gi 2067391329 224 SGHKLYGPTGIGVLWGR 240
Cdd:cd01494 154 SLHKNLGGEGGGVVIVK 170
|
|
| SepCysS |
cd06452 |
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ... |
92-246 |
7.48e-09 |
|
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: 57.02 E-value: 7.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 92 TRGTTEAINLVAQSWGmselRAGDEIVLSTLEHHANIVpwqlVAQRTGAVIRVIPLDERGD--LDLAAYHAML------- 162
Cdd:cd06452 65 TPGAREGKFAVMHSLC----EKGDWVVVDGLAHYTSYV----AAERAGLNVREVPNTGHPEyhITPEGYAEVIeevkdef 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 163 GPRTRLVSVAHVSNALGTVTPVKEMVAAAKAVGSLSLIDGAQAVAHLEVDVQAIGCDFYAFSGHKLYGPTG-IGVLWGRT 241
Cdd:cd06452 137 GKPPALALLTHVDGNYGNLHDAKKIAKVCHEYGVPLLLNGAYTVGRMPVSGKELGADFIVGSGHKSMAASApIGVLATTE 216
|
....*
gi 2067391329 242 ELLER 246
Cdd:cd06452 217 EWADI 221
|
|
| PRK09331 |
PRK09331 |
Sep-tRNA:Cys-tRNA synthetase; Provisional |
75-237 |
1.10e-08 |
|
Sep-tRNA:Cys-tRNA synthetase; Provisional
Pssm-ID: 236469 Cd Length: 387 Bit Score: 56.48 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 75 ETVARFINASrshEVIWTRGTTEAINLVAQSWGmselRAGDEIVLSTLEHHANIVpwqlVAQRTGAVIRVIPLDERGD-- 152
Cdd:PRK09331 70 EDLAEFLGMD---EARVTHGAREGKFAVMHSLC----KKGDYVVLDGLAHYTSYV----AAERAGLNVREVPKTGYPEyk 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 153 LDLAAYHAML-------GPRTRLVSVAHVSNALGTVTPVKEMVAAAKAVGSLSLIDGAQAVAHLEVDVQAIGCDFYAFSG 225
Cdd:PRK09331 139 ITPEAYAEKIeevkeetGKPPALALLTHVDGNYGNLADAKKVAKVAHEYGIPFLLNGAYTVGRMPVDGKKLGADFIVGSG 218
|
170
....*....|...
gi 2067391329 226 HKLYGPTG-IGVL 237
Cdd:PRK09331 219 HKSMAASApSGVL 231
|
|
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
8-242 |
4.04e-07 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 52.18 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 8 RLRG-QFPALAQevnghpLVYLDNAATTQKPQAVLDAINHYYradNANVHRAAHA---LSGRATRAFEDARETVARFINA 83
Cdd:PLN02724 23 ELRAtEFARLKG------VVYLDHAGATLYSESQLEAALADF---SSNVYGNPHSqsdSSMRSSDTIESARQQVLEYFNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 84 SRS-HEVIWTRGTTEAINLVAQSWGMSElragDEIVLSTLEHHANIVPWQLVA-QRTGAVIRV-------IPLDERGDLD 154
Cdd:PLN02724 94 PPSdYACVFTSGATAALKLVGETFPWSS----ESHFCYTLENHNSVLGIREYAlEKGAAAIAVdieeaanQPTNSQGSVV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 155 LAayHAMLGPRTRLVSVAHVSNA--------------------LGTVTPVKEM--VAAAKAVGSLSLIDGAQAVAHLEVD 212
Cdd:PLN02724 170 VK--SRGLQRRNTSKLQKREDDGeaynlfafpsecnfsgakfpLDLVKLIKDNqhSNFSKSGRWMVLLDAAKGCGTSPPD 247
|
250 260 270
....*....|....*....|....*....|.
gi 2067391329 213 VQAIGCDFYAFSGHKLYG-PTGIGVLWGRTE 242
Cdd:PLN02724 248 LSRYPADFVVVSFYKIFGyPTGLGALLVRRD 278
|
|
| PRK06836 |
PRK06836 |
pyridoxal phosphate-dependent aminotransferase; |
37-192 |
3.31e-06 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180720 Cd Length: 394 Bit Score: 48.65 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 37 PQAVLDAINHYYRADNANVHRAAHAlSGratraFEDARETVARFINA------SRSHeVIWTRGTTEAINLVaqswgmse 110
Cdd:PRK06836 48 PAAVKEALRELAEEEDPGLHGYMPN-AG-----YPEVREAIAESLNRrfgtplTADH-IVMTCGAAGALNVA-------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 111 LRA----GDE-IVLSTLehhanIVPWQLVAQRTGAVIRVIPLDERG-DLDLAAYHAMLGPRTRLVSVAHVSNALGTVTPV 184
Cdd:PRK06836 113 LKAilnpGDEvIVFAPY-----FVEYRFYVDNHGGKLVVVPTDTDTfQPDLDALEAAITPKTKAVIINSPNNPTGVVYSE 187
|
....*...
