|
Name |
Accession |
Description |
Interval |
E-value |
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
1-380 |
2.49e-179 |
|
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: 503.04 E-value: 2.49e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 1 MIYFDNAATTQVYPEVLKTYTEVATKIWGNPSSLHSLGSQATRILEASRKQIAELLGKDSKEIFFTSGGTEGDNWVIKGV 80
Cdd:COG1104 3 MIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSSLHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNLAIKGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 81 AFEKAHLGKHIIVSAIEHPAVKESALWLKTQGFEVDLAPVNTQGFVDVSALESLIRPDTTLVSIMAVNNEIGSIQPIQEI 160
Cdd:COG1104 83 ARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQPIAEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 161 SQLLADKPTIsFHVDAVQAIGKVPTEgyLTD-RVDFASFSGHKFHSVRGVGFVYVKAGKKIAPLLTGGGQESDKRSTTEN 239
Cdd:COG1104 163 AEIAKEHGVL-FHTDAVQAVGKIPVD--VKElGVDLLSLSAHKIYGPKGVGALYVRKGVRLEPLIHGGGQERGLRSGTEN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 240 VAGIAATAKALRLTLDKAVDSQKRLAAMKQILVDEL-GKYADVTVFSGLEDFVPSIVTFGIKNIRGEVIVHAFEDHQIYI 318
Cdd:COG1104 240 VPGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLlAAIPGVVINGDPENRLPNTLNFSFPGVEGEALLLALDLAGIAV 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 656223624 319 STTSACSSKAGKPAGTLIAMGVPQKLAQTAVRISLDDDNDMGQIEQFLTIFKQIYQNTQKVR 380
Cdd:COG1104 320 SSGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARLRKLS 381
|
|
| FeS_nifS |
TIGR03402 |
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related ... |
2-372 |
5.35e-120 |
|
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related families of cysteine desulfurase involved in iron-sulfur (FeS) cluster biosynthesis. NifS is part of the NIF system, usually associated with other nif genes involved in nitrogenase expression and nitrogen fixation. The protein family is given a fairly broad interpretation here. It includes a clade nearly always found in extended nitrogen fixation genomic regions, plus a second clade more closely related to the first than to IscS and also part of NifS-like/NifU-like systems. This model does not extend to a more distantly clade found in the epsilon proteobacteria such as Helicobacter pylori, also named NifS in the literature, built instead in TIGR03403.
Pssm-ID: 132443 [Multi-domain] Cd Length: 379 Bit Score: 352.30 E-value: 5.35e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 2 IYFDNAATTQVYPEVLKTYTEVATKIWGNPSSLHSLGSQATRILEASRKQIAELLGKDSKEIFFTSGGTEGDNWVIKGVA 81
Cdd:TIGR03402 1 IYLDNNATTRVDPEVLEAMLPYFTEYFGNPSSMHSFGGEVGKAVEEAREQVAKLLGAEPDEIIFTSGGTESDNTAIKSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 82 FekAHLGK-HIIVSAIEHPAVKESALWLKTQGFEVDLAPVNTQGFVDVSALESLIRPDTTLVSIMAVNNEIGSIQPIQEI 160
Cdd:TIGR03402 81 A--AQPEKrHIITTAVEHPAVLSLCQHLEKQGYKVTYLPVDEEGRLDLEELRAAITDDTALVSVMWANNETGTIFPIEEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 161 SQLLADKpTISFHVDAVQAIGKVPTEGYLTDrVDFASFSGHKFHSVRGVGFVYVKAGKKIAPLLTGGGQESDKRSTTENV 240
Cdd:TIGR03402 159 GEIAKER-GALFHTDAVQAVGKIPIDLKEMN-IDMLSLSGHKLHGPKGVGALYIRKGTRFRPLLRGGHQERGRRAGTENV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 241 AGIAATAKALRLTLDKAVDSQKRLAAMKQILVDE-LGKYADVTVFSGLEDFVPSIVTFGIKNIRGEVIVHAFEDHQIYIS 319
Cdd:TIGR03402 237 PGIVGLGKAAELATEHLEEENTRVRALRDRLEAGlLARIPDARLNGDPTKRLPNTVNISFEYIEGEAILLLLDMEGICAS 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 656223624 320 TTSACSSKAGKPAGTLIAMGVPQKLAQTAVRISLDDDNDMGQIEQFLTIFKQI 372
Cdd:TIGR03402 317 SGSACTSGSLEPSHVLRAMGVPHTAAHGSIRFSLSRYNTEEDIDYVLEVLPPI 369
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
2-353 |
7.81e-95 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 287.71 E-value: 7.81e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 2 IYFDNAATTQVYPEVLKTYTEVATKIWGNPSSL-HSLGSQATRILEASRKQIAELLGKDSKEIFFTSGGTEGDNWVIKGV 80
Cdd:PLN02651 1 LYLDMQATTPIDPRVLDAMLPFLIEHFGNPHSRtHLYGWESEDAVEKARAQVAALIGADPKEIIFTSGATESNNLAIKGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 81 A-FEKAHlGKHIIVSAIEHPAVKESALWLKTQGFEVDLAPVNTQGFVDVSALESLIRPDTTLVSIMAVNNEIGSIQPIQE 159
Cdd:PLN02651 81 MhFYKDK-KKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 160 ISQlLADKPTISFHVDAVQAIGKVPTEGYLTDrVDFASFSGHKFHSVRGVGFVYVKAGKKIA--PLLTGGGQESDKRSTT 237
Cdd:PLN02651 160 IGE-LCREKKVLFHTDAAQAVGKIPVDVDDLG-VDLMSISGHKIYGPKGVGALYVRRRPRVRlePLMSGGGQERGRRSGT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 238 ENVAGIAATAKALRLTLDKAVDSQKRLAAMKQILVDELGKYADVTVFSGLEDF---VPSIVTFGIKNIRGEVIVHAFEDh 314
Cdd:PLN02651 238 ENTPLVVGLGAACELAMKEMDYDEKHMKALRERLLNGLRAKLGGVRVNGPRDPekrYPGTLNLSFAYVEGESLLMGLKE- 316
|
330 340 350
....*....|....*....|....*....|....*....
