|
Name |
Accession |
Description |
Interval |
E-value |
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
11-372 |
3.43e-160 |
|
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: 454.89 E-value: 3.43e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 11 IYLDNAATTKAFEEVLDTYLKVNQSMYYNPNSPHKAGLQANQLLQQAKAQINAMINSKTNyDVVFTSGATESNNLALKGI 90
Cdd:COG1104 4 IYLDNAATTPVDPEVLEAMLPYLTEYFGNPSSLHSFGREARAALEEAREQVAALLGADPE-EIIFTSGGTEANNLAIKGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 91 AYRKFDTAKEIITSVLEHPSVLEVVRYLEaHEGFKVKYVDVKKDGSINLEHFKELVSDKVGLVTCMYVNNVTGQIQPIPQ 170
Cdd:COG1104 83 ARAYRKKGKHIITSAIEHPAVLETARFLE-KEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQPIAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 171 MAKVIKNYpKAHFHVDAVQAFGKISMDLN--NIDSISLSGHKFNGLKGQGVLLVNHIQNVEPTVHGGGQEYGVRSGTVNL 248
Cdd:COG1104 162 IAEIAKEH-GVLFHTDAVQAVGKIPVDVKelGVDLLSLSAHKIYGPKGVGALYVRKGVRLEPLIHGGGQERGLRSGTENV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 249 PNDIAMVKAMKIANENFEALNAFVTELNNDVRQFLNK-YHGVYINSS-TSGSPFVLNISFPGVKGEVLVNAFSKYDIMIS 326
Cdd:COG1104 241 PGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAaIPGVVINGDpENRLPNTLNFSFPGVEGEALLLALDLAGIAVS 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 586220849 327 TTSACSSKRNKLNEVLAAMGLSDKSIEGSIRLSFGATTTKEDIARF 372
Cdd:COG1104 321 SGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRA 366
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
11-369 |
4.50e-93 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 284.91 E-value: 4.50e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 11 IYLDNAATTKAFEEVLDT---YLKVNqSMYYNPNS-PHKAGLQANQLLQQAKAQINAMINSKTNyDVVFTSGATESNNLA 86
Cdd:PRK14012 5 IYLDYSATTPVDPRVAEKmmpYLTMD-GTFGNPASrSHRFGWQAEEAVDIARNQIADLIGADPR-EIVFTSGATESDNLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 87 LKGIA--YRKfdTAKEIITSVLEHPSVLEVVRYLEaHEGFKVKYVDVKKDGSINLEHFKELVSDKVGLVTCMYVNNVTGQ 164
Cdd:PRK14012 83 IKGAAhfYQK--KGKHIITSKTEHKAVLDTCRQLE-REGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 165 IQPIPQMAKVIKNYpKAHFHVDAVQAFGKISMDLN--NIDSISLSGHKFNGLKGQGVLLVNHIQNV--EPTVHGGGQEYG 240
Cdd:PRK14012 160 IQDIAAIGEICRER-GIIFHVDAAQSVGKVPIDLSklKVDLMSFSAHKIYGPKGIGALYVRRKPRVrlEAQMHGGGHERG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 241 VRSGTVNLPNDIAMVKAMKIANENFEALNAFVTELNNDVRQFLNKYHGVYINSS-TSGSPFVLNISFPGVKGEVLVNAFS 319
Cdd:PRK14012 239 MRSGTLPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGIKDIEEVYLNGDlEQRVPGNLNVSFNYVEGESLIMALK 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 586220849 320 kyDIMISTTSACSSKRNKLNEVLAAMGLSDKSIEGSIRLSFGATTTKEDI 369
Cdd:PRK14012 319 --DLAVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEI 366
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
11-372 |
8.01e-72 |
|
