|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
53-452 |
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 58618884 53 PLYMDVQATTPLDPRVLDAMLPYLVN--YYGNPHSRTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAI 130
Cdd:PRK14012 4 PIYLDYSATTPVDPRVAEKMMPYLTMdgTFGNPASRSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDNLAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 131 KGVARFYRSRKKHLVTTQTEHKCVLDSCRSLEAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPI 210
Cdd:PRK14012 84 KGAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVIQDI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 211 AEIGQICSSRKLYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRRPRVRVEALQSGGGQERGMRSGT 290
Cdd:PRK14012 164 AAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRLEAQMHGGGHERGMRSGT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 291 VPTPLVVGLGAACELAQQEMEYDHKRISKLAERLIQKImKNLPDVVMNGDPKQHYPGCINLSFAYVEGESLLMALKDVAL 370
Cdd:PRK14012 244 LPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGI-KDIEEVYLNGDLEQRVPGNLNVSFNYVEGESLIMALKDLAV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 371 SSGSACTSASLEPSYVLRAIGMDEDLAHSSIRFGIGRFTTEEEVDYTVQKCIHHVKRLREMSPLWEMVQDGIDLKSIKWT 450
Cdd:PRK14012 323 SSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGKLRELSPLWEMFKEGVDLNSIEWA 402
|
..
gi 58618884 451 QH 452
Cdd:PRK14012 403 HH 404
|
|
| IscS |
TIGR02006 |
cysteine desulfurase IscS; This model represents IscS, one of several cysteine desulfurases ... |
53-452 |
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: 663.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 53 PLYMDVQATTPLDPRVLDAMLPYLVNYYGNPHSRTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIKG 132
Cdd:TIGR02006 4 PIYLDYAATTPVDPRVAEKMMPYLTEKFGNPASRSHSFGWEAEEAVENARNQVAELIGADSREIVFTSGATESNNLAIKG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 133 VARFYRSRKKHLVTTQTEHKCVLDSCRSLEAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAE 212
Cdd:TIGR02006 84 IAHFYKSKGNHIITSKTEHKAVLDTCRYLEREGFEVTYLPPKSNGLIDLEELKAAIRDDTILVSIMHVNNEIGVIQDIAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 213 IGQICSSRKLYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRRPRVRVEALQSGGGQERGMRSGTVP 292
Cdd:TIGR02006 164 IGEICRERKVFFHVDAAQSVGKIPINVNELKVDLMSISGHKIYGPKGIGALYVRRKPRVRLEALIHGGGHERGMRSGTLP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 293 TPLVVGLGAACELAQQEMEYDHKRISKLAERLIQKImKNLPDVVMNGDPKQHYPGCINLSFAYVEGESLLMALKDVALSS 372
Cdd:TIGR02006 244 THQIVGMGEAFRIAKEEMAQDTAHVLALRDRLLNGI-KSIEEVYLNGDLEHRVPGNLNVSFNYVEGESLIMALKDLAVSS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 373 GSACTSASLEPSYVLRAIGMDEDLAHSSIRFGIGRFTTEEEVDYTVQKCIHHVKRLREMSPLWEMVQDGIDLKSIKWTQH 452
Cdd:TIGR02006 323 GSACTSASLEPSYVLRALGINDELAHSSIRFTIGRFTTEEEIDYAVKLVKSAIDKLRELSPLWEMFKEGVDLNSIEWAAH 402
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
52-432 |
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: 630.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 52 RPLYMDVQATTPLDPRVLDAMLPYLVNYYGNPHSrTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIK 131
Cdd:COG1104 2 MMIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSS-LHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNLAIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 132 GVARFYRSRKKHLVTTQTEHKCVLDSCRSLEAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIA 211
Cdd:COG1104 81 GAARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 212 EIGQICSSRKLYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRrpRVRVEALQSGGGQERGMRSGTV 291
Cdd:COG1104 161 EIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRK--GVRLEPLIHGGGQERGLRSGTE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 292 PTPLVVGLGAACELAQQEMEYDHKRISKLAERLIQKIMKNLPDVVMNGDPKQHYPGCINLSFAYVEGESLLMAL--KDVA 369
Cdd:COG1104 239 NVPGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAAIPGVVINGDPENRLPNTLNFSFPGVEGEALLLALdlAGIA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58618884 370 LSSGSACTSASLEPSYVLRAIGMDEDLAHSSIRFGIGRFTTEEEVDYTVQKCIHHVKRLREMS 432
Cdd:COG1104 319 VSSGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARLRKLS 381
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
55-416 |
3.55e-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: 3.55e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 55 YMDVQATTPLDPRVLDAMLPYLVNYYGNPHSRTHAYGWESEAAMERARQQVASLIGA-DPREIIFTSGATESNNIAIKGV 133
