|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
60-459 |
0e+00 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 732.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 60 PLYMDVQATTPLDPRVLDAMLPYLVN--YYGNPHSRTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAI 137
Cdd:PRK14012 4 PIYLDYSATTPVDPRVAEKMMPYLTMdgTFGNPASRSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDNLAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 138 KGVARFYRSRKKHLVTTQTEHKCVLDSCRSLEAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPI 217
Cdd:PRK14012 84 KGAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVIQDI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 218 AEIGQICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRRPRVRVEALQSGGGQERGMRSGT 297
Cdd:PRK14012 164 AAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRLEAQMHGGGHERGMRSGT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 298 VPTPLVVGLGAACELAQQEMEYDHKRISKLAERLVQNImKNLPDVVMNGDPKQHYPGCINLSFAYVEGESLLMALKDVAL 377
Cdd:PRK14012 244 LPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGI-KDIEEVYLNGDLEQRVPGNLNVSFNYVEGESLIMALKDLAV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 378 SSGSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVDYTAEKCIHHVKRLREMSPLWEMVQDGIDLKSIKWT 457
Cdd:PRK14012 323 SSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGKLRELSPLWEMFKEGVDLNSIEWA 402
|
..
gi 161016824 458 QH 459
Cdd:PRK14012 403 HH 404
|
|
| IscS |
TIGR02006 |
cysteine desulfurase IscS; This model represents IscS, one of several cysteine desulfurases ... |
60-459 |
0e+00 |
|
cysteine desulfurase IscS; This model represents IscS, one of several cysteine desulfurases from a larger protein family designated (misleadingly, in this case) class V aminotransferases. IscS is one of at least 6 enzymes characteristic of the IscSUA-hscAB-fsx system of iron-sulfur cluster assembly. Scoring almost as well as proteobacterial sequences included in the model are mitochondrial cysteine desulfurases, apparently from an analogous system in eukaryotes. The sulfur, taken from cysteine, may be used in other systems as well, such as tRNA base modification and biosynthesis of other cofactors. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 131061 [Multi-domain] Cd Length: 402 Bit Score: 664.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 60 PLYMDVQATTPLDPRVLDAMLPYLVNYYGNPHSRTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIKG 139
Cdd:TIGR02006 4 PIYLDYAATTPVDPRVAEKMMPYLTEKFGNPASRSHSFGWEAEEAVENARNQVAELIGADSREIVFTSGATESNNLAIKG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 140 VARFYRSRKKHLVTTQTEHKCVLDSCRSLEAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAE 219
Cdd:TIGR02006 84 IAHFYKSKGNHIITSKTEHKAVLDTCRYLEREGFEVTYLPPKSNGLIDLEELKAAIRDDTILVSIMHVNNEIGVIQDIAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 220 IGQICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRRPRVRVEALQSGGGQERGMRSGTVP 299
Cdd:TIGR02006 164 IGEICRERKVFFHVDAAQSVGKIPINVNELKVDLMSISGHKIYGPKGIGALYVRRKPRVRLEALIHGGGHERGMRSGTLP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 300 TPLVVGLGAACELAQQEMEYDHKRISKLAERLVQNImKNLPDVVMNGDPKQHYPGCINLSFAYVEGESLLMALKDVALSS 379
Cdd:TIGR02006 244 THQIVGMGEAFRIAKEEMAQDTAHVLALRDRLLNGI-KSIEEVYLNGDLEHRVPGNLNVSFNYVEGESLIMALKDLAVSS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 380 GSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVDYTAEKCIHHVKRLREMSPLWEMVQDGIDLKSIKWTQH 459
Cdd:TIGR02006 323 GSACTSASLEPSYVLRALGINDELAHSSIRFTIGRFTTEEEIDYAVKLVKSAIDKLRELSPLWEMFKEGVDLNSIEWAAH 402
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
59-439 |
0e+00 |
|
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: 628.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 59 RPLYMDVQATTPLDPRVLDAMLPYLVNYYGNPHSrTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIK 138
Cdd:COG1104 2 MMIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSS-LHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNLAIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 139 GVARFYRSRKKHLVTTQTEHKCVLDSCRSLEAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIA 218
Cdd:COG1104 81 GAARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 219 EIGQICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRrpRVRVEALQSGGGQERGMRSGTV 298
Cdd:COG1104 161 EIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRK--GVRLEPLIHGGGQERGLRSGTE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 299 PTPLVVGLGAACELAQQEMEYDHKRISKLAERLVQNIMKNLPDVVMNGDPKQHYPGCINLSFAYVEGESLLMAL--KDVA 376
Cdd:COG1104 239 NVPGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAAIPGVVINGDPENRLPNTLNFSFPGVEGEALLLALdlAGIA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161016824 377 LSSGSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVDYTAEKCIHHVKRLREMS 439
Cdd:COG1104 319 VSSGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARLRKLS 381
