|
Name |
Accession |
Description |
Interval |
E-value |
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
11-410 |
0e+00 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 593.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 11 DIARIRADFPilsqtVHGKKLVFLDSGASAQKPRAVIDAMVRSMETRYANVHRGLHWLSERASDDYEAARDKAAAFLNAA 90
Cdd:COG0520 1 DVEAIRADFP-----VLGKPLVYLDNAATGQKPRPVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 91 -REEIVFVRNATEGINLVAATFGRsaLRPGDAVVVSEMEHHANLVPWQMLRDSHGIELRIAKITDAGELDFADLERQFaD 169
Cdd:COG0520 76 sPDEIIFTRGTTEAINLVAYGLGR--LKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDGELDLEALEALL-T 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 170 GRVRLLAITHMSNVLGTYTPAERLAAFAHERGARLLLDGAQAVVHRAVDVRAIDADFYVFSGHKLYGPSGIGVLFGKREL 249
Cdd:COG0520 153 PRTKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKREL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 250 LDAMPPFLGGGDMIRSVSYEKSTWAEPPYRFEAGTPAIVEAVGLAAAIDYVNAIGFPAIASHERALTDHALATLDAIGGV 329
Cdd:COG0520 233 LEALPPFLGGGGMIEWVSFDGTTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAIPGV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 330 HVVGRA--QDRGGVVAFTMDGVHAHDVATLLDKQGIAVRAGHHCAEPLTRRLGLDSTARATFGVYTTMEEIDALAAGLRR 407
Cdd:COG0520 313 RILGPAdpEDRSGIVSFNVDGVHPHDVAALLDDEGIAVRAGHHCAQPLMRRLGVPGTVRASFHLYNTEEEIDRLVEALKK 392
|
...
gi 737201594 408 VQQ 410
Cdd:COG0520 393 LAE 395
|
|
| sufS |
TIGR01979 |
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine ... |
13-413 |
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: 585.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 13 ARIRADFPILSQTVHGKKLVFLDSGASAQKPRAVIDAMVRSMETRYANVHRGLHWLSERASDDYEAARDKAAAFLNAA-R 91
Cdd:TIGR01979 1 KNIRADFPILKRKINGKPLVYLDSAATSQKPQQVIDAVAEYYRNSNANVHRGIHTLSVRATEAYEAVREKVAKFINAAsD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 92 EEIVFVRNATEGINLVAATFGRSALRPGDAVVVSEMEHHANLVPWQMLRDSHGIELRIAKITDAGELDFADLERQFADgR 171
Cdd:TIGR01979 81 EEIVFTRGTTESINLVAYSWGDSNLKAGDEIVISEMEHHANIVPWQLLAERTGATLKFIPLDDDGTLDLDDLEKLLTE-K 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 172 VRLLAITHMSNVLGTYTPAERLAAFAHERGARLLLDGAQAVVHRAVDVRAIDADFYVFSGHKLYGPSGIGVLFGKRELLD 251
Cdd:TIGR01979 160 TKLVAITHVSNVLGTVNPVEEIAKLAHQVGAKVLVDGAQAVPHMPVDVQALDCDFYVFSGHKMYGPTGIGVLYGKEELLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 252 AMPPFLGGGDMIRSVSYEKSTWAEPPYRFEAGTPAIVEAVGLAAAIDYVNAIGFPAIASHERALTDHALATLDAIGGVHV 331
Cdd:TIGR01979 240 QMPPFLGGGEMIAEVSFEETTYNEAPHKFEAGTPNIAGVIGLGAAIDYLEAIGLENIEAHEHELTAYALERLGEIPGLRI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 332 VG--RAQDRGGVVAFTMDGVHAHDVATLLDKQGIAVRAGHHCAEPLTRRLGLDSTARATFGVYTTMEEIDALAAGLRRVQ 409
Cdd:TIGR01979 320 YGprDAEDRGGIISFNVEGVHPHDVGTILDEEGIAVRSGHHCAQPLMRRFGVPATCRASFYIYNTEEDIDALVEALKKVR 399
|
....
gi 737201594 410 QVFG 413
Cdd:TIGR01979 400 KFFG 403
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
32-405 |
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: 581.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 32 VFLDSGASAQKPRAVIDAMVRSMETRYANVHRGLHWLSERASDDYEAARDKAAAFLNAA-REEIVFVRNATEGINLVAAT 110
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINAPsPDEIIFTRNTTEAINLVAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 111 FGRsALRPGDAVVVSEMEHHANLVPWQMLRDSHGIELRIAKITDAGELDFADLERQFADgRVRLLAITHMSNVLGTYTPA 190
Cdd:cd06453 81 LGR-ANKPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTE-RTKLVAVTHVSNVLGTINPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 191 ERLAAFAHERGARLLLDGAQAVVHRAVDVRAIDADFYVFSGHKLYGPSGIGVLFGKRELLDAMPPFLGGGDMIRSVSYEK 270
Cdd:cd06453 159 KEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMIEEVSFEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 271 STWAEPPYRFEAGTPAIVEAVGLAAAIDYVNAIGFPAIASHERALTDHALATLDAIGGVHVVGRAQDRGGVVAFTMDGVH 350
Cdd:cd06453 239 TTYADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEIPGVRVYGDAEDRAGVVSFNLEGIH 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 737201594 351 AHDVATLLDKQGIAVRAGHHCAEPLTRRLGLDSTARATFGVYTTMEEIDALAAGL 405
Cdd:cd06453 319 PHDVATILDQYGIAVRAGHHCAQPLMRRLGVPGTVRASFGLYNTEEEIDALVEAL 373
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
3-407 |
2.08e-177 |
|
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: 508.63 E-value: 2.08e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 3 AAIEQPGFDIARIRADFPILSQTVHGKKLVFLDSGASAQKPRAVIDAMVRSMETRYANVHRGLHWLSERASDDYEAARDK 82
Cdd:NF041166 218 LASAHPPFDVNAVRRDFPILQERVNGKPLVWFDNAATTQKPQAVIDRLSYFYEHENSNIHRAAHELAARATDAYEGAREK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 83 AAAFLNAAR-EEIVFVRNATEGINLVAATFGRSALRPGDAVVVSEMEHHANLVPWQMLRDSHGIELRIAKITDAGELDFA 161
Cdd:NF041166 298 VRRFIGAPSvDEIIFVRGTTEAINLVAKSWGRQNIGAGDEIIVSHLEHHANIVPWQQLAQETGAKLRVIPVDDSGQILLD 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 162 DLERQFADgRVRLLAITHMSNVLGTYTPAERLAAFAHERGARLLLDGAQAVVHRAVDVRAIDADFYVFSGHKLYGPSGIG 241
Cdd:NF041166 378 EYAKLLNP-RTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGIG 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 242 VLFGKRELLDAMPPFLGGGDMIRSVSYEKSTWAEPPYRFEAGTPAIVEAVGLAAAIDYVNAIGFPAIASHERALTDHALA 321
Cdd:NF041166 457 VVYGKRDLLEAMPPWQGGGNMIADVTFEKTVYQPAPNRFEAGTGNIADAVGLGAALDYVERIGIENIARYEHDLLEYATA 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 322 TLDAIGGVHVVGRAQDRGGVVAFTMDGVHAHDVATLLDKQGIAVRAGHHCAEPLTRRLGLDSTARATFGVYTTMEEIDAL 401
Cdd:NF041166 537 GLAEVPGLRLIGTAADKASVLSFVLDGYSTEEVGKALNQEGIAVRSGHHCAQPILRRFGVEATVRPSLAFYNTCEEVDAL 616
|
....*.