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: 229.06 E-value: 8.01e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 11 IYLDNAATTKAFEEVLDTYLKVNQSMYYNP-NSPHKAGLQANQLLQQAKAQINAMINSKTNYDVVFTSGATESNNLALKG 89
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVhRGVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 90 IAyRKFDTAKEIITSVLEHPSVLEVVRYLEAHEGFKVKYVDVKKDGSINLEHFKELVSDKVGLVTCMYVNNVTGQIQPIP 169
Cdd:pfam00266 81 LG-RSLKPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 170 QMAKVIKNYpKAHFHVDAVQAFGKISMDLN--NIDSISLSGHKFNGLKGQGVLLV--NHIQNVEPTVHGGG-------QE 238
Cdd:pfam00266 160 EIGKLAHQY-GALVLVDAAQAIGHRPIDVQklGVDFLAFSGHKLYGPTGIGVLYGrrDLLEKMPPLLGGGGmietvslQE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 239 YGV-------RSGTVNLPNDIAMVKAMK-IANENFEALNAFVTELNNDVRQFLNKYHGVYINSSTSGSPfVLNISFPGVK 310
Cdd:pfam00266 239 STFadapwkfEAGTPNIAGIIGLGAALEyLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPERRAS-IISFNFKGVH 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 586220849 311 GEVLVNAFSKYDIMISTTSACSSKRNKLnevlaamglsdKSIEGSIRLSFGATTTKEDIARF 372
Cdd:pfam00266 318 PHDVATLLDESGIAVRSGHHCAQPLMVR-----------LGLGGTVRASFYIYNTQEDVDRL 368
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
11-372 |
3.62e-42 |
|
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: 151.46 E-value: 3.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 11 IYLDNAATTKAFEEVLDT----YLKVNQsmyyNPN-SPHKAGLQANQLLQQAKAQINAMINSKTNYDVVFTSGATESNNL 85
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAivdyYRHYNA----NVHrGVHELSARATDAYEAAREKVARFINAPSPDEIIFTRNTTEAINL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 86 ALKGIAyRKFDTAKEIITSVLEHPSVLEVVRYLEAHEGFKVKYVDVKKDGSINLEHFKELVSDKVGLVTCMYVNNVTGQI 165
Cdd:cd06453 77 VAYGLG-RANKPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 166 QPIPQMAKViknypkAHFH-----VDAVQAFGKISMDLN--NIDSISLSGHKFNGLKGQGVLLVN--HIQNVEPtVHGGG 236
Cdd:cd06453 156 NPVKEIGEI------AHEAgvpvlVDGAQSAGHMPVDVQdlGCDFLAFSGHKMLGPTGIGVLYGKeeLLEEMPP-YGGGG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 237 -------------QEYGVR--SGTVNLPNDIAMVKAMK-IANENFEALNAFVTELNNDVRQFLNKYHGVYINSSTSGSPF 300
Cdd:cd06453 229 emieevsfeettyADLPHKfeAGTPNIAGAIGLGAAIDyLEKIGMEAIAAHEHELTAYALERLSEIPGVRVYGDAEDRAG 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 586220849 301 VLNISFPGVKGEVLVNAFSKYDIMISTTSACsskrnklnevlaAMGLSDK-SIEGSIRLSFGATTTKEDIARF 372
Cdd:cd06453 309 VVSFNLEGIHPHDVATILDQYGIAVRAGHHC------------AQPLMRRlGVPGTVRASFGLYNTEEEIDAL 369
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
10-220 |
1.74e-06 |
|
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: 49.85 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 10 LIYLDNAATTKAFEEVLD--TYLkvnqsmYYNPNSP-HKAglqANQLLQQA---------KAQ--INAminSKTNyDVVF 75
Cdd:NF041166 246 LVWFDNAATTQKPQAVIDrlSYF------YEHENSNiHRA---AHELAARAtdayegareKVRrfIGA---PSVD-EIIF 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 76 TSGATESNNLalkgIAY---RKF----DtakEIITSVLEH-----PSVLevvryLEAHEGFKVKYVDVKKDGSINLEHFK 143