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
62-423 |
4.67e-111 |
|
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: 332.29 E-value: 4.67e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 62 YMDVQATTPLDPRVLDAMLPYLVNYYGNPHSRTHAYGWESEAAMERARQQVASLIGA-DPREIIFTSGATESNNIAIKGV 140
Cdd:pfam00266 2 YLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINApSNDEIIFTSGTTEAINLVALSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 141 ARFYRsRKKHLVTTQTEHKCVLDSCRSL-EAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAE 219
Cdd:pfam00266 82 GRSLK-PGDEIVITEMEHHANLVPWQELaKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 220 IGQICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRRPRVRVEALQSGGG-------QERG 292
Cdd:pfam00266 161 IGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGmietvslQEST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 293 M-------RSGTVPTPLVVGLGAACE-LAQQEMEYDHKRISKLAERLVQnIMKNLPDVVMNGDPKQhyPGCINLSFAYVE 364
Cdd:pfam00266 241 FadapwkfEAGTPNIAGIIGLGAALEyLSEIGLEAIEKHEHELAQYLYE-RLLSLPGIRLYGPERR--ASIISFNFKGVH 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161016824 365 GESLLMALKD--VALSSGSACTsaslEPSYVLRAIgtdedlaHSSIRFGIGRFTTEEEVDY 423
Cdd:pfam00266 318 PHDVATLLDEsgIAVRSGHHCA----QPLMVRLGL-------GGTVRASFYIYNTQEDVDR 367
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
62-422 |
1.01e-63 |
|
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: 210.40 E-value: 1.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 62 YMDVQATTPLDPRVLDAMLPYLVNYYGNPHSRTHAYGWESEAAMERARQQVASLIGA-DPREIIFTSGATESNNIAIKGV 140
Cdd:cd06453 2 YLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINApSPDEIIFTRNTTEAINLVAYGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 141 ARfyrSRKK--HLVTTQTEHKCVLDSCRSLEAE-GFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPI 217
Cdd:cd06453 82 GR---ANKPgdEIVTSVMEHHSNIVPWQQLAERtGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 218 AEIGQICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRRPRVRVEALQSGGG--------- 288
Cdd:cd06453 159 KEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEmieevsfee 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 289 ---QERGMR--SGTVPTPLVVGLGAACELAQQE-ME----YDHKRISKLAERLVQnimknLPDVVMNGDPKQHYPGcinL 358
Cdd:cd06453 239 ttyADLPHKfeAGTPNIAGAIGLGAAIDYLEKIgMEaiaaHEHELTAYALERLSE-----IPGVRVYGDAEDRAGV---V 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161016824 359 SFAyVEG---ESLLMAL--KDVALSSGSACTsaslEPsyVLRAIGtdedlAHSSIRFGIGRFTTEEEVD 422
Cdd:cd06453 311 SFN-LEGihpHDVATILdqYGIAVRAGHHCA----QP--LMRRLG-----VPGTVRASFGLYNTEEEID 367
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
104-287 |
2.58e-16 |
|
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: 81.44 E-value: 2.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 104 AMERARQQVASLIGA-DPREIIFTSGATEsnniAIKGVARFYRsrKKHL------VTTQTEHK---------Cvldscrs 167
Cdd:NF041166 290 AYEGAREKVRRFIGApSVDEIIFVRGTTE----AINLVAKSWG--RQNIgagdeiIVSHLEHHanivpwqqlA------- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 168 lEAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEIGQICssrkvyfH-------TDAAQAVG 240
Cdd:NF041166 357 -QETGAKLRVIPVDDSGQILLDEYAKLLNPRTKLVSVTQVSNALGTVTPVKEIIALA-------HragakvlVDGAQSVS 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 161016824 241 KIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRrprvrvEAL------QSGG 287
Cdd:NF041166 429 HMPVDVQALDADFFVFSGHKVFGPTGIGVVYGKR------DLLeamppwQGGG 475
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
60-459 |
0e+00 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 732.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 60 PLYMDVQATTPLDPRVLDAMLPYLVN--YYGNPHSRTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAI 137
Cdd:PRK14012 4 PIYLDYSATTPVDPRVAEKMMPYLTMdgTFGNPASRSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDNLAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 138 KGVARFYRSRKKHLVTTQTEHKCVLDSCRSLEAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPI 217
Cdd:PRK14012 84 KGAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVIQDI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 218 AEIGQICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRRPRVRVEALQSGGGQERGMRSGT 297
Cdd:PRK14012 164 AAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRLEAQMHGGGHERGMRSGT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 298 VPTPLVVGLGAACELAQQEMEYDHKRISKLAERLVQNImKNLPDVVMNGDPKQHYPGCINLSFAYVEGESLLMALKDVAL 377
Cdd:PRK14012 244 LPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGI-KDIEEVYLNGDLEQRVPGNLNVSFNYVEGESLIMALKDLAV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 378 SSGSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVDYTAEKCIHHVKRLREMSPLWEMVQDGIDLKSIKWT 457
Cdd:PRK14012 323 SSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGKLRELSPLWEMFKEGVDLNSIEWA 402
|
..