gi 737201594 402 AAGLRR 407
Cdd:NF041166 617 VAVLRR 622
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
13-405 |
1.28e-170 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 484.25 E-value: 1.28e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 13 ARIRADFPILSQTVHGKKLVFLDSGASAQKPRAVIDAMVRSMETRYANVHRGLHWLSERASDDYEAARDKAAAFLNAA-R 91
Cdd:PLN02855 15 AETRPDFPILDQTVNGSKLVYLDNAATSQKPAAVLDALQDYYEEYNSNVHRGIHALSAKATDAYELARKKVAAFINAStS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 92 EEIVFVRNATEGINLVAATFGRSALRPGDAVVVSEMEHHANLVPWQMLRDSHGIELRIAKITDAGELDFADLeRQFADGR 171
Cdd:PLN02855 95 REIVFTRNATEAINLVAYTWGLANLKPGDEVILSVAEHHSNIVPWQLVAQKTGAVLKFVGLTPDEVLDVEQL-KELLSEK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 172 VRLLAITHMSNVLGTYTPAERLAAFAHERGARLLLDGAQAVVHRAVDVRAIDADFYVFSGHKLYGPSGIGVLFGKRELLD 251
Cdd:PLN02855 174 TKLVATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLWGKSDLLE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 252 AMPPFLGGGDMIRSVSYEKSTWAEPPYRFEAGTPAIVEAVGLAAAIDYVNAIGFPAIASHERALTDHALATLDAIGGVHV 331
Cdd:PLN02855 254 SMPPFLGGGEMISDVFLDHSTYAPPPSRFEAGTPAIGEAIGLGAAIDYLSEIGMDRIHEYEVELGTYLYEKLSSVPGVRI 333
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 737201594 332 VG----RAQDRGGVVAFTMDGVHAHDVATLLDKQ-GIAVRAGHHCAEPLTRRLGLDSTARATFGVYTTMEEIDALAAGL 405
Cdd:PLN02855 334 YGpkpsEGVGRAALCAFNVEGIHPTDLSTFLDQQhGVAIRSGHHCAQPLHRYLGVNASARASLYFYNTKEEVDAFIHAL 412
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
32-401 |
3.13e-167 |
|
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: 473.27 E-value: 3.13e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 32 VFLDSGASAQKPRAVIDAMVRSMETRYANVHRGLHWLSERASDDYEAARDKAAAFLNAA-REEIVFVRNATEGINLVAAT 110
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPsNDEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 111 FGRSaLRPGDAVVVSEMEHHANLVPWQMLRDSHGIELRIAKITDAGELDFADLERQFADgRVRLLAITHMSNVLGTYTPA 190
Cdd:pfam00266 81 LGRS-LKPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLITP-KTKLVAITHVSNVTGTIQPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 191 ERLAAFAHERGARLLLDGAQAVVHRAVDVRAIDADFYVFSGHKLYGPSGIGVLFGKRELLDAMPPFLGGGDMIRSVSYEK 270
Cdd:pfam00266 159 PEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGMIETVSLQE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 271 STWAEPPYRFEAGTPAIVEAVGLAAAIDYVNAIGFPAIASHERALTDHALATLDAIGGVHVVGrAQDRGGVVAFTMDGVH 350
Cdd:pfam00266 239 STFADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYG-PERRASIISFNFKGVH 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 737201594 351 AHDVATLLDKQGIAVRAGHHCAEPLTRRLGLDSTARATFGVYTTMEEIDAL 401
Cdd:pfam00266 318 PHDVATLLDESGIAVRSGHHCAQPLMVRLGLGGTVRASFYIYNTQEDVDRL 368
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
11-410 |
0e+00 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 593.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 11 DIARIRADFPilsqtVHGKKLVFLDSGASAQKPRAVIDAMVRSMETRYANVHRGLHWLSERASDDYEAARDKAAAFLNAA 90
Cdd:COG0520 1 DVEAIRADFP-----VLGKPLVYLDNAATGQKPRPVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 91 -REEIVFVRNATEGINLVAATFGRsaLRPGDAVVVSEMEHHANLVPWQMLRDSHGIELRIAKITDAGELDFADLERQFaD 169
Cdd:COG0520 76 sPDEIIFTRGTTEAINLVAYGLGR--LKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDGELDLEALEALL-T 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 170 GRVRLLAITHMSNVLGTYTPAERLAAFAHERGARLLLDGAQAVVHRAVDVRAIDADFYVFSGHKLYGPSGIGVLFGKREL 249
Cdd:COG0520 153 PRTKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKREL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 250 LDAMPPFLGGGDMIRSVSYEKSTWAEPPYRFEAGTPAIVEAVGLAAAIDYVNAIGFPAIASHERALTDHALATLDAIGGV 329
Cdd:COG0520 233 LEALPPFLGGGGMIEWVSFDGTTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAIPGV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 330 HVVGRA--QDRGGVVAFTMDGVHAHDVATLLDKQGIAVRAGHHCAEPLTRRLGLDSTARATFGVYTTMEEIDALAAGLRR 407
Cdd:COG0520 313 RILGPAdpEDRSGIVSFNVDGVHPHDVAALLDDEGIAVRAGHHCAQPLMRRLGVPGTVRASFHLYNTEEEIDRLVEALKK 392
|
...