Cdd:pfam00266 2 YLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINApSNDEIIFTSGTTEAINLVALSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 134 ARFYRsRKKHLVTTQTEHKCVLDSCRSL-EAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAE 212
Cdd:pfam00266 82 GRSLK-PGDEIVITEMEHHANLVPWQELaKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 213 IGQICSSRKLYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRRPRVRVEALQSGGG-------QERG 285
Cdd:pfam00266 161 IGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGmietvslQEST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 286 M-------RSGTVPTPLVVGLGAACE-LAQQEMEYDHKRISKLAERLiQKIMKNLPDVVMNGDPKQhyPGCINLSFAYVE 357
Cdd:pfam00266 241 FadapwkfEAGTPNIAGIIGLGAALEyLSEIGLEAIEKHEHELAQYL-YERLLSLPGIRLYGPERR--ASIISFNFKGVH 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58618884 358 GESLLMALKD--VALSSGSACTsaslEPSYVLRAIgmdedlaHSSIRFGIGRFTTEEEVDY 416
Cdd:pfam00266 318 PHDVATLLDEsgIAVRSGHHCA----QPLMVRLGL-------GGTVRASFYIYNTQEDVDR 367
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
55-415 |
1.68e-64 |
|
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: 211.94 E-value: 1.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 55 YMDVQATTPLDPRVLDAMLPYLVNYYGNPHSRTHAYGWESEAAMERARQQVASLIGA-DPREIIFTSGATESNNIAIKGV 133
Cdd:cd06453 2 YLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINApSPDEIIFTRNTTEAINLVAYGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 134 ARfyrSRKK--HLVTTQTEHKCVLDSCRSLEAE-GFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPI 210
Cdd:cd06453 82 GR---ANKPgdEIVTSVMEHHSNIVPWQQLAERtGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 211 AEIGQICSSRKLYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRRPRVRVEALQSGGG--------- 281
Cdd:cd06453 159 KEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEmieevsfee 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 282 ---QERGMR--SGTVPTPLVVGLGAACELAQQE-MEYDHKRISKLAERLIQKiMKNLPDVVMNGDPKQHYPGcinLSFAy 355
Cdd:cd06453 239 ttyADLPHKfeAGTPNIAGAIGLGAAIDYLEKIgMEAIAAHEHELTAYALER-LSEIPGVRVYGDAEDRAGV---VSFN- 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 58618884 356 VEG---ESLLMAL--KDVALSSGSACTsaslEPsyVLRAIGmdedlAHSSIRFGIGRFTTEEEVD 415
Cdd:cd06453 314 LEGihpHDVATILdqYGIAVRAGHHCA----QP--LMRRLG-----VPGTVRASFGLYNTEEEID 367
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
97-280 |
1.94e-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: 81.82 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 97 AMERARQQVASLIGA-DPREIIFTSGATEsnniAIKGVARFYRsrKKHL------VTTQTEHK---------Cvldscrs 160
Cdd:NF041166 290 AYEGAREKVRRFIGApSVDEIIFVRGTTE----AINLVAKSWG--RQNIgagdeiIVSHLEHHanivpwqqlA------- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 161 lEAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEIGQICssrklyfH-------TDAAQAVG 233
Cdd:NF041166 357 -QETGAKLRVIPVDDSGQILLDEYAKLLNPRTKLVSVTQVSNALGTVTPVKEIIALA-------HragakvlVDGAQSVS 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 58618884 234 KIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRrprvrvEAL------QSGG 280
Cdd:NF041166 429 HMPVDVQALDADFFVFSGHKVFGPTGIGVVYGKR------DLLeamppwQGGG 475
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
53-452 |
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 58618884 53 PLYMDVQATTPLDPRVLDAMLPYLVN--YYGNPHSRTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAI 130
Cdd:PRK14012 4 PIYLDYSATTPVDPRVAEKMMPYLTMdgTFGNPASRSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDNLAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 131 KGVARFYRSRKKHLVTTQTEHKCVLDSCRSLEAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPI 210
Cdd:PRK14012 84 KGAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVIQDI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 211 AEIGQICSSRKLYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRRPRVRVEALQSGGGQERGMRSGT 290
Cdd:PRK14012 164 AAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRLEAQMHGGGHERGMRSGT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 291 VPTPLVVGLGAACELAQQEMEYDHKRISKLAERLIQKImKNLPDVVMNGDPKQHYPGCINLSFAYVEGESLLMALKDVAL 370
Cdd:PRK14012 244 LPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGI-KDIEEVYLNGDLEQRVPGNLNVSFNYVEGESLIMALKDLAV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 371 SSGSACTSASLEPSYVLRAIGMDEDLAHSSIRFGIGRFTTEEEVDYTVQKCIHHVKRLREMSPLWEMVQDGIDLKSIKWT 450
Cdd:PRK14012 323 SSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGKLRELSPLWEMFKEGVDLNSIEWA 402
|
..