Cdd:NF041166 313 VRGTTEAINL----VAKswgRQNigagD---EIIVSHLEHhanivPWQQ-----LAQETGAKLRVIPVDDSGQILLDEYA 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 144 ELVSDKVGLVTCMYVNNVTGQIQPIPQM--------AKVIknypkahfhVDAVQAfgkIS-MDLN----NIDSISLSGHK 210
Cdd:NF041166 381 KLLNPRTKLVSVTQVSNALGTVTPVKEIialahragAKVL---------VDGAQS---VShMPVDvqalDADFFVFSGHK 448
|
250
....*....|
gi 586220849 211 FNGLKGQGVL 220
Cdd:NF041166 449 VFGPTGIGVV 458
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
11-372 |
3.43e-160 |
|
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: 454.89 E-value: 3.43e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 11 IYLDNAATTKAFEEVLDTYLKVNQSMYYNPNSPHKAGLQANQLLQQAKAQINAMINSKTNyDVVFTSGATESNNLALKGI 90
Cdd:COG1104 4 IYLDNAATTPVDPEVLEAMLPYLTEYFGNPSSLHSFGREARAALEEAREQVAALLGADPE-EIIFTSGGTEANNLAIKGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 91 AYRKFDTAKEIITSVLEHPSVLEVVRYLEaHEGFKVKYVDVKKDGSINLEHFKELVSDKVGLVTCMYVNNVTGQIQPIPQ 170
Cdd:COG1104 83 ARAYRKKGKHIITSAIEHPAVLETARFLE-KEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQPIAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 171 MAKVIKNYpKAHFHVDAVQAFGKISMDLN--NIDSISLSGHKFNGLKGQGVLLVNHIQNVEPTVHGGGQEYGVRSGTVNL 248
Cdd:COG1104 162 IAEIAKEH-GVLFHTDAVQAVGKIPVDVKelGVDLLSLSAHKIYGPKGVGALYVRKGVRLEPLIHGGGQERGLRSGTENV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 249 PNDIAMVKAMKIANENFEALNAFVTELNNDVRQFLNK-YHGVYINSS-TSGSPFVLNISFPGVKGEVLVNAFSKYDIMIS 326
Cdd:COG1104 241 PGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAaIPGVVINGDpENRLPNTLNFSFPGVEGEALLLALDLAGIAVS 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 586220849 327 TTSACSSKRNKLNEVLAAMGLSDKSIEGSIRLSFGATTTKEDIARF 372
Cdd:COG1104 321 SGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRA 366
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
11-369 |
4.50e-93 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 284.91 E-value: 4.50e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 11 IYLDNAATTKAFEEVLDT---YLKVNqSMYYNPNS-PHKAGLQANQLLQQAKAQINAMINSKTNyDVVFTSGATESNNLA 86
Cdd:PRK14012 5 IYLDYSATTPVDPRVAEKmmpYLTMD-GTFGNPASrSHRFGWQAEEAVDIARNQIADLIGADPR-EIVFTSGATESDNLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 87 LKGIA--YRKfdTAKEIITSVLEHPSVLEVVRYLEaHEGFKVKYVDVKKDGSINLEHFKELVSDKVGLVTCMYVNNVTGQ 164
Cdd:PRK14012 83 IKGAAhfYQK--KGKHIITSKTEHKAVLDTCRQLE-REGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 165 IQPIPQMAKVIKNYpKAHFHVDAVQAFGKISMDLN--NIDSISLSGHKFNGLKGQGVLLVNHIQNV--EPTVHGGGQEYG 240
Cdd:PRK14012 160 IQDIAAIGEICRER-GIIFHVDAAQSVGKVPIDLSklKVDLMSFSAHKIYGPKGIGALYVRRKPRVrlEAQMHGGGHERG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 241 VRSGTVNLPNDIAMVKAMKIANENFEALNAFVTELNNDVRQFLNKYHGVYINSS-TSGSPFVLNISFPGVKGEVLVNAFS 319