gi 656223624 315 qIYISTTSACSSKAGKPAGTLIAMGVPQKLAQTAVRISL 353
Cdd:PLN02651 317 -VAVSSGSACTSASLEPSYVLRALGVPEEMAHGSLRLGV 354
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
2-365 |
1.79e-76 |
|
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: 240.61 E-value: 1.79e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 2 IYFDNAATTQVYPEVLKTYTEVATKIWGNP-SSLHSLGSQATRILEASRKQIAELLG-KDSKEIFFTSGGTEGDNWVIKG 79
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVhRGVHTLGKEATQAYEEAREKVAEFINaPSNDEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 80 VA--FEKahlGKHIIVSAIEHPAVKESALWL-KTQGFEVDLAPVNTQGFVDVSALESLIRPDTTLVSIMAVNNEIGSIQP 156
Cdd:pfam00266 81 LGrsLKP---GDEIVITEMEHHANLVPWQELaKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 157 IQEISQlLADKPTISFHVDAVQAIGKVPTEGYLTDrVDFASFSGHKFHSVRGVGFVYVK--AGKKIAPLLTGGGQESDK- 233
Cdd:pfam00266 158 VPEIGK-LAHQYGALVLVDAAQAIGHRPIDVQKLG-VDFLAFSGHKLYGPTGIGVLYGRrdLLEKMPPLLGGGGMIETVs 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 234 -------------RSTTENVAGIAATAKALRLTLDKAVD-SQKRLAAMKQILVDELGKYADVTVFSGLEDfvPSIVTFGI 299
Cdd:pfam00266 236 lqestfadapwkfEAGTPNIAGIIGLGAALEYLSEIGLEaIEKHEHELAQYLYERLLSLPGIRLYGPERR--ASIISFNF 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 656223624 300 KNIRGEVIVHAFEDHQIYISTTSACSskagKPAGTLIAMgvpqklaQTAVRISLDDDNDMGQIEQF 365
Cdd:pfam00266 314 KGVHPHDVATLLDESGIAVRSGHHCA----QPLMVRLGL-------GGTVRASFYIYNTQEDVDRL 368
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
2-320 |
3.72e-49 |
|
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: 169.95 E-value: 3.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 2 IYFDNAATTQVYPEVLKTYTEVATKIWGNPS-SLHSLGSQATRILEASRKQIAELLG-KDSKEIFFTSGGTEGDNWVIKG 79
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHrGVHELSARATDAYEAAREKVARFINaPSPDEIIFTRNTTEAINLVAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 80 VAFEKAHlGKHIIVSAIEHPAVkesaL--WL---KTQGFEVDLAPVNTQGFVDVSALESLIRPDTTLVSIMAVNNEIGSI 154
Cdd:cd06453 81 LGRANKP-GDEIVTSVMEHHSN----IvpWQqlaERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 155 QPIQEISQlLADKPTISFHVDAVQAIG--KVPTEGYltdRVDFASFSGHKFHSVRGVGFVYVKAGKKIAPLLTGGGQESD 232
Cdd:cd06453 156 NPVKEIGE-IAHEAGVPVLVDGAQSAGhmPVDVQDL---GCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 233 KRST----------------TENVAGIAATAKALR----LTLDKAVDSQKRLAAMkqiLVDELGKYADVTVFSGLEDFVp 292
Cdd:cd06453 232 EEVSfeettyadlphkfeagTPNIAGAIGLGAAIDylekIGMEAIAAHEHELTAY---ALERLSEIPGVRVYGDAEDRA- 307
|
330 340
....*....|....*....|....*...
gi 656223624 293 SIVTFGIKNIRGEVIVHAFEDHQIYIST 320
Cdd:cd06453 308 GVVSFNLEGIHPHDVATILDQYGIAVRA 335
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
2-216 |
1.31e-14 |
|
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: 75.28 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 2 IYFDNAATTQvypevlktytevatKiwgnPSSL-------------------HSLGSQATRILEASRKQIAELLG-KDSK 61
Cdd:NF041166 247 VWFDNAATTQ--------------K----PQAVidrlsyfyehensnihraaHELAARATDAYEGAREKVRRFIGaPSVD 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 62 EIFFTSGGTEGDNWVIKgvAFEKAHL--GKHIIVSAIEHPA--------VKESALWLKtqgfevdLAPVNTQGFVDVSAL 131
Cdd:NF041166 309 EIIFVRGTTEAINLVAK--SWGRQNIgaGDEIIVSHLEHHAnivpwqqlAQETGAKLR-------VIPVDDSGQILLDEY 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 132 ESLIRPDTTLVSIMAVNNEIGSIQPIQEISQL--------LAD-KPTISfH--VDaVQAIGkvptegyltdrVDFASFSG 200
Cdd:NF041166 380 AKLLNPRTKLVSVTQVSNALGTVTPVKEIIALahragakvLVDgAQSVS-HmpVD-VQALD-----------ADFFVFSG 446
|
250
....*....|....*.