gi 737201594 408 VQQ 410
Cdd:COG0520 393 LAE 395
|
|
| sufS |
TIGR01979 |
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine ... |
13-413 |
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: 585.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 13 ARIRADFPILSQTVHGKKLVFLDSGASAQKPRAVIDAMVRSMETRYANVHRGLHWLSERASDDYEAARDKAAAFLNAA-R 91
Cdd:TIGR01979 1 KNIRADFPILKRKINGKPLVYLDSAATSQKPQQVIDAVAEYYRNSNANVHRGIHTLSVRATEAYEAVREKVAKFINAAsD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 92 EEIVFVRNATEGINLVAATFGRSALRPGDAVVVSEMEHHANLVPWQMLRDSHGIELRIAKITDAGELDFADLERQFADgR 171
Cdd:TIGR01979 81 EEIVFTRGTTESINLVAYSWGDSNLKAGDEIVISEMEHHANIVPWQLLAERTGATLKFIPLDDDGTLDLDDLEKLLTE-K 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 172 VRLLAITHMSNVLGTYTPAERLAAFAHERGARLLLDGAQAVVHRAVDVRAIDADFYVFSGHKLYGPSGIGVLFGKRELLD 251
Cdd:TIGR01979 160 TKLVAITHVSNVLGTVNPVEEIAKLAHQVGAKVLVDGAQAVPHMPVDVQALDCDFYVFSGHKMYGPTGIGVLYGKEELLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 252 AMPPFLGGGDMIRSVSYEKSTWAEPPYRFEAGTPAIVEAVGLAAAIDYVNAIGFPAIASHERALTDHALATLDAIGGVHV 331
Cdd:TIGR01979 240 QMPPFLGGGEMIAEVSFEETTYNEAPHKFEAGTPNIAGVIGLGAAIDYLEAIGLENIEAHEHELTAYALERLGEIPGLRI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 332 VG--RAQDRGGVVAFTMDGVHAHDVATLLDKQGIAVRAGHHCAEPLTRRLGLDSTARATFGVYTTMEEIDALAAGLRRVQ 409
Cdd:TIGR01979 320 YGprDAEDRGGIISFNVEGVHPHDVGTILDEEGIAVRSGHHCAQPLMRRFGVPATCRASFYIYNTEEDIDALVEALKKVR 399
|
....
gi 737201594 410 QVFG 413
Cdd:TIGR01979 400 KFFG 403
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
32-405 |
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: 581.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 32 VFLDSGASAQKPRAVIDAMVRSMETRYANVHRGLHWLSERASDDYEAARDKAAAFLNAA-REEIVFVRNATEGINLVAAT 110
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINAPsPDEIIFTRNTTEAINLVAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 111 FGRsALRPGDAVVVSEMEHHANLVPWQMLRDSHGIELRIAKITDAGELDFADLERQFADgRVRLLAITHMSNVLGTYTPA 190
Cdd:cd06453 81 LGR-ANKPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTE-RTKLVAVTHVSNVLGTINPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 191 ERLAAFAHERGARLLLDGAQAVVHRAVDVRAIDADFYVFSGHKLYGPSGIGVLFGKRELLDAMPPFLGGGDMIRSVSYEK 270
Cdd:cd06453 159 KEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMIEEVSFEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 271 STWAEPPYRFEAGTPAIVEAVGLAAAIDYVNAIGFPAIASHERALTDHALATLDAIGGVHVVGRAQDRGGVVAFTMDGVH 350
Cdd:cd06453 239 TTYADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEIPGVRVYGDAEDRAGVVSFNLEGIH 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 737201594 351 AHDVATLLDKQGIAVRAGHHCAEPLTRRLGLDSTARATFGVYTTMEEIDALAAGL 405
Cdd:cd06453 319 PHDVATILDQYGIAVRAGHHCAQPLMRRLGVPGTVRASFGLYNTEEEIDALVEAL 373
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
3-407 |
2.08e-177 |
|
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: 508.63 E-value: 2.08e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 3 AAIEQPGFDIARIRADFPILSQTVHGKKLVFLDSGASAQKPRAVIDAMVRSMETRYANVHRGLHWLSERASDDYEAARDK 82
Cdd:NF041166 218 LASAHPPFDVNAVRRDFPILQERVNGKPLVWFDNAATTQKPQAVIDRLSYFYEHENSNIHRAAHELAARATDAYEGAREK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 83 AAAFLNAAR-EEIVFVRNATEGINLVAATFGRSALRPGDAVVVSEMEHHANLVPWQMLRDSHGIELRIAKITDAGELDFA 161
Cdd:NF041166 298 VRRFIGAPSvDEIIFVRGTTEAINLVAKSWGRQNIGAGDEIIVSHLEHHANIVPWQQLAQETGAKLRVIPVDDSGQILLD 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 162 DLERQFADgRVRLLAITHMSNVLGTYTPAERLAAFAHERGARLLLDGAQAVVHRAVDVRAIDADFYVFSGHKLYGPSGIG 241
Cdd:NF041166 378 EYAKLLNP-RTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGIG 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 242 VLFGKRELLDAMPPFLGGGDMIRSVSYEKSTWAEPPYRFEAGTPAIVEAVGLAAAIDYVNAIGFPAIASHERALTDHALA 321
Cdd:NF041166 457 VVYGKRDLLEAMPPWQGGGNMIADVTFEKTVYQPAPNRFEAGTGNIADAVGLGAALDYVERIGIENIARYEHDLLEYATA 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 322 TLDAIGGVHVVGRAQDRGGVVAFTMDGVHAHDVATLLDKQGIAVRAGHHCAEPLTRRLGLDSTARATFGVYTTMEEIDAL 401
Cdd:NF041166 537 GLAEVPGLRLIGTAADKASVLSFVLDGYSTEEVGKALNQEGIAVRSGHHCAQPILRRFGVEATVRPSLAFYNTCEEVDAL 616
|
....*.