gi 58618884 451 QH 452
Cdd:PRK14012 403 HH 404
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
54-415 |
0e+00 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 672.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 54 LYMDVQATTPLDPRVLDAMLPYLVNYYGNPHSRTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIKGV 133
Cdd:PLN02651 1 LYLDMQATTPIDPRVLDAMLPFLIEHFGNPHSRTHLYGWESEDAVEKARAQVAALIGADPKEIIFTSGATESNNLAIKGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 134 ARFYRSRKKHLVTTQTEHKCVLDSCRSLEAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEI 213
Cdd:PLN02651 81 MHFYKDKKKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVEEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 214 GQICSSRKLYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRRPRVRVEALQSGGGQERGMRSGTVPT 293
Cdd:PLN02651 161 GELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRLEPLMSGGGQERGRRSGTENT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 294 PLVVGLGAACELAQQEMEYDHKRISKLAERLIQKIMKNLPDVVMNG--DPKQHYPGCINLSFAYVEGESLLMALKDVALS 371
Cdd:PLN02651 241 PLVVGLGAACELAMKEMDYDEKHMKALRERLLNGLRAKLGGVRVNGprDPEKRYPGTLNLSFAYVEGESLLMGLKEVAVS 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 58618884 372 SGSACTSASLEPSYVLRAIGMDEDLAHSSIRFGIGRFTTEEEVD 415
Cdd:PLN02651 321 SGSACTSASLEPSYVLRALGVPEEMAHGSLRLGVGRFTTEEEVD 364
|
|
| IscS |
TIGR02006 |
cysteine desulfurase IscS; This model represents IscS, one of several cysteine desulfurases ... |
53-452 |
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: 663.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 53 PLYMDVQATTPLDPRVLDAMLPYLVNYYGNPHSRTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIKG 132
Cdd:TIGR02006 4 PIYLDYAATTPVDPRVAEKMMPYLTEKFGNPASRSHSFGWEAEEAVENARNQVAELIGADSREIVFTSGATESNNLAIKG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 133 VARFYRSRKKHLVTTQTEHKCVLDSCRSLEAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAE 212
Cdd:TIGR02006 84 IAHFYKSKGNHIITSKTEHKAVLDTCRYLEREGFEVTYLPPKSNGLIDLEELKAAIRDDTILVSIMHVNNEIGVIQDIAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 213 IGQICSSRKLYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRRPRVRVEALQSGGGQERGMRSGTVP 292
Cdd:TIGR02006 164 IGEICRERKVFFHVDAAQSVGKIPINVNELKVDLMSISGHKIYGPKGIGALYVRRKPRVRLEALIHGGGHERGMRSGTLP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 293 TPLVVGLGAACELAQQEMEYDHKRISKLAERLIQKImKNLPDVVMNGDPKQHYPGCINLSFAYVEGESLLMALKDVALSS 372
Cdd:TIGR02006 244 THQIVGMGEAFRIAKEEMAQDTAHVLALRDRLLNGI-KSIEEVYLNGDLEHRVPGNLNVSFNYVEGESLIMALKDLAVSS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 373 GSACTSASLEPSYVLRAIGMDEDLAHSSIRFGIGRFTTEEEVDYTVQKCIHHVKRLREMSPLWEMVQDGIDLKSIKWTQH 452
Cdd:TIGR02006 323 GSACTSASLEPSYVLRALGINDELAHSSIRFTIGRFTTEEEIDYAVKLVKSAIDKLRELSPLWEMFKEGVDLNSIEWAAH 402
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
52-432 |
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: 630.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 52 RPLYMDVQATTPLDPRVLDAMLPYLVNYYGNPHSrTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIK 131
Cdd:COG1104 2 MMIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSS-LHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNLAIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 132 GVARFYRSRKKHLVTTQTEHKCVLDSCRSLEAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIA 211