gi 656223624 201 HKFHSVRGVGFVYVKA 216
Cdd:NF041166 447 HKVFGPTGIGVVYGKR 462
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
1-380 |
2.49e-179 |
|
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: 503.04 E-value: 2.49e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 1 MIYFDNAATTQVYPEVLKTYTEVATKIWGNPSSLHSLGSQATRILEASRKQIAELLGKDSKEIFFTSGGTEGDNWVIKGV 80
Cdd:COG1104 3 MIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSSLHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNLAIKGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 81 AFEKAHLGKHIIVSAIEHPAVKESALWLKTQGFEVDLAPVNTQGFVDVSALESLIRPDTTLVSIMAVNNEIGSIQPIQEI 160
Cdd:COG1104 83 ARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQPIAEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 161 SQLLADKPTIsFHVDAVQAIGKVPTEgyLTD-RVDFASFSGHKFHSVRGVGFVYVKAGKKIAPLLTGGGQESDKRSTTEN 239
Cdd:COG1104 163 AEIAKEHGVL-FHTDAVQAVGKIPVD--VKElGVDLLSLSAHKIYGPKGVGALYVRKGVRLEPLIHGGGQERGLRSGTEN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 240 VAGIAATAKALRLTLDKAVDSQKRLAAMKQILVDEL-GKYADVTVFSGLEDFVPSIVTFGIKNIRGEVIVHAFEDHQIYI 318
Cdd:COG1104 240 VPGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLlAAIPGVVINGDPENRLPNTLNFSFPGVEGEALLLALDLAGIAV 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 656223624 319 STTSACSSKAGKPAGTLIAMGVPQKLAQTAVRISLDDDNDMGQIEQFLTIFKQIYQNTQKVR 380
Cdd:COG1104 320 SSGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARLRKLS 381
|
|
| FeS_nifS |
TIGR03402 |
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related ... |
2-372 |
5.35e-120 |
|
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related families of cysteine desulfurase involved in iron-sulfur (FeS) cluster biosynthesis. NifS is part of the NIF system, usually associated with other nif genes involved in nitrogenase expression and nitrogen fixation. The protein family is given a fairly broad interpretation here. It includes a clade nearly always found in extended nitrogen fixation genomic regions, plus a second clade more closely related to the first than to IscS and also part of NifS-like/NifU-like systems. This model does not extend to a more distantly clade found in the epsilon proteobacteria such as Helicobacter pylori, also named NifS in the literature, built instead in TIGR03403.
Pssm-ID: 132443 [Multi-domain] Cd Length: 379 Bit Score: 352.30 E-value: 5.35e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 2 IYFDNAATTQVYPEVLKTYTEVATKIWGNPSSLHSLGSQATRILEASRKQIAELLGKDSKEIFFTSGGTEGDNWVIKGVA 81
Cdd:TIGR03402 1 IYLDNNATTRVDPEVLEAMLPYFTEYFGNPSSMHSFGGEVGKAVEEAREQVAKLLGAEPDEIIFTSGGTESDNTAIKSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 82 FekAHLGK-HIIVSAIEHPAVKESALWLKTQGFEVDLAPVNTQGFVDVSALESLIRPDTTLVSIMAVNNEIGSIQPIQEI 160
Cdd:TIGR03402 81 A--AQPEKrHIITTAVEHPAVLSLCQHLEKQGYKVTYLPVDEEGRLDLEELRAAITDDTALVSVMWANNETGTIFPIEEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 161 SQLLADKpTISFHVDAVQAIGKVPTEGYLTDrVDFASFSGHKFHSVRGVGFVYVKAGKKIAPLLTGGGQESDKRSTTENV 240
Cdd:TIGR03402 159 GEIAKER-GALFHTDAVQAVGKIPIDLKEMN-IDMLSLSGHKLHGPKGVGALYIRKGTRFRPLLRGGHQERGRRAGTENV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 241 AGIAATAKALRLTLDKAVDSQKRLAAMKQILVDE-LGKYADVTVFSGLEDFVPSIVTFGIKNIRGEVIVHAFEDHQIYIS 319
Cdd:TIGR03402 237 PGIVGLGKAAELATEHLEEENTRVRALRDRLEAGlLARIPDARLNGDPTKRLPNTVNISFEYIEGEAILLLLDMEGICAS 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 656223624 320 TTSACSSKAGKPAGTLIAMGVPQKLAQTAVRISLDDDNDMGQIEQFLTIFKQI 372
Cdd:TIGR03402 317 SGSACTSGSLEPSHVLRAMGVPHTAAHGSIRFSLSRYNTEEDIDYVLEVLPPI 369
|
|
| DNA_S_dndA |
TIGR03235 |
cysteine desulfurase DndA; This model describes DndA, a protein related to IscS and part of a ... |
3-353 |
2.88e-99 |
|
cysteine desulfurase DndA; This model describes DndA, a protein related to IscS and part of a larger family of cysteine desulfurases. It is encoded, typically, divergently from a conserved, sparsely distributed operon for sulfur modification of DNA. This modification system is designated dnd, after the phenotype of DNA degradation during electrophoresis. The system is sporadically distributed in bacteria, much like some restriction enzyme operons. DndB is described as a putative ATPase. [DNA metabolism, Restriction/modification]