gi 2067391329 185 KEMVAAAK 192
Cdd:PRK06836 188 ETLKALAA 195
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
72-201 |
8.76e-06 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 47.30 E-value: 8.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 72 DARETVARFINAS------RSHEVIWTRGTTEAINLVAQSWGMselrAGDEIVLSTLeHHANIVPwqlVAQRTGAVIRVI 145
Cdd:pfam00155 43 ELREALAKFLGRSpvlkldREAAVVFGSGAGANIEALIFLLAN----PGDAILVPAP-TYASYIR---IARLAGGEVVRY 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2067391329 146 PLDERGD--LDLAAYHAMLGPRTRLVSVAHVSNALGTVTP---VKEMVAAAKAVGSLSLID 201
Cdd:pfam00155 115 PLYDSNDfhLDFDALEAALKEKPKVVLHTSPHNPTGTVATleeLEKLLDLAKEHNILLLVD 175
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
108-246 |
4.07e-05 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 44.90 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 108 MSELRAGDEIVLstlEHHANIVPWQL--VAQRTGAVIRVIPLDERGDLDLAAYHAML-------GPRTRLVSVAHVSN-A 177
Cdd:pfam01212 65 MAHCQRGDEVIC---GEPAHIHFDETggHAELGGVQPRPLDGDEAGNMDLEDLEAAIrevgadiFPPTGLISLENTHNsA 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2067391329 178 LGTVTPVKEMVAA---AKAVGSLSLIDGAQ---AVAHLEVDVQAI--GCDFYAFSGHK-LYGPTGiGVLWGRTELLER 246
Cdd:pfam01212 142 GGQVVSLENLREIaalAREHGIPVHLDGARfanAAVALGVIVKEItsYADSVTMCLSKgLGAPVG-SVLAGSDDFIAK 218
|
|
| SelA |
COG1921 |
Seryl-tRNA(Sec) selenium transferase [Translation, ribosomal structure and biogenesis]; |
158-247 |
2.36e-04 |
|
Seryl-tRNA(Sec) selenium transferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441524 Cd Length: 399 Bit Score: 43.19 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 158 YHAMLGPRTRLVSVAHVSNA--LGTV--TPVKEMVAAAKA--------VGSLSLIDGAQAVAHLEVDVQAI---GCDFYA 222
Cdd:COG1921 147 YEAAITENTAALLKVHTSNYriVGFTeeVSLAELAELAHEhglpvivdLGSGSLVDLSKYGLPHEPTVQEYlaaGADLVT 226
|
90 100
....*....|....*....|....*.
gi 2067391329 223 FSGHKLY-GPTGiGVLWGRTELLERM 247
Cdd:COG1921 227 FSGDKLLgGPQA-GIIVGKKELIERI 251
|
|
| AspB |
COG0436 |
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ... |
37-192 |
4.41e-04 |
|
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: 42.04 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 37 PQAVLDAInhyYRADNANVHRAAHAlsgratRAFEDARETVARFINASRSH-----EVIWTRGTTEAINLVAQSWgmseL 111
Cdd:COG0436 45 PDHIREAA---IEALDDGVTGYTPS------AGIPELREAIAAYYKRRYGVdldpdEILVTNGAKEALALALLAL----L 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 112 RAGDEIvlstlehhanIVP------WQLVAQRTGAVIRVIPLDERGD--LDLAAYHAMLGPRTRLVSVAHVSNALGTVTP 183
Cdd:COG0436 112 NPGDEV----------LVPdpgypsYRAAVRLAGGKPVPVPLDEENGflPDPEALEAAITPRTKAIVLNSPNNPTGAVYS 181
|
....*....
