|
Name |
Accession |
Description |
Interval |
E-value |
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
7-406 |
0e+00 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 531.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 7 DPKTIRNDFPtlnqtINGYPLVYLDSAATTQKPQCVIDATNEFYTYQNANVHRGRHTLSEQATTAYELVRQRVADYFQV- 85
Cdd:COG0520 1 DVEAIRADFP-----VLGKPLVYLDNAATGQKPRPVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAa 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 86 SGNEIVWTKGATEAINLVAHGLrNTLTTDDTILISPIEHHANIVPWQELAAYTGATLKVLPLNDDATFDISqccDVIKL- 164
Cdd:COG0520 76 SPDEIIFTRGTTEAINLVAYGL-GRLKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDGELDLE---ALEALl 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 165 -TKPALLAITQASNALGNITDLTPLITAAKAVNALTLVDGAQGALHLRPNLIKLDCDFYVFSAHKMLGPTGLGGLYGRYS 243
Cdd:COG0520 152 tPRTKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 244 ALNALSPYQTGGEMIEKVTLTQSTYRDAPAKFEAGTPNIAGVLGFGAALEYIIALDQQTLKHYEQQLFIYAANALNQIDG 323
Cdd:COG0520 232 LLEALPPFLGGGGMIEWVSFDGTTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAIPG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 324 ISIY--SDLKSNIGTLCFNYKNEHPYDLATLLDGYGIAVRSGHHCTQPLMTHLKLNGSLRASFAFYNTTKDVDQFITALK 401
Cdd:COG0520 312 VRILgpADPEDRSGIVSFNVDGVHPHDVAALLDDEGIAVRAGHHCAQPLMRRLGVPGTVRASFHLYNTEEEIDRLVEALK 391
|
....*
gi 1590405280 402 ECIAL 406
Cdd:COG0520 392 KLAEL 396
|
|
| sufS |
TIGR01979 |
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine ... |
9-401 |
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: 522.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 9 KTIRNDFPTLNQTINGYPLVYLDSAATTQKPQCVIDATNEFYTYQNANVHRGRHTLSEQATTAYELVRQRVADYFQV-SG 87
Cdd:TIGR01979 1 KNIRADFPILKRKINGKPLVYLDSAATSQKPQQVIDAVAEYYRNSNANVHRGIHTLSVRATEAYEAVREKVAKFINAaSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 88 NEIVWTKGATEAINLVAHGL-RNTLTTDDTILISPIEHHANIVPWQELAAYTGATLKVLPLNDDATFDISQCCDVIKlTK 166
Cdd:TIGR01979 81 EEIVFTRGTTESINLVAYSWgDSNLKAGDEIVISEMEHHANIVPWQLLAERTGATLKFIPLDDDGTLDLDDLEKLLT-EK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 167 PALLAITQASNALGNITDLTPLITAAKAVNALTLVDGAQGALHLRPNLIKLDCDFYVFSAHKMLGPTGLGGLYGRYSALN 246
Cdd:TIGR01979 160 TKLVAITHVSNVLGTVNPVEEIAKLAHQVGAKVLVDGAQAVPHMPVDVQALDCDFYVFSGHKMYGPTGIGVLYGKEELLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 247 ALSPYQTGGEMIEKVTLTQSTYRDAPAKFEAGTPNIAGVLGFGAALEYIIALDQQTLKHYEQQLFIYAANALNQIDGISI 326
Cdd:TIGR01979 240 QMPPFLGGGEMIAEVSFEETTYNEAPHKFEAGTPNIAGVIGLGAAIDYLEAIGLENIEAHEHELTAYALERLGEIPGLRI 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590405280 327 Y--SDLKSNIGTLCFNYKNEHPYDLATLLDGYGIAVRSGHHCTQPLMTHLKLNGSLRASFAFYNTTKDVDQFITALK 401
Cdd:TIGR01979 320 YgpRDAEDRGGIISFNVEGVHPHDVGTILDEEGIAVRSGHHCAQPLMRRFGVPATCRASFYIYNTEEDIDALVEALK 396
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
28-400 |
2.95e-179 |
|
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: 503.54 E-value: 2.95e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 28 VYLDSAATTQKPQCVIDATNEFYTYQNANVHRGRHTLSEQATTAYELVRQRVADYFQV-SGNEIVWTKGATEAINLVAHG 106
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINApSPDEIIFTRNTTEAINLVAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 107 LRNTLTTDDTILISPIEHHANIVPWQELAAYTGATLKVLPLNDDATFDISQCCDVIKlTKPALLAITQASNALGNITDLT 186
Cdd:cd06453 81 LGRANKPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLT-ERTKLVAVTHVSNVLGTINPVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 187 PLITAAKAVNALTLVDGAQGALHLRPNLIKLDCDFYVFSAHKMLGPTGLGGLYGRYSALNALSPYQTGGEMIEKVTLTQS 266
Cdd:cd06453 160 EIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMIEEVSFEET 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 267 TYRDAPAKFEAGTPNIAGVLGFGAALEYIIALDQQTLKHYEQQLFIYAANALNQIDGISIYSDLKSNIGTLCFNYKNEHP 346
Cdd:cd06453 240 TYADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEIPGVRVYGDAEDRAGVVSFNLEGIHP 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1590405280 347 YDLATLLDGYGIAVRSGHHCTQPLMTHLKLNGSLRASFAFYNTTKDVDQFITAL 400
Cdd:cd06453 320 HDVATILDQYGIAVRAGHHCAQPLMRRLGVPGTVRASFGLYNTEEEIDALVEAL 373