gi 161016824 458 QH 459
Cdd:PRK14012 403 HH 404
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
61-422 |
0e+00 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 671.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 61 LYMDVQATTPLDPRVLDAMLPYLVNYYGNPHSRTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIKGV 140
Cdd:PLN02651 1 LYLDMQATTPIDPRVLDAMLPFLIEHFGNPHSRTHLYGWESEDAVEKARAQVAALIGADPKEIIFTSGATESNNLAIKGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 141 ARFYRSRKKHLVTTQTEHKCVLDSCRSLEAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEI 220
Cdd:PLN02651 81 MHFYKDKKKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVEEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 221 GQICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRRPRVRVEALQSGGGQERGMRSGTVPT 300
Cdd:PLN02651 161 GELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRLEPLMSGGGQERGRRSGTENT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 301 PLVVGLGAACELAQQEMEYDHKRISKLAERLVQNIMKNLPDVVMNG--DPKQHYPGCINLSFAYVEGESLLMALKDVALS 378
Cdd:PLN02651 241 PLVVGLGAACELAMKEMDYDEKHMKALRERLLNGLRAKLGGVRVNGprDPEKRYPGTLNLSFAYVEGESLLMGLKEVAVS 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 161016824 379 SGSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVD 422
Cdd:PLN02651 321 SGSACTSASLEPSYVLRALGVPEEMAHGSLRLGVGRFTTEEEVD 364
|
|
| IscS |
TIGR02006 |
cysteine desulfurase IscS; This model represents IscS, one of several cysteine desulfurases ... |
60-459 |
0e+00 |
|
cysteine desulfurase IscS; This model represents IscS, one of several cysteine desulfurases from a larger protein family designated (misleadingly, in this case) class V aminotransferases. IscS is one of at least 6 enzymes characteristic of the IscSUA-hscAB-fsx system of iron-sulfur cluster assembly. Scoring almost as well as proteobacterial sequences included in the model are mitochondrial cysteine desulfurases, apparently from an analogous system in eukaryotes. The sulfur, taken from cysteine, may be used in other systems as well, such as tRNA base modification and biosynthesis of other cofactors. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 131061 [Multi-domain] Cd Length: 402 Bit Score: 664.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 60 PLYMDVQATTPLDPRVLDAMLPYLVNYYGNPHSRTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIKG 139
Cdd:TIGR02006 4 PIYLDYAATTPVDPRVAEKMMPYLTEKFGNPASRSHSFGWEAEEAVENARNQVAELIGADSREIVFTSGATESNNLAIKG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 140 VARFYRSRKKHLVTTQTEHKCVLDSCRSLEAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAE 219
Cdd:TIGR02006 84 IAHFYKSKGNHIITSKTEHKAVLDTCRYLEREGFEVTYLPPKSNGLIDLEELKAAIRDDTILVSIMHVNNEIGVIQDIAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 220 IGQICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRRPRVRVEALQSGGGQERGMRSGTVP 299
Cdd:TIGR02006 164 IGEICRERKVFFHVDAAQSVGKIPINVNELKVDLMSISGHKIYGPKGIGALYVRRKPRVRLEALIHGGGHERGMRSGTLP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 300 TPLVVGLGAACELAQQEMEYDHKRISKLAERLVQNImKNLPDVVMNGDPKQHYPGCINLSFAYVEGESLLMALKDVALSS 379
Cdd:TIGR02006 244 THQIVGMGEAFRIAKEEMAQDTAHVLALRDRLLNGI-KSIEEVYLNGDLEHRVPGNLNVSFNYVEGESLIMALKDLAVSS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 380 GSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVDYTAEKCIHHVKRLREMSPLWEMVQDGIDLKSIKWTQH 459
Cdd:TIGR02006 323 GSACTSASLEPSYVLRALGINDELAHSSIRFTIGRFTTEEEIDYAVKLVKSAIDKLRELSPLWEMFKEGVDLNSIEWAAH 402
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
59-439 |
0e+00 |
|
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: 628.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 59 RPLYMDVQATTPLDPRVLDAMLPYLVNYYGNPHSrTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIK 138
Cdd:COG1104 2 MMIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSS-LHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNLAIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 139 GVARFYRSRKKHLVTTQTEHKCVLDSCRSLEAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIA 218
Cdd:COG1104 81 GAARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 219 EIGQICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRrpRVRVEALQSGGGQERGMRSGTV 298
Cdd:COG1104 161 EIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRK--GVRLEPLIHGGGQERGLRSGTE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 299 PTPLVVGLGAACELAQQEMEYDHKRISKLAERLVQNIMKNLPDVVMNGDPKQHYPGCINLSFAYVEGESLLMAL--KDVA 376
Cdd:COG1104 239 NVPGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAAIPGVVINGDPENRLPNTLNFSFPGVEGEALLLALdlAGIA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161016824 377 LSSGSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVDYTAEKCIHHVKRLREMS 439
Cdd:COG1104 319 VSSGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARLRKLS 381
|
|
| FeS_nifS |
TIGR03402 |
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related ... |
62-441 |
0e+00 |
|
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: 522.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 62 YMDVQATTPLDPRVLDAMLPYLVNYYGNPhSRTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIKGVA 141
Cdd:TIGR03402 2 YLDNNATTRVDPEVLEAMLPYFTEYFGNP-SSMHSFGGEVGKAVEEAREQVAKLLGAEPDEIIFTSGGTESDNTAIKSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 142 RFYRSrKKHLVTTQTEHKCVLDSCRSLEAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEIG 221
Cdd:TIGR03402 81 AAQPE-KRHIITTAVEHPAVLSLCQHLEKQGYKVTYLPVDEEGRLDLEELRAAITDDTALVSVMWANNETGTIFPIEEIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 222 QICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRrpRVRVEALQSGGGQERGMRSGTVPTP 301
Cdd:TIGR03402 160 EIAKERGALFHTDAVQAVGKIPIDLKEMNIDMLSLSGHKLHGPKGVGALYIRK--GTRFRPLLRGGHQERGRRAGTENVP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 302 LVVGLGAACELAQQEMEYDHKRISKLAERLVQNIMKNLPDVVMNGDPKQHYPGCINLSFAYVEGESLLMAL--KDVALSS 379
Cdd:TIGR03402 238 GIVGLGKAAELATEHLEEENTRVRALRDRLEAGLLARIPDARLNGDPTKRLPNTVNISFEYIEGEAILLLLdmEGICASS 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161016824 380 GSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVDYTAEKCIHHVKRLREMSPL 441
Cdd:TIGR03402 318 GSACTSGSLEPSHVLRAMGVPHTAAHGSIRFSLSRYNTEEDIDYVLEVLPPIIARLRAMSPF 379
|
|
| DNA_S_dndA |
TIGR03235 |
cysteine desulfurase DndA; This model describes DndA, a protein related to IscS and part of a ... |
62-410 |
2.15e-154 |
|
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: 441.93 E-value: 2.15e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 62 YMDVQATTPLDPRVLDAMLPYLVNYYGNPHSRTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIKGVA 141
Cdd:TIGR03235 1 YLDHNATTPIDPAVAEAMLPWLLEEFGNPSSRTHEFGHNAKKAVERARKQVAEALGADTEEVIFTSGATESNNLAILGLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 142 RFY-RSRKKHLVTTQTEHKCVLDSCRSLEAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEI 220
Cdd:TIGR03235 81 RAGeQKGKKHIITSAIEHPAVLEPIRALERNGFTVTYLPVDESGRIDVDELADAIRPDTLLVSIMHVNNETGSIQPIREI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 221 GQICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRR--PRVRVEALQSGGGQERGMRSGTV 298
Cdd:TIGR03235 161 AEVLEAHEAFFHVDAAQVVGKITVDLSADRIDLISCSGHKIYGPKGIGALVIRKRgkPKAPLKPIMFGGGQERGLRPGTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 299 PTPLVVGLGAACELAQQEMEYDHKRISKLAERLVQNImkNLPDVVMNGDPKQHYPGCINLSFAYVEGESLLMALK-DVAL 377
Cdd:TIGR03235 241 PVHLIVGMGEAAEIARRNAQAWEVKLRAMRNQLRDAL--QTLGVKLNGDPAETIPHILNFSIDGVNSEALIVNLRaDAAV 318
|
330 340 350
....*....|....*....|....*....|...