Pssm-ID: 163191 [Multi-domain] Cd Length: 353 Bit Score: 298.63 E-value: 2.88e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 3 YFDNAATTQVYPEVLKTYTEVATKIWGNPSSL-HSLGSQATRILEASRKQIAELLGKDSKEIFFTSGGTEGDNWVIKGVA 81
Cdd:TIGR03235 1 YLDHNATTPIDPAVAEAMLPWLLEEFGNPSSRtHEFGHNAKKAVERARKQVAEALGADTEEVIFTSGATESNNLAILGLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 82 -FEKAHLGKHIIVSAIEHPAVKESALWLKTQGFEVDLAPVNTQGFVDVSALESLIRPDTTLVSIMAVNNEIGSIQPIQEI 160
Cdd:TIGR03235 81 rAGEQKGKKHIITSAIEHPAVLEPIRALERNGFTVTYLPVDESGRIDVDELADAIRPDTLLVSIMHVNNETGSIQPIREI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 161 SQLLADKPTIsFHVDAVQAIGKVPTEgyLT-DRVDFASFSGHKFHSVRGVGFVYVKAGKK----IAPLLTGGGQESDKRS 235
Cdd:TIGR03235 161 AEVLEAHEAF-FHVDAAQVVGKITVD--LSaDRIDLISCSGHKIYGPKGIGALVIRKRGKpkapLKPIMFGGGQERGLRP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 236 TTENVAGIAATAKALRLTLDKAVDSQKRLAAMKQILVDELGKyADVTVFSGLEDFVPSIVTFGIKNIRGEVIVHAFEDhQ 315
Cdd:TIGR03235 238 GTLPVHLIVGMGEAAEIARRNAQAWEVKLRAMRNQLRDALQT-LGVKLNGDPAETIPHILNFSIDGVNSEALIVNLRA-D 315
|
330 340 350
....*....|....*....|....*....|....*...
gi 656223624 316 IYISTTSACSSKAGKPAGTLIAMGVPQKLAQTAVRISL 353
Cdd:TIGR03235 316 AAVSTGSACSSSKYEPSHVLQAMGLDTDRARGAIRFSW 353
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
2-353 |
7.81e-95 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 287.71 E-value: 7.81e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 2 IYFDNAATTQVYPEVLKTYTEVATKIWGNPSSL-HSLGSQATRILEASRKQIAELLGKDSKEIFFTSGGTEGDNWVIKGV 80
Cdd:PLN02651 1 LYLDMQATTPIDPRVLDAMLPFLIEHFGNPHSRtHLYGWESEDAVEKARAQVAALIGADPKEIIFTSGATESNNLAIKGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 81 A-FEKAHlGKHIIVSAIEHPAVKESALWLKTQGFEVDLAPVNTQGFVDVSALESLIRPDTTLVSIMAVNNEIGSIQPIQE 159
Cdd:PLN02651 81 MhFYKDK-KKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 160 ISQlLADKPTISFHVDAVQAIGKVPTEGYLTDrVDFASFSGHKFHSVRGVGFVYVKAGKKIA--PLLTGGGQESDKRSTT 237
Cdd:PLN02651 160 IGE-LCREKKVLFHTDAAQAVGKIPVDVDDLG-VDLMSISGHKIYGPKGVGALYVRRRPRVRlePLMSGGGQERGRRSGT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 238 ENVAGIAATAKALRLTLDKAVDSQKRLAAMKQILVDELGKYADVTVFSGLEDF---VPSIVTFGIKNIRGEVIVHAFEDh 314
Cdd:PLN02651 238 ENTPLVVGLGAACELAMKEMDYDEKHMKALRERLLNGLRAKLGGVRVNGPRDPekrYPGTLNLSFAYVEGESLLMGLKE- 316
|
330 340 350
....*....|....*....|....*....|....*....
gi 656223624 315 qIYISTTSACSSKAGKPAGTLIAMGVPQKLAQTAVRISL 353
Cdd:PLN02651 317 -VAVSSGSACTSASLEPSYVLRALGVPEEMAHGSLRLGV 354
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
1-374 |
1.56e-90 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 277.38 E-value: 1.56e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 1 MIYFDNAATTQVYPEVLKTYTEVATKIWGNPSSLHSLGSQATRILEASRKQIAELLGKDSKEIFFTSGGTEGDNWVIKGV 80
Cdd:PRK02948 1 MIYLDYAATTPMSKEALQTYQKAASQYFGNESSLHDIGGTASSLLQVCRKTFAEMIGGEEQGIYFTSGGTESNYLAIQSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 81 AFEKAHLGKHIIVSAIEHPAVKESALWLKTQGFEVDLAPVNTQGFVDVSALESLIRPDTTLVSIMAVNNEIGSIQPIQEI 160
Cdd:PRK02948 81 LNALPQNKKHIITTPMEHASIHSYFQSLESQGYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQPIAEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 161 SQLLADKPTIsFHVDAVQAIGKVPTEgylTDR--VDFASFSGHKFHSVRGVGFVYVKAGKKIAPLLTGGGQESDKRSTTE 238
Cdd:PRK02948 161 GALLKKYNVL-FHSDCVQTFGKLPID---VFEmgIDSLSVSAHKIYGPKGVGAVYINPQVRWKPVFPGTTHEKGFRPGTV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 239 NVAGIAATAKALRLTLDKAVDSQKRLAAMKQILVDELG-KYADVTVFSGLEDFVPSIVTFGIKNIRGEVIVHAFEDHQIY 317
Cdd:PRK02948 237 NVPGIAAFLTAAENILKNMQEESLRFKELRSYFLEQIQtLPLPIEVEGHSTSCLPHIIGVTIKGIEGQYTMLECNRRGIA 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 656223624 318 ISTTSACSSKAGKPAGTLIAMGVPQKLAQTAVRISLDDDNDMGQIEQFLTIFKQIYQ 374
Cdd:PRK02948 317 ISTGSACQVGKQEPSKTMLAIGKTYEEAKQFVRFSFGQQTTKDQIDTTIHALETIGN 373
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
2-353 |