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
28-396 |
1.33e-162 |
|
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: 461.33 E-value: 1.33e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 28 VYLDSAATTQKPQCVIDATNEFYTYQNANVHRGRHTLSEQATTAYELVRQRVADYFQVSGN-EIVWTKGATEAINLVAHG 106
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNdEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 107 LRNTLTTDDTILISPIEHHANIVPWQELAAYTGATLKVLPLNDDATFDISQCCDVIKlTKPALLAITQASNALGNITDLT 186
Cdd:pfam00266 81 LGRSLKPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLIT-PKTKLVAITHVSNVTGTIQPVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 187 PLITAAKAVNALTLVDGAQGALHLRPNLIKLDCDFYVFSAHKMLGPTGLGGLYGRYSALNALSPYQTGGEMIEKVTLTQS 266
Cdd:pfam00266 160 EIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGMIETVSLQES 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 267 TYRDAPAKFEAGTPNIAGVLGFGAALEYIIALDQQTLKHYEQQLFIYAANALNQIDGISIYSDLKsNIGTLCFNYKNEHP 346
Cdd:pfam00266 240 TFADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPER-RASIISFNFKGVHP 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1590405280 347 YDLATLLDGYGIAVRSGHHCTQPLMTHLKLNGSLRASFAFYNTTKDVDQF 396
Cdd:pfam00266 319 HDVATLLDESGIAVRSGHHCAQPLMVRLGLGGTVRASFYIYNTQEDVDRL 368
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
11-408 |
7.38e-154 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 441.11 E-value: 7.38e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 11 IRNDFPTLNQTINGYPLVYLDSAATTQKPQCVIDATNEFYTYQNANVHRGRHTLSEQATTAYELVRQRVADYFQV-SGNE 89
Cdd:PLN02855 17 TRPDFPILDQTVNGSKLVYLDNAATSQKPAAVLDALQDYYEEYNSNVHRGIHALSAKATDAYELARKKVAAFINAsTSRE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 90 IVWTKGATEAINLVAH--GLRNtLTTDDTILISPIEHHANIVPWQELAAYTGATLKVLPLNDDATFDISQCCDVIKlTKP 167
Cdd:PLN02855 97 IVFTRNATEAINLVAYtwGLAN-LKPGDEVILSVAEHHSNIVPWQLVAQKTGAVLKFVGLTPDEVLDVEQLKELLS-EKT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 168 ALLAITQASNALGNITDLTPLITAAKAVNALTLVDGAQGALHLRPNLIKLDCDFYVFSAHKMLGPTGLGGLYGRYSALNA 247
Cdd:PLN02855 175 KLVATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLWGKSDLLES 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 248 LSPYQTGGEMIEKVTLTQSTYRDAPAKFEAGTPNIAGVLGFGAALEYIIALDQQTLKHYEQQLFIYAANALNQIDGISIY 327
Cdd:PLN02855 255 MPPFLGGGEMISDVFLDHSTYAPPPSRFEAGTPAIGEAIGLGAAIDYLSEIGMDRIHEYEVELGTYLYEKLSSVPGVRIY 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 328 ---SDLKSNIGTLC-FNYKNEHPYDLATLLD-GYGIAVRSGHHCTQPLMTHLKLNGSLRASFAFYNTTKDVDQFITALKE 402
Cdd:PLN02855 335 gpkPSEGVGRAALCaFNVEGIHPTDLSTFLDqQHGVAIRSGHHCAQPLHRYLGVNASARASLYFYNTKEEVDAFIHALKD 414
|
....*.
gi 1590405280 403 CIALLD 408
Cdd:PLN02855 415 TIAFFS 420
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
6-400 |
1.11e-153 |
|
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: 448.15 E-value: 1.11e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 6 FDPKTIRNDFPTLNQTINGYPLVYLDSAATTQKPQCVIDATNEFYTYQNANVHRGRHTLSEQATTAYELVRQRVADYFQV 85
Cdd:NF041166 225 FDVNAVRRDFPILQERVNGKPLVWFDNAATTQKPQAVIDRLSYFYEHENSNIHRAAHELAARATDAYEGAREKVRRFIGA 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 86 -SGNEIVWTKGATEAINLVAH--GLRNtLTTDDTILISPIEHHANIVPWQELAAYTGATLKVLPLNDDATFDISQccdVI 162
Cdd:NF041166 305 pSVDEIIFVRGTTEAINLVAKswGRQN-IGAGDEIIVSHLEHHANIVPWQQLAQETGAKLRVIPVDDSGQILLDE---YA 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 163 KL----TKpaLLAITQASNALGNITDLTPLITAAKAVNALTLVDGAQGALHLRPNLIKLDCDFYVFSAHKMLGPTGLGGL 238
Cdd:NF041166 381 KLlnprTK--LVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGIGVV 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 239 YGRYSALNALSPYQTGGEMIEKVTLTQSTYRDAPAKFEAGTPNIAGVLGFGAALEYIIALDQQTLKHYEQQLFIYAANAL 318
Cdd:NF041166 459 YGKRDLLEAMPPWQGGGNMIADVTFEKTVYQPAPNRFEAGTGNIADAVGLGAALDYVERIGIENIARYEHDLLEYATAGL 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 319 NQIDGISIysdlksnIGT-------LCFN---YKNEhpyDLATLLDGYGIAVRSGHHCTQPLMTHLKLNGSLRASFAFYN 388
Cdd:NF041166 539 AEVPGLRL-------IGTaadkasvLSFVldgYSTE---EVGKALNQEGIAVRSGHHCAQPILRRFGVEATVRPSLAFYN 608
|
410
....*....|..
