|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
3-427 |
0e+00 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 841.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 3 SPLPTPVPAQLALGAALRAEFPILDQKVNGLPLVYLDNAATSQKPRAVLDALSRCYTEYNANVHRGVHALSAKATNEYEE 82
Cdd:PLN02855 1 SSAPAASAASVSLGAETRPDFPILDQTVNGSKLVYLDNAATSQKPAAVLDALQDYYEEYNSNVHRGIHALSAKATDAYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 83 ARAKVAAFIGASTSREVVIVRNATEGINLVSNTWGAANIKQGDEIILSVAEHHANLVPWQLLAARTGAVLRHVRLTPDKS 162
Cdd:PLN02855 81 ARKKVAAFINASTSREIVFTRNATEAINLVAYTWGLANLKPGDEVILSVAEHHSNIVPWQLVAQKTGAVLKFVGLTPDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 163 qLDMDHFRSLLSPRTRLVSLVHVSNVLGCVLDTAYVAEQARRVGAKLLLDCCQSVPHMPVDVCSLGADWIVASSHKFCGP 242
Cdd:PLN02855 161 -LDVEQLKELLSEKTKLVATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 243 SGVGFLWGRYDVLESMEPWMGGGEMIADVFLDQSTYAPPPMRFEAGTPAIAEAIGMGAAAEWLQQLGMDRVHAFEEEIGT 322
Cdd:PLN02855 240 TGIGFLWGKSDLLESMPPFLGGGEMISDVFLDHSTYAPPPSRFEAGTPAIGEAIGLGAAIDYLSEIGMDRIHEYEVELGT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 323 YLYERLVAVsPRVTVYGPRPGAPRGRASLAAFNVEGLHATDVSTLLDMA-GVAVRSGHHCAQPLHRELGVPASARASAYI 401
Cdd:PLN02855 320 YLYEKLSSV-PGVRIYGPKPSEGVGRAALCAFNVEGIHPTDLSTFLDQQhGVAIRSGHHCAQPLHRYLGVNASARASLYF 398
|
410 420
....*....|....*....|....*.
gi 302843952 402 YNTAAEIDTFIEALKDTIKFFDDAHG 427
Cdd:PLN02855 399 YNTKEEVDAFIHALKDTIAFFSSFKG 424
|
|
| sufS |
TIGR01979 |
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine ... |
17-422 |
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: 611.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 17 AALRAEFPILDQKVNGLPLVYLDNAATSQKPRAVLDALSRCYTEYNANVHRGVHALSAKATNEYEEARAKVAAFIGASTS 96
Cdd:TIGR01979 1 KNIRADFPILKRKINGKPLVYLDSAATSQKPQQVIDAVAEYYRNSNANVHRGIHTLSVRATEAYEAVREKVAKFINAASD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 97 REVVIVRNATEGINLVSNTWGAANIKQGDEIILSVAEHHANLVPWQLLAARTGAVLRHVRLTPDkSQLDMDHFRSLLSPR 176
Cdd:TIGR01979 81 EEIVFTRGTTESINLVAYSWGDSNLKAGDEIVISEMEHHANIVPWQLLAERTGATLKFIPLDDD-GTLDLDDLEKLLTEK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 177 TRLVSLVHVSNVLGCVLDTAYVAEQARRVGAKLLLDCCQSVPHMPVDVCSLGADWIVASSHKFCGPSGVGFLWGRYDVLE 256
Cdd:TIGR01979 160 TKLVAITHVSNVLGTVNPVEEIAKLAHQVGAKVLVDGAQAVPHMPVDVQALDCDFYVFSGHKMYGPTGIGVLYGKEELLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 257 SMEPWMGGGEMIADVFLDQSTYAPPPMRFEAGTPAIAEAIGMGAAAEWLQQLGMDRVHAFEEEIGTYLYERLVAVsPRVT 336
Cdd:TIGR01979 240 QMPPFLGGGEMIAEVSFEETTYNEAPHKFEAGTPNIAGVIGLGAAIDYLEAIGLENIEAHEHELTAYALERLGEI-PGLR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 337 VYGPRPGAPRGraSLAAFNVEGLHATDVSTLLDMAGVAVRSGHHCAQPLHRELGVPASARASAYIYNTAAEIDTFIEALK 416
Cdd:TIGR01979 319 IYGPRDAEDRG--GIISFNVEGVHPHDVGTILDEEGIAVRSGHHCAQPLMRRFGVPATCRASFYIYNTEEDIDALVEALK 396
|
....*.
gi 302843952 417 DTIKFF 422
Cdd:TIGR01979 397 KVRKFF 402
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
17-421 |
0e+00 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 583.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 17 AALRAEFPildqkVNGLPLVYLDNAATSQKPRAVLDALSRCYTEYNANVHRGVHALSAKATNEYEEARAKVAAFIGASTS 96
Cdd:COG0520 3 EAIRADFP-----VLGKPLVYLDNAATGQKPRPVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAASP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 97 REVVIVRNATEGINLVSNTWGaaNIKQGDEIILSVAEHHANLVPWQLLAARTGAVLRHVRLTPDKsQLDMDHFRSLLSPR 176
Cdd:COG0520 78 DEIIFTRGTTEAINLVAYGLG--RLKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDG-ELDLEALEALLTPR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 177 TRLVSLVHVSNVLGCVLDTAYVAEQARRVGAKLLLDCCQSVPHMPVDVCSLGADWIVASSHKFCGPSGVGFLWGRYDVLE 256
Cdd:COG0520 155 TKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELLE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 257 SMEPWMGGGEMIADVFLDQSTYAPPPMRFEAGTPAIAEAIGMGAAAEWLQQLGMDRVHAFEEEIGTYLYERLVAVsPRVT 336
Cdd:COG0520 235 ALPPFLGGGGMIEWVSFDGTTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAI-PGVR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 337 VYGPRPgaPRGRASLAAFNVEGLHATDVSTLLDMAGVAVRSGHHCAQPLHRELGVPASARASAYIYNTAAEIDTFIEALK 416
Cdd:COG0520 314 ILGPAD--PEDRSGIVSFNVDGVHPHDVAALLDDEGIAVRAGHHCAQPLMRRLGVPGTVRASFHLYNTEEEIDRLVEALK 391
|
....*
gi 302843952 417 DTIKF 421
Cdd:COG0520 392 KLAEL 396
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
36-415 |
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: 575.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 36 VYLDNAATSQKPRAVLDALSRCYTEYNANVHRGVHALSAKATNEYEEARAKVAAFIGASTSREVVIVRNATEGINLVSNT 115
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINAPSPDEIIFTRNTTEAINLVAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 116 WGAANiKQGDEIILSVAEHHANLVPWQLLAARTGAVLRHVRLTPDkSQLDMDHFRSLLSPRTRLVSLVHVSNVLGCVLDT 195