gi 737201594 402 AAGLRR 407
Cdd:NF041166 617 VAVLRR 622
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
13-405 |
1.28e-170 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 484.25 E-value: 1.28e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 13 ARIRADFPILSQTVHGKKLVFLDSGASAQKPRAVIDAMVRSMETRYANVHRGLHWLSERASDDYEAARDKAAAFLNAA-R 91
Cdd:PLN02855 15 AETRPDFPILDQTVNGSKLVYLDNAATSQKPAAVLDALQDYYEEYNSNVHRGIHALSAKATDAYELARKKVAAFINAStS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 92 EEIVFVRNATEGINLVAATFGRSALRPGDAVVVSEMEHHANLVPWQMLRDSHGIELRIAKITDAGELDFADLeRQFADGR 171
Cdd:PLN02855 95 REIVFTRNATEAINLVAYTWGLANLKPGDEVILSVAEHHSNIVPWQLVAQKTGAVLKFVGLTPDEVLDVEQL-KELLSEK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 172 VRLLAITHMSNVLGTYTPAERLAAFAHERGARLLLDGAQAVVHRAVDVRAIDADFYVFSGHKLYGPSGIGVLFGKRELLD 251
Cdd:PLN02855 174 TKLVATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLWGKSDLLE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 252 AMPPFLGGGDMIRSVSYEKSTWAEPPYRFEAGTPAIVEAVGLAAAIDYVNAIGFPAIASHERALTDHALATLDAIGGVHV 331
Cdd:PLN02855 254 SMPPFLGGGEMISDVFLDHSTYAPPPSRFEAGTPAIGEAIGLGAAIDYLSEIGMDRIHEYEVELGTYLYEKLSSVPGVRI 333
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 737201594 332 VG----RAQDRGGVVAFTMDGVHAHDVATLLDKQ-GIAVRAGHHCAEPLTRRLGLDSTARATFGVYTTMEEIDALAAGL 405
Cdd:PLN02855 334 YGpkpsEGVGRAALCAFNVEGIHPTDLSTFLDQQhGVAIRSGHHCAQPLHRYLGVNASARASLYFYNTKEEVDAFIHAL 412
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
10-413 |
1.43e-170 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 483.10 E-value: 1.43e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 10 FDIARIRADFPILSQTVHGKKLVFLDSGASAQKPRAVIDAMVRSMETRYANVHRGLHWLSERASDDYEAARDKAAAFLNA 89
Cdd:PRK09295 3 FSVEKVRADFPVLSREVNGLPLAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKQAALFINA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 90 AR-EEIVFVRNATEGINLVAATFGRSALRPGDAVVVSEMEHHANLVPWQMLRDSHGIELRIAKITDAGELDFADLERQFa 168
Cdd:PRK09295 83 RSaEELVFVRGTTEGINLVANSWGNSNVRAGDNIIISEMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPALF- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 169 DGRVRLLAITHMSNVLGTYTPAERLAAFAHERGARLLLDGAQAVVHRAVDVRAIDADFYVFSGHKLYGPSGIGVLFGKRE 248
Cdd:PRK09295 162 DERTRLLAITHVSNVLGTENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKEA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 249 LLDAMPPFLGGGDMIRSVSY-EKSTWAEPPYRFEAGTPAIVEAVGLAAAIDYVNAIGFPAIASHERALTDHALATLDAIG 327
Cdd:PRK09295 242 LLQEMPPWEGGGSMIATVSLtEGTTWAKAPWRFEAGTPNTGGIIGLGAALDYVSALGLNNIAEYEQNLMHYALSQLESVP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 328 GVHVVGRAQdRGGVVAFTMDGVHAHDVATLLDKQGIAVRAGHHCAEPLTRRLGLDSTARATFGVYTTMEEIDALAAGLRR 407
Cdd:PRK09295 322 DLTLYGPQN-RLGVIAFNLGKHHAYDVGSFLDNYGIAVRTGHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVAGLQR 400
|
....*.
gi 737201594 408 VQQVFG 413
Cdd:PRK09295 401 IHRLLG 406
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
32-401 |
3.13e-167 |
|
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: 473.27 E-value: 3.13e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 32 VFLDSGASAQKPRAVIDAMVRSMETRYANVHRGLHWLSERASDDYEAARDKAAAFLNAA-REEIVFVRNATEGINLVAAT 110
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPsNDEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 111 FGRSaLRPGDAVVVSEMEHHANLVPWQMLRDSHGIELRIAKITDAGELDFADLERQFADgRVRLLAITHMSNVLGTYTPA 190
Cdd:pfam00266 81 LGRS-LKPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLITP-KTKLVAITHVSNVTGTIQPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 191 ERLAAFAHERGARLLLDGAQAVVHRAVDVRAIDADFYVFSGHKLYGPSGIGVLFGKRELLDAMPPFLGGGDMIRSVSYEK 270
Cdd:pfam00266 159 PEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGMIETVSLQE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 271 STWAEPPYRFEAGTPAIVEAVGLAAAIDYVNAIGFPAIASHERALTDHALATLDAIGGVHVVGrAQDRGGVVAFTMDGVH 350
Cdd:pfam00266 239 STFADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYG-PERRASIISFNFKGVH 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 737201594 351 AHDVATLLDKQGIAVRAGHHCAEPLTRRLGLDSTARATFGVYTTMEEIDAL 401
Cdd:pfam00266 318 PHDVATLLDESGIAVRSGHHCAQPLMVRLGLGGTVRASFYIYNTQEDVDRL 368
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
10-407 |
7.26e-132 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 384.78 E-value: 7.26e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 10 FDIARIRADFPILSQtvhgkKLVFLDSGASAQKPRAVIDAMVRSMETRYANVHRGLHWLSERASDDYEAARDKAAAFLNA 89
Cdd:PRK10874 4 FNPAQFRAQFPALQD-----AGVYLDSAATALKPQAVIEATQQFYSLSAGNVHRSQFAAAQRLTARYEAAREQVAQLLNA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 90 AREE-IVFVRNATEGINLVAATFGRSALRPGDAVVVSEMEHHANLVPWQMLRDSHGIelRIAKI-TDAGELdfADLER-- 165
Cdd:PRK10874 79 PDAKnIVWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLVPWLMVAQQTGA--KVVKLpLGADRL--PDVDLlp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 166 QFADGRVRLLAITHMSNVLGTYTPAERLAAFAHERGARLLLDGAQAVVHRAVDVRAIDADFYVFSGHKLYGPSGIGVLFG 245
Cdd:PRK10874 155 ELITPRTRILALGQMSNVTGGCPDLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 246 KRELLDAMPPFLGGGDMIRSVSYEKSTWAEPPYRFEAGTPAIVEAVGLAAAIDYVNAIGFPAIASHERALTDHALATLDA 325
Cdd:PRK10874 235 KSELLEAMSPWQGGGKMLTEVSFDGFTPQSAPWRFEAGTPNVAGVIGLSAALEWLADIDINQAESWSRSLATLAEDALAK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 326 IGGVHVVgRAQDrGGVVAFTMDGVHAHDVATLLDKQGIAVRAGHHCAEPLTRRLGLDSTARATFGVYTTMEEIDALAAGL 405
Cdd:PRK10874 315 LPGFRSF-RCQD-SSLLAFDFAGVHHSDLVTLLAEYGIALRAGQHCAQPLLAALGVTGTLRASFAPYNTQSDVDALVNAV 392
|
..