gi 1590405280 389 TTKDVDQFITAL 400
Cdd:NF041166 609 TCEEVDALVAVL 620
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
7-406 |
0e+00 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 531.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 7 DPKTIRNDFPtlnqtINGYPLVYLDSAATTQKPQCVIDATNEFYTYQNANVHRGRHTLSEQATTAYELVRQRVADYFQV- 85
Cdd:COG0520 1 DVEAIRADFP-----VLGKPLVYLDNAATGQKPRPVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAa 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 86 SGNEIVWTKGATEAINLVAHGLrNTLTTDDTILISPIEHHANIVPWQELAAYTGATLKVLPLNDDATFDISqccDVIKL- 164
Cdd:COG0520 76 SPDEIIFTRGTTEAINLVAYGL-GRLKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDGELDLE---ALEALl 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 165 -TKPALLAITQASNALGNITDLTPLITAAKAVNALTLVDGAQGALHLRPNLIKLDCDFYVFSAHKMLGPTGLGGLYGRYS 243
Cdd:COG0520 152 tPRTKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 244 ALNALSPYQTGGEMIEKVTLTQSTYRDAPAKFEAGTPNIAGVLGFGAALEYIIALDQQTLKHYEQQLFIYAANALNQIDG 323
Cdd:COG0520 232 LLEALPPFLGGGGMIEWVSFDGTTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAIPG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 324 ISIY--SDLKSNIGTLCFNYKNEHPYDLATLLDGYGIAVRSGHHCTQPLMTHLKLNGSLRASFAFYNTTKDVDQFITALK 401
Cdd:COG0520 312 VRILgpADPEDRSGIVSFNVDGVHPHDVAALLDDEGIAVRAGHHCAQPLMRRLGVPGTVRASFHLYNTEEEIDRLVEALK 391
|
....*
gi 1590405280 402 ECIAL 406
Cdd:COG0520 392 KLAEL 396
|
|
| sufS |
TIGR01979 |
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine ... |
9-401 |
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: 522.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 9 KTIRNDFPTLNQTINGYPLVYLDSAATTQKPQCVIDATNEFYTYQNANVHRGRHTLSEQATTAYELVRQRVADYFQV-SG 87
Cdd:TIGR01979 1 KNIRADFPILKRKINGKPLVYLDSAATSQKPQQVIDAVAEYYRNSNANVHRGIHTLSVRATEAYEAVREKVAKFINAaSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 88 NEIVWTKGATEAINLVAHGL-RNTLTTDDTILISPIEHHANIVPWQELAAYTGATLKVLPLNDDATFDISQCCDVIKlTK 166
Cdd:TIGR01979 81 EEIVFTRGTTESINLVAYSWgDSNLKAGDEIVISEMEHHANIVPWQLLAERTGATLKFIPLDDDGTLDLDDLEKLLT-EK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 167 PALLAITQASNALGNITDLTPLITAAKAVNALTLVDGAQGALHLRPNLIKLDCDFYVFSAHKMLGPTGLGGLYGRYSALN 246
Cdd:TIGR01979 160 TKLVAITHVSNVLGTVNPVEEIAKLAHQVGAKVLVDGAQAVPHMPVDVQALDCDFYVFSGHKMYGPTGIGVLYGKEELLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 247 ALSPYQTGGEMIEKVTLTQSTYRDAPAKFEAGTPNIAGVLGFGAALEYIIALDQQTLKHYEQQLFIYAANALNQIDGISI 326
Cdd:TIGR01979 240 QMPPFLGGGEMIAEVSFEETTYNEAPHKFEAGTPNIAGVIGLGAAIDYLEAIGLENIEAHEHELTAYALERLGEIPGLRI 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590405280 327 Y--SDLKSNIGTLCFNYKNEHPYDLATLLDGYGIAVRSGHHCTQPLMTHLKLNGSLRASFAFYNTTKDVDQFITALK 401
Cdd:TIGR01979 320 YgpRDAEDRGGIISFNVEGVHPHDVGTILDEEGIAVRSGHHCAQPLMRRFGVPATCRASFYIYNTEEDIDALVEALK 396
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
28-400 |
2.95e-179 |
|
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: 503.54 E-value: 2.95e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 28 VYLDSAATTQKPQCVIDATNEFYTYQNANVHRGRHTLSEQATTAYELVRQRVADYFQV-SGNEIVWTKGATEAINLVAHG 106
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINApSPDEIIFTRNTTEAINLVAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 107 LRNTLTTDDTILISPIEHHANIVPWQELAAYTGATLKVLPLNDDATFDISQCCDVIKlTKPALLAITQASNALGNITDLT 186
Cdd:cd06453 81 LGRANKPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLT-ERTKLVAVTHVSNVLGTINPVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 187 PLITAAKAVNALTLVDGAQGALHLRPNLIKLDCDFYVFSAHKMLGPTGLGGLYGRYSALNALSPYQTGGEMIEKVTLTQS 266
Cdd:cd06453 160 EIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMIEEVSFEET 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 267 TYRDAPAKFEAGTPNIAGVLGFGAALEYIIALDQQTLKHYEQQLFIYAANALNQIDGISIYSDLKSNIGTLCFNYKNEHP 346
Cdd:cd06453 240 TYADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEIPGVRVYGDAEDRAGVVSFNLEGIHP 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1590405280 347 YDLATLLDGYGIAVRSGHHCTQPLMTHLKLNGSLRASFAFYNTTKDVDQFITAL 400
Cdd:cd06453 320 HDVATILDQYGIAVRAGHHCAQPLMRRLGVPGTVRASFGLYNTEEEIDALVEAL 373