Cdd:cd06453 81 LGRAN-KPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDD-GQLDLEALEKLLTERTKLVAVTHVSNVLGTINPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 196 AYVAEQARRVGAKLLLDCCQSVPHMPVDVCSLGADWIVASSHKFCGPSGVGFLWGRYDVLESMEPWMGGGEMIADVFLDQ 275
Cdd:cd06453 159 KEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMIEEVSFEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 276 STYAPPPMRFEAGTPAIAEAIGMGAAAEWLQQLGMDRVHAFEEEIGTYLYERLVAVsPRVTVYGPrpgaPRGRASLAAFN 355
Cdd:cd06453 239 TTYADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEI-PGVRVYGD----AEDRAGVVSFN 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 356 VEGLHATDVSTLLDMAGVAVRSGHHCAQPLHRELGVPASARASAYIYNTAAEIDTFIEAL 415
Cdd:cd06453 314 LEGIHPHDVATILDQYGIAVRAGHHCAQPLMRRLGVPGTVRASFGLYNTEEEIDALVEAL 373
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
18-415 |
1.94e-168 |
|
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: 486.67 E-value: 1.94e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 18 ALRAEFPILDQKVNGLPLVYLDNAATSQKPRAVLDALSRCYTEYNANVHRGVHALSAKATNEYEEARAKVAAFIGASTSR 97
Cdd:NF041166 229 AVRRDFPILQERVNGKPLVWFDNAATTQKPQAVIDRLSYFYEHENSNIHRAAHELAARATDAYEGAREKVRRFIGAPSVD 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 98 EVVIVRNATEGINLVSNTWGAANIKQGDEIILSVAEHHANLVPWQLLAARTGAVLRHVrltP--DKSQLDMDHFRSLLSP 175
Cdd:NF041166 309 EIIFVRGTTEAINLVAKSWGRQNIGAGDEIIVSHLEHHANIVPWQQLAQETGAKLRVI---PvdDSGQILLDEYAKLLNP 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 176 RTRLVSLVHVSNVLGCVLDTAYVAEQARRVGAKLLLDCCQSVPHMPVDVCSLGADWIVASSHKFCGPSGVGFLWGRYDVL 255
Cdd:NF041166 386 RTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGIGVVYGKRDLL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 256 ESMEPWMGGGEMIADVFLDQSTYAPPPMRFEAGTPAIAEAIGMGAAAEWLQQLGMDRVHAFEEEIGTYLYERLVAVSprv 335
Cdd:NF041166 466 EAMPPWQGGGNMIADVTFEKTVYQPAPNRFEAGTGNIADAVGLGAALDYVERIGIENIARYEHDLLEYATAGLAEVP--- 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 336 tvyGPRP-GAPRGRASLAAFNVEGLHATDVSTLLDMAGVAVRSGHHCAQPLHRELGVPASARASAYIYNTAAEIDTFIEA 414
Cdd:NF041166 543 ---GLRLiGTAADKASVLSFVLDGYSTEEVGKALNQEGIAVRSGHHCAQPILRRFGVEATVRPSLAFYNTCEEVDALVAV 619
|
.
gi 302843952 415 L 415
Cdd:NF041166 620 L 620
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
36-411 |
2.58e-166 |
|
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: 471.73 E-value: 2.58e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 36 VYLDNAATSQKPRAVLDALSRCYTEYNANVHRGVHALSAKATNEYEEARAKVAAFIGASTSREVVIVRNATEGINLVSNT 115
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 116 WGAAnIKQGDEIILSVAEHHANLVPWQLLAARTGAVLRHVRLTPDKSqLDMDHFRSLLSPRTRLVSLVHVSNVLGCVLDT 195
Cdd:pfam00266 81 LGRS-LKPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDEDGL-LDLDELEKLITPKTKLVAITHVSNVTGTIQPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 196 AYVAEQARRVGAKLLLDCCQSVPHMPVDVCSLGADWIVASSHKFCGPSGVGFLWGRYDVLESMEPWMGGGEMIADVFLDQ 275
Cdd:pfam00266 159 PEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGMIETVSLQE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 276 STYAPPPMRFEAGTPAIAEAIGMGAAAEWLQQLGMDRVHAFEEEIGTYLYERLVAvSPRVTVYGPRPgaprgRASLAAFN 355
Cdd:pfam00266 239 STFADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLS-LPGIRLYGPER-----RASIISFN 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 302843952 356 VEGLHATDVSTLLDMAGVAVRSGHHCAQPLHRELGVPASARASAYIYNTAAEIDTF 411
Cdd:pfam00266 313 FKGVHPHDVATLLDESGIAVRSGHHCAQPLMVRLGLGGTVRASFYIYNTQEDVDRL 368
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
3-427 |
0e+00 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 841.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 3 SPLPTPVPAQLALGAALRAEFPILDQKVNGLPLVYLDNAATSQKPRAVLDALSRCYTEYNANVHRGVHALSAKATNEYEE 82
Cdd:PLN02855 1 SSAPAASAASVSLGAETRPDFPILDQTVNGSKLVYLDNAATSQKPAAVLDALQDYYEEYNSNVHRGIHALSAKATDAYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 83 ARAKVAAFIGASTSREVVIVRNATEGINLVSNTWGAANIKQGDEIILSVAEHHANLVPWQLLAARTGAVLRHVRLTPDKS 162
Cdd:PLN02855 81 ARKKVAAFINASTSREIVFTRNATEAINLVAYTWGLANLKPGDEVILSVAEHHSNIVPWQLVAQKTGAVLKFVGLTPDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 163 qLDMDHFRSLLSPRTRLVSLVHVSNVLGCVLDTAYVAEQARRVGAKLLLDCCQSVPHMPVDVCSLGADWIVASSHKFCGP 242
Cdd:PLN02855 161 -LDVEQLKELLSEKTKLVATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 243 SGVGFLWGRYDVLESMEPWMGGGEMIADVFLDQSTYAPPPMRFEAGTPAIAEAIGMGAAAEWLQQLGMDRVHAFEEEIGT 322
Cdd:PLN02855 240 TGIGFLWGKSDLLESMPPFLGGGEMISDVFLDHSTYAPPPSRFEAGTPAIGEAIGLGAAIDYLSEIGMDRIHEYEVELGT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 323 YLYERLVAVsPRVTVYGPRPGAPRGRASLAAFNVEGLHATDVSTLLDMA-GVAVRSGHHCAQPLHRELGVPASARASAYI 401
Cdd:PLN02855 320 YLYEKLSSV-PGVRIYGPKPSEGVGRAALCAFNVEGIHPTDLSTFLDQQhGVAIRSGHHCAQPLHRYLGVNASARASLYF 398
|
410 420
....*....|....*....|....*.