3.63e-89 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 274.51 E-value: 3.63e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 2 IYFDNAATTQVYPEVLKTYTEVATK--IWGNPSSL-HSLGSQATRILEASRKQIAELLGKDSKEIFFTSGGTEGDNWVIK 78
Cdd:PRK14012 5 IYLDYSATTPVDPRVAEKMMPYLTMdgTFGNPASRsHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDNLAIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 79 GVAFEKAHLGKHIIVSAIEHPAVKESALWLKTQGFEVDLAPVNTQGFVDVSALESLIRPDTTLVSIMAVNNEIGSIQPIQ 158
Cdd:PRK14012 85 GAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVIQDIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 159 EISQLLADKPTIsFHVDAVQAIGKVPTEgyLTD-RVDFASFSGHKFHSVRGVGFVYV--KAGKKIAPLLTGGGQESDKRS 235
Cdd:PRK14012 165 AIGEICRERGII-FHVDAAQSVGKVPID--LSKlKVDLMSFSAHKIYGPKGIGALYVrrKPRVRLEAQMHGGGHERGMRS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 236 TTENVAGIAATAKALRLTLDKAVDSQKRLAAMKQILVDELGKYADVTVFSGLEDFVPSIVTFGIKNIRGEVIVHAFEDhq 315
Cdd:PRK14012 242 GTLPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGIKDIEEVYLNGDLEQRVPGNLNVSFNYVEGESLIMALKD-- 319
|
330 340 350
....*....|....*....|....*....|....*...
gi 656223624 316 IYISTTSACSSKAGKPAGTLIAMGVPQKLAQTAVRISL 353
Cdd:PRK14012 320 LAVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSL 357
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
2-365 |
1.79e-76 |
|
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: 240.61 E-value: 1.79e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 2 IYFDNAATTQVYPEVLKTYTEVATKIWGNP-SSLHSLGSQATRILEASRKQIAELLG-KDSKEIFFTSGGTEGDNWVIKG 79
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVhRGVHTLGKEATQAYEEAREKVAEFINaPSNDEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 80 VA--FEKahlGKHIIVSAIEHPAVKESALWL-KTQGFEVDLAPVNTQGFVDVSALESLIRPDTTLVSIMAVNNEIGSIQP 156
Cdd:pfam00266 81 LGrsLKP---GDEIVITEMEHHANLVPWQELaKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 157 IQEISQlLADKPTISFHVDAVQAIGKVPTEGYLTDrVDFASFSGHKFHSVRGVGFVYVK--AGKKIAPLLTGGGQESDK- 233
Cdd:pfam00266 158 VPEIGK-LAHQYGALVLVDAAQAIGHRPIDVQKLG-VDFLAFSGHKLYGPTGIGVLYGRrdLLEKMPPLLGGGGMIETVs 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 234 -------------RSTTENVAGIAATAKALRLTLDKAVD-SQKRLAAMKQILVDELGKYADVTVFSGLEDfvPSIVTFGI 299
Cdd:pfam00266 236 lqestfadapwkfEAGTPNIAGIIGLGAALEYLSEIGLEaIEKHEHELAQYLYERLLSLPGIRLYGPERR--ASIISFNF 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 656223624 300 KNIRGEVIVHAFEDHQIYISTTSACSskagKPAGTLIAMgvpqklaQTAVRISLDDDNDMGQIEQF 365
Cdd:pfam00266 314 KGVHPHDVATLLDESGIAVRSGHHCA----QPLMVRLGL-------GGTVRASFYIYNTQEDVDRL 368
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
2-353 |
3.73e-57 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 191.51 E-value: 3.73e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 2 IYFDNAATTQVYPEVLKTYTEVATKIWGNPS-SLHSLGSQATRILEASRKQIAELLG-KDSKEIFFTSGGTEGDNWVIKG 79
Cdd:COG0520 17 VYLDNAATGQKPRPVIDAIRDYYEPYNANVHrGAHELSAEATDAYEAAREKVARFIGaASPDEIIFTRGTTEAINLVAYG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 80 VAFEKAhlGKHIIVSAIEHPAVKESALWL-KTQGFEVDLAPVNTQGFVDVSALESLIRPDTTLVSIMAVNNEIGSIQPIQ 158
Cdd:COG0520 97 LGRLKP--GDEILITEMEHHSNIVPWQELaERTGAEVRVIPLDEDGELDLEALEALLTPRTKLVAVTHVSNVTGTVNPVK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 159 EISQLLADKPTISFhVDAVQAIGKVPTEgyLTD-RVDFASFSGHKFHSVRGVGFVYVKAG--KKIAPLLTGGG---QESD 232
Cdd:COG0520 175 EIAALAHAHGALVL-VDGAQSVPHLPVD--VQAlGCDFYAFSGHKLYGPTGIGVLYGKREllEALPPFLGGGGmieWVSF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 233 KRST-----------TENVAGIAATAKALRLTLD---KAVdsQKRLAAMKQILVDELGKYADVTVFsGLEDFVP--SIVT 296
Cdd:COG0520 252 DGTTyadlprrfeagTPNIAGAIGLGAAIDYLEAigmEAI--EARERELTAYALEGLAAIPGVRIL-GPADPEDrsGIVS 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 656223624 297 FGIKNIRGEVIVHAFEDHQIYISTTSACsskagkpAGTLI-AMGVPqklaqTAVRISL 353
Cdd:COG0520 329 FNVDGVHPHDVAALLDDEGIAVRAGHHC-------AQPLMrRLGVP-----GTVRASF 374
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
2-320 |
3.72e-49 |
|