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
28-396 |
1.33e-162 |
|
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: 461.33 E-value: 1.33e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 28 VYLDSAATTQKPQCVIDATNEFYTYQNANVHRGRHTLSEQATTAYELVRQRVADYFQVSGN-EIVWTKGATEAINLVAHG 106
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNdEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 107 LRNTLTTDDTILISPIEHHANIVPWQELAAYTGATLKVLPLNDDATFDISQCCDVIKlTKPALLAITQASNALGNITDLT 186
Cdd:pfam00266 81 LGRSLKPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLIT-PKTKLVAITHVSNVTGTIQPVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 187 PLITAAKAVNALTLVDGAQGALHLRPNLIKLDCDFYVFSAHKMLGPTGLGGLYGRYSALNALSPYQTGGEMIEKVTLTQS 266
Cdd:pfam00266 160 EIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGMIETVSLQES 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 267 TYRDAPAKFEAGTPNIAGVLGFGAALEYIIALDQQTLKHYEQQLFIYAANALNQIDGISIYSDLKsNIGTLCFNYKNEHP 346
Cdd:pfam00266 240 TFADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPER-RASIISFNFKGVHP 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1590405280 347 YDLATLLDGYGIAVRSGHHCTQPLMTHLKLNGSLRASFAFYNTTKDVDQF 396
Cdd:pfam00266 319 HDVATLLDESGIAVRSGHHCAQPLMVRLGLGGTVRASFYIYNTQEDVDRL 368
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
11-408 |
7.38e-154 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 441.11 E-value: 7.38e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 11 IRNDFPTLNQTINGYPLVYLDSAATTQKPQCVIDATNEFYTYQNANVHRGRHTLSEQATTAYELVRQRVADYFQV-SGNE 89
Cdd:PLN02855 17 TRPDFPILDQTVNGSKLVYLDNAATSQKPAAVLDALQDYYEEYNSNVHRGIHALSAKATDAYELARKKVAAFINAsTSRE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 90 IVWTKGATEAINLVAH--GLRNtLTTDDTILISPIEHHANIVPWQELAAYTGATLKVLPLNDDATFDISQCCDVIKlTKP 167
Cdd:PLN02855 97 IVFTRNATEAINLVAYtwGLAN-LKPGDEVILSVAEHHSNIVPWQLVAQKTGAVLKFVGLTPDEVLDVEQLKELLS-EKT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 168 ALLAITQASNALGNITDLTPLITAAKAVNALTLVDGAQGALHLRPNLIKLDCDFYVFSAHKMLGPTGLGGLYGRYSALNA 247
Cdd:PLN02855 175 KLVATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLWGKSDLLES 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 248 LSPYQTGGEMIEKVTLTQSTYRDAPAKFEAGTPNIAGVLGFGAALEYIIALDQQTLKHYEQQLFIYAANALNQIDGISIY 327
Cdd:PLN02855 255 MPPFLGGGEMISDVFLDHSTYAPPPSRFEAGTPAIGEAIGLGAAIDYLSEIGMDRIHEYEVELGTYLYEKLSSVPGVRIY 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 328 ---SDLKSNIGTLC-FNYKNEHPYDLATLLD-GYGIAVRSGHHCTQPLMTHLKLNGSLRASFAFYNTTKDVDQFITALKE 402
Cdd:PLN02855 335 gpkPSEGVGRAALCaFNVEGIHPTDLSTFLDqQHGVAIRSGHHCAQPLHRYLGVNASARASLYFYNTKEEVDAFIHALKD 414
|
....*.
gi 1590405280 403 CIALLD 408
Cdd:PLN02855 415 TIAFFS 420
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
6-400 |
1.11e-153 |
|
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: 448.15 E-value: 1.11e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 6 FDPKTIRNDFPTLNQTINGYPLVYLDSAATTQKPQCVIDATNEFYTYQNANVHRGRHTLSEQATTAYELVRQRVADYFQV 85
Cdd:NF041166 225 FDVNAVRRDFPILQERVNGKPLVWFDNAATTQKPQAVIDRLSYFYEHENSNIHRAAHELAARATDAYEGAREKVRRFIGA 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 86 -SGNEIVWTKGATEAINLVAH--GLRNtLTTDDTILISPIEHHANIVPWQELAAYTGATLKVLPLNDDATFDISQccdVI 162
Cdd:NF041166 305 pSVDEIIFVRGTTEAINLVAKswGRQN-IGAGDEIIVSHLEHHANIVPWQQLAQETGAKLRVIPVDDSGQILLDE---YA 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 163 KL----TKpaLLAITQASNALGNITDLTPLITAAKAVNALTLVDGAQGALHLRPNLIKLDCDFYVFSAHKMLGPTGLGGL 238
Cdd:NF041166 381 KLlnprTK--LVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGIGVV 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 239 YGRYSALNALSPYQTGGEMIEKVTLTQSTYRDAPAKFEAGTPNIAGVLGFGAALEYIIALDQQTLKHYEQQLFIYAANAL 318
Cdd:NF041166 459 YGKRDLLEAMPPWQGGGNMIADVTFEKTVYQPAPNRFEAGTGNIADAVGLGAALDYVERIGIENIARYEHDLLEYATAGL 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 319 NQIDGISIysdlksnIGT-------LCFN---YKNEhpyDLATLLDGYGIAVRSGHHCTQPLMTHLKLNGSLRASFAFYN 388
Cdd:NF041166 539 AEVPGLRL-------IGTaadkasvLSFVldgYSTE---EVGKALNQEGIAVRSGHHCAQPILRRFGVEATVRPSLAFYN 608
|
410
....*....|..