gi 302843952 402 YNTAAEIDTFIEALKDTIKFFDDAHG 427
Cdd:PLN02855 399 YNTKEEVDAFIHALKDTIAFFSSFKG 424
|
|
| sufS |
TIGR01979 |
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine ... |
17-422 |
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: 611.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 17 AALRAEFPILDQKVNGLPLVYLDNAATSQKPRAVLDALSRCYTEYNANVHRGVHALSAKATNEYEEARAKVAAFIGASTS 96
Cdd:TIGR01979 1 KNIRADFPILKRKINGKPLVYLDSAATSQKPQQVIDAVAEYYRNSNANVHRGIHTLSVRATEAYEAVREKVAKFINAASD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 97 REVVIVRNATEGINLVSNTWGAANIKQGDEIILSVAEHHANLVPWQLLAARTGAVLRHVRLTPDkSQLDMDHFRSLLSPR 176
Cdd:TIGR01979 81 EEIVFTRGTTESINLVAYSWGDSNLKAGDEIVISEMEHHANIVPWQLLAERTGATLKFIPLDDD-GTLDLDDLEKLLTEK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 177 TRLVSLVHVSNVLGCVLDTAYVAEQARRVGAKLLLDCCQSVPHMPVDVCSLGADWIVASSHKFCGPSGVGFLWGRYDVLE 256
Cdd:TIGR01979 160 TKLVAITHVSNVLGTVNPVEEIAKLAHQVGAKVLVDGAQAVPHMPVDVQALDCDFYVFSGHKMYGPTGIGVLYGKEELLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 257 SMEPWMGGGEMIADVFLDQSTYAPPPMRFEAGTPAIAEAIGMGAAAEWLQQLGMDRVHAFEEEIGTYLYERLVAVsPRVT 336
Cdd:TIGR01979 240 QMPPFLGGGEMIAEVSFEETTYNEAPHKFEAGTPNIAGVIGLGAAIDYLEAIGLENIEAHEHELTAYALERLGEI-PGLR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 337 VYGPRPGAPRGraSLAAFNVEGLHATDVSTLLDMAGVAVRSGHHCAQPLHRELGVPASARASAYIYNTAAEIDTFIEALK 416
Cdd:TIGR01979 319 IYGPRDAEDRG--GIISFNVEGVHPHDVGTILDEEGIAVRSGHHCAQPLMRRFGVPATCRASFYIYNTEEDIDALVEALK 396
|
....*.
gi 302843952 417 DTIKFF 422
Cdd:TIGR01979 397 KVRKFF 402
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
17-421 |
0e+00 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 583.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 17 AALRAEFPildqkVNGLPLVYLDNAATSQKPRAVLDALSRCYTEYNANVHRGVHALSAKATNEYEEARAKVAAFIGASTS 96
Cdd:COG0520 3 EAIRADFP-----VLGKPLVYLDNAATGQKPRPVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAASP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 97 REVVIVRNATEGINLVSNTWGaaNIKQGDEIILSVAEHHANLVPWQLLAARTGAVLRHVRLTPDKsQLDMDHFRSLLSPR 176
Cdd:COG0520 78 DEIIFTRGTTEAINLVAYGLG--RLKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDG-ELDLEALEALLTPR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 177 TRLVSLVHVSNVLGCVLDTAYVAEQARRVGAKLLLDCCQSVPHMPVDVCSLGADWIVASSHKFCGPSGVGFLWGRYDVLE 256
Cdd:COG0520 155 TKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELLE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 257 SMEPWMGGGEMIADVFLDQSTYAPPPMRFEAGTPAIAEAIGMGAAAEWLQQLGMDRVHAFEEEIGTYLYERLVAVsPRVT 336
Cdd:COG0520 235 ALPPFLGGGGMIEWVSFDGTTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAI-PGVR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 337 VYGPRPgaPRGRASLAAFNVEGLHATDVSTLLDMAGVAVRSGHHCAQPLHRELGVPASARASAYIYNTAAEIDTFIEALK 416
Cdd:COG0520 314 ILGPAD--PEDRSGIVSFNVDGVHPHDVAALLDDEGIAVRAGHHCAQPLMRRLGVPGTVRASFHLYNTEEEIDRLVEALK 391
|
....*
gi 302843952 417 DTIKF 421
Cdd:COG0520 392 KLAEL 396
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
36-415 |
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: 575.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 36 VYLDNAATSQKPRAVLDALSRCYTEYNANVHRGVHALSAKATNEYEEARAKVAAFIGASTSREVVIVRNATEGINLVSNT 115
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINAPSPDEIIFTRNTTEAINLVAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 116 WGAANiKQGDEIILSVAEHHANLVPWQLLAARTGAVLRHVRLTPDkSQLDMDHFRSLLSPRTRLVSLVHVSNVLGCVLDT 195
Cdd:cd06453 81 LGRAN-KPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDD-GQLDLEALEKLLTERTKLVAVTHVSNVLGTINPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 196 AYVAEQARRVGAKLLLDCCQSVPHMPVDVCSLGADWIVASSHKFCGPSGVGFLWGRYDVLESMEPWMGGGEMIADVFLDQ 275
Cdd:cd06453 159 KEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMIEEVSFEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 276 STYAPPPMRFEAGTPAIAEAIGMGAAAEWLQQLGMDRVHAFEEEIGTYLYERLVAVsPRVTVYGPrpgaPRGRASLAAFN 355
Cdd:cd06453 239 TTYADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEI-PGVRVYGD----AEDRAGVVSFN 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 356 VEGLHATDVSTLLDMAGVAVRSGHHCAQPLHRELGVPASARASAYIYNTAAEIDTFIEAL 415
Cdd:cd06453 314 LEGIHPHDVATILDQYGIAVRAGHHCAQPLMRRLGVPGTVRASFGLYNTEEEIDALVEAL 373
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
18-415 |
1.94e-168 |
|
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: 486.67 E-value: 1.94e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 18 ALRAEFPILDQKVNGLPLVYLDNAATSQKPRAVLDALSRCYTEYNANVHRGVHALSAKATNEYEEARAKVAAFIGASTSR 97
Cdd:NF041166 229 AVRRDFPILQERVNGKPLVWFDNAATTQKPQAVIDRLSYFYEHENSNIHRAAHELAARATDAYEGAREKVRRFIGAPSVD 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 98 EVVIVRNATEGINLVSNTWGAANIKQGDEIILSVAEHHANLVPWQLLAARTGAVLRHVrltP--DKSQLDMDHFRSLLSP 175
Cdd:NF041166 309 EIIFVRGTTEAINLVAKSWGRQNIGAGDEIIVSHLEHHANIVPWQQLAQETGAKLRVI---PvdDSGQILLDEYAKLLNP 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 176 RTRLVSLVHVSNVLGCVLDTAYVAEQARRVGAKLLLDCCQSVPHMPVDVCSLGADWIVASSHKFCGPSGVGFLWGRYDVL 255
Cdd:NF041166 386 RTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGIGVVYGKRDLL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 256 ESMEPWMGGGEMIADVFLDQSTYAPPPMRFEAGTPAIAEAIGMGAAAEWLQQLGMDRVHAFEEEIGTYLYERLVAVSprv 335
Cdd:NF041166 466 EAMPPWQGGGNMIADVTFEKTVYQPAPNRFEAGTGNIADAVGLGAALDYVERIGIENIARYEHDLLEYATAGLAEVP--- 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 336 tvyGPRP-GAPRGRASLAAFNVEGLHATDVSTLLDMAGVAVRSGHHCAQPLHRELGVPASARASAYIYNTAAEIDTFIEA 414
Cdd:NF041166 543 ---GLRLiGTAADKASVLSFVLDGYSTEEVGKALNQEGIAVRSGHHCAQPILRRFGVEATVRPSLAFYNTCEEVDALVAV 619
|
.