gi 737201594 406 RR 407
Cdd:PRK10874 393 DR 394
|
|
| FeS_syn_CsdA |
TIGR03392 |
cysteine desulfurase, catalytic subunit CsdA; Members of this protein family are CsdS. This ... |
10-412 |
2.85e-121 |
|
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: 357.61 E-value: 2.85e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 10 FDIARIRADFPILSQtvhgkKLVFLDSGASAQKPRAVIDAMVRSMETRYANVHRGLHWLSERASDDYEAARDKAAAFLNA 89
Cdd:TIGR03392 1 FNPAQFRRQFPALQD-----ATVYLDSAATALKPQAVIDATQQFYRLSSGTVHRSQHQEAQSLTARYEAAREQVAQLLNA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 90 AR-EEIVFVRNATEGINLVAATFGRSALRPGDAVVVSEMEHHANLVPWQMLRDSHGIelRIAKI-TDAGELDFADLERQF 167
Cdd:TIGR03392 76 PDaENIVWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLIPWLMVAQQTGA--KVVKLpIGADLLPDIDQLPEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 168 ADGRVRLLAITHMSNVLGTYTPAERLAAFAHERGARLLLDGAQAVVHRAVDVRAIDADFYVFSGHKLYGPSGIGVLFGKR 247
Cdd:TIGR03392 154 LTPRTRILALGQMSNVTGGCPDLARAITLAHQYGCVVVVDGAQGVVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 248 ELLDAMPPFLGGGDMIRSVSYEKSTWAEPPYRFEAGTPAIVEAVGLAAAIDYVNAIGFPAIASHERALTDHALATLDAIG 327
Cdd:TIGR03392 234 ELLEAMPPWQGGGKMLSHVSFDGFTPQAVPWRFEAGTPNIAGVIGLSAALEWLADIDINAAESWSVSLATLAEEALAQLP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 328 GVHVVgRAQDrGGVVAFTMDGVHAHDVATLLDKQGIAVRAGHHCAEPLTRRLGLDSTARATFGVYTTMEEIDALAAGLRR 407
Cdd:TIGR03392 314 GFRSF-RCQG-SSLLAFDFAGVHHSDLVTLLAEQGIALRAGQHCAQPLMAALGVSGTLRASFAPYNTQQDVDALVNAVGR 391
|
....*
gi 737201594 408 VQQVF 412
Cdd:TIGR03392 392 ALELL 396
|
|
| am_tr_V_VC1184 |
TIGR01976 |
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of ... |
10-405 |
4.71e-78 |
|
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: 246.97 E-value: 4.71e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 10 FDIARIRADFPILSQTVhgkkLVFLDSGASAQKPRAVIDAMVRSMeTRYaNVHRGLHWLSERASDDY-EAARDKAAAFLN 88
Cdd:TIGR01976 1 FDVEAVRGQFPALADGD----RVFFDNPAGTQIPQSVADAVSAAL-TRS-NANRGGAYESSRRADQVvDDAREAVADLLN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 89 AAREEIVFVRNATEGINLVAATFGRSaLRPGDAVVVSEMEHHANLVPWQMLRDSHGIELRIAKITDA-GELDFADLERQF 167
Cdd:TIGR01976 75 ADPPEVVFGANATSLTFLLSRAISRR-WGPGDEVIVTRLDHEANISPWLQAAERAGAKVKWARVDEAtGELHPDDLASLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 168 ADgRVRLLAITHMSNVLGTYTPAERLAAFAHERGARLLLDGAQAVVHRAVDVRAIDADFYVFSGHKLYGPSgIGVLFGKR 247
Cdd:TIGR01976 154 SP-RTRLVAVTAASNTLGSIVDLAAITELVHAAGALVVVDAVHYAPHGLIDVQATGADFLTCSAYKFFGPH-MGILWGRP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 248 ELLDAMPPFLgggdmirsvsyEKSTWAEPPYRFEAGTPAIVEAVGLAAAIDYVNAIG--------------FPAIASHER 313
Cdd:TIGR01976 232 ELLMNLPPYK-----------LTFSYDTGPERFELGTPQYELLAGVVAAVDYLAGLGesangsrrerlvasFQAIDAYEN 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 314 ALTDHALATLDAIGGVHVVG--RAQDRGGVVAFTMDGVHAHDVATLLDKQGIAVRAGHHCAEPLTRRLGL---DSTARAT 388
Cdd:TIGR01976 301 RLAEYLLVGLSDLPGVTLYGvaRLAARVPTVSFTVHGLPPQRVVRRLADQGIDAWAGHFYAVRLLRRLGLndeGGVVRVG 380
|
410
....*....|....*..
gi 737201594 389 FGVYTTMEEIDALAAGL 405
Cdd:TIGR01976 381 LAHYNTAEEVDRLLEAL 397
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
29-408 |
3.76e-57 |
|
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: 191.80 E-value: 3.76e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 29 KKLVFLDSGASAQKPRAVIDAMVRSMETRYANVHRgLHWLSERASDDYEAARDKAAAFLNAAREEIVFVRNATEGINLVA 108
Cdd:COG1104 1 MMMIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSS-LHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 109 ATFGRSALRPGDAVVVSEMEHHANLVPWQMLRdSHGIELRIAKITDAGELDFADLERQFADgRVRLLAITHMSNVLGTYT 188
Cdd:COG1104 80 KGAARAYRKKGKHIITSAIEHPAVLETARFLE-KEGFEVTYLPVDEDGRVDLEALEAALRP-DTALVSVMHANNETGTIQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 189 PAERLAAFAHERGARLLLDGAQAVVHRAVDVRAIDADFYVFSGHKLYGPSGIGVLFGKRELldAMPPFLGGGDMIRSvsy 268
Cdd:COG1104 158 PIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRKGV--RLEPLIHGGGQERG--- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 269 ekstwaeppYRfeAGTPAIVEAVGLAAAIDYVNAiGFPAIASHERALTDHALATL-DAIGGVHVVGRAQDR-GGVVAFTM 346
Cdd:COG1104 233 ---------LR--SGTENVPGIVGLGKAAELAAE-ELEEEAARLRALRDRLEEGLlAAIPGVVINGDPENRlPNTLNFSF 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 737201594 347 DGVHAHDVATLLDKQGIAVRAGHHCA----EP---LtRRLGLDSTA-----RATFGVYTTMEEIDALAAGLRRV 408
Cdd:COG1104 301 PGVEGEALLLALDLAGIAVSSGSACSsgslEPshvL-LAMGLDEELahgsiRFSLGRFTTEEEIDRAIEALKEI 373
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
32-399 |
1.44e-26 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 109.36 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 32 VFLD-SGASAQKPRaVIDAMVRSMETRYANVHRGLH---WLSERAsddYEAARDKAAAFLNAAREEIVFVRNATEGINLV 107
Cdd:PLN02651 1 LYLDmQATTPIDPR-VLDAMLPFLIEHFGNPHSRTHlygWESEDA---VEKARAQVAALIGADPKEIIFTSGATESNNLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 108 AATFGRSALRPGDAVVVSEMEHHANLVPWQMLRdSHGIELRIAKITDAGELDFADLErqfadGRVR----LLAITHMSNV 183
Cdd:PLN02651 77 IKGVMHFYKDKKKHVITTQTEHKCVLDSCRHLQ-QEGFEVTYLPVKSDGLVDLDELA-----AAIRpdtaLVSVMAVNNE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 184 LGTYTPAERLAAFAHERGARLLLDGAQAVVHRAVDVRAIDADFYVFSGHKLYGPSGIGVLFGKRELLDAMPPFLGGGDMI 263
Cdd:PLN02651 151 IGVIQPVEEIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRLEPLMSGGGQE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 264 RSvsyekstwaeppyrFEAGTPAIVEAVGLAAAIDYVNAIGfPAIASHERALTDHALATLDA-IGGVHVVGRAQDRG--- 339