gi 1590405280 389 TTKDVDQFITAL 400
Cdd:NF041166 609 TCEEVDALVAVL 620
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
5-407 |
2.22e-148 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 426.86 E-value: 2.22e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 5 SFDPKTIRNDFPTLNQTINGYPLVYLDSAATTQKPQCVIDATNEFYTYQNANVHRGRHTLSEQATTAYELVRQRVADYFQ 84
Cdd:PRK09295 2 TFSVEKVRADFPVLSREVNGLPLAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKQAALFIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 85 -VSGNEIVWTKGATEAINLVAHGLRNT-LTTDDTILISPIEHHANIVPWQELAAYTGATLKVLPLNDDATFDISQCCDVI 162
Cdd:PRK09295 82 aRSAEELVFVRGTTEGINLVANSWGNSnVRAGDNIIISEMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPALF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 163 KlTKPALLAITQASNALGNITDLTPLITAAKAVNALTLVDGAQGALHLRPNLIKLDCDFYVFSAHKMLGPTGLGGLYGRY 242
Cdd:PRK09295 162 D-ERTRLLAITHVSNVLGTENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 243 SALNALSPYQTGGEMIEKVTLTQ-STYRDAPAKFEAGTPNIAGVLGFGAALEYIIALDQQTLKHYEQQLFIYAANALNQI 321
Cdd:PRK09295 241 ALLQEMPPWEGGGSMIATVSLTEgTTWAKAPWRFEAGTPNTGGIIGLGAALDYVSALGLNNIAEYEQNLMHYALSQLESV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 322 DGISIYSDlKSNIGTLCFNYKNEHPYDLATLLDGYGIAVRSGHHCTQPLMTHLKLNGSLRASFAFYNTTKDVDQFITALK 401
Cdd:PRK09295 321 PDLTLYGP-QNRLGVIAFNLGKHHAYDVGSFLDNYGIAVRTGHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVAGLQ 399
|
....*.
gi 1590405280 402 ECIALL 407
Cdd:PRK09295 400 RIHRLL 405
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
5-407 |
6.02e-142 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 410.20 E-value: 6.02e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 5 SFDPKTIRNDFPTLNQtingyPLVYLDSAATTQKPQCVIDATNEFYTYQNANVHRGRHTLSEQATTAYELVRQRVADYFQ 84
Cdd:PRK10874 3 VFNPAQFRAQFPALQD-----AGVYLDSAATALKPQAVIEATQQFYSLSAGNVHRSQFAAAQRLTARYEAAREQVAQLLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 85 V-SGNEIVWTKGATEAINLVAHG-LRNTLTTDDTILISPIEHHANIVPWQELAAYTGATLKVLPLNDDATFDISQCCDVI 162
Cdd:PRK10874 78 ApDAKNIVWTRGTTESINLVAQSyARPRLQPGDEIIVSEAEHHANLVPWLMVAQQTGAKVVKLPLGADRLPDVDLLPELI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 163 KlTKPALLAITQASNALGNITDLTPLITAAKAVNALTLVDGAQGALHLRPNLIKLDCDFYVFSAHKMLGPTGLGGLYGRY 242
Cdd:PRK10874 158 T-PRTRILALGQMSNVTGGCPDLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 243 SALNALSPYQTGGEMIEKVTLTQSTYRDAPAKFEAGTPNIAGVLGFGAALEYIIALDQQTLKHYEQQLFIYAANALNQID 322
Cdd:PRK10874 237 ELLEAMSPWQGGGKMLTEVSFDGFTPQSAPWRFEAGTPNVAGVIGLSAALEWLADIDINQAESWSRSLATLAEDALAKLP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 323 GISIYSDLKSNIgtLCFNYKNEHPYDLATLLDGYGIAVRSGHHCTQPLMTHLKLNGSLRASFAFYNTTKDVDQFITALKE 402
Cdd:PRK10874 317 GFRSFRCQDSSL--LAFDFAGVHHSDLVTLLAEYGIALRAGQHCAQPLLAALGVTGTLRASFAPYNTQSDVDALVNAVDR 394
|
....*
gi 1590405280 403 CIALL 407
Cdd:PRK10874 395 ALELL 399
|
|
| FeS_syn_CsdA |
TIGR03392 |
cysteine desulfurase, catalytic subunit CsdA; Members of this protein family are CsdS. This ... |
6-407 |
8.59e-132 |
|
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: 384.19 E-value: 8.59e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 6 FDPKTIRNDFPTLNQTingypLVYLDSAATTQKPQCVIDATNEFYTYQNANVHRGRHTLSEQATTAYELVRQRVADYFQV 85
Cdd:TIGR03392 1 FNPAQFRRQFPALQDA-----TVYLDSAATALKPQAVIDATQQFYRLSSGTVHRSQHQEAQSLTARYEAAREQVAQLLNA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 86 SGNE-IVWTKGATEAINLVAHG-LRNTLTTDDTILISPIEHHANIVPWQELAAYTGATLKVLPLNDDATFDISQCCDVIK 163
Cdd:TIGR03392 76 PDAEnIVWTRGTTESINLVAQSyARPRLQPGDEIIVSEAEHHANLIPWLMVAQQTGAKVVKLPIGADLLPDIDQLPELLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 164 lTKPALLAITQASNALGNITDLTPLITAAKAVNALTLVDGAQGALHLRPNLIKLDCDFYVFSAHKMLGPTGLGGLYGRYS 243
Cdd:TIGR03392 156 -PRTRILALGQMSNVTGGCPDLARAITLAHQYGCVVVVDGAQGVVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKTE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 244 ALNALSPYQTGGEMIEKVTLTQSTYRDAPAKFEAGTPNIAGVLGFGAALEYIIALDQQTLKHYEQQLFIYAANALNQIDG 323
Cdd:TIGR03392 235 LLEAMPPWQGGGKMLSHVSFDGFTPQAVPWRFEAGTPNIAGVIGLSAALEWLADIDINAAESWSVSLATLAEEALAQLPG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 324 ISIYSDLKSNIgtLCFNYKNEHPYDLATLLDGYGIAVRSGHHCTQPLMTHLKLNGSLRASFAFYNTTKDVDQFITALKEC 403
Cdd:TIGR03392 315 FRSFRCQGSSL--LAFDFAGVHHSDLVTLLAEQGIALRAGQHCAQPLMAALGVSGTLRASFAPYNTQQDVDALVNAVGRA 392
|
....