gi 161016824 378 SSGSACTSASLEPSYVLRAIGTDEDLAHSSIRF 410
Cdd:TIGR03235 319 STGSACSSSKYEPSHVLQAMGLDTDRARGAIRF 351
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
62-423 |
4.67e-111 |
|
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: 332.29 E-value: 4.67e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 62 YMDVQATTPLDPRVLDAMLPYLVNYYGNPHSRTHAYGWESEAAMERARQQVASLIGA-DPREIIFTSGATESNNIAIKGV 140
Cdd:pfam00266 2 YLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINApSNDEIIFTSGTTEAINLVALSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 141 ARFYRsRKKHLVTTQTEHKCVLDSCRSL-EAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAE 219
Cdd:pfam00266 82 GRSLK-PGDEIVITEMEHHANLVPWQELaKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 220 IGQICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRRPRVRVEALQSGGG-------QERG 292
Cdd:pfam00266 161 IGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGmietvslQEST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 293 M-------RSGTVPTPLVVGLGAACE-LAQQEMEYDHKRISKLAERLVQnIMKNLPDVVMNGDPKQhyPGCINLSFAYVE 364
Cdd:pfam00266 241 FadapwkfEAGTPNIAGIIGLGAALEyLSEIGLEAIEKHEHELAQYLYE-RLLSLPGIRLYGPERR--ASIISFNFKGVH 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161016824 365 GESLLMALKD--VALSSGSACTsaslEPSYVLRAIgtdedlaHSSIRFGIGRFTTEEEVDY 423
Cdd:pfam00266 318 PHDVATLLDEsgIAVRSGHHCA----QPLMVRLGL-------GGTVRASFYIYNTQEDVDR 367
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
61-424 |
2.96e-103 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 312.82 E-value: 2.96e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 61 LYMDVQATTPLDPRVLDAMLPYLVNYYGNPHSrTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIKGV 140
Cdd:PRK02948 2 IYLDYAATTPMSKEALQTYQKAASQYFGNESS-LHDIGGTASSLLQVCRKTFAEMIGGEEQGIYFTSGGTESNYLAIQSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 141 ARFYRSRKKHLVTTQTEHKCVLDSCRSLEAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEI 220
Cdd:PRK02948 81 LNALPQNKKHIITTPMEHASIHSYFQSLESQGYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQPIAEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 221 GQICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIrrRPRVRVEALQSGGGQERGMRSGTVPT 300
Cdd:PRK02948 161 GALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYI--NPQVRWKPVFPGTTHEKGFRPGTVNV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 301 PLVVGLGAACELAQQEMEYDHKRISKLAERLVQNI-MKNLPdVVMNGDPKQHYPGCINLSFAYVEGESLLMAL--KDVAL 377
Cdd:PRK02948 239 PGIAAFLTAAENILKNMQEESLRFKELRSYFLEQIqTLPLP-IEVEGHSTSCLPHIIGVTIKGIEGQYTMLECnrRGIAI 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 161016824 378 SSGSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVDYT 424
Cdd:PRK02948 318 STGSACQVGKQEPSKTMLAIGKTYEEAKQFVRFSFGQQTTKDQIDTT 364
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
62-438 |
7.55e-70 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 226.94 E-value: 7.55e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 62 YMDVQATTPLdPR-VLDAMLPYLVNYYGNPHSRTHAYGWESEAAMERARQQVASLIGA-DPREIIFTSGATESNNIAIKG 139
Cdd:COG0520 18 YLDNAATGQK-PRpVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAaSPDEIIFTRGTTEAINLVAYG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 140 VARFyrSRKKHLVTTQTEHKCVLDSCRSLEAE-GFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIA 218
Cdd:COG0520 97 LGRL--KPGDEILITEMEHHSNIVPWQELAERtGAEVRVIPLDEDGELDLEALEALLTPRTKLVAVTHVSNVTGTVNPVK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 219 EIGQICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRRPRVRVEALQSGGG---------- 288
Cdd:COG0520 175 EIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELLEALPPFLGGGGmiewvsfdgt 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 289 --QERGMR--SGTVPTPLVVGLGAACELAQQ-EMEYDHKRISKLAERLVQNiMKNLPDVVMNGDPKQHYPGCInLSFaYV 363
Cdd:COG0520 255 tyADLPRRfeAGTPNIAGAIGLGAAIDYLEAiGMEAIEARERELTAYALEG-LAAIPGVRILGPADPEDRSGI-VSF-NV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 364 EG---ESLLMALKD--VALSSGSACTsaslEPsyVLRAIGTDedlahSSIRFGIGRFTTEEEVDYtaekCIHHVKRLREM 438