Cdd:PLN02651 231 RG--------------RRSGTENTPLVVGLGAACELAMKEM-DYDEKHMKALRERLLNGLRAkLGGVRVNGPRDPEKryp 295
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 737201594 340 GVVAFTMDGVHAHdvATLLDKQGIAVRAGHHC----AEP--LTRRLGLD-----STARATFGVYTTMEEID 399
Cdd:PLN02651 296 GTLNLSFAYVEGE--SLLMGLKEVAVSSGSACtsasLEPsyVLRALGVPeemahGSLRLGVGRFTTEEEVD 364
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
32-399 |
4.25e-23 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 100.02 E-value: 4.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 32 VFLDSGASAQKPRAVIDAMVR--SMETRYANVHRGLH---WLSERAsddYEAARDKAAAFLNAAREEIVFVRNATEGINL 106
Cdd:PRK14012 5 IYLDYSATTPVDPRVAEKMMPylTMDGTFGNPASRSHrfgWQAEEA---VDIARNQIADLIGADPREIVFTSGATESDNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 107 V---AATFGRSAlrpGDAVVVSEMEHHANLVPWQMLrDSHGIELRIAKITDAGELDFADLERQFADGRVrLLAITHMSNV 183
Cdd:PRK14012 82 AikgAAHFYQKK---GKHIITSKTEHKAVLDTCRQL-EREGFEVTYLDPQSNGIIDLEKLEAAMRDDTI-LVSIMHVNNE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 184 LGTYTPAERLAAFAHERGARLLLDGAQAVVHRAVDVRAIDADFYVFSGHKLYGPSGIGVLFGKRELLDAMPPFLGGGDMI 263
Cdd:PRK14012 157 IGVIQDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRLEAQMHGGGHE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 264 RSvsyekstwaeppyrFEAGTPAIVEAVGL--AAAIDYvnaIGFPAIASHERALTDHALATLDAIGGVHVVGRAQDR-GG 340
Cdd:PRK14012 237 RG--------------MRSGTLPTHQIVGMgeAARIAK---EEMATENERIRALRDRLWNGIKDIEEVYLNGDLEQRvPG 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 341 VVAFTMDGVHAHDVATLLdkQGIAVRAGHHCA----EP--LTRRLGLD-----STARATFGVYTTMEEID 399
Cdd:PRK14012 300 NLNVSFNYVEGESLIMAL--KDLAVSSGSACTsaslEPsyVLRALGLNdelahSSIRFSLGRFTTEEEID 367
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
76-246 |
2.37e-19 |
|
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: 84.74 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 76 YEAARDKAAAFLNAAREEIVFVRNATEGINLVAatfgRSALRPGDAVVVSEMEHHANLvpWQMlRDSHGIELRIAKITDA 155
Cdd:cd01494 2 LEELEEKLARLLQPGNDKAVFVPSGTGANEAAL----LALLGPGDEVIVDANGHGSRY--WVA-AELAGAKPVPVPVDDA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 156 --GELDFADLERQFADGRVRLLAITHMSNVLGTYTPAERLAAFAHERGARLLLDGAQAVVHRA---VDVRAIDADFYVFS 230
Cdd:cd01494 75 gyGGLDVAILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPapgVLIPEGGADVVTFS 154
|
170
....*....|....*.
gi 737201594 231 GHKLYGPSGIGVLFGK 246
Cdd:cd01494 155 LHKNLGGEGGGVVIVK 170
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
31-414 |
5.05e-16 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 79.00 E-value: 5.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 31 LVFLDSGASAQKPRAVIDAMVRSMETRYANvHRGLHWLSERASDDYEAARDKAAAFLNAAREEIVFVRNATEGiNLVAAt 110
Cdd:PRK02948 1 MIYLDYAATTPMSKEALQTYQKAASQYFGN-ESSLHDIGGTASSLLQVCRKTFAEMIGGEEQGIYFTSGGTES-NYLAI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 111 fgRSAL----RPGDAVVVSEMEHHANLVPWQMLrDSHGIELRIAKITDAGELDFADLERQFADGRVrLLAITHMSNVLGT 186
Cdd:PRK02948 78 --QSLLnalpQNKKHIITTPMEHASIHSYFQSL-ESQGYTVTEIPVDKSGLIRLVDLERAITPDTV-LASIQHANSEIGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 187 YTPAERLAAFAHERGARLLLDGAQAVVHRAVDVRAIDADFYVFSGHKLYGPSGIGVLFgKRELLDAMPPFLGggdmirsV 266
Cdd:PRK02948 154 IQPIAEIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVY-INPQVRWKPVFPG-------T 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 267 SYEKStwaeppyrFEAGT---PAIveAVGLAAAIDYVNAIgfPAIASHERALTDHALATLDAIG-GVHVVGRAQDR-GGV 341
Cdd:PRK02948 226 THEKG--------FRPGTvnvPGI--AAFLTAAENILKNM--QEESLRFKELRSYFLEQIQTLPlPIEVEGHSTSClPHI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 342 VAFTMDGVHAHDVATLLDKQGIAVRAGHHCA----EPLTRRLGLDSTA-------RATFGVYTTMEEIDALAAGLRRVQQ 410
Cdd:PRK02948 294 IGVTIKGIEGQYTMLECNRRGIAISTGSACQvgkqEPSKTMLAIGKTYeeakqfvRFSFGQQTTKDQIDTTIHALETIGN 373
|
....
gi 737201594 411 VFGG 414
Cdd:PRK02948 374 QFYR 377
|
|
| SepCysS |
cd06452 |
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ... |
81-248 |
9.93e-12 |
|
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: 65.88 E-value: 9.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 81 DKAAAFLNAarEEIVFVRNATEGINLVAATFGRsalrPGDAVVVSEMEHHANLVPwqmlrdSHGIELRIAKITDAGELDF 160
Cdd:cd06452 51 HDLAEFLGM--DEARVTPGAREGKFAVMHSLCE----KGDWVVVDGLAHYTSYVA------AERAGLNVREVPNTGHPEY 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 161 A-----------DLERQFADgRVRLLAITHMSNVLGTYTPAERLAAFAHERGARLLLDGAQAVVHRAVDVRAIDADFYVF 229
Cdd:cd06452 119 HitpegyaevieEVKDEFGK-PPALALLTHVDGNYGNLHDAKKIAKVCHEYGVPLLLNGAYTVGRMPVSGKELGADFIVG 197
|
170 180
....*....|....*....|
gi 737201594 230 SGHKLYGPSG-IGVLFGKRE 248
Cdd:cd06452 198 SGHKSMAASApIGVLATTEE 217
|
|
| PRK09331 |
PRK09331 |
Sep-tRNA:Cys-tRNA synthetase; Provisional |
84-243 |
1.86e-09 |
|
Sep-tRNA:Cys-tRNA synthetase; Provisional
Pssm-ID: 236469 Cd Length: 387 Bit Score: 59.17 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 84 AAFLNAarEEIVFVRNATEGINLVAATFGRsalrPGDAVVVSEMEHHANLVPWQMLRdshgieLRIAKITDAGELDFA-- 161
Cdd:PRK09331 73 AEFLGM--DEARVTHGAREGKFAVMHSLCK----KGDYVVLDGLAHYTSYVAAERAG------LNVREVPKTGYPEYKit 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 162 ---------DLERQFADgRVRLLAITHMSNVLGTYTPAERLAAFAHERGARLLLDGAQAVVHRAVDVRAIDADFYVFSGH 232
Cdd:PRK09331 141 peayaekieEVKEETGK-PPALALLTHVDGNYGNLADAKKVAKVAHEYGIPFLLNGAYTVGRMPVDGKKLGADFIVGSGH 219
|
170
....*....|..