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: 169.95 E-value: 3.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 2 IYFDNAATTQVYPEVLKTYTEVATKIWGNPS-SLHSLGSQATRILEASRKQIAELLG-KDSKEIFFTSGGTEGDNWVIKG 79
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHrGVHELSARATDAYEAAREKVARFINaPSPDEIIFTRNTTEAINLVAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 80 VAFEKAHlGKHIIVSAIEHPAVkesaL--WL---KTQGFEVDLAPVNTQGFVDVSALESLIRPDTTLVSIMAVNNEIGSI 154
Cdd:cd06453 81 LGRANKP-GDEIVTSVMEHHSN----IvpWQqlaERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 155 QPIQEISQlLADKPTISFHVDAVQAIG--KVPTEGYltdRVDFASFSGHKFHSVRGVGFVYVKAGKKIAPLLTGGGQESD 232
Cdd:cd06453 156 NPVKEIGE-IAHEAGVPVLVDGAQSAGhmPVDVQDL---GCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 233 KRST----------------TENVAGIAATAKALR----LTLDKAVDSQKRLAAMkqiLVDELGKYADVTVFSGLEDFVp 292
Cdd:cd06453 232 EEVSfeettyadlphkfeagTPNIAGAIGLGAAIDylekIGMEAIAAHEHELTAY---ALERLSEIPGVRVYGDAEDRA- 307
|
330 340
....*....|....*....|....*...
gi 656223624 293 SIVTFGIKNIRGEVIVHAFEDHQIYIST 320
Cdd:cd06453 308 GVVSFNLEGIHPHDVATILDQYGIAVRA 335
|
|
| am_tr_V_EF2568 |
TIGR01977 |
cysteine desulfurase family protein; This model describes a subfamily of probable pyridoxal ... |
2-372 |
5.35e-42 |
|
cysteine desulfurase family protein; This model describes a subfamily of probable pyridoxal phosphate-dependent enzymes in the aminotransferase class V family. Related families contain members active as cysteine desulfurases, selenocysteine lyases, or both. The members of this family form a distinct clade and all are shorter at the N-terminus. The function of this subfamily is unknown. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 131032 [Multi-domain] Cd Length: 376 Bit Score: 150.99 E-value: 5.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 2 IYFDNAATT-----QVYPEVLKTYTEVAtkiwGNPS-SLHSLGSQATRILEASRKQIAELLG-KDSKEIFFTSGGTEGDN 74
Cdd:TIGR01977 1 IYFDNAATTypkpdEVYEAMADFYKNYG----GSPGrGRYRLALRASREVEETRQLLAKLFNaPSSAHVVFTNNATTALN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 75 WVIKGVAFEkahlGKHIIVSAIEHPAVKESALWLKTQ-GFEVDLAPVNTQGFVDVSALESLIRPDTTLVSIMAVNNEIGS 153
Cdd:TIGR01977 77 IALKGLLKE----GDHVITTPMEHNSVARPLECLKEQiGVEITIVKCDNEGLISPERIKRAIKTNTKLIVVSHASNVTGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 154 IQPIQEISQlLADKPTISFHVDAVQAIGKVPTEGYLtDRVDFASFSGHK-FHSVRGVGFVYVKAGKKIAPLLTGG-GQES 231
Cdd:TIGR01977 153 ILPIEEIGE-LAQENGIFFILDAAQTAGVIPIDMTE-LAIDMLAFTGHKgLLGPQGTGGLYIREGIKLKPLKSGGtGSHS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 232 ----------DK-RSTTENVAGIAATAKALRLTLDKAVDS-QKRLAAMKQILVDELGKYADVTVFSG--LEDFVPsIVTF 297
Cdd:TIGR01977 231 alidqpselpDRfESGTLNTPGIAGLNAGIKFIEKIGIANiAKKECMLTEKLLNGLREINKVKIYGPadPANRVG-VVSF 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 656223624 298 GIKNIRGEVIVHAF-EDHQIYISTTSACSSKAGKPAGTliamgvpqkLAQTAVRISLDDDNDMGQIEQFLTIFKQI 372
Cdd:TIGR01977 310 TVEGIDSEEVADILdEKFDIATRTGLHCAPLAHKTIGT---------FATGTIRLSLGYFNTEEEIEKLLEALSEI 376
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
1-322 |
3.21e-26 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 108.68 E-value: 3.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 1 MIYFDNAATTQVYPEVLKTYTEVATKIWGN-PSSLHSLGSQATRILEASRKQIAELLG-KDSKEIFFTSGGTEGDNWVIK 78
Cdd:PLN02855 33 LVYLDNAATSQKPAAVLDALQDYYEEYNSNvHRGIHALSAKATDAYELARKKVAAFINaSTSREIVFTRNATEAINLVAY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 79 --GVAFEKAhlGKHIIVSAIEHPA--VKESALWLKTqGFEVDLAPVNTQGFVDVSALESLIRPDTTLVSIMAVNNEIGSI 154
Cdd:PLN02855 113 twGLANLKP--GDEVILSVAEHHSniVPWQLVAQKT-GAVLKFVGLTPDEVLDVEQLKELLSEKTKLVATHHVSNVLGSI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 155 QPIQEISQlLADKPTISFHVDAVQAIGKVPTEGYLTDrVDFASFSGHKFHSVRGVGFVYVKAG--KKIAPLLTGGGQESD 232
Cdd:PLN02855 190 LPVEDIVH-WAHAVGAKVLVDACQSVPHMPVDVQTLG-ADFLVASSHKMCGPTGIGFLWGKSDllESMPPFLGGGEMISD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 233 ---KRST-----TENVAGIAATAKALRL----------TLDKAVDSQKRLAAmkqILVDELGKYADVTVF---SGLEDFV 291
Cdd:PLN02855 268 vflDHSTyapppSRFEAGTPAIGEAIGLgaaidylseiGMDRIHEYEVELGT---YLYEKLSSVPGVRIYgpkPSEGVGR 344
|
330 340 350
....*....|....*....|....*....|....*.