Cdd:COG0520 332 DGvhpHDVAALLDDegIAVRAGHHCA----QP--LMRRLGVP-----GTVRASFHLYNTEEEIDR----LVEALKKLAEL 396
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
62-422 |
1.01e-63 |
|
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: 210.40 E-value: 1.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 62 YMDVQATTPLDPRVLDAMLPYLVNYYGNPHSRTHAYGWESEAAMERARQQVASLIGA-DPREIIFTSGATESNNIAIKGV 140
Cdd:cd06453 2 YLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINApSPDEIIFTRNTTEAINLVAYGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 141 ARfyrSRKK--HLVTTQTEHKCVLDSCRSLEAE-GFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPI 217
Cdd:cd06453 82 GR---ANKPgdEIVTSVMEHHSNIVPWQQLAERtGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 218 AEIGQICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRRPRVRVEALQSGGG--------- 288
Cdd:cd06453 159 KEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEmieevsfee 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 289 ---QERGMR--SGTVPTPLVVGLGAACELAQQE-ME----YDHKRISKLAERLVQnimknLPDVVMNGDPKQHYPGcinL 358
Cdd:cd06453 239 ttyADLPHKfeAGTPNIAGAIGLGAAIDYLEKIgMEaiaaHEHELTAYALERLSE-----IPGVRVYGDAEDRAGV---V 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161016824 359 SFAyVEG---ESLLMAL--KDVALSSGSACTsaslEPsyVLRAIGtdedlAHSSIRFGIGRFTTEEEVD 422
Cdd:cd06453 311 SFN-LEGihpHDVATILdqYGIAVRAGHHCA----QP--LMRRLG-----VPGTVRASFGLYNTEEEID 367
|
|
| sufS |
TIGR01979 |
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine ... |
62-342 |
6.35e-45 |
|
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: 161.28 E-value: 6.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 62 YMDVQATTpLDPR-VLDAMLPYLVNYYGNPHSRTHAYGWESEAAMERARQQVASLIGA-DPREIIFTSGATESNNIAIKG 139
Cdd:TIGR01979 21 YLDSAATS-QKPQqVIDAVAEYYRNSNANVHRGIHTLSVRATEAYEAVREKVAKFINAaSDEEIVFTRGTTESINLVAYS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 140 VARFYRSRKKHLVTTQTEHKCVLDSCRSL-EAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIA 218
Cdd:TIGR01979 100 WGDSNLKAGDEIVISEMEHHANIVPWQLLaERTGATLKFIPLDDDGTLDLDDLEKLLTEKTKLVAITHVSNVLGTVNPVE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 219 EIGQICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRRPRVRVEALQSGGG---------- 288
Cdd:TIGR01979 180 EIAKLAHQVGAKVLVDGAQAVPHMPVDVQALDCDFYVFSGHKMYGPTGIGVLYGKEELLEQMPPFLGGGEmiaevsfeet 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 161016824 289 --QERGMR--SGTVPTPLVVGLGAACE-LAQQEMEYDHKRISKLAERLVQNIMKnLPDV 342
Cdd:TIGR01979 260 tyNEAPHKfeAGTPNIAGVIGLGAAIDyLEAIGLENIEAHEHELTAYALERLGE-IPGL 317
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
59-433 |
1.07e-31 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 125.63 E-value: 1.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 59 RPL-YMDVQATTPLDPRVLDAMLPYLVNYYGNPHSRTHAYGWESEAAMERARQQVASLIGA-DPREIIFTSGATEsnniA 136
Cdd:PLN02855 31 SKLvYLDNAATSQKPAAVLDALQDYYEEYNSNVHRGIHALSAKATDAYELARKKVAAFINAsTSREIVFTRNATE----A 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 137 IKGVARFY-RSRKK---HLVTTQTEHKCVLDSCRSLEAE-GFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEI 211
Cdd:PLN02855 107 INLVAYTWgLANLKpgdEVILSVAEHHSNIVPWQLVAQKtGAVLKFVGLTPDEVLDVEQLKELLSEKTKLVATHHVSNVL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 212 GVKQPIAEIGQICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYirrrprVRVEALQS-----G 286
Cdd:PLN02855 187 GSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLW------GKSDLLESmppflG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 287 GGQergM-------RSGTVPTPL-----------VVGLGAACE-LAQQEMEYDHKRISKLAERLVQNIMKnLPDVVMNGD 347
Cdd:PLN02855 261 GGE---MisdvfldHSTYAPPPSrfeagtpaigeAIGLGAAIDyLSEIGMDRIHEYEVELGTYLYEKLSS-VPGVRIYGP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 348 PKQHYPGCINLSFAYVEG------ESLLMALKDVALSSGSACTsaslEPSYvlRAIGTDEDlAHSSIRFgigrFTTEEEV 421
Cdd:PLN02855 337 KPSEGVGRAALCAFNVEGihptdlSTFLDQQHGVAIRSGHHCA----QPLH--RYLGVNAS-ARASLYF----YNTKEEV 405
|
410
....*....|..