Cdd:PRK14012 239 MRSGTLPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGIKDIEEVYLNGDlEQRVPGNLNVSFNYVEGESLIMALK 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 586220849 320 kyDIMISTTSACSSKRNKLNEVLAAMGLSDKSIEGSIRLSFGATTTKEDI 369
Cdd:PRK14012 319 --DLAVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEI 366
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
11-369 |
2.33e-84 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 261.13 E-value: 2.33e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 11 IYLDNAATTKAFEEVLDTYLKVNQSMYYNPNSP-HKAGLQANQLLQQAKAQINAMINSKTNyDVVFTSGATESNNLALKG 89
Cdd:PLN02651 1 LYLDMQATTPIDPRVLDAMLPFLIEHFGNPHSRtHLYGWESEDAVEKARAQVAALIGADPK-EIIFTSGATESNNLAIKG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 90 IAYRKFDTAKEIITSVLEHPSVLEVVRYLEAhEGFKVKYVDVKKDGSINLEHFKELVSDKVGLVTCMYVNNVTGQIQPIP 169
Cdd:PLN02651 80 VMHFYKDKKKHVITTQTEHKCVLDSCRHLQQ-EGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 170 QMAKVIKNYpKAHFHVDAVQAFGKISMDLN--NIDSISLSGHKFNGLKGQGVLLVNHIQ--NVEPTVHGGGQEYGVRSGT 245
Cdd:PLN02651 159 EIGELCREK-KVLFHTDAAQAVGKIPVDVDdlGVDLMSISGHKIYGPKGVGALYVRRRPrvRLEPLMSGGGQERGRRSGT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 246 VNLPNDIAMVKAMKIANENFEALNAFVTELNNDVRQFL-NKYHGVYIN---SSTSGSPFVLNISFPGVKGEVLVNAFSky 321
Cdd:PLN02651 238 ENTPLVVGLGAACELAMKEMDYDEKHMKALRERLLNGLrAKLGGVRVNgprDPEKRYPGTLNLSFAYVEGESLLMGLK-- 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 586220849 322 DIMISTTSACSSKRNKLNEVLAAMGLSDKSIEGSIRLSFGATTTKEDI 369
Cdd:PLN02651 316 EVAVSSGSACTSASLEPSYVLRALGVPEEMAHGSLRLGVGRFTTEEEV 363
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
11-372 |
8.01e-72 |
|
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: 229.06 E-value: 8.01e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 11 IYLDNAATTKAFEEVLDTYLKVNQSMYYNP-NSPHKAGLQANQLLQQAKAQINAMINSKTNYDVVFTSGATESNNLALKG 89
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVhRGVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 90 IAyRKFDTAKEIITSVLEHPSVLEVVRYLEAHEGFKVKYVDVKKDGSINLEHFKELVSDKVGLVTCMYVNNVTGQIQPIP 169
Cdd:pfam00266 81 LG-RSLKPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 170 QMAKVIKNYpKAHFHVDAVQAFGKISMDLN--NIDSISLSGHKFNGLKGQGVLLV--NHIQNVEPTVHGGG-------QE 238
Cdd:pfam00266 160 EIGKLAHQY-GALVLVDAAQAIGHRPIDVQklGVDFLAFSGHKLYGPTGIGVLYGrrDLLEKMPPLLGGGGmietvslQE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 239 YGV-------RSGTVNLPNDIAMVKAMK-IANENFEALNAFVTELNNDVRQFLNKYHGVYINSSTSGSPfVLNISFPGVK 310
Cdd:pfam00266 239 STFadapwkfEAGTPNIAGIIGLGAALEyLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPERRAS-IISFNFKGVH 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 586220849 311 GEVLVNAFSKYDIMISTTSACSSKRNKLnevlaamglsdKSIEGSIRLSFGATTTKEDIARF 372
Cdd:pfam00266 318 PHDVATLLDESGIAVRSGHHCAQPLMVR-----------LGLGGTVRASFYIYNTQEDVDRL 368
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
10-372 |