Cdd:COG1104 81 GAARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 212 EIGQICSSRKLYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRrpRVRVEALQSGGGQERGMRSGTV 291
Cdd:COG1104 161 EIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRK--GVRLEPLIHGGGQERGLRSGTE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 292 PTPLVVGLGAACELAQQEMEYDHKRISKLAERLIQKIMKNLPDVVMNGDPKQHYPGCINLSFAYVEGESLLMAL--KDVA 369
Cdd:COG1104 239 NVPGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAAIPGVVINGDPENRLPNTLNFSFPGVEGEALLLALdlAGIA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58618884 370 LSSGSACTSASLEPSYVLRAIGMDEDLAHSSIRFGIGRFTTEEEVDYTVQKCIHHVKRLREMS 432
Cdd:COG1104 319 VSSGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARLRKLS 381
|
|
| FeS_nifS |
TIGR03402 |
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related ... |
55-434 |
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: 524.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 55 YMDVQATTPLDPRVLDAMLPYLVNYYGNPhSRTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIKGVA 134
Cdd:TIGR03402 2 YLDNNATTRVDPEVLEAMLPYFTEYFGNP-SSMHSFGGEVGKAVEEAREQVAKLLGAEPDEIIFTSGGTESDNTAIKSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 135 RFYRSrKKHLVTTQTEHKCVLDSCRSLEAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEIG 214
Cdd:TIGR03402 81 AAQPE-KRHIITTAVEHPAVLSLCQHLEKQGYKVTYLPVDEEGRLDLEELRAAITDDTALVSVMWANNETGTIFPIEEIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 215 QICSSRKLYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRrpRVRVEALQSGGGQERGMRSGTVPTP 294
Cdd:TIGR03402 160 EIAKERGALFHTDAVQAVGKIPIDLKEMNIDMLSLSGHKLHGPKGVGALYIRK--GTRFRPLLRGGHQERGRRAGTENVP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 295 LVVGLGAACELAQQEMEYDHKRISKLAERLIQKIMKNLPDVVMNGDPKQHYPGCINLSFAYVEGESLLMAL--KDVALSS 372
Cdd:TIGR03402 238 GIVGLGKAAELATEHLEEENTRVRALRDRLEAGLLARIPDARLNGDPTKRLPNTVNISFEYIEGEAILLLLdmEGICASS 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 58618884 373 GSACTSASLEPSYVLRAIGMDEDLAHSSIRFGIGRFTTEEEVDYTVQKCIHHVKRLREMSPL 434
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 ... |
55-403 |
2.22e-155 |
|
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: 444.24 E-value: 2.22e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 55 YMDVQATTPLDPRVLDAMLPYLVNYYGNPHSRTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIKGVA 134
Cdd:TIGR03235 1 YLDHNATTPIDPAVAEAMLPWLLEEFGNPSSRTHEFGHNAKKAVERARKQVAEALGADTEEVIFTSGATESNNLAILGLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 135 RFY-RSRKKHLVTTQTEHKCVLDSCRSLEAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEI 213
Cdd:TIGR03235 81 RAGeQKGKKHIITSAIEHPAVLEPIRALERNGFTVTYLPVDESGRIDVDELADAIRPDTLLVSIMHVNNETGSIQPIREI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 214 GQICSSRKLYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRR--PRVRVEALQSGGGQERGMRSGTV 291
Cdd:TIGR03235 161 AEVLEAHEAFFHVDAAQVVGKITVDLSADRIDLISCSGHKIYGPKGIGALVIRKRgkPKAPLKPIMFGGGQERGLRPGTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 292 PTPLVVGLGAACELAQQEMEYDHKRISKLAERLIQKImkNLPDVVMNGDPKQHYPGCINLSFAYVEGESLLMALK-DVAL 370
Cdd:TIGR03235 241 PVHLIVGMGEAAEIARRNAQAWEVKLRAMRNQLRDAL--QTLGVKLNGDPAETIPHILNFSIDGVNSEALIVNLRaDAAV 318
|
330 340 350
....*....|....*....|....*....|...