gi 302843952 415 L 415
Cdd:NF041166 620 L 620
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
36-411 |
2.58e-166 |
|
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: 471.73 E-value: 2.58e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 36 VYLDNAATSQKPRAVLDALSRCYTEYNANVHRGVHALSAKATNEYEEARAKVAAFIGASTSREVVIVRNATEGINLVSNT 115
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 116 WGAAnIKQGDEIILSVAEHHANLVPWQLLAARTGAVLRHVRLTPDKSqLDMDHFRSLLSPRTRLVSLVHVSNVLGCVLDT 195
Cdd:pfam00266 81 LGRS-LKPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDEDGL-LDLDELEKLITPKTKLVAITHVSNVTGTIQPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 196 AYVAEQARRVGAKLLLDCCQSVPHMPVDVCSLGADWIVASSHKFCGPSGVGFLWGRYDVLESMEPWMGGGEMIADVFLDQ 275
Cdd:pfam00266 159 PEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGMIETVSLQE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 276 STYAPPPMRFEAGTPAIAEAIGMGAAAEWLQQLGMDRVHAFEEEIGTYLYERLVAvSPRVTVYGPRPgaprgRASLAAFN 355
Cdd:pfam00266 239 STFADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLS-LPGIRLYGPER-----RASIISFN 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 302843952 356 VEGLHATDVSTLLDMAGVAVRSGHHCAQPLHRELGVPASARASAYIYNTAAEIDTF 411
Cdd:pfam00266 313 FKGVHPHDVATLLDESGIAVRSGHHCAQPLMVRLGLGGTVRASFYIYNTQEDVDRL 368
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
20-416 |
1.76e-146 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 422.62 E-value: 1.76e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 20 RAEFPILDQKVNGLPLVYLDNAATSQKPRAVLDALSRCYTEYNANVHRGVHALSAKATNEYEEARAKVAAFIGASTSREV 99
Cdd:PRK09295 9 RADFPVLSREVNGLPLAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKQAALFINARSAEEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 100 VIVRNATEGINLVSNTWGAANIKQGDEIILSVAEHHANLVPWQLLAARTGAVLRHVRLTPDkSQLDMDHFRSLLSPRTRL 179
Cdd:PRK09295 89 VFVRGTTEGINLVANSWGNSNVRAGDNIIISEMEHHANIVPWQMLCARVGAELRVIPLNPD-GTLQLETLPALFDERTRL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 180 VSLVHVSNVLGCVLDTAYVAEQARRVGAKLLLDCCQSVPHMPVDVCSLGADWIVASSHKFCGPSGVGFLWGRYDVLESME 259
Cdd:PRK09295 168 LAITHVSNVLGTENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKEALLQEMP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 260 PWMGGGEMIADVFLDQ-STYAPPPMRFEAGTPAIAEAIGMGAAAEWLQQLGMDRVHAFEEEIGTYLYERLVAVsPRVTVY 338
Cdd:PRK09295 248 PWEGGGSMIATVSLTEgTTWAKAPWRFEAGTPNTGGIIGLGAALDYVSALGLNNIAEYEQNLMHYALSQLESV-PDLTLY 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 302843952 339 GprpgaPRGRASLAAFNVEGLHATDVSTLLDMAGVAVRSGHHCAQPLHRELGVPASARASAYIYNTAAEIDTFIEALK 416
Cdd:PRK09295 327 G-----PQNRLGVIAFNLGKHHAYDVGSFLDNYGIAVRTGHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVAGLQ 399
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
17-424 |
9.82e-120 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 354.34 E-value: 9.82e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 17 AALRAEFPILDQkvnglPLVYLDNAATSQKPRAVLDALSRCYTEYNANVHRGVHALSAKATNEYEEARAKVAAFIGASTS 96
Cdd:PRK10874 7 AQFRAQFPALQD-----AGVYLDSAATALKPQAVIEATQQFYSLSAGNVHRSQFAAAQRLTARYEAAREQVAQLLNAPDA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 97 REVVIVRNATEGINLVSNTWGAANIKQGDEIILSVAEHHANLVPWQLLAARTGAvlRHVRLTPDKSQL-DMDHFRSLLSP 175
Cdd:PRK10874 82 KNIVWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLVPWLMVAQQTGA--KVVKLPLGADRLpDVDLLPELITP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 176 RTRLVSLVHVSNVLGCVLDTAYVAEQARRVGAKLLLDCCQSVPHMPVDVCSLGADWIVASSHKFCGPSGVGFLWGRYDVL 255
Cdd:PRK10874 160 RTRILALGQMSNVTGGCPDLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKSELL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 256 ESMEPWMGGGEMIADVFLDQSTYAPPPMRFEAGTPAIAEAIGMGAAAEWLQQLGMDRVHAFEEEIGTYLYERLVAvsprv 335
Cdd:PRK10874 240 EAMSPWQGGGKMLTEVSFDGFTPQSAPWRFEAGTPNVAGVIGLSAALEWLADIDINQAESWSRSLATLAEDALAK----- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 336 tvygpRPGAPRGRA---SLAAFNVEGLHATDVSTLLDMAGVAVRSGHHCAQPLHRELGVPASARASAYIYNTAAEIDTFI 412
Cdd:PRK10874 315 -----LPGFRSFRCqdsSLLAFDFAGVHHSDLVTLLAEYGIALRAGQHCAQPLLAALGVTGTLRASFAPYNTQSDVDALV 389
|
410
....*....|..