gi 656223624 292 PSIVTFGIKNIrgevivHA-----FEDHQIYISTTS 322
Cdd:PLN02855 345 AALCAFNVEGI------HPtdlstFLDQQHGVAIRS 374
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
1-215 |
2.18e-25 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 105.99 E-value: 2.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 1 MIYFDNAATTQVYPEVLKT--------YTEVATKIwgnpsslHSLGSQATRILEASRKQIAELLGKDS-KEIFFTSGGTE 71
Cdd:PRK09295 24 LAYLDSAASAQKPSQVIDAeaefyrhgYAAVHRGI-------HTLSAQATEKMENVRKQAALFINARSaEELVFVRGTTE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 72 GDNWVIKGVAFEKAHLGKHIIVSAIEHPA-VKESALWLKTQGFEVDLAPVNTQGFVDVSALESLIRPDTTLVSIMAVNNE 150
Cdd:PRK09295 97 GINLVANSWGNSNVRAGDNIIISEMEHHAnIVPWQMLCARVGAELRVIPLNPDGTLQLETLPALFDERTRLLAITHVSNV 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 656223624 151 IGSIQPIQEISQlLADKPTISFHVDAVQAIGKVPTEGYLTDrVDFASFSGHKFHSVRGVGFVYVK 215
Cdd:PRK09295 177 LGTENPLAEMIA-LAHQHGAKVLVDGAQAVMHHPVDVQALD-CDFYVFSGHKLYGPTGIGILYVK 239
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
2-250 |
1.89e-16 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 80.08 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 2 IYFDNAATTQVYPEVLKTYTEVATKIWGN-PSSLHSLGSQATRILEASRKQIAELLG-KDSKEIFFTSGGTEGDNWVIKG 79
Cdd:PRK10874 21 VYLDSAATALKPQAVIEATQQFYSLSAGNvHRSQFAAAQRLTARYEAAREQVAQLLNaPDAKNIVWTRGTTESINLVAQS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 80 VAFEKAHLGKHIIVSAIEHPAVKESALWLKTQ-GFEVDLAPVNTQGFVDVSALESLIRPDTTLVSIMAVNNEIGSIQPIQ 158
Cdd:PRK10874 101 YARPRLQPGDEIIVSEAEHHANLVPWLMVAQQtGAKVVKLPLGADRLPDVDLLPELITPRTRILALGQMSNVTGGCPDLA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 159 EISQlLADKPTISFHVDAVQAIGKVPTEGYLTDrVDFASFSGHKFHSVRGVGFVYVKAG--KKIAPLLtGGG-------- 228
Cdd:PRK10874 181 RAIT-LAHQAGMVVMVDGAQGAVHFPADVQALD-IDFYAFSGHKLYGPTGIGVLYGKSEllEAMSPWQ-GGGkmltevsf 257
|
250 260
....*....|....*....|....*....
gi 656223624 229 -----QESDKR--STTENVAGIAATAKAL 250
Cdd:PRK10874 258 dgftpQSAPWRfeAGTPNVAGVIGLSAAL 286
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
2-216 |
1.31e-14 |
|
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: 75.28 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 2 IYFDNAATTQvypevlktytevatKiwgnPSSL-------------------HSLGSQATRILEASRKQIAELLG-KDSK 61
Cdd:NF041166 247 VWFDNAATTQ--------------K----PQAVidrlsyfyehensnihraaHELAARATDAYEGAREKVRRFIGaPSVD 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 62 EIFFTSGGTEGDNWVIKgvAFEKAHL--GKHIIVSAIEHPA--------VKESALWLKtqgfevdLAPVNTQGFVDVSAL 131
Cdd:NF041166 309 EIIFVRGTTEAINLVAK--SWGRQNIgaGDEIIVSHLEHHAnivpwqqlAQETGAKLR-------VIPVDDSGQILLDEY 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 132 ESLIRPDTTLVSIMAVNNEIGSIQPIQEISQL--------LAD-KPTISfH--VDaVQAIGkvptegyltdrVDFASFSG 200
Cdd:NF041166 380 AKLLNPRTKLVSVTQVSNALGTVTPVKEIIALahragakvLVDgAQSVS-HmpVD-VQALD-----------ADFFVFSG 446
|
250
....*....|....*.