gi 58618884 371 SSGSACTSASLEPSYVLRAIGMDEDLAHSSIRF 403
Cdd:TIGR03235 319 STGSACSSSKYEPSHVLQAMGLDTDRARGAIRF 351
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
55-416 |
3.55e-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: 3.55e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 55 YMDVQATTPLDPRVLDAMLPYLVNYYGNPHSRTHAYGWESEAAMERARQQVASLIGA-DPREIIFTSGATESNNIAIKGV 133
Cdd:pfam00266 2 YLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINApSNDEIIFTSGTTEAINLVALSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 134 ARFYRsRKKHLVTTQTEHKCVLDSCRSL-EAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAE 212
Cdd:pfam00266 82 GRSLK-PGDEIVITEMEHHANLVPWQELaKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 213 IGQICSSRKLYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRRPRVRVEALQSGGG-------QERG 285
Cdd:pfam00266 161 IGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGmietvslQEST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 286 M-------RSGTVPTPLVVGLGAACE-LAQQEMEYDHKRISKLAERLiQKIMKNLPDVVMNGDPKQhyPGCINLSFAYVE 357
Cdd:pfam00266 241 FadapwkfEAGTPNIAGIIGLGAALEyLSEIGLEAIEKHEHELAQYL-YERLLSLPGIRLYGPERR--ASIISFNFKGVH 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58618884 358 GESLLMALKD--VALSSGSACTsaslEPSYVLRAIgmdedlaHSSIRFGIGRFTTEEEVDY 416
Cdd:pfam00266 318 PHDVATLLDEsgIAVRSGHHCA----QPLMVRLGL-------GGTVRASFYIYNTQEDVDR 367
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
54-418 |
5.32e-103 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 311.66 E-value: 5.32e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 54 LYMDVQATTPLDPRVLDAMLPYLVNYYGNPHSrTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIKGV 133
Cdd:PRK02948 2 IYLDYAATTPMSKEALQTYQKAASQYFGNESS-LHDIGGTASSLLQVCRKTFAEMIGGEEQGIYFTSGGTESNYLAIQSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 134 ARFYRSRKKHLVTTQTEHKCVLDSCRSLEAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEI 213
Cdd:PRK02948 81 LNALPQNKKHIITTPMEHASIHSYFQSLESQGYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQPIAEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 214 GQICSSRKLYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIrrRPRVRVEALQSGGGQERGMRSGTVPT 293
Cdd:PRK02948 161 GALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYI--NPQVRWKPVFPGTTHEKGFRPGTVNV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 294 PLVVGLGAACELAQQEMEYDHKRISKLAERLIQKI-MKNLPdVVMNGDPKQHYPGCINLSFAYVEGESLLMAL--KDVAL 370
Cdd:PRK02948 239 PGIAAFLTAAENILKNMQEESLRFKELRSYFLEQIqTLPLP-IEVEGHSTSCLPHIIGVTIKGIEGQYTMLECnrRGIAI 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 58618884 371 SSGSACTSASLEPSYVLRAIGMDEDLAHSSIRFGIGRFTTEEEVDYTV 418
Cdd:PRK02948 318 STGSACQVGKQEPSKTMLAIGKTYEEAKQFVRFSFGQQTTKDQIDTTI 365
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
55-431 |
2.12e-70 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 228.10 E-value: 2.12e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 55 YMDVQATTPLdPR-VLDAMLPYLVNYYGNPHSRTHAYGWESEAAMERARQQVASLIGA-DPREIIFTSGATESNNIAIKG 132
Cdd:COG0520 18 YLDNAATGQK-PRpVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAaSPDEIIFTRGTTEAINLVAYG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 133 VARFyrSRKKHLVTTQTEHKCVLDSCRSLEAE-GFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIA 211
Cdd:COG0520 97 LGRL--KPGDEILITEMEHHSNIVPWQELAERtGAEVRVIPLDEDGELDLEALEALLTPRTKLVAVTHVSNVTGTVNPVK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 212 EIGQICSSRKLYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRRPRVRVEALQSGGG---------- 281
Cdd:COG0520 175 EIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELLEALPPFLGGGGmiewvsfdgt 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 282 --QERGMR--SGTVPTPLVVGLGAACELAQQ-EMEYDHKRISKLAERLIQKiMKNLPDVVMNGDPKQHYPGCInLSFaYV 356
Cdd:COG0520 255 tyADLPRRfeAGTPNIAGAIGLGAAIDYLEAiGMEAIEARERELTAYALEG-LAAIPGVRILGPADPEDRSGI-VSF-NV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 357 EG---ESLLMALKD--VALSSGSACTsaslEPsyVLRAIGMDedlahSSIRFGIGRFTTEEEVDYtvqkCIHHVKRLREM 431
Cdd:COG0520 332 DGvhpHDVAALLDDegIAVRAGHHCA----QP--LMRRLGVP-----GTVRASFHLYNTEEEIDR----LVEALKKLAEL 396
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
55-415 |
1.68e-64 |
|
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: 211.94 E-value: 1.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 55 YMDVQATTPLDPRVLDAMLPYLVNYYGNPHSRTHAYGWESEAAMERARQQVASLIGA-DPREIIFTSGATESNNIAIKGV 133
Cdd:cd06453 2 YLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINApSPDEIIFTRNTTEAINLVAYGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 134 ARfyrSRKK--HLVTTQTEHKCVLDSCRSLEAE-GFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPI 210
Cdd:cd06453 82 GR---ANKPgdEIVTSVMEHHSNIVPWQQLAERtGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 211 AEIGQICSSRKLYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRRPRVRVEALQSGGG--------- 281
Cdd:cd06453 159 KEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEmieevsfee 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 282 ---QERGMR--SGTVPTPLVVGLGAACELAQQE-MEYDHKRISKLAERLIQKiMKNLPDVVMNGDPKQHYPGcinLSFAy 355
Cdd:cd06453 239 ttyADLPHKfeAGTPNIAGAIGLGAAIDYLEKIgMEAIAAHEHELTAYALER-LSEIPGVRVYGDAEDRAGV---VSFN- 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 58618884 356 VEG---ESLLMAL--KDVALSSGSACTsaslEPsyVLRAIGmdedlAHSSIRFGIGRFTTEEEVD 415
Cdd:cd06453 314 LEGihpHDVATILdqYGIAVRAGHHCA----QP--LMRRLG-----VPGTVRASFGLYNTEEEID 367
|
|
| sufS |
TIGR01979 |
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine ... |
55-428 |
8.91e-46 |
|
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: 163.60 E-value: 8.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 55 YMDVQATTpLDPR-VLDAMLPYLVNYYGNPHSRTHAYGWESEAAMERARQQVASLIGA-DPREIIFTSGATESNNIAIKG 132
Cdd:TIGR01979 21 YLDSAATS-QKPQqVIDAVAEYYRNSNANVHRGIHTLSVRATEAYEAVREKVAKFINAaSDEEIVFTRGTTESINLVAYS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 133 VARFYRSRKKHLVTTQTEHKCVLDSCRSL-EAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIA 211
Cdd:TIGR01979 100 WGDSNLKAGDEIVISEMEHHANIVPWQLLaERTGATLKFIPLDDDGTLDLDDLEKLLTEKTKLVAITHVSNVLGTVNPVE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 212 EIGQICSSRKLYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRRPRVRVEALQSGGG---------- 281
Cdd:TIGR01979 180 EIAKLAHQVGAKVLVDGAQAVPHMPVDVQALDCDFYVFSGHKMYGPTGIGVLYGKEELLEQMPPFLGGGEmiaevsfeet 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 282 --QERGMR--SGTVPTPLVVGLGAACE-LAQQEMEYDHKRISKLAERLIQKIMKnLPDVVMNGdPKQHYP--GCINLSFA 354
Cdd:TIGR01979 260 tyNEAPHKfeAGTPNIAGVIGLGAAIDyLEAIGLENIEAHEHELTAYALERLGE-IPGLRIYG-PRDAEDrgGIISFNVE 337
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58618884 355 YVEGESLLMALKD--VALSSGSACTsaslEPsyVLRAIGmdedlAHSSIRFGIGRFTTEEEVDYTVQKcIHHVKRL 428
Cdd:TIGR01979 338 GVHPHDVGTILDEegIAVRSGHHCA----QP--LMRRFG-----VPATCRASFYIYNTEEDIDALVEA-LKKVRKF 401