gi 302843952 413 EALKDTIKFFDD 424
Cdd:PRK10874 390 NAVDRALELLVD 401
|
|
| FeS_syn_CsdA |
TIGR03392 |
cysteine desulfurase, catalytic subunit CsdA; Members of this protein family are CsdS. This ... |
17-424 |
7.21e-113 |
|
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: 336.81 E-value: 7.21e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 17 AALRAEFPILDQKvnglpLVYLDNAATSQKPRAVLDALSRCYTEYNANVHRGVHALSAKATNEYEEARAKVAAFIGASTS 96
Cdd:TIGR03392 4 AQFRRQFPALQDA-----TVYLDSAATALKPQAVIDATQQFYRLSSGTVHRSQHQEAQSLTARYEAAREQVAQLLNAPDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 97 REVVIVRNATEGINLVSNTWGAANIKQGDEIILSVAEHHANLVPWQLLAARTGAVLRHVRLTPDKSQlDMDHFRSLLSPR 176
Cdd:TIGR03392 79 ENIVWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLIPWLMVAQQTGAKVVKLPIGADLLP-DIDQLPELLTPR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 177 TRLVSLVHVSNVLGCVLDTAYVAEQARRVGAKLLLDCCQSVPHMPVDVCSLGADWIVASSHKFCGPSGVGFLWGRYDVLE 256
Cdd:TIGR03392 158 TRILALGQMSNVTGGCPDLARAITLAHQYGCVVVVDGAQGVVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKTELLE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 257 SMEPWMGGGEMIADVFLDQSTYAPPPMRFEAGTPAIAEAIGMGAAAEWLQQLGMDRVHAFEEEIGTYLYERLVAvsprvt 336
Cdd:TIGR03392 238 AMPPWQGGGKMLSHVSFDGFTPQAVPWRFEAGTPNIAGVIGLSAALEWLADIDINAAESWSVSLATLAEEALAQ------ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 337 vygpRPGAPRGR---ASLAAFNVEGLHATDVSTLLDMAGVAVRSGHHCAQPLHRELGVPASARASAYIYNTAAEIDTFIE 413
Cdd:TIGR03392 312 ----LPGFRSFRcqgSSLLAFDFAGVHHSDLVTLLAEQGIALRAGQHCAQPLMAALGVSGTLRASFAPYNTQQDVDALVN 387
|
410
....*....|.
gi 302843952 414 ALKDTIKFFDD 424
Cdd:TIGR03392 388 AVGRALELLVD 398
|
|
| am_tr_V_VC1184 |
TIGR01976 |
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of ... |
17-415 |
1.90e-76 |
|
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: 243.12 E-value: 1.90e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 17 AALRAEFPILDQKVnglpLVYLDNAATSQKPRAVLDALSRCYTEYNANvhRGVHALSAKATNEY-EEARAKVAAFIGAST 95
Cdd:TIGR01976 4 EAVRGQFPALADGD----RVFFDNPAGTQIPQSVADAVSAALTRSNAN--RGGAYESSRRADQVvDDAREAVADLLNADP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 96 SrEVVIVRNATEGINLVSNTWGAaNIKQGDEIILSVAEHHANLVPWQLLAARTGAVLRHVRLTPDKSQLDMDHFRSLLSP 175
Cdd:TIGR01976 78 P-EVVFGANATSLTFLLSRAISR-RWGPGDEVIVTRLDHEANISPWLQAAERAGAKVKWARVDEATGELHPDDLASLLSP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 176 RTRLVSLVHVSNVLGCVLDTAYVAEQARRVGAKLLLDCCQSVPHMPVDVCSLGADWIVASSHKFCGPSgVGFLWGRYDVL 255
Cdd:TIGR01976 156 RTRLVAVTAASNTLGSIVDLAAITELVHAAGALVVVDAVHYAPHGLIDVQATGADFLTCSAYKFFGPH-MGILWGRPELL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 256 ESMEPwmgggemiadvFLDQSTYAPPPMRFEAGTPAIAEAIGMGAAAEWLQQLG--------------MDRVHAFEEEIG 321
Cdd:TIGR01976 235 MNLPP-----------YKLTFSYDTGPERFELGTPQYELLAGVVAAVDYLAGLGesangsrrerlvasFQAIDAYENRLA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 322 TYLYERLVAVsPRVTVYGPRpgAPRGRASLAAFNVEGLHATDVSTLLDMAGVAVRSGHHCAQPLHRELGVPAS---ARAS 398
Cdd:TIGR01976 304 EYLLVGLSDL-PGVTLYGVA--RLAARVPTVSFTVHGLPPQRVVRRLADQGIDAWAGHFYAVRLLRRLGLNDEggvVRVG 380
|
410
....*....|....*..
gi 302843952 399 AYIYNTAAEIDTFIEAL 415
Cdd:TIGR01976 381 LAHYNTAEEVDRLLEAL 397
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
36-420 |
2.70e-62 |
|
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: 206.05 E-value: 2.70e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 36 VYLDNAATSQKPRAVLDALSRCYTEYNANVHRgVHALSAKATNEYEEARAKVAAFIGAStSREVVIVRNATEGINLVSNT 115
Cdd:COG1104 4 IYLDNAATTPVDPEVLEAMLPYLTEYFGNPSS-LHSFGREARAALEEAREQVAALLGAD-PEEIIFTSGGTEANNLAIKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 116 WGAANIKQGDEIILSVAEHHANLVPWQLLAARTGAVlrhVRLTPDKS-QLDMDHFRSLLSPRTRLVSLVHVSNVLGCVLD 194
Cdd:COG1104 82 AARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEV---TYLPVDEDgRVDLEALEAALRPDTALVSVMHANNETGTIQP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 195 TAYVAEQARRVGAKLLLDCCQSVPHMPVDVCSLGADWIVASSHKFCGPSGVGFLWGRYDVleSMEPWMGGGEMIADvfld 274
Cdd:COG1104 159 IAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRKGV--RLEPLIHGGGQERG---- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 275 qstyapppMRfeAGTPAIAEAIGMGAAAEWLQQlGMDRVHAFEEEIGTYLYERLVAVSPRVTVYGPR-PGAPrgraSLAA 353
Cdd:COG1104 233 --------LR--SGTENVPGIVGLGKAAELAAE-ELEEEAARLRALRDRLEEGLLAAIPGVVINGDPeNRLP----NTLN 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 302843952 354 FNVEGLHATDVSTLLDMAGVAVRSGHHCA----QPLH--RELGVPAsARASAYI------YNTAAEIDTFIEALKDTIK 420
Cdd:COG1104 298 FSFPGVEGEALLLALDLAGIAVSSGSACSsgslEPSHvlLAMGLDE-ELAHGSIrfslgrFTTEEEIDRAIEALKEIVA 375
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
36-409 |
6.74e-33 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 127.46 E-value: 6.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 36 VYLD-NAATSQKPRaVLDALSRCYTEYNANVHRGVHALSAKATNEYEEARAKVAAFIGAStSREVVIVRNATEGINLVSN 114
Cdd:PLN02651 1 LYLDmQATTPIDPR-VLDAMLPFLIEHFGNPHSRTHLYGWESEDAVEKARAQVAALIGAD-PKEIIFTSGATESNNLAIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 115 twGAANI--KQGDEIILSVAEHHANLvpwqllaartgAVLRH-------VRLTPDKSQ--LDMDHFRSLLSPRTRLVSLV 183