gi 737201594 233 KLYGPSG-IGVL 243
Cdd:PRK09331 220 KSMAASApSGVL 231
|
|
| GLY1 |
COG2008 |
Threonine aldolase [Amino acid transport and metabolism]; |
77-408 |
2.63e-09 |
|
Threonine aldolase [Amino acid transport and metabolism];
Pssm-ID: 441611 [Multi-domain] Cd Length: 333 Bit Score: 58.15 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 77 EAARDKAAAFLNaaREEIVFVRNATEGiNLVAAtfgRSALRPGDAVVVSEMEHHANlvpwqmlrD-------SHGIELRI 149
Cdd:COG2008 38 NRLEERVAELFG--KEAALFVPSGTMA-NQLAL---RAHTRPGDEVICHETAHIYV--------DeggapeaLSGVKLLP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 150 AKiTDAGELDFADLERQFADG-----RVRLLAITHMSNvLGT-YTPAE--RLAAFAHERGARLLLDGA---QAVVHRAVD 218
Cdd:COG2008 104 VP-GEDGKLTPEDLEAAIRPGdvhfpQPGLVSLENTTE-GGTvYPLEElrAIAAVAREHGLPLHLDGArlfNAAAALGVS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 219 VRAIDADFYV--FSGHK-LYGPSGiGVLFGKRELLDAMPPF--LGGGDMIRSvsyekstwaeppyRFeagtpaiveavgL 293
Cdd:COG2008 182 LAEITAGVDSvsFGLTKgLGAPGG-AVLAGDPEFIEEARRWrkRLGGLMRQA-------------GF------------L 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 294 AAAIDYvnaigfpAIASH-ERALTDHALAT-----LDAIGGVHVVGRAQdrGGVVAFTMDGvhahDVATLLDKQGIAVRA 367
Cdd:COG2008 236 AAQGLA-------ALEDDlERLAEDHAMARrlaegLAALPGVRVPEPVE--TNIVFVILPD----ELAERLREKGVLFYP 302
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 737201594 368 GHHCAepltrrlgldstARATFGVYTTMEEIDALAAGLRRV 408
Cdd:COG2008 303 WGPGA------------VRLVTHWDTTEEDVDAFLAALAEL 331
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
43-407 |
2.82e-09 |
|
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.
Pssm-ID: 99734 [Multi-domain] Cd Length: 350 Bit Score: 58.12 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 43 PRAVIDAMVRSMETRYANvHRGlhwlserASDDYEAARDKAAAFLN------AAREEIVFVRNATEGINLVAATFgrsaL 116
Cdd:cd00609 13 PPEVLEALAAAALRAGLL-GYY-------PDPGLPELREAIAEWLGrrggvdVPPEEIVVTNGAQEALSLLLRAL----L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 117 RPGDAVVVSEmehhanlvP-WQMLRDS---HGIELRIAKITDAGE-LDFADLERQFADGRVRLLAITHMSNVLGTYTPAE 191
Cdd:cd00609 81 NPGDEVLVPD--------PtYPGYEAAarlAGAEVVPVPLDEEGGfLLDLELLEAAKTPKTKLLYLNNPNNPTGAVLSEE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 192 R---LAAFAHERGARLLLDGA-------QAVVHRAVDVRAIDADFYVFSGHKLYGPSG--IGVLFGKRELLDamppflgg 259
Cdd:cd00609 153 EleeLAELAKKHGILIISDEAyaelvydGEPPPALALLDAYERVIVLRSFSKTFGLPGlrIGYLIAPPEELL-------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 260 gDMIRSVSyekstwaeppyRFEAGTPAIVEAVGLAAAIDYVNAIgFPAIASHERALTDHALATLDAIGGVHVVGraqDRG 339
Cdd:cd00609 225 -ERLKKLL-----------PYTTSGPSTLSQAAAAAALDDGEEH-LEELRERYRRRRDALLEALKELGPLVVVK---PSG 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 340 GVVAFT--MDGVHAHDVATLLDKQGIAVRAGHHCAEPLTRRLgldstaRATFGvyTTMEEIDALAAGLRR 407
Cdd:cd00609 289 GFFLWLdlPEGDDEEFLERLLLEAGVVVRPGSAFGEGGEGFV------RLSFA--TPEEELEEALERLAE 350
|
|
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
12-371 |
6.90e-08 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 54.87 E-value: 6.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 12 IARIRA-DFPILSQTVhgkklvFLDSGASAQKPRAVIDAMVRSMETR-YANVHRGLHwLSERASDDYEAARDKAAAFLNA 89
Cdd:PLN02724 21 IDELRAtEFARLKGVV------YLDHAGATLYSESQLEAALADFSSNvYGNPHSQSD-SSMRSSDTIESARQQVLEYFNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 90 AREE--IVFVRNATEGINLVAATFGRS---------------------ALRPGDAVVVSEMEHHANlvpwQMLRDSHGIE 146
Cdd:PLN02724 94 PPSDyaCVFTSGATAALKLVGETFPWSseshfcytlenhnsvlgireyALEKGAAAIAVDIEEAAN----QPTNSQGSVV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 147 LRIAKITDAGEldfADLERQFADGR-VRLLAITHMSNVLGTYTP---AERLAAFAHERGAR-----LLLDGAQAVVHRAV 217
Cdd:PLN02724 170 VKSRGLQRRNT---SKLQKREDDGEaYNLFAFPSECNFSGAKFPldlVKLIKDNQHSNFSKsgrwmVLLDAAKGCGTSPP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 218 DVRAIDADFYVFSGHKLYG-PSGIGVLFGKRELLDAM-PPFLGGGDMIRSVS----YEKSTWAEPpyRFEAGTPAIVEAV 291
Cdd:PLN02724 247 DLSRYPADFVVVSFYKIFGyPTGLGALLVRRDAAKLLkKKYFGGGTVAASIAdidfVKRRERVEQ--RFEDGTISFLSIA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 292 GLAAAIDYVNAIGFPAIASHERALTDHALATLDAI-----GGVHVVGRAQ-------DRGGVVAFTM---DG--VHAHDV 354
Cdd:PLN02724 325 ALRHGFKLLNRLTISAIAMHTWALTHYVANSLRNLkhgngAPVCVLYGNHtfklefhIQGPIVTFNLkraDGswVGHREV 404
|
410
....*....|....*..