gi 161016824 422 DYTaekcIHHVK 433
Cdd:PLN02855 406 DAF----IHALK 413
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
62-396 |
9.30e-26 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 108.59 E-value: 9.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 62 YMDvQATTPLDPR-VLDAMLPYLVNYYGNPHSRTHAYGWESEAAMERARQQVASLIGA-DPREIIFTSGATESNNIAIKG 139
Cdd:PRK10874 22 YLD-SAATALKPQaVIEATQQFYSLSAGNVHRSQFAAAQRLTARYEAAREQVAQLLNApDAKNIVWTRGTTESINLVAQS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 140 VARFYRSRKKHLVTTQTEHKCVLDSCRSL-EAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIA 218
Cdd:PRK10874 101 YARPRLQPGDEIIVSEAEHHANLVPWLMVaQQTGAKVVKLPLGADRLPDVDLLPELITPRTRILALGQMSNVTGGCPDLA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 219 EIGQICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRRPRVRVEALQSGGGQER-----GM 293
Cdd:PRK10874 181 RAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMSPWQGGGKMLTevsfdGF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 294 RSGTVP------TPL---VVGLGAACE-LAQQEMEYDHKRISKLAErLVQNIMKNLPdvvmnGDPKQHYPGCINLSF--A 361
Cdd:PRK10874 261 TPQSAPwrfeagTPNvagVIGLSAALEwLADIDINQAESWSRSLAT-LAEDALAKLP-----GFRSFRCQDSSLLAFdfA 334
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 161016824 362 YVEGESL--LMALKDVALSSGSACTS---ASLEPSYVLRA 396
Cdd:PRK10874 335 GVHHSDLvtLLAEYGIALRAGQHCAQpllAALGVTGTLRA 374
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
60-311 |
1.46e-24 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 105.22 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 60 PL-YMDVQATTPLDPRVLDAMLPYLVNYYGNPHSRTHAYGWESEAAMERARQQVASLIGA-DPREIIFTSGATESNNIAI 137
Cdd:PRK09295 23 PLaYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKQAALFINArSAEELVFVRGTTEGINLVA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 138 KGVARFYRSRKKHLVTTQTEHKCVLDSCRSL-EAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQP 216
Cdd:PRK09295 103 NSWGNSNVRAGDNIIISEMEHHANIVPWQMLcARVGAELRVIPLNPDGTLQLETLPALFDERTRLLAITHVSNVLGTENP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 217 IAEIgqICSSRK--VYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRrprvrvEALQS-----GGGQ 289
Cdd:PRK09295 183 LAEM--IALAHQhgAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKE------ALLQEmppweGGGS 254
|
250 260 270
....*....|....*....|....*....|....*...
gi 161016824 290 -------ERGM---------RSGTVPTPLVVGLGAACE 311
Cdd:PRK09295 255 miatvslTEGTtwakapwrfEAGTPNTGGIIGLGAALD 292
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
104-287 |
2.58e-16 |
|
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: 81.44 E-value: 2.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 104 AMERARQQVASLIGA-DPREIIFTSGATEsnniAIKGVARFYRsrKKHL------VTTQTEHK---------Cvldscrs 167
Cdd:NF041166 290 AYEGAREKVRRFIGApSVDEIIFVRGTTE----AINLVAKSWG--RQNIgagdeiIVSHLEHHanivpwqqlA------- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 168 lEAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEIGQICssrkvyfH-------TDAAQAVG 240
Cdd:NF041166 357 -QETGAKLRVIPVDDSGQILLDEYAKLLNPRTKLVSVTQVSNALGTVTPVKEIIALA-------HragakvlVDGAQSVS 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 161016824 241 KIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRrprvrvEAL------QSGG 287
Cdd:NF041166 429 HMPVDVQALDADFFVFSGHKVFGPTGIGVVYGKR------DLLeamppwQGGG 475
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
102-273 |
1.48e-13 |
|
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: 68.56 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 102 EAAMERARQqvASLIGADprEIIFTSGATESNNIAIKgvarFYRSRKKHLVTTQTEHKCVLDScrSLEAEGFRVTYLPVQ 181
Cdd:cd01494 3 EELEEKLAR--LLQPGND--KAVFVPSGTGANEAALL----ALLGPGDEVIVDANGHGSRYWV--AAELAGAKPVPVPVD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 182 KS--GIIDLKELE-AAIQPDTSLVSVMTVNNEIGVKQPIAEIGQICSSRKVYFHTDAAQAVGKIP---LDVNDMKIDLMS 255
Cdd:cd01494 73 DAgyGGLDVAILEeLKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPapgVLIPEGGADVVT 152
|
170
....*....|....*...
gi 161016824 256 ISGHKLYGPKGVGAIYIR 273
Cdd:cd01494 153 FSLHKNLGGEGGGVVIVK 170
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
103-275 |
7.36e-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: 70.25 E-value: 7.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 103 AAMER-ARQQVASLIGADPREI-IFTSGATESNNIAIKgVARFY----RSRKKHL--------VTTQTEHKCVLDSCRSL 168
Cdd:COG0076 106 TELEReVVRWLADLLGLPEGAGgVFTSGGTEANLLALL-AARDRalarRVRAEGLpgaprpriVVSEEAHSSVDKAARLL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 169 EAEGFRVTYLPVQKSGIIDLKELEAAIQPDTS-------LV-SVMTVNneIGVKQPIAEIGQICSSRKVYFHTDAA---- 236
Cdd:COG0076 185 GLGRDALRKVPVDEDGRMDPDALEAAIDEDRAaglnpiaVVaTAGTTN--TGAIDPLAEIADIAREHGLWLHVDAAyggf 262
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 161016824 237 --------QAVGKIPLdvndmkIDLMSISGHK-LYGPKGVGAIYIRRR 275
Cdd:COG0076 263 alpspelrHLLDGIER------ADSITVDPHKwLYVPYGCGAVLVRDP 304
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
112-273 |
4.61e-11 |
|
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: 64.15 E-value: 4.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 112 VASLIGADPREI--IFTSGATESNNIAIKGVARFYRSRKKH----------LVTTQTEHKCVLDSCRSLEAEgfrVTYLP 179
Cdd:cd06450 47 LAKLFGLPSEDAdgVFTSGGSESNLLALLAARDRARKRLKAgggrgidklvIVCSDQAHVSVEKAAAYLDVK---VRLVP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 180 VQKSGIIDLKELEAAIQPD------TSLVSVMTVNNEIGVKQPIAEIGQICSSRKVYFHTDAAQAVGKIPLDVNDMKI-- 251
Cdd:cd06450 124 VDEDGRMDPEALEAAIDEDkaeglnPIMVVATAGTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDfg 203
|
170 180
....*....|....*....|....*..