Cdd:PLN02651 79 --GVMHFykDKKKHVITTQTEHKCVL-----------DSCRHlqqegfeVTYLPVKSDglVDLDELAAAIRPDTALVSVM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 184 HVSNVLGCVLDTAYVAEQARRVGAKLLLDCCQSVPHMPVDVCSLGADWIVASSHKFCGPSGVGFLWGRYDVLESMEPWM- 262
Cdd:PLN02651 146 AVNNEIGVIQPVEEIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRLEPLMs 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 263 GGGEMIAdvfldqstyapppmrFEAGTPAIAEAIGMGAAAEWLQQlGMDRVHAFEEEIGTYLYERLVAVSPRVTVYGPRP 342
Cdd:PLN02651 226 GGGQERG---------------RRSGTENTPLVVGLGAACELAMK-EMDYDEKHMKALRERLLNGLRAKLGGVRVNGPRD 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 343 GAPR--GRASLAAFNVEGlhatdVSTLLDMAGVAVRSGHHC----AQPLH--RELGVP-----ASARASAYIYNTAAEID 409
Cdd:PLN02651 290 PEKRypGTLNLSFAYVEG-----ESLLMGLKEVAVSSGSACtsasLEPSYvlRALGVPeemahGSLRLGVGRFTTEEEVD 364
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
33-303 |
6.79e-26 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 108.49 E-value: 6.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 33 LPlVYLDNAATSQKPRAVLDALSRCYTEYN--ANVHRGVHALSAKATNEYEEARAKVAAFIGAStSREVVIVRNATEGIN 110
Cdd:PRK14012 3 LP-IYLDYSATTPVDPRVAEKMMPYLTMDGtfGNPASRSHRFGWQAEEAVDIARNQIADLIGAD-PREIVFTSGATESDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 111 LVSNtwGAANI--KQGDEIILSVAEHHANLVPWQLLAaRTGAVLRHvrLTPDKSQL-DMDHFRSLLSPRTRLVSLVHVSN 187
Cdd:PRK14012 81 LAIK--GAAHFyqKKGKHIITSKTEHKAVLDTCRQLE-REGFEVTY--LDPQSNGIiDLEKLEAAMRDDTILVSIMHVNN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 188 VLGCVLDTAYVAEQARRVGAKLLLDCCQSVPHMPVDVCSLGADWIVASSHKFCGPSGVGFLWGRYDVLESMEPWM-GGGE 266
Cdd:PRK14012 156 EIGVIQDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRLEAQMhGGGH 235
|
250 260 270
....*....|....*....|....*....|....*..
gi 302843952 267 MIAdvfldqstyapppMRfeAGTPAIAEAIGMGAAAE 303
Cdd:PRK14012 236 ERG-------------MR--SGTLPTHQIVGMGEAAR 257
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
35-339 |
3.59e-16 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 79.77 E-value: 3.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 35 LVYLDNAATSQKPRAVLDALSRCYTEYNANvHRGVHALSAKATNEYEEARAKVAAFIGAStSREVVIVRNATEGINLVSN 114
Cdd:PRK02948 1 MIYLDYAATTPMSKEALQTYQKAASQYFGN-ESSLHDIGGTASSLLQVCRKTFAEMIGGE-EQGIYFTSGGTESNYLAIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 115 TWGAANIKQGDEIILSVAEHHANLVPWQLLAARTGAVlrhVRLTPDKS-QLDMDHFRSLLSPRTRLVSLVHVSNVLGCVL 193
Cdd:PRK02948 79 SLLNALPQNKKHIITTPMEHASIHSYFQSLESQGYTV---TEIPVDKSgLIRLVDLERAITPDTVLASIQHANSEIGTIQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 194 DTAYVAEQARRVGAKLLLDCCQSVPHMPVDVCSLGADWIVASSHKFCGPSGVGFLWGRYDVlesmePWmgggEMIADVFL 273
Cdd:PRK02948 156 PIAEIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYINPQV-----RW----KPVFPGTT 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 302843952 274 DQSTyapppmrFEAGT---PAIAEAIgmgAAAEWLQQlGMDRVHAFEEEIGTYLYERLVAVSPRVTVYG 339
Cdd:PRK02948 227 HEKG-------FRPGTvnvPGIAAFL---TAAENILK-NMQEESLRFKELRSYFLEQIQTLPLPIEVEG 284
|
|
| SepCysS |
cd06452 |
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ... |
85-245 |
2.42e-10 |
|
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: 61.64 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 85 AKVAAFIGASTSRevvIVRNATEGINLVSNTWGaaniKQGDEIILSVAEHHANLVPwqllAARTGAVLRHV--------R 156
Cdd:cd06452 51 HDLAEFLGMDEAR---VTPGAREGKFAVMHSLC----EKGDWVVVDGLAHYTSYVA----AERAGLNVREVpntghpeyH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 157 LTPDKSQLDMDHFRSLLSPRTRLVSLVHVSNVLGCVLDTAYVAEQARRVGAKLLLDCCQSVPHMPVDVCSLGADWIVASS 236
Cdd:cd06452 120 ITPEGYAEVIEEVKDEFGKPPALALLTHVDGNYGNLHDAKKIAKVCHEYGVPLLLNGAYTVGRMPVSGKELGADFIVGSG 199
|
170
....*....|..
gi 302843952 237 HK---FCGPSGV 245
Cdd:cd06452 200 HKsmaASAPIGV 211
|
|
| PRK09331 |
PRK09331 |
Sep-tRNA:Cys-tRNA synthetase; Provisional |
87-245 |
8.80e-10 |
|
Sep-tRNA:Cys-tRNA synthetase; Provisional
Pssm-ID: 236469 Cd Length: 387 Bit Score: 59.94 E-value: 8.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 87 VAAFIGASTSRevvIVRNATEGINLVSNTWGaaniKQGDEIILSVAEHHANLVPwqllAARTGAVLRHV--------RLT 158
Cdd:PRK09331 72 LAEFLGMDEAR---VTHGAREGKFAVMHSLC----KKGDYVVLDGLAHYTSYVA----AERAGLNVREVpktgypeyKIT 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 159 PDKSQLDMDHFRSLLSPRTRLVSLVHVSNVLGCVLDTAYVAEQARRVGAKLLLDCCQSVPHMPVDVCSLGADWIVASSHK 238
Cdd:PRK09331 141 PEAYAEKIEEVKEETGKPPALALLTHVDGNYGNLADAKKVAKVAHEYGIPFLLNGAYTVGRMPVDGKKLGADFIVGSGHK 220
|
170
....*....|
gi 302843952 239 ---FCGPSGV 245
Cdd:PRK09331 221 smaASAPSGV 230
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
80-251 |
2.30e-09 |
|
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: 56.24 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 80 YEEARAKVAAFIGASTSReVVIVRNATEGINLVsnTWGAAniKQGDEIILSVAEHHANLVpwqLLAARTGAVLRHVRLTP 159
Cdd:cd01494 2 LEELEEKLARLLQPGNDK-AVFVPSGTGANEAA--LLALL--GPGDEVIVDANGHGSRYW---VAAELAGAKPVPVPVDD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 160 DKSQLD--MDHFRSLLSPRTRLVSLVHVSNVLGCVLDTAYVAEQARRVGAKLLLDCCQSVPHMPVDVCSL---GADWIVA 234
Cdd:cd01494 74 AGYGGLdvAILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIpegGADVVTF 153
|
170
....*....|....*..