3.72e-68 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 219.99 E-value: 3.72e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 10 LIYLDNAATTKAFEEVLDTYLKVNQSMYYNPNSPHKAGLQANQLLQQAKAQINAMINSKTNyDVVFTSGATESNNLALKG 89
Cdd:PRK02948 1 MIYLDYAATTPMSKEALQTYQKAASQYFGNESSLHDIGGTASSLLQVCRKTFAEMIGGEEQ-GIYFTSGGTESNYLAIQS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 90 IAYRKFDTAKEIITSVLEHPSVLEVVRYLEAhEGFKVKYVDVKKDGSINLEHFKELVSDKVGLVTCMYVNNVTGQIQPIP 169
Cdd:PRK02948 80 LLNALPQNKKHIITTPMEHASIHSYFQSLES-QGYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQPIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 170 QMAKVIKNYpKAHFHVDAVQAFGKISMDLNN--IDSISLSGHKFNGLKGQGVLLVNHIQNVEPTVHGGGQEYGVRSGTVN 247
Cdd:PRK02948 159 EIGALLKKY-NVLFHSDCVQTFGKLPIDVFEmgIDSLSVSAHKIYGPKGVGAVYINPQVRWKPVFPGTTHEKGFRPGTVN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 248 LPNDIAMVKAMKIANENFEAlnafVTELNNDVRQFLnkYHGVYINS--------STSGSPFVLNISFPGVKGEVLVNAFS 319
Cdd:PRK02948 238 VPGIAAFLTAAENILKNMQE----ESLRFKELRSYF--LEQIQTLPlpieveghSTSCLPHIIGVTIKGIEGQYTMLECN 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 586220849 320 KYDIMISTTSACSSKRNKLNEVLAAMGLSDKSIEGSIRLSFGATTTKEDIARF 372
Cdd:PRK02948 312 RRGIAISTGSACQVGKQEPSKTMLAIGKTYEEAKQFVRFSFGQQTTKDQIDTT 364
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
10-372 |
1.45e-57 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 192.66 E-value: 1.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 10 LIYLDNAATTKAFEEVLDTYLKVNQSMYYNPN-SPHKAGLQANQLLQQAKAQINAMINSKTNYDVVFTSGATESNNLALK 88
Cdd:COG0520 16 LVYLDNAATGQKPRPVIDAIRDYYEPYNANVHrGAHELSAEATDAYEAAREKVARFIGAASPDEIIFTRGTTEAINLVAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 89 GIAyrKFDTAKEIITSVLEHPSVLEVVRYLEAHEGFKVKYVDVKKDGSINLEHFKELVSDKVGLVTCMYVNNVTGQIQPI 168
Cdd:COG0520 96 GLG--RLKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDGELDLEALEALLTPRTKLVAVTHVSNVTGTVNPV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 169 PQMAKVIKNYPkAHFHVDAVQAFGKISMDLN--NIDSISLSGHKFNGLKGQGVLLVN--HIQNVEPTVHGGG-------Q 237
Cdd:COG0520 174 KEIAALAHAHG-ALVLVDGAQSVPHLPVDVQalGCDFYAFSGHKLYGPTGIGVLYGKreLLEALPPFLGGGGmiewvsfD 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 238 EYGVRS-------GTVNLPNDIAMVKAMKIANE-NFEALNAFVTELNNDVRQFLNKYHGVYINSSTSGSPFVLNISF--P 307
Cdd:COG0520 253 GTTYADlprrfeaGTPNIAGAIGLGAAIDYLEAiGMEAIEARERELTAYALEGLAAIPGVRILGPADPEDRSGIVSFnvD 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 586220849 308 GVKGEVLVNAFSKYDIMISTTSACsskrnklnevlaAMGLSDK-SIEGSIRLSFGATTTKEDIARF 372
Cdd:COG0520 333 GVHPHDVAALLDDEGIAVRAGHHC------------AQPLMRRlGVPGTVRASFHLYNTEEEIDRL 386
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
11-372 |
3.62e-42 |
|
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: 151.46 E-value: 3.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 11 IYLDNAATTKAFEEVLDT----YLKVNQsmyyNPN-SPHKAGLQANQLLQQAKAQINAMINSKTNYDVVFTSGATESNNL 85