gi 737201594 355 ATLLDKQGIAVRAGHHC 371
Cdd:PLN02724 405 EKLASLSGIQLRTGCFC 421
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
75-251 |
3.09e-06 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 48.37 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 75 DYEAARDKAAAFLNAarEEIVFVRNATEGiNLVAAtfgRSALRPGDAVVVSEMEH--------HANLvpwqmlrdsHGIE 146
Cdd:pfam01212 33 TVNRLEDRVAELFGK--EAALFVPSGTAA-NQLAL---MAHCQRGDEVICGEPAHihfdetggHAEL---------GGVQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 147 LRIAKITDAGELDFADLERQFADG------RVRLLAITHMSNVLG--TYTPAE--RLAAFAHERGARLLLDGAQ---AVV 213
Cdd:pfam01212 98 PRPLDGDEAGNMDLEDLEAAIREVgadifpPTGLISLENTHNSAGgqVVSLENlrEIAALAREHGIPVHLDGARfanAAV 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 737201594 214 HRAVDVRAI--DADFYVFSGHK-LYGPSGiGVLFGKRELLD 251
Cdd:pfam01212 178 ALGVIVKEItsYADSVTMCLSKgLGAPVG-SVLAGSDDFIA 217
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
113-408 |
3.19e-06 |
|
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.
Pssm-ID: 99744 [Multi-domain] Cd Length: 356 Bit Score: 48.83 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 113 RSALRPGDAVVVSEMEHHANLVPwQMLRdSHGIELRIAKiTDAGE-LDFADLERQFADGRVRLLAITHMSNVLGTYTPAE 191
Cdd:cd06451 68 SNLLEPGDKVLVGVNGVFGDRWA-DMAE-RYGADVDVVE-KPWGEaVSPEEIAEALEQHDIKAVTLTHNETSTGVLNPLE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 192 RLAAFAHERGARLLLDGAQAVVHRAVDVRAIDADfYVFSGHK--LYGPSGIG-VLFGKR---ELLDAMPPFLGGGDMIRS 265
Cdd:cd06451 145 GIGALAKKHDALLIVDAVSSLGGEPFRMDEWGVD-VAYTGSQkaLGAPPGLGpIAFSERaleRIKKKTKPKGFYFDLLLL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 266 VSYekstWAEppYRFEAGTPAIVEAVGLAAAIDYVNAIGFPA-IASHERaLTDHALATLDAIG-GVHVVGRAQDRGGVVA 343
Cdd:cd06451 224 LKY----WGE--GYSYPHTPPVNLLYALREALDLILEEGLENrWARHRR-LAKALREGLEALGlKLLAKPELRSPTVTAV 296
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 737201594 344 FTMDGVHAHDVA-TLLDKQGIAVRAGHHCAEPLTRRLGLdstaratFGvYTTMEEIDALAAGLRRV 408
Cdd:cd06451 297 LVPEGVDGDEVVrRLMKRYNIEIAGGLGPTAGKVFRIGH-------MG-EATREDVLGVLSALEEA 354
|
|
| ARO8 |
COG1167 |
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ... |
87-202 |
2.88e-04 |
|
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain [Transcription, Amino acid transport and metabolism]; DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 440781 [Multi-domain] Cd Length: 471 Bit Score: 42.89 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 87 LNAAREEIVFVRNATEGINLVAATFgrsaLRPGDAVVVSEMEHHANLvpwQMLRdSHGieLRIAKI-TDAGELDFADLER 165
Cdd:COG1167 166 VPASPDQILITSGAQQALDLALRAL----LRPGDTVAVESPTYPGAL---AALR-AAG--LRLVPVpVDEDGLDLDALEA 235
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 737201594 166 QFADGRVRLLAIT-HMSNVLGTYTPAER---LAAFAHERGA 202
Cdd:COG1167 236 ALRRHRPRAVYVTpSHQNPTGATMSLERrraLLELARRHGV 276
|
|
| PRK06225 |
PRK06225 |
pyridoxal phosphate-dependent aminotransferase; |
41-253 |
2.25e-03 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235749 [Multi-domain] Cd Length: 380 Bit Score: 40.12 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 41 QKPRAVIDAMVRSMETRYANVH---RGLHWLSERASDDYEAarDKAAAFLNAAreeivfvrnATEGINLVAatfgRSALR 117
Cdd:PRK06225 41 GPHEEVREAMIRCIEEGEYCKYpppEGFPELRELILKDLGL--DDDEALITAG---------ATESLYLVM----RAFLS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 118 PGDAVVVSEMEHhanLVPWQMLRdSHGIELRIAKITDAgELDF---ADLERQFADGRVRLLAITHMSNVLGT-YTPAE-- 191
Cdd:PRK06225 106 PGDNAVTPDPGY---LIIDNFAS-RFGAEVIEVPIYSE-ECNYkltPELVKENMDENTRLIYLIDPLNPLGSsYTEEEik 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 737201594 192 RLAAFAHERGARLLLD------------GAQAVVHRAVDVraidadfYVFSghKLYGPSG--IGVLFGKRELLDAM 253
Cdd:PRK06225 181 EFAEIARDNDAFLLHDctyrdfarehtlAAEYAPEHTVTS-------YSFS--KIFGMAGlrIGAVVATPDLIEVV 247
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
73-249 |
9.09e-03 |
|
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.
Pssm-ID: 99748 [Multi-domain] Cd Length: 338 Bit Score: 38.08 E-value: 9.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 73 SDDY-EAARDKAAAFLNaaREEIVFVRNATEGiNLVAAtfgRSALRPGDAVVVSEmEHHANLVPWQMLRDSHGIELRIAK 151
Cdd:cd06502 30 EDPTtAKLEARAAELFG--KEAALFVPSGTAA-NQLAL---AAHTQPGGSVICHE-TAHIYTDEAGAPEFLSGVKLLPVP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737201594 152 iTDAGELDFADLERQFADG------RVRLLAITHMSNVLGTYTPAE--RLAAFAHERGARLLLDGAQ---AVVHRAVDVR 220
Cdd:cd06502 103 -GENGKLTPEDLEAAIRPRddihfpPPSLVSLENTTEGGTVYPLDElkAISALAKENGLPLHLDGARlanAAAALGVALK 181
|
170 180 190
....*....|....*....|....*....|.
gi 737201594 221 AI--DADFYVFSGHKLYGPSGIGVLFGKREL 249
Cdd:cd06502 182 TYksGVDSVSFCLSKGGGAPVGAVVVGNRDF 212
|
|
| |