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
52-419 |
2.59e-32 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 127.17 E-value: 2.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 52 RPL-YMDVQATTPLDPRVLDAMLPYLVNYYGNPHSRTHAYGWESEAAMERARQQVASLIGA-DPREIIFTSGATEsnniA 129
Cdd:PLN02855 31 SKLvYLDNAATSQKPAAVLDALQDYYEEYNSNVHRGIHALSAKATDAYELARKKVAAFINAsTSREIVFTRNATE----A 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 130 IKGVARFY-RSRKK---HLVTTQTEHKCVLDSCRSLEAE-GFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEI 204
Cdd:PLN02855 107 INLVAYTWgLANLKpgdEVILSVAEHHSNIVPWQLVAQKtGAVLKFVGLTPDEVLDVEQLKELLSEKTKLVATHHVSNVL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 205 GVKQPIAEIGQICSSRKLYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYirrrprVRVEALQS-----G 279
Cdd:PLN02855 187 GSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLW------GKSDLLESmppflG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 280 GGQergM-------RSGTVPTPL-----------VVGLGAACE-LAQQEMEYDHKRISKLAERLIQKIMKnLPDVVMNGD 340
Cdd:PLN02855 261 GGE---MisdvfldHSTYAPPPSrfeagtpaigeAIGLGAAIDyLSEIGMDRIHEYEVELGTYLYEKLSS-VPGVRIYGP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 341 PKQHYPGCINLSFAYVEG------ESLLMALKDVALSSGSACTsaslEPSYvlRAIGMDEDlAHSSIRFgigrFTTEEEV 414
Cdd:PLN02855 337 KPSEGVGRAALCAFNVEGihptdlSTFLDQQHGVAIRSGHHCA----QPLH--RYLGVNAS-ARASLYF----YNTKEEV 405
|
....*
gi 58618884 415 DYTVQ 419
Cdd:PLN02855 406 DAFIH 410
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
55-311 |
1.76e-25 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 107.43 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 55 YMDvQATTPLDPR-VLDAMLPYLVNYYGNPHSRTHAYGWESEAAMERARQQVASLIGA-DPREIIFTSGATESNNIAIKG 132
Cdd:PRK10874 22 YLD-SAATALKPQaVIEATQQFYSLSAGNVHRSQFAAAQRLTARYEAAREQVAQLLNApDAKNIVWTRGTTESINLVAQS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 133 VARFYRSRKKHLVTTQTEHKCVLDSCRSL-EAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIA 211
Cdd:PRK10874 101 YARPRLQPGDEIIVSEAEHHANLVPWLMVaQQTGAKVVKLPLGADRLPDVDLLPELITPRTRILALGQMSNVTGGCPDLA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 212 EIGQICSSRKLYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRRPRVRVEALQSGGGQER-----GM 286
Cdd:PRK10874 181 RAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMSPWQGGGKMLTevsfdGF 260
|
250 260 270
....*....|....*....|....*....|....*
gi 58618884 287 RSGTVP------TPL---VVGLGAACE-LAQQEME 311
Cdd:PRK10874 261 TPQSAPwrfeagTPNvagVIGLSAALEwLADIDIN 295
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
53-304 |
1.08e-24 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 105.22 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 53 PL-YMDVQATTPLDPRVLDAMLPYLVNYYGNPHSRTHAYGWESEAAMERARQQVASLIGA-DPREIIFTSGATESNNIAI 130
Cdd:PRK09295 23 PLaYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKQAALFINArSAEELVFVRGTTEGINLVA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 131 KGVARFYRSRKKHLVTTQTEHKCVLDSCRSL-EAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQP 209
Cdd:PRK09295 103 NSWGNSNVRAGDNIIISEMEHHANIVPWQMLcARVGAELRVIPLNPDGTLQLETLPALFDERTRLLAITHVSNVLGTENP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 210 IAEIgqICSSRKL--YFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRrprvrvEALQS-----GGGQ 282
Cdd:PRK09295 183 LAEM--IALAHQHgaKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKE------ALLQEmppweGGGS 254
|
250 260 270
....*....|....*....|....*....|....*...