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAivdyYRHYNA----NVHrGVHELSARATDAYEAAREKVARFINAPSPDEIIFTRNTTEAINL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 86 ALKGIAyRKFDTAKEIITSVLEHPSVLEVVRYLEAHEGFKVKYVDVKKDGSINLEHFKELVSDKVGLVTCMYVNNVTGQI 165
Cdd:cd06453 77 VAYGLG-RANKPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 166 QPIPQMAKViknypkAHFH-----VDAVQAFGKISMDLN--NIDSISLSGHKFNGLKGQGVLLVN--HIQNVEPtVHGGG 236
Cdd:cd06453 156 NPVKEIGEI------AHEAgvpvlVDGAQSAGHMPVDVQdlGCDFLAFSGHKMLGPTGIGVLYGKeeLLEEMPP-YGGGG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 237 -------------QEYGVR--SGTVNLPNDIAMVKAMK-IANENFEALNAFVTELNNDVRQFLNKYHGVYINSSTSGSPF 300
Cdd:cd06453 229 emieevsfeettyADLPHKfeAGTPNIAGAIGLGAAIDyLEKIGMEAIAAHEHELTAYALERLSEIPGVRVYGDAEDRAG 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 586220849 301 VLNISFPGVKGEVLVNAFSKYDIMISTTSACsskrnklnevlaAMGLSDK-SIEGSIRLSFGATTTKEDIARF 372
Cdd:cd06453 309 VVSFNLEGIHPHDVATILDQYGIAVRAGHHC------------AQPLMRRlGVPGTVRASFGLYNTEEEIDAL 369
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
10-220 |
8.37e-31 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 121.78 E-value: 8.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 10 LIYLDNAATTKAFEEVLDTYLkvNQSMYYNPN---SPHKAGLQANQLLQQAKAQINAMINSKTNYDVVFTSGATESNNLA 86
Cdd:PLN02855 33 LVYLDNAATSQKPAAVLDALQ--DYYEEYNSNvhrGIHALSAKATDAYELARKKVAAFINASTSREIVFTRNATEAINLV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 87 LKGIAYRKFDTAKEIITSVLEHPSVLEVVRYLEAHEGFKVKYVDVKKDGSINLEHFKELVSDKVGLVTCMYVNNVTGQIQ 166
Cdd:PLN02855 111 AYTWGLANLKPGDEVILSVAEHHSNIVPWQLVAQKTGAVLKFVGLTPDEVLDVEQLKELLSEKTKLVATHHVSNVLGSIL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 586220849 167 PIPQMAKVIKNYpKAHFHVDAVQAFGKISMDLN--NIDSISLSGHKFNGLKGQGVL 220
Cdd:PLN02855 191 PVEDIVHWAHAV-GAKVLVDACQSVPHMPVDVQtlGADFLVASSHKMCGPTGIGFL 245
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
10-236 |
1.12e-15 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 77.87 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 10 LIYLDNAATTKAFEEVLDT--------YLKVNQSMyynpnspHKAGLQANQLLQQAKAQINAMINSKTNYDVVFTSGATE 81
Cdd:PRK09295 24 LAYLDSAASAQKPSQVIDAeaefyrhgYAAVHRGI-------HTLSAQATEKMENVRKQAALFINARSAEELVFVRGTTE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 82 SNNLALKGIAYRKFDTAKEIITSVLEHPSVLEVVRYLEAHEGFKVKYVDVKKDGSINLEHFKELVSDKVGLVTCMYVNNV 161
Cdd:PRK09295 97 GINLVANSWGNSNVRAGDNIIISEMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPALFDERTRLLAITHVSNV 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 586220849 162 TGQIQPIPQMAKVIKNYpKAHFHVDAVQAFGKISMDLNNIDS--ISLSGHKFNGLKGQGVLLVNH-IQNVEPTVHGGG 236
Cdd:PRK09295 177 LGTENPLAEMIALAHQH-GAKVLVDGAQAVMHHPVDVQALDCdfYVFSGHKLYGPTGIGILYVKEaLLQEMPPWEGGG 253
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
11-371 |
4.74e-15 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 75.84 E-value: 4.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 11 IYLDNAATTKAFEEVLDtylkVNQSMYYNPN-----SPHKAGLQANQLLQQAKAQINAMINSKTNYDVVFTSGATESNNL 85