gi 2067391329 184 VKEMVAAAK 192
Cdd:COG0436 182 REELEALAE 190
|
|
| SelA |
pfam03841 |
L-seryl-tRNA selenium transferase; |
158-247 |
4.79e-04 |
|
L-seryl-tRNA selenium transferase;
Pssm-ID: 309101 Cd Length: 367 Bit Score: 41.94 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 158 YHAMLGPRTRLVSVAHVSN----ALGTVTPVKEMVAAAKAV--------GSLSLIDGAQAVAHLEVDVQ---AIGCDFYA 222
Cdd:pfam03841 129 YEQAINENTALLMKVHTSNyriqGFTKEVELAELVELGHEKglpvyedlGSGSLVDLSQYGLPKEPTVQeliAQGVDLVS 208
|
90 100
....*....|....*....|....*
gi 2067391329 223 FSGHKLYGPTGIGVLWGRTELLERM 247
Cdd:pfam03841 209 FSGDKLLGGPQAGIIVGKKELIERI 233
|
|
| PRK07777 |
PRK07777 |
putative succinyldiaminopimelate transaminase DapC; |
88-191 |
7.21e-04 |
|
putative succinyldiaminopimelate transaminase DapC;
Pssm-ID: 236095 [Multi-domain] Cd Length: 387 Bit Score: 41.56 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 88 EVIWTRGTTEAInlVAQSWGMSElrAGDEIVLstlehhanIVP----WQLVAQRTGAVIRVIPLDERGD---LDLAAYHA 160
Cdd:PRK07777 87 EVLVTVGATEAI--AAAVLGLVE--PGDEVLL--------IEPyydsYAAVIAMAGAHRVPVPLVPDGRgfaLDLDALRA 154
|
90 100 110
....*....|....*....|....*....|.
gi 2067391329 161 MLGPRTRLVSVAHVSNALGTVTPVKEMVAAA 191
Cdd:PRK07777 155 AVTPRTRALIVNSPHNPTGTVLTAAELAAIA 185
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
111-399 |
1.07e-03 |
|
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: 40.74 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 111 LRAGDEIVLSTLEHHANIvpWQLVAQRTGAVIRVIPLDERGDLDLAAYHAML-GPRTRLVSVAHVSNALGTVTPVKEMVA 189
Cdd:cd06451 71 LEPGDKVLVGVNGVFGDR--WADMAERYGADVDVVEKPWGEAVSPEEIAEALeQHDIKAVTLTHNETSTGVLNPLEGIGA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 190 AAKAVGSLSLIDGAQAVAHLEVDVQAIGCDfYAFSGHK--LYGPTGIGVLWGRTELLERMPpwqagGEMIDRVSFAGTTF 267
Cdd:cd06451 149 LAKKHDALLIVDAVSSLGGEPFRMDEWGVD-VAYTGSQkaLGAPPGLGPIAFSERALERIK-----KKTKPKGFYFDLLL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 268 NTLPFKFEAGTPHIAGAIGL---AAAIDFVMKQDRDSLASHEAALTDYLVAGLQQVpGLRLVGEPGQRAGAVSFLL--ED 342
Cdd:cd06451 223 LLKYWGEGYSYPHTPPVNLLyalREALDLILEEGLENRWARHRRLAKALREGLEAL-GLKLLAKPELRSPTVTAVLvpEG 301
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2067391329 343 IHPQD-AATLLDMQGIALRVGHHcamPLmeslgVGGTMRASLACYNNRDDVDALLAAL 399
Cdd:cd06451 302 VDGDEvVRRLMKRYNIEIAGGLG---PT-----AGKVFRIGHMGEATREDVLGVLSAL 351
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
108-201 |
1.56e-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: 40.26 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 108 MSELRAGDEIVLSTLEHHANIVPWQLVAQRTGAVIRVIPLDERGDLDLAayhamLGPRTRLVSVAHVSNALGTVTPVKEM 187
Cdd:cd00614 73 LALLKAGDHVVASDDLYGGTYRLFERLLPKLGIEVTFVDPDDPEALEAA-----IKPETKLVYVESPTNPTLKVVDIEAI 147
|
90
....*....|....
gi 2067391329 188 VAAAKAVGSLSLID 201
Cdd:cd00614 148 AELAHEHGALLVVD 161
|
|
| PRK08912 |
PRK08912 |
aminotransferase; |
88-187 |
7.27e-03 |
|
aminotransferase;
Pssm-ID: 181580 Cd Length: 387 Bit Score: 38.42 E-value: 7.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067391329 88 EVIWTRGTTEAInlvAQSWgMSELRAGDEIVLstlehhanIVP----WQLVAQRTGAVIRVIPLDE-RGDLDLAAYHAML 162
Cdd:PRK08912 89 EVMVTSGATEAL---AAAL-LALVEPGDEVVL--------FQPlydaYLPLIRRAGGVPRLVRLEPpHWRLPRAALAAAF 156
|
90 100
....*....|....*....|....*
gi 2067391329 163 GPRTRLVSVAHVSNALGTVTPVKEM 187
Cdd:PRK08912 157 SPRTKAVLLNNPLNPAGKVFPREEL 181
|
|
| |