gi 161016824 252 ----DLMSISGHKLYG-PKGVGAIYIR 273
Cdd:cd06450 204 iervDSISVDPHKYGLvPLGCSAVLVR 230
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
107-331 |
5.76e-10 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 59.92 E-value: 5.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 107 RARQQVASLIGADprEIIFTSGATESNNIAIKGVARfyrsRKKHLVTTQTEHKCvLDSCRSL-EAEGFRVTYLPVQKSGI 185
Cdd:pfam01212 36 RLEDRVAELFGKE--AALFVPSGTAANQLALMAHCQ----RGDEVICGEPAHIH-FDETGGHaELGGVQPRPLDGDEAGN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 186 IDLKELEAAI-------QPDTSLVSVmTVNNEIGVKQP-----IAEIGQICSSRKVYFHTDAAQ---AVGKIPLDVNDMK 250
Cdd:pfam01212 109 MDLEDLEAAIrevgadiFPPTGLISL-ENTHNSAGGQVvslenLREIAALAREHGIPVHLDGARfanAAVALGVIVKEIT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 251 --IDLMSISGHK-LYGPkgVGAI------YIRRRPRVRveaLQSGGGqergMRSGTVPTplVVGLGAaCELAQQEMEYDH 321
Cdd:pfam01212 188 syADSVTMCLSKgLGAP--VGSVlagsddFIAKAIRQR---KYLGGG----LRQAGVLA--AAGLRA-LEEGVARLARDH 255
|
250
....*....|
gi 161016824 322 KRISKLAERL 331
Cdd:pfam01212 256 ATARRLAEGL 265
|
|
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
85-274 |
2.36e-08 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 56.41 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 85 NYYGNPHSRTHAYGWESEaAMERARQQVASLIGADPRE--IIFTSGATEsnniAIKGVAR-FYRSRKKHLVTTQTEHKCV 161
Cdd:PLN02724 61 NVYGNPHSQSDSSMRSSD-TIESARQQVLEYFNAPPSDyaCVFTSGATA----ALKLVGEtFPWSSESHFCYTLENHNSV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 162 L---------------------DSCRSLEAEGFRVTYLPVQKSGIIDLkELEAAIQPDTSLVSVMTVNNEIGVKQPIAEI 220
Cdd:PLN02724 136 LgireyalekgaaaiavdieeaANQPTNSQGSVVVKSRGLQRRNTSKL-QKREDDGEAYNLFAFPSECNFSGAKFPLDLV 214
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161016824 221 GQICSSRKVYFHT--------DAAQAVGKIPLDVNDMKIDLMSISGHKLYG-PKGVGAIYIRR 274
Cdd:PLN02724 215 KLIKDNQHSNFSKsgrwmvllDAAKGCGTSPPDLSRYPADFVVVSFYKIFGyPTGLGALLVRR 277
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
73-430 |
1.53e-05 |
|
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.
Pssm-ID: 99748 [Multi-domain] Cd Length: 338 Bit Score: 46.94 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 73 PRVLDAMlpYLVNYygnphsRTHAYGwESEAAmERARQQVASLIGADprEIIFTSGATESNNIAIKGVARFYRSrkkhLV 152
Cdd:cd06502 12 PEMLEAM--AAANV------GDDVYG-EDPTT-AKLEARAAELFGKE--AALFVPSGTAANQLALAAHTQPGGS----VI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 153 TTQTEHKCvLDSCRSLEAEGfRVTYLPVQ-KSGIIDLKELEAAIQPD-------TSLVSVMTVNNEIGVKQP--IAEIGQ 222
Cdd:cd06502 76 CHETAHIY-TDEAGAPEFLS-GVKLLPVPgENGKLTPEDLEAAIRPRddihfppPSLVSLENTTEGGTVYPLdeLKAISA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 223 ICSSRKVYFHTDAAQ-----AVGKIPLDVNDMKIDLMSISGHK-LYGPkgVGAI------YIRRRPRVRVealQSGGgqe 290
Cdd:cd06502 154 LAKENGLPLHLDGARlanaaAALGVALKTYKSGVDSVSFCLSKgGGAP--VGAVvvgnrdFIARARRRRK---QAGG--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 291 rGMR-SGTVPTPLVVGLGAACELAQqeMEYDHKRISKLAERLvqnimKNLPDVVMNGDPkqhypgciNLSFAYVEGEsll 369
Cdd:cd06502 226 -GMRqSGFLAAAGLAALENDLWLRR--LRHDHEMARRLAEAL-----EELGGLESEVQT--------NIVLLDPVEA--- 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161016824 370 malkDVALSSGSACTSASLEPSYVLRAIGtdedlaHSSIRFGIGRFTTEEEVDYTAEKCIH 430
Cdd:cd06502 287 ----NAVFVELSKEAIERRGEGVLFYAWG------EGGVRFVTHWDTTEEDVDELLSALKA 337
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
168-316 |
2.36e-05 |
|
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: 46.13 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 168 LEAEGFRVTYLPVQKSGIIDLKELEAAI-QPDTSLVSVMTVNNEIGVKQPIAEIGQICSSRKVYFHTDAAQAVGKIPLDV 246
Cdd:cd06451 93 AERYGADVDVVEKPWGEAVSPEEIAEALeQHDIKAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVDAVSSLGGEPFRM 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 247 NDMKIDLMSISGHK-LYGPKGVGAIYIRRRPRVRVEALQSGGG------------QERGMRSGTVPTPLVVGLGAACELA 313
Cdd:cd06451 173 DEWGVDVAYTGSQKaLGAPPGLGPIAFSERALERIKKKTKPKGfyfdlllllkywGEGYSYPHTPPVNLLYALREALDLI 252
|
...