gi 1590405280 404 IALL 407
Cdd:TIGR03392 393 LELL 396
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
28-405 |
6.99e-54 |
|
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: 183.33 E-value: 6.99e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 28 VYLDSAATTQKPQCVIDATNEFYTYQNAN---VHR-GRhtlseQATTAYELVRQRVADYFQVSGNEIVWTKGATEAINLV 103
Cdd:COG1104 4 IYLDNAATTPVDPEVLEAMLPYLTEYFGNpssLHSfGR-----EARAALEEAREQVAALLGADPEEIIFTSGGTEANNLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 104 AHGLRNTLTTD-DTILISPIEHHANIVPWQELAAYtGATLKVLPLNDDATFDISQCCDVIKlTKPALLAITQASNALGNI 182
Cdd:COG1104 79 IKGAARAYRKKgKHIITSAIEHPAVLETARFLEKE-GFEVTYLPVDEDGRVDLEALEAALR-PDTALVSVMHANNETGTI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 183 TDLTPLITAAKAVNALTLVDGAQGALHLRPNLIKLDCDFYVFSAHKMLGPTGLGGLYGRYSAlnALSPYQTGGEMiekvt 262
Cdd:COG1104 157 QPIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRKGV--RLEPLIHGGGQ----- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 263 ltQSTYRdapakfeAGTPNIAGVLGFGAALEyiIALDQ--------QTLKHY-EQQLfiyaanaLNQIDGISIYSDLKSN 333
Cdd:COG1104 230 --ERGLR-------SGTENVPGIVGLGKAAE--LAAEEleeeaarlRALRDRlEEGL-------LAAIPGVVINGDPENR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 334 I-GTLCFNYKNEHPYDLATLLDGYGIAVRSGHHCT----QP---LM----THLKLNGSLRASFAFYNTTKDVDQFITALK 401
Cdd:COG1104 292 LpNTLNFSFPGVEGEALLLALDLAGIAVSSGSACSsgslEPshvLLamglDEELAHGSIRFSLGRFTTEEEIDRAIEALK 371
|
....
gi 1590405280 402 ECIA 405
Cdd:COG1104 372 EIVA 375
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
28-394 |
9.89e-23 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 98.57 E-value: 9.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 28 VYLDSAATTQ-KPQcVIDATNEFYTYQNANVHRGRHTLSEQATTAYELVRQRVADYFQVSGNEIVWTKGATE----AINL 102
Cdd:PLN02651 1 LYLDMQATTPiDPR-VLDAMLPFLIEHFGNPHSRTHLYGWESEDAVEKARAQVAALIGADPKEIIFTSGATEsnnlAIKG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 103 VAHGLRNtltTDDTILISPIEHHANIVPWQELAAyTGATLKVLPLNDDATFDISQCCDVIKlTKPALLAITQASNALGNI 182
Cdd:PLN02651 80 VMHFYKD---KKKHVITTQTEHKCVLDSCRHLQQ-EGFEVTYLPVKSDGLVDLDELAAAIR-PDTALVSVMAVNNEIGVI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 183 TDLTPLITAAKAVNALTLVDGAQGALHLRPNLIKLDCDFYVFSAHKMLGPTGLGGLYGRYSALNALSPYQTGGemiekvt 262
Cdd:PLN02651 155 QPVEEIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRLEPLMSGG------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 263 lTQSTYRdapakfEAGTPNIAGVLGFGAALEyiIAL-----DQQTLKHYEQQLFiyaaNAL-NQIDGISI---YSDLKSN 333
Cdd:PLN02651 228 -GQERGR------RSGTENTPLVVGLGAACE--LAMkemdyDEKHMKALRERLL----NGLrAKLGGVRVngpRDPEKRY 294
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590405280 334 IGTLCFNYKNEHPydlATLLDGY-GIAVRSGHHCTQPL---------------MTHlklnGSLRASFAFYNTTKDVD 394
Cdd:PLN02651 295 PGTLNLSFAYVEG---ESLLMGLkEVAVSSGSACTSASlepsyvlralgvpeeMAH----GSLRLGVGRFTTEEEVD 364
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
28-407 |
5.44e-20 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 91.16 E-value: 5.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 28 VYLDSAATTQKPQCVIDATNEFYTYQN--ANVHRGRHTLSEQATTAYELVRQRVADYFQVSGNEIVWTKGATEAINL--- 102
Cdd:PRK14012 5 IYLDYSATTPVDPRVAEKMMPYLTMDGtfGNPASRSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDNLaik 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 103 -VAHGLRNTlttDDTILISPIEHHANIVPWQELAAyTGATLKVLPLNDDATFDISQCCDVIKlTKPALLAITQASNALGN 181
Cdd:PRK14012 85 gAAHFYQKK---GKHIITSKTEHKAVLDTCRQLER-EGFEVTYLDPQSNGIIDLEKLEAAMR-DDTILVSIMHVNNEIGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 182 ITDLTPLITAAKAVNALTLVDGAQGALHLRPNLIKLDCDFYVFSAHKMLGPTGLGGLYGRYSALNALSPYQTGGEMiEKv 261
Cdd:PRK14012 160 IQDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRLEAQMHGGGH-ER- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 262 tltqstyrdapaKFEAGTPNIAGVLGFGAAleYIIAL-----DQQTLKHYEQQLFiyaaNALNQIDGISIYSDLKSNIG- 335
Cdd:PRK14012 238 ------------GMRSGTLPTHQIVGMGEA--ARIAKeematENERIRALRDRLW----NGIKDIEEVYLNGDLEQRVPg 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 336 --TLCFNYKNEHPYDLAtLLDgygIAVRSGHHCT----QP--LMTHLKLN-----GSLRASFAFYNTTKDVDQFITALKE 402
Cdd:PRK14012 300 nlNVSFNYVEGESLIMA-LKD---LAVSSGSACTsaslEPsyVLRALGLNdelahSSIRFSLGRFTTEEEIDYAIELVRK 375
|
....*
gi 1590405280 403 CIALL 407
Cdd:PRK14012 376 SIGKL 380
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
72-241 |
1.73e-12 |
|
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: 65.10 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 72 YELVRQRVADYFQVSGNEIVWTKGATEAINLVAHGLrntLTTDDTILISPIEHHANIVPWQELAaytGATLKVLPLNDDA 151
Cdd:cd01494 2 LEELEEKLARLLQPGNDKAVFVPSGTGANEAALLAL---LGPGDEVIVDANGHGSRYWVAAELA---GAKPVPVPVDDAG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 152 TFDIsQCCDVI--KLTKPALLAITQASNALGNITDLTPLI-TAAKAVNALTLVDGAQGALHLRPNLIKLD---CDFYVFS 225
Cdd:cd01494 76 YGGL-DVAILEelKAKPNVALIVITPNTTSGGVLVPLKEIrKIAKEYGILLLVDAASAGGASPAPGVLIPeggADVVTFS 154
|
170
....*....|....*.