gi 302843952 235 SSHKFCGPSGVGFLWGR 251
Cdd:cd01494 154 SLHKNLGGEGGGVVIVK 170
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
121-379 |
2.36e-07 |
|
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: 52.29 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 121 IKQGDEIILSVAEHHANLvpWQLLAARTGAVLRHVRLTPDKSqLDMDHFRSLLS-PRTRLVSLVHVSNVLGCVLDTAYVA 199
Cdd:cd06451 71 LEPGDKVLVGVNGVFGDR--WADMAERYGADVDVVEKPWGEA-VSPEEIAEALEqHDIKAVTLTHNETSTGVLNPLEGIG 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 200 EQARRVGAKLLLDCCQSVPHMPVDVCSLGADWIVASSHK-FCGPSGVGFL------WGRYDVLESMEPWmgggemiadvF 272
Cdd:cd06451 148 ALAKKHDALLIVDAVSSLGGEPFRMDEWGVDVAYTGSQKaLGAPPGLGPIafseraLERIKKKTKPKGF----------Y 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 273 LDQSTYAPPPMRFEA--GTPAIAEAIGMGAAAEWLQQLGMDRVHAFEEEIGTYLYERLVAV-----------SPRVTVYG 339
Cdd:cd06451 218 FDLLLLLKYWGEGYSypHTPPVNLLYALREALDLILEEGLENRWARHRRLAKALREGLEALglkllakpelrSPTVTAVL 297
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 302843952 340 PRPGAPRG---RASLAAFNVE---GLHATdvstlldmAGVAVRSGH 379
Cdd:cd06451 298 VPEGVDGDevvRRLMKRYNIEiagGLGPT--------AGKVFRIGH 335
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
77-217 |
1.87e-06 |
|
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.
Pssm-ID: 395827 Cd Length: 360 Bit Score: 49.59 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 77 TNEYEEArakVAAFIGAstsREVVIVRNATEGINLVSNtwgAANIKQGDEIILS----VAEHHAnlvpwqllAARTGAVL 152
Cdd:pfam01041 26 VREFERA---FAAYLGV---KHAIAVSSGTAALHLALR---ALGVGPGDEVITPsftfVATANA--------ALRLGAKP 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 302843952 153 RHVRLTPDKSQLDMDHFRSLLSPRTRLVSLVHvsnVLGCVLDTAYVAEQARRVGAKLLLDCCQSV 217
Cdd:pfam01041 89 VFVDIDPDTYNIDPEAIEAAITPRTKAIIPVH---LYGQPADMDAIRAIAARHGLPVIEDAAHAL 150
|
|
| AHBA_syn |
cd00616 |
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ... |
75-217 |
2.23e-05 |
|
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The members of this CD are involved in various biosynthetic pathways for secondary metabolites. Some well studied proteins in this CD are AHBA_synthase, protein product of pleiotropic regulatory gene degT, Arnb aminotransferase and pilin glycosylation protein. The prototype of this family, the AHBA_synthase, is a dimeric PLP dependent enzyme. AHBA_syn is the terminal enzyme of 3-amino-5-hydroxybenzoic acid (AHBA) formation which is involved in the biosynthesis of ansamycin antibiotics, including rifamycin B. Some members of this CD are involved in 4-amino-6-deoxy-monosaccharide D-perosamine synthesis. Perosamine is an important element in the glycosylation of several cell products, such as antibiotics and lipopolysaccharides of gram-positive and gram-negative bacteria. The pilin glycosylation protein encoded by gene pglA, is a galactosyltransferase involved in pilin glycosylation. Additionally, this CD consists of ArnB (PmrH) aminotransferase, a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme. This CD also consists of several predicted pyridoxal phosphate-dependent enzymes apparently involved in regulation of cell wall biogenesis. The catalytic lysine which is present in all characterized PLP dependent enzymes is replaced by histidine in some members of this CD.
Pssm-ID: 99740 [Multi-domain] Cd Length: 352 Bit Score: 46.38 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 75 KATNEYEEArakVAAFIGAstsREVVIVRNATEG--INLVsntwgAANIKQGDEIILS----VAEHHAnlvpwqllAART 148
Cdd:cd00616 18 PKVREFEKA---FAEYLGV---KYAVAVSSGTAAlhLALR-----ALGIGPGDEVIVPsftfVATANA--------ILLL 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 302843952 149 GAVLRHVRLTPDKSQLDMDHFRSLLSPRTRLVSLVHvsnVLGCVLDTAYVAEQARRVGAKLLLDCCQSV 217
Cdd:cd00616 79 GATPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVH---LYGNPADMDAIMAIAKRHGLPVIEDAAQAL 144
|
|
| PRK05994 |
PRK05994 |
O-acetylhomoserine aminocarboxypropyltransferase; Validated |
165-264 |
8.87e-05 |
|
O-acetylhomoserine aminocarboxypropyltransferase; Validated
Pssm-ID: 180344 [Multi-domain] Cd Length: 427 Bit Score: 44.70 E-value: 8.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 165 DMDHFRSLLSPRTRLVSLVHVSNVLGCVLDTAYVAEQARRVGAKLLLDCCQSVPHM--PVDvcsLGADWIVASSHKFCGP 242
Cdd:PRK05994 137 DPASFERAITPRTKAIFIESIANPGGTVTDIAAIAEVAHRAGLPLIVDNTLASPYLirPIE---HGADIVVHSLTKFLGG 213
|
90 100 110
....*....|....*....|....*....|....*
gi 302843952 243 SG--VG--------FLW---GRYDVLESMEPWMGG 264
Cdd:PRK05994 214 HGnsMGgiivdggtFDWsksGKYPMLSEPRPEYHG 248
|
|
| PRK06836 |
PRK06836 |
pyridoxal phosphate-dependent aminotransferase; |
47-180 |
1.10e-04 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180720 Cd Length: 394 Bit Score: 44.03 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 47 PRAVLDALSRCYTEYNANVHRGVHALSakatneYEEARAKVAAFIGAS-----TSREVVIVRNATEGINLVSNTWgaanI 121
Cdd:PRK06836 48 PAAVKEALRELAEEEDPGLHGYMPNAG------YPEVREAIAESLNRRfgtplTADHIVMTCGAAGALNVALKAI----L 117
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 302843952 122 KQGDEIILsVAEHhanLVPWQLLAARTGAVLRHVRLTPDKSQLDMDHFRSLLSPRTRLV 180
Cdd:PRK06836 118 NPGDEVIV-FAPY---FVEYRFYVDNHGGKLVVVPTDTDTFQPDLDALEAAITPKTKAV 172
|
|
| PRK07324 |
PRK07324 |
transaminase; Validated |
121-212 |
2.97e-04 |
|
transaminase; Validated
Pssm-ID: 235989 Cd Length: 373 Bit Score: 42.62 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 121 IKQGDEIIlSVAEHHANL--VPWQLlaartGAVLRHVRLTPDKSQL-DMDHFRSLLSPRTRLVSLVHVSNVLGCVLDTAY 197
Cdd:PRK07324 101 VEPGDHVI-SVYPTYQQLydIPESL-----GAEVDYWQLKEENGWLpDLDELRRLVRPNTKLICINNANNPTGALMDRAY 174
|
90
....*....|....*...