gi 161016824 314 QQE 316
Cdd:cd06451 253 LEE 255
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
70-344 |
1.27e-03 |
|
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: 40.79 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 70 PLDPRVLDAMLpyLVNYYGNPHSRTHAYGweseaaMERARQQVASLIG------ADPREIIFTSGATEsnniAIKGVARF 143
Cdd:cd00609 11 PPPPEVLEALA--AAALRAGLLGYYPDPG------LPELREAIAEWLGrrggvdVPPEEIVVTNGAQE----ALSLLLRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 144 YRSRKKHLVTTQ---TEHKcvldscRSLEAEGFRVTYLPVQKSGII--DLKELEAAIQPDTSLVSVMTVNNEIGV---KQ 215
Cdd:cd00609 79 LLNPGDEVLVPDptyPGYE------AAARLAGAEVVPVPLDEEGGFllDLELLEAAKTPKTKLLYLNNPNNPTGAvlsEE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 216 PIAEIGQICSSRKVY---------FHTDAAQAvgkIPLDVNDMKIDLMSISGH-KLYGPKG--VGAIYIrrRPRVRVEAL 283
Cdd:cd00609 153 ELEELAELAKKHGILiisdeayaeLVYDGEPP---PALALLDAYERVIVLRSFsKTFGLPGlrIGYLIA--PPEELLERL 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161016824 284 QSgggqERGMRSGTVPTPLVVGLGAACELAQQEMEYDHKRISKLAERLVQNIMKNLPDVVM 344
Cdd:cd00609 228 KK----LLPYTTSGPSTLSQAAAAAALDDGEEHLEELRERYRRRRDALLEALKELGPLVVV 284
|
|
| GDC-P |
cd00613 |
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ... |
140-268 |
4.15e-03 |
|
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine cleavage system P-proteins EC:1.4.4.2 from bacterial, mammalian and plant sources. The P protein is part of the glycine decarboxylase multienzyme complex EC:2.1.2.10 (GDC) also annotated as glycine cleavage system or glycine synthase. GDC consists of four proteins P, H, L and T. The reaction catalysed by this protein is: Glycine + lipoylprotein <=> S-aminomethyldihydrolipoylprotein + CO2. Alpha-beta-type dimers associate to form an alpha(2)beta(2) tetramer, where the alpha- and beta-subunits are structurally similar and appear to have arisen by gene duplication and subsequent divergence with a loss of one active site. The members of this CD are widely dispersed among all three forms of cellular life.
Pssm-ID: 99737 [Multi-domain] Cd Length: 398 Bit Score: 39.14 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 140 VARFYRSRKKHLV--TTQTEHKCVLDSCrsLEAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPI 217
Cdd:cd00613 101 AIRAYHKRNKVLVpdSAHPTNPAVARTR--GEPLGIEVVEVPSDEGGTVDLEALKEEVSEEVAALMVQYPNTLGVFEDLI 178
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 161016824 218 AEIGQICSSRKVYFHTDAA--QAVGKIPldVNDMKIDLMSISGHKLYGPKGVG 268
Cdd:cd00613 179 KEIADIAHSAGALVYVDGDnlNLTGLKP--PGEYGADIVVGNLQKTGVPHGGG 229
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
124-285 |
5.69e-03 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 38.94 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 124 IFTSGATESNNIAIKGV-ARFYRSRKKH--------------LVTTQTEHKCVLdscRSLEAEGFRVTYLPVQKSGIIDL 188
Cdd:pfam00282 106 VLQPGSSESNLLALLAArTKWIKRMKAAgkpadssgilaklvAYTSDQAHSSIE---KAALYGGVKLREIPSDDNGKMRG 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 189 KELEAAIQPDTSLVSV-MTVNNEIGVK-----QPIAEIGQICSSRKVYFHTDAAQAVGKI------PLDVNDMKIDLMSI 256
Cdd:pfam00282 183 MDLEKAIEEDKENGLIpFFVVATLGTTgsgafDDLQELGDICAKHNLWLHVDAAYGGSAFicpefrHWLFGIERADSITF 262
|
170 180 190
....*....|....*....|....*....|
gi 161016824 257 SGHKLYG-PKGVGAIYIRRRprvrvEALQS 285
Cdd:pfam00282 263 NPHKWMLvLLDCSAVWVKDK-----EALQQ 287
|
|
| PRK05939 |
PRK05939 |
cystathionine gamma-synthase family protein; |
167-234 |
7.65e-03 |
|
cystathionine gamma-synthase family protein;
Pssm-ID: 235650 [Multi-domain] Cd Length: 397 Bit Score: 38.52 E-value: 7.65e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161016824 167 SLEAEGFRVTYLPVqksgiIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEIGQICSSRKVYFHTD 234
Cdd:PRK05939 105 TLRGLGVEVTMVDA-----TDVQNVAAAIRPNTRMVFVETIANPGTQVADLAGIGALCRERGLLYVVD 167
|
|
| PLN02721 |
PLN02721 |
threonine aldolase |
178-334 |
8.46e-03 |
|
threonine aldolase
Pssm-ID: 178323 [Multi-domain] Cd Length: 353 Bit Score: 38.13 E-value: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 178 LPVQKSGIIDLKELEAAIQPD-------TSLVSVMTVNNEIGVK----QPIAEIGQICSSRKVYFHTDAAQ------AVG 240
Cdd:PLN02721 110 VKNNEDGTMDLDAIEAAIRPKgddhfptTRLICLENTHANCGGRclsvEYTDKVGELAKRHGLKLHIDGARifnasvALG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016824 241 kIPLDVNDMKIDLMSISGHK-LYGPKG---VG-AIYIRRRPRVRvEALqsGGgqerGMRSGTVptplvvgLGAACELAQQ 315
Cdd:PLN02721 190 -VPVHRLVKAADSVSVCLSKgLGAPVGsviVGsKSFIRKAKRLR-KTL--GG----GMRQVGV-------LAAAALVALQ 254
|
170 180
....*....|....*....|...
gi 161016824 316 EM----EYDHKRISKLAERLVQN 334
Cdd:PLN02721 255 ENvpklEDDHKKAKLLAEGLNQI 277
|
|
| |