gi 656223624 201 HKFHSVRGVGFVYVKA 216
Cdd:NF041166 447 HKVFGPTGIGVVYGKR 462
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
45-215 |
8.42e-10 |
|
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: 57.39 E-value: 8.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 45 LEASRKQIAELLGKDSKEIFFTSGGTEGDNWVIKGVafekAHLGKHIIVSAIEHpavkESALWLKTQGFEVDLAPV---- 120
Cdd:cd01494 2 LEELEEKLARLLQPGNDKAVFVPSGTGANEAALLAL----LGPGDEVIVDANGH----GSRYWVAAELAGAKPVPVpvdd 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 121 NTQGFVDVSALESLIRPDTT-LVSIMAVNNEIGSIQPIQEISQlLADKPTISFHVDAVQAIGKVPTEGYLTD--RVDFAS 197
Cdd:cd01494 74 AGYGGLDVAILEELKAKPNVaLIVITPNTTSGGVLVPLKEIRK-IAKEYGILLLVDAASAGGASPAPGVLIPegGADVVT 152
|
170
....*....|....*...
gi 656223624 198 FSGHKFHSVRGVGFVYVK 215
Cdd:cd01494 153 FSLHKNLGGEGGGVVIVK 170
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
14-218 |
1.38e-08 |
|
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to DOPA/tyrosine decarboxylase (DDC), histidine decarboxylase (HDC), and glutamate decarboxylase (GDC). DDC is active as a dimer and catalyzes the decarboxylation of tyrosine. GDC catalyzes the decarboxylation of glutamate and HDC catalyzes the decarboxylation of histidine.
Pssm-ID: 99743 [Multi-domain] Cd Length: 345 Bit Score: 55.67 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 14 PEVLKTYTEVATK-IWGNPSSLhslgSQATRILEAS-RKQIAELLGKDSKEI--FFTSGGTEG---------DNWVIKGV 80
Cdd:cd06450 11 PPALLLEMLTSAKnAIDFTWDE----SPAATEMEAEvVNWLAKLFGLPSEDAdgVFTSGGSESnllallaarDRARKRLK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 81 AFEKAHLGKHIIV-SAIEHPAVKESALWLKTqgfEVDLAPVNTQGFVDVSALESLIRPDTT--LVSIMAV----NNEIGS 153
Cdd:cd06450 87 AGGGRGIDKLVIVcSDQAHVSVEKAAAYLDV---KVRLVPVDEDGRMDPEALEAAIDEDKAegLNPIMVVatagTTDTGA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 656223624 154 IQPIQEISQLlADKPTISFHVDAvqAIGKV----PTEGYLTDRVDFA---SFSGHK-FHSVRGVGFVYVKAGK 218
Cdd:cd06450 164 IDPLEEIADL-AEKYDLWLHVDA--AYGGFllpfPEPRHLDFGIERVdsiSVDPHKyGLVPLGCSAVLVRALK 233
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
65-217 |
1.23e-07 |
|
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism]; Glutamate or tyrosine decarboxylase or a related PLP-dependent protein is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 439846 [Multi-domain] Cd Length: 460 Bit Score: 53.30 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 65 FTSGGTEG---------DNWVIKGVAFEKAHLGKH--IIVSAIEHPAVKESALWLktqGFEVD---LAPVNTQGFVDVSA 130
Cdd:COG0076 130 FTSGGTEAnllallaarDRALARRVRAEGLPGAPRprIVVSEEAHSSVDKAARLL---GLGRDalrKVPVDEDGRMDPDA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 131 LESLIRPDTTLVS-IMAV-----NNEIGSIQPIQEISQLLADKPtISFHVDAvqAIGK----VPTEGYLTDRVDFA---S 197
Cdd:COG0076 207 LEAAIDEDRAAGLnPIAVvatagTTNTGAIDPLAEIADIAREHG-LWLHVDA--AYGGfalpSPELRHLLDGIERAdsiT 283
|
170 180
....*....|....*....|
gi 656223624 198 FSGHKFhsvrgvGFVYVKAG 217
Cdd:COG0076 284 VDPHKW------LYVPYGCG 297
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
38-277 |
6.50e-04 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 41.52 E-value: 6.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 38 GSQATRILEASRKQIAELLGKDSK-------EIFFTSGGTEgdnwVIKGVAFEKAHLGKHIIVSAIEHPAVKESALWLKT 110
Cdd:pfam00155 34 LYGPTDGHPELREALAKFLGRSPVlkldreaAVVFGSGAGA----NIEALIFLLANPGDAILVPAPTYASYIRIARLAGG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 111 QGFEVDLAPVNTQGfVDVSALESLIRPDTTLVSIMAVNNEIGSIQPIQEISQLLADKPTISFH--VDAVQAIGKVPTEGY 188
Cdd:pfam00155 110 EVVRYPLYDSNDFH-LDFDALEAALKEKPKVVLHTSPHNPTGTVATLEELEKLLDLAKEHNILllVDEAYAGFVFGSPDA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223624 189 LTDRVDFA---------SFSghKFHSVRG--VGFVY-----VKAGKKIAPLLTgggqesdkrSTTenvAGIAATAKALR- 251
Cdd:pfam00155 189 VATRALLAegpnllvvgSFS--KAFGLAGwrVGYILgnaavISQLRKLARPFY---------SST---HLQAAAAAALSd 254
|
250 260
....*....|....*....|....*...
gi 656223624 252 --LTLDKAVDSQKRLAAMKQILVDELGK 277
Cdd:pfam00155 255 plLVASELEEMRQRIKERRDYLRDGLQA 282
|
|
| |