gi 302843952 198 ---VAEQARRVGAKLLLD 212
Cdd:PRK07324 175 leeIVEIARSVDAYVLSD 192
|
|
| PRK09082 |
PRK09082 |
methionine aminotransferase; Validated |
85-180 |
1.08e-03 |
|
methionine aminotransferase; Validated
Pssm-ID: 181642 [Multi-domain] Cd Length: 386 Bit Score: 41.05 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 85 AKVAAFIGASTS--REVVIVRNATEGINlvsnTWGAANIKQGDEIIlsVAE-HHANLVPWQLLAartGAVLRHVRLTPDK 161
Cdd:PRK09082 78 AKTARLYGRQYDadSEITVTAGATEALF----AAILALVRPGDEVI--VFDpSYDSYAPAIELA---GGRAVRVALQPPD 148
|
90
....*....|....*....
gi 302843952 162 SQLDMDHFRSLLSPRTRLV 180
Cdd:PRK09082 149 FRVDWQRFAAAISPRTRLI 167
|
|
| PRK07811 |
PRK07811 |
cystathionine gamma-synthase; Provisional |
165-241 |
1.31e-03 |
|
cystathionine gamma-synthase; Provisional
Pssm-ID: 236104 [Multi-domain] Cd Length: 388 Bit Score: 40.78 E-value: 1.31e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 302843952 165 DMDHFRSLLSPRTRLVSLVHVSNVLGCVLDTAYVAEQARRVGAKLLLDCCQSVPHM--PVdvcSLGADWIVASSHKFCG 241
Cdd:PRK07811 135 DLDAVRAAITPRTKLIWVETPTNPLLSITDIAALAELAHDAGAKVVVDNTFASPYLqqPL---ALGADVVVHSTTKYIG 210
|
|
| PMEI_like |
cd14859 |
pectin methylesterase inhibitor and related proteins; Pectin methylesterase (PME; ... |
37-98 |
3.03e-03 |
|
pectin methylesterase inhibitor and related proteins; Pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy class 8 of carbohydrate esterases) catalyzes the demethylesterification of homogalacturonans in the cell wall. Its activity is regulated by the proteinaceous PME inhibitor (PMEI) which inhibits PME and invertase through formation of a non-covalent 1:1 complex. Depending on the mode of demethylesterification, PMEI activity results in either loosening or rigidification of the cell wall. PMEI has been implicated in the regulation of fruit development, carbohydrate metabolism and cell wall extension. It may also be involved in inhibiting microbial pathogen PMEs. Thus, PMEI probably plays an important physiological role in PME regulation in plants, possessing several potential applications in a food-technological context. CIF (cell-wall inhibitor of beta-fructosidase from tobacco) is structurally similar to PMEI and these members are also included in this model. Comparison of the CIF/INV1 structure with the complex between PMEI/PME suggests a common targeting mechanism in PMEI and CIF. However, CIF and PMEI use distinct surface areas to selectively inhibit very different enzymatic scaffolds.
Pssm-ID: 275438 [Multi-domain] Cd Length: 140 Bit Score: 37.80 E-value: 3.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 302843952 37 YLDNAATSQKPRAVLDALSRCYTEYNANVHRGVHALSAKATNEYEEARAKV-AAFIGASTSRE 98
Cdd:cd14859 46 FIAKLLKSTKDPALKKALRDCADDYDDAVDDLEDAINALLSGDYDDAKTHVsAALDDADTCEE 108
|
|
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
77-216 |
3.78e-03 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 39.28 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 77 TNEYEEArakVAAFIGAstsREVVIVRNATEGINLvsnTWGAANIKQGDEIILS----VAEHHAnlvpwqllAARTGAVL 152
Cdd:COG0399 32 VKEFEEE---FAAYLGV---KHAVAVSSGTAALHL---ALRALGIGPGDEVITPaftfVATANA--------ILYVGATP 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 302843952 153 RHVRLTPDKSQLDMDHFRSLLSPRTRLVSLVHvsnVLGCVLDTAYVAEQARRVGAKLLLDCCQS 216
Cdd:COG0399 95 VFVDIDPDTYNIDPEALEAAITPRTKAIIPVH---LYGQPADMDAIMAIAKKHGLKVIEDAAQA 155
|
|
| PRK08912 |
PRK08912 |
aminotransferase; |
97-204 |
7.50e-03 |
|
aminotransferase;
Pssm-ID: 181580 Cd Length: 387 Bit Score: 38.42 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302843952 97 REVVIVRNATEGINlvsntwGA--ANIKQGDEIILSVAEHHANLVpwqlLAARTGAVLRHVRLTPDKSQLDMDHFRSLLS 174
Cdd:PRK08912 88 TEVMVTSGATEALA------AAllALVEPGDEVVLFQPLYDAYLP----LIRRAGGVPRLVRLEPPHWRLPRAALAAAFS 157
|
90 100 110
....*....|....*....|....*....|...
gi 302843952 175 PRTRLVSLVHVSNVLGCVL---DTAYVAEQARR 204
Cdd:PRK08912 158 PRTKAVLLNNPLNPAGKVFpreELALLAEFCQR 190
|
|
| PRK07504 |
PRK07504 |
O-succinylhomoserine sulfhydrylase; Reviewed |
164-238 |
9.05e-03 |
|
O-succinylhomoserine sulfhydrylase; Reviewed
Pssm-ID: 168979 [Multi-domain] Cd Length: 398 Bit Score: 38.20 E-value: 9.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 302843952 164 LDMDHFRSLLSPRTRLVSLVHVSNVLGCVLDTAYVAEQARRVGAKLLLDCCQSVP--HMPVDvcsLGADWIVASSHK 238
Cdd:PRK07504 138 LDLDNWEKAVRPNTKVFFLESPTNPTLEVIDIAAVAKIANQAGAKLVVDNVFATPlfQKPLE---LGAHIVVYSATK 211
|
|
| |