Cdd:PRK10874 21 VYLDSAATALKPQAVIE----ATQQFYSLSAgnvhrSQFAAAQRLTARYEAAREQVAQLLNAPDAKNIVWTRGTTESINL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 86 ALKGIAYRKFDTAKEIITSVLEHPSVLevVRYLEAHE--GFKVKYVDVKKDGSINLEHFKELVSDKVGLVTCMYVNNVTG 163
Cdd:PRK10874 97 VAQSYARPRLQPGDEIIVSEAEHHANL--VPWLMVAQqtGAKVVKLPLGADRLPDVDLLPELITPRTRILALGQMSNVTG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 164 QiqpIPQMAKVIknyPKAHFH-----VDAVQAFGKISMDLN--NIDSISLSGHKFNGLKGQGVL-----LVNHIqnvePT 231
Cdd:PRK10874 175 G---CPDLARAI---TLAHQAgmvvmVDGAQGAVHFPADVQalDIDFYAFSGHKLYGPTGIGVLygkseLLEAM----SP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 232 VHGGGQ---------------EYGVRSGTVNLPNDIAMVKAMK-IANENFEALNAFVTELNNDVRQFLNKYHGvYINSST 295
Cdd:PRK10874 245 WQGGGKmltevsfdgftpqsaPWRFEAGTPNVAGVIGLSAALEwLADIDINQAESWSRSLATLAEDALAKLPG-FRSFRC 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 586220849 296 SGSPfVLNISFPGVKGEVLVNAFSKYDIMISTTSACSSKrnklneVLAAMGLSdksieGSIRLSFGATTTKEDIAR 371
Cdd:PRK10874 324 QDSS-LLAFDFAGVHHSDLVTLLAEYGIALRAGQHCAQP------LLAALGVT-----GTLRASFAPYNTQSDVDA 387
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
74-222 |
2.09e-14 |
|
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: 73.78 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 74 VFTSGATESNNLALKGIAYRKFDTAK----------EIITSVLEHPSVLEVVRYLEAhegfKVKYVDVKKDGSINLEHFK 143
Cdd:cd06450 61 VFTSGGSESNLLALLAARDRARKRLKagggrgidklVIVCSDQAHVSVEKAAAYLDV----KVRLVPVDEDGRMDPEALE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 144 ELVSD--KVGLVTCMYV----NNVTGQIQPIPQMAKVIKNYpKAHFHVDAvqAFGK---ISMD-------LNNIDSISLS 207
Cdd:cd06450 137 AAIDEdkAEGLNPIMVVatagTTDTGAIDPLEEIADLAEKY-DLWLHVDA--AYGGfllPFPEprhldfgIERVDSISVD 213
|
170
....*....|....*..
gi 586220849 208 GHKFnGL--KGQGVLLV 222
Cdd:cd06450 214 PHKY-GLvpLGCSAVLV 229
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
24-222 |
1.20e-13 |
|
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: 72.17 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 24 EVLDTYLkvNQSMYYNPNSPhkaglQANQLLQQAKAQINAMINSKTNYDVVFTSGATESNNLALKgIA---YRKFDTAKE 100
Cdd:COG0076 86 DLLASAL--NQNMGDWDTSP-----AATELEREVVRWLADLLGLPEGAGGVFTSGGTEANLLALL-AArdrALARRVRAE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 101 ---------IITSVLEHPSVLEVVRYLeaheGFK---VKYVDVKKDGSINLEHFKELVSD--KVGLVTCMYVNNV----T 162
Cdd:COG0076 158 glpgaprprIVVSEEAHSSVDKAARLL----GLGrdaLRKVPVDEDGRMDPDALEAAIDEdrAAGLNPIAVVATAgttnT 233
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 586220849 163 GQIQPIPQMAKVIKNYpKAHFHVDAvqAFG---KISMD----LNNI---DSISLSGHKFnGL--KGQGVLLV 222
Cdd:COG0076 234 GAIDPLAEIADIAREH-GLWLHVDA--AYGgfaLPSPElrhlLDGIeraDSITVDPHKW-LYvpYGCGAVLV 301
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
70-223 |
6.23e-09 |
|
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).
Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 54.70 E-value: 6.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 70 NYDVVFTSGATESNNLALKGIAYRKfdtaKEIITSVLEHPSVLEVVRylEAHeGFKVKYVDVKKDGS--------INLEH 141
Cdd:cd01494 17 NDKAVFVPSGTGANEAALLALLGPG----DEVIVDANGHGSRYWVAA--ELA-GAKPVPVPVDDAGYggldvailEELKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 142 FKElvsdKVGLVTCMYVNNvTGQIQPIPQMAKVIKNYpKAHFHVDAVQAFG-----KISMDLNNIDSISLSGHKFNGLKG 216
Cdd:cd01494 90 KPN----VALIVITPNTTS-GGVLVPLKEIRKIAKEY-GILLLVDAASAGGaspapGVLIPEGGADVVTFSLHKNLGGEG 163
|
....*..
gi 586220849 217 QGVLLVN 223
Cdd:cd01494 164 GGVVIVK 170
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
10-220 |
1.74e-06 |
|
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: 49.85 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 10 LIYLDNAATTKAFEEVLD--TYLkvnqsmYYNPNSP-HKAglqANQLLQQA---------KAQ--INAminSKTNyDVVF 75
Cdd:NF041166 246 LVWFDNAATTQKPQAVIDrlSYF------YEHENSNiHRA---AHELAARAtdayegareKVRrfIGA---PSVD-EIIF 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 76 TSGATESNNLalkgIAY---RKF----DtakEIITSVLEH-----PSVLevvryLEAHEGFKVKYVDVKKDGSINLEHFK 143
Cdd:NF041166 313 VRGTTEAINL----VAKswgRQNigagD---EIIVSHLEHhanivPWQQ-----LAQETGAKLRVIPVDDSGQILLDEYA 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 144 ELVSDKVGLVTCMYVNNVTGQIQPIPQM--------AKVIknypkahfhVDAVQAfgkIS-MDLN----NIDSISLSGHK 210
Cdd:NF041166 381 KLLNPRTKLVSVTQVSNALGTVTPVKEIialahragAKVL---------VDGAQS---VShMPVDvqalDADFFVFSGHK 448
|
250
....*....|
gi 586220849 211 FNGLKGQGVL 220
Cdd:NF041166 449 VFGPTGIGVV 458
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
65-192 |
2.65e-04 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 42.68 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 65 INSKTNYDVVFTSGATEsNNLALKGIAYRKFDtakEIITSVLEHPSVLEVVRYleahEGFKVKYV--DVKKDGSINLEHF 142
Cdd:pfam00155 58 LKLDREAAVVFGSGAGA-NIEALIFLLANPGD---AILVPAPTYASYIRIARL----AGGEVVRYplYDSNDFHLDFDAL 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 586220849 143 KELVSDKV-GLVTCmYVNNVTGQIQPIPQMAKVIKNYPKAHFHV---DAVQAFG 192
Cdd:pfam00155 130 EAALKEKPkVVLHT-SPHNPTGTVATLEELEKLLDLAKEHNILLlvdEAYAGFV 182
|
|
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
11-117 |
1.65e-03 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 40.62 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586220849 11 IYLDNAATT----KAFEEVLDTYlkvNQSMYYNPNSPHKAGLQANQLLQQAKAQINAMIN-SKTNYDVVFTSGATESnnL 85
Cdd:PLN02724 36 VYLDHAGATlyseSQLEAALADF---SSNVYGNPHSQSDSSMRSSDTIESARQQVLEYFNaPPSDYACVFTSGATAA--L 110
|
90 100 110
....*....|....*....|....*....|..
gi 586220849 86 ALKGIAYrKFDTAKEIITSVLEHPSVLEVVRY 117
Cdd:PLN02724 111 KLVGETF-PWSSESHFCYTLENHNSVLGIREY 141
|
|
| |