gi 1590405280 226 AHKMLGPTGLGGLYGR 241
Cdd:cd01494 155 LHKNLGGEGGGVVIVK 170
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
27-400 |
5.69e-12 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 66.68 E-value: 5.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 27 LVYLDSAATTQKPQCVIDATNEFYT--YQNANvhrGRHTLSEQATTAYELVRQRVADYfqVSGNE--IVWTKGATEAINL 102
Cdd:PRK02948 1 MIYLDYAATTPMSKEALQTYQKAASqyFGNES---SLHDIGGTASSLLQVCRKTFAEM--IGGEEqgIYFTSGGTESNYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 103 VAHGLRNTLT-TDDTILISPIEHHANIVPWQELAAyTGATLKVLPLNDDATFDISQCCDVIKlTKPALLAITQASNALGN 181
Cdd:PRK02948 76 AIQSLLNALPqNKKHIITTPMEHASIHSYFQSLES-QGYTVTEIPVDKSGLIRLVDLERAIT-PDTVLASIQHANSEIGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 182 ITDLTPLITAAKAVNALTLVDGAQGALHLRPNLIKLDCDFYVFSAHKMLGPTGLGGLYgrysalnaLSPyQTGGEMIEKV 261
Cdd:PRK02948 154 IQPIAEIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVY--------INP-QVRWKPVFPG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 262 TLTQSTYRdapakfeAGTPNIAGVLGFGAALEYIIAlDQQTLKHYEQQLFIYAANALnQIDGISIYSD------LKSNIG 335
Cdd:PRK02948 225 TTHEKGFR-------PGTVNVPGIAAFLTAAENILK-NMQEESLRFKELRSYFLEQI-QTLPLPIEVEghstscLPHIIG 295
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1590405280 336 tlCFNYKNEHPYdlaTLLD--GYGIAVRSGHHCT----QPLMTHLKLNGS-------LRASFAFYNTTKDVDQFITAL 400
Cdd:PRK02948 296 --VTIKGIEGQY---TMLEcnRRGIAISTGSACQvgkqEPSKTMLAIGKTyeeakqfVRFSFGQQTTKDQIDTTIHAL 368
|
|
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
14-344 |
5.29e-11 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 64.50 E-value: 5.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 14 DFPTLNQTingyplVYLDSAATTQKPQCVIDAT-NEFytyqNANVHRGRHTLSE---QATTAYELVRQRVADYFQVSGNE 89
Cdd:PLN02724 28 EFARLKGV------VYLDHAGATLYSESQLEAAlADF----SSNVYGNPHSQSDssmRSSDTIESARQQVLEYFNAPPSD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 90 --IVWTKGATEAINLVAHGLRntlTTDDTILISPIEHHANIVPWQELAAYTGATLKVLPLNDDATFDISQCCDViKLTKP 167
Cdd:PLN02724 98 yaCVFTSGATAALKLVGETFP---WSSESHFCYTLENHNSVLGIREYALEKGAAAIAVDIEEAANQPTNSQGSV-VVKSR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 168 AL----LAITQASNALGNI------------------TDLTPLITAAKAVNA------LTLVDGAQGALHLRPNLIKLDC 219
Cdd:PLN02724 174 GLqrrnTSKLQKREDDGEAynlfafpsecnfsgakfpLDLVKLIKDNQHSNFsksgrwMVLLDAAKGCGTSPPDLSRYPA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 220 DFYVFSAHKMLG-PTGLGGLYGRYSALNALS-PYQTGGEMieKVTLTQSTY---RDAPAK-FEAGTPNIAGVLGFGAALE 293
Cdd:PLN02724 254 DFVVVSFYKIFGyPTGLGALLVRRDAAKLLKkKYFGGGTV--AASIADIDFvkrRERVEQrFEDGTISFLSIAALRHGFK 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1590405280 294 YIIALDQQTLKHYEQQLFIYAANALnqidgisiySDLK-SNIGTLCFNYKNE 344
Cdd:PLN02724 332 LLNRLTISAIAMHTWALTHYVANSL---------RNLKhGNGAPVCVLYGNH 374
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
55-402 |
9.73e-06 |
|
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: 47.34 E-value: 9.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 55 ANVHRGRHTLSEQATTAYELVRQRVADYFQVSGN------EIVWTKGATEAINLVAHGLRNtltTDDTILISPIEHHani 128
Cdd:cd00609 21 AAAALRAGLLGYYPDPGLPELREAIAEWLGRRGGvdvppeEIVVTNGAQEALSLLLRALLN---PGDEVLVPDPTYP--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 129 vPWQELAAYTGATLKVLPLNDDATF-DISQCCDVIKLTKPALLAITQASNALGNITD---LTPLITAAKAVNALTLVDGA 204
Cdd:cd00609 95 -GYEAAARLAGAEVVPVPLDEEGGFlLDLELLEAAKTPKTKLLYLNNPNNPTGAVLSeeeLEELAELAKKHGILIISDEA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 205 ------QGALH-LRPNLIKLDCDFYVFSAHKMLGPTGL--GGLYGRysalnalspyqtGGEMIEKVTLTQStyrdapakF 275
Cdd:cd00609 174 yaelvyDGEPPpALALLDAYERVIVLRSFSKTFGLPGLriGYLIAP------------PEELLERLKKLLP--------Y 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 276 EAGTPNIAGVLGfgaaleyIIALDQQTLKHYEQQLFIYAAN------ALNQIDGISIYSDLKSNIGTLCFNyKNEHPYDL 349
Cdd:cd00609 234 TTSGPSTLSQAA-------AAAALDDGEEHLEELRERYRRRrdalleALKELGPLVVVKPSGGFFLWLDLP-EGDDEEFL 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1590405280 350 ATLLDGYGIAVRSGHHCtqplmtHLKLNGSLRASFAfyNTTKDVDQFITALKE 402
Cdd:cd00609 306 ERLLLEAGVVVRPGSAF------GEGGEGFVRLSFA--TPEEELEEALERLAE 350
|
|
| HisC |
COG0079 |
Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid ... |
70-215 |
2.40e-05 |
|
Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid transport and metabolism]; Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 439849 [Multi-domain] Cd Length: 341 Bit Score: 45.89 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 70 TAYELvRQRVADYFQVSGNEIVWTKGATEAINLVAHGLrntLTTDDTILISPI---EHhanivpwQELAAYTGATLKVLP 146
Cdd:COG0079 49 DATAL-REALAEYYGVPPEQVLVGNGSDELIQLLARAF---LGPGDEVLVPEPtfsEY-------PIAARAAGAEVVEVP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 147 LNDDATFDISQCCDVIKlTKPALLAITQASNALGNITDLTPLITAAKAVNALTLV----------DGAQGALHL---RPN 213
Cdd:COG0079 118 LDEDFSLDLDALLAAIT-ERTDLVFLCNPNNPTGTLLPREELEALLEALPADGLVvvdeayaefvPEEDSALPLlarYPN 196
|
..
gi 1590405280 214 LI 215
Cdd:COG0079 197 LV 198
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
95-236 |
1.34e-03 |
|
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.
Pssm-ID: 99744 [Multi-domain] Cd Length: 356 Bit Score: 40.74 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 95 GATEAinlvahGLRNTLTTDDTILISPIEHHANIvpWQELAAYTGATLKVLPLNDDATFDISQCCDVIKLTKPALLAITQ 174
Cdd:cd06451 61 GAMEA------ALSNLLEPGDKVLVGVNGVFGDR--WADMAERYGADVDVVEKPWGEAVSPEEIAEALEQHDIKAVTLTH 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590405280 175 ASNALGNITDLTPLITAAKAVNALTLVDG--AQGALHLRPNLIKLDCdfyVFSA-HKMLG-PTGLG 236
Cdd:cd06451 133 NETSTGVLNPLEGIGALAKKHDALLIVDAvsSLGGEPFRMDEWGVDV---AYTGsQKALGaPPGLG 195
|
|
| SepCysS |
cd06452 |
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ... |
93-329 |
1.92e-03 |
|
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: 40.07 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 93 TKGATEAINLVAHGLrntLTTDDTILISPIEHHANIVPwQELAaytGATLKVLPLNDDATFDIS--QCCDVIKLTK---- 166
Cdd:cd06452 65 TPGAREGKFAVMHSL---CEKGDWVVVDGLAHYTSYVA-AERA---GLNVREVPNTGHPEYHITpeGYAEVIEEVKdefg 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 167 --PALLAITQASNALGNITDLTPLITAAKAVNALTLVDGAQGALHLRPNLIKLDCDFYVFSAHKMLGPTGLGGLYGrysa 244
Cdd:cd06452 138 kpPALALLTHVDGNYGNLHDAKKIAKVCHEYGVPLLLNGAYTVGRMPVSGKELGADFIVGSGHKSMAASAPIGVLA---- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 245 lnalspyqTGGEMIEKVTLTQSTYRDAPAKFEAGTPNIAGVLGFGAALEYIIaldqQTLKHYEQQL--FIYAANALNQID 322
Cdd:cd06452 214 --------TTEEWADIVFRTSQMFKIKEVELLGCTLRGAPLVTLMASFPHVK----ERVKRWDEEVekARWFVAELEKIE 281
|
....*..
gi 1590405280 323 GISIYSD 329
Cdd:cd06452 282 GIKQLGE 288
|
|
| PRK06836 |
PRK06836 |
pyridoxal phosphate-dependent aminotransferase; |
39-155 |
7.94e-03 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180720 Cd Length: 394 Bit Score: 38.25 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405280 39 PQCVIDATNEFYTYQNANVHR-----GrhtlseqattaYELVRQRVADYFQ------VSGNEIVWTKGATEAINLVahgL 107
Cdd:PRK06836 48 PAAVKEALRELAEEEDPGLHGympnaG-----------YPEVREAIAESLNrrfgtpLTADHIVMTCGAAGALNVA---L 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1590405280 108 RnTLTT--DDTILISP--------IEHHanivpwqelaaytGATLKVLPLNDDaTFDI 155
Cdd:PRK06836 114 K-AILNpgDEVIVFAPyfveyrfyVDNH-------------GGKLVVVPTDTD-TFQP 156
|
|
| |