gi 58618884 283 -------ERGM---------RSGTVPTPLVVGLGAACE 304
Cdd:PRK09295 255 miatvslTEGTtwakapwrfEAGTPNTGGIIGLGAALD 292
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
97-280 |
1.94e-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: 81.82 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 97 AMERARQQVASLIGA-DPREIIFTSGATEsnniAIKGVARFYRsrKKHL------VTTQTEHK---------Cvldscrs 160
Cdd:NF041166 290 AYEGAREKVRRFIGApSVDEIIFVRGTTE----AINLVAKSWG--RQNIgagdeiIVSHLEHHanivpwqqlA------- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 161 lEAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEIGQICssrklyfH-------TDAAQAVG 233
Cdd:NF041166 357 -QETGAKLRVIPVDDSGQILLDEYAKLLNPRTKLVSVTQVSNALGTVTPVKEIIALA-------HragakvlVDGAQSVS 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 58618884 234 KIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRrprvrvEAL------QSGG 280
Cdd:NF041166 429 HMPVDVQALDADFFVFSGHKVFGPTGIGVVYGKR------DLLeamppwQGGG 475
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
95-266 |
2.48e-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: 67.79 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 95 EAAMERARQqvASLIGADprEIIFTSGATESNNIAIKgvarFYRSRKKHLVTTQTEHKCVLDScrSLEAEGFRVTYLPVQ 174
Cdd:cd01494 3 EELEEKLAR--LLQPGND--KAVFVPSGTGANEAALL----ALLGPGDEVIVDANGHGSRYWV--AAELAGAKPVPVPVD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 175 KS--GIIDLKELE-AAIQPDTSLVSVMTVNNEIGVKQPIAEIGQICSSRKLYFHTDAAQAVGKIP---LDVNDMKIDLMS 248
Cdd:cd01494 73 DAgyGGLDVAILEeLKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPapgVLIPEGGADVVT 152
|
170
....*....|....*...
gi 58618884 249 ISGHKLYGPKGVGAIYIR 266
Cdd:cd01494 153 FSLHKNLGGEGGGVVIVK 170
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
96-268 |
3.27e-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: 71.02 E-value: 3.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 96 AAMER-ARQQVASLIGADPREI-IFTSGATESNNIAIKgVARFY----RSRKKHL--------VTTQTEHKCVLDSCRSL 161
Cdd:COG0076 106 TELEReVVRWLADLLGLPEGAGgVFTSGGTEANLLALL-AARDRalarRVRAEGLpgaprpriVVSEEAHSSVDKAARLL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 162 EAEGFRVTYLPVQKSGIIDLKELEAAIQPDTS-------LV-SVMTVNneIGVKQPIAEIGQICSSRKLYFHTDAA---- 229
Cdd:COG0076 185 GLGRDALRKVPVDEDGRMDPDALEAAIDEDRAaglnpiaVVaTAGTTN--TGAIDPLAEIADIAREHGLWLHVDAAyggf 262
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 58618884 230 --------QAVGKIPLdvndmkIDLMSISGHK-LYGPKGVGAIYIRRR 268
Cdd:COG0076 263 alpspelrHLLDGIER------ADSITVDPHKwLYVPYGCGAVLVRDP 304
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
105-341 |
2.98e-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: 64.53 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 105 VASLIGADPREI--IFTSGATESNNIAIKGVARFYRSRKKH----------LVTTQTEHKCVLDSCRSLEAEgfrVTYLP 172
Cdd:cd06450 47 LAKLFGLPSEDAdgVFTSGGSESNLLALLAARDRARKRLKAgggrgidklvIVCSDQAHVSVEKAAAYLDVK---VRLVP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 173 VQKSGIIDLKELEAAIQPD------TSLVSVMTVNNEIGVKQPIAEIGQICSSRKLYFHTDAAQAVGKIPLDVNDMKI-- 244
Cdd:cd06450 124 VDEDGRMDPEALEAAIDEDkaeglnPIMVVATAGTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDfg 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 245 ----DLMSISGHKLYG-PKGVGAIYirrrprVRVEA----LQSGGgqergmrsgtvptplVVGLGAACelaqqemeydhK 315
Cdd:cd06450 204 iervDSISVDPHKYGLvPLGCSAVL------VRALKlwatLRRFG---------------RDGYGEHI-----------D 251
|
250 260
....*....|....*....|....*.
gi 58618884 316 RISKLAERLIQKImKNLPDVVMNGDP 341
Cdd:cd06450 252 RIVDLAKYLAELI-RADPGFELLGEP 276
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
100-324 |
2.19e-10 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 61.46 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 100 RARQQVASLIGADprEIIFTSGATESNNIAIKGVARfyrsRKKHLVTTQTEHKCvLDSCRSL-EAEGFRVTYLPVQKSGI 178
Cdd:pfam01212 36 RLEDRVAELFGKE--AALFVPSGTAANQLALMAHCQ----RGDEVICGEPAHIH-FDETGGHaELGGVQPRPLDGDEAGN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 179 IDLKELEAAI-------QPDTSLVSVmTVNNEIGVKQP-----IAEIGQICSSRKLYFHTDAAQ---AVGKIPLDVNDMK 243
Cdd:pfam01212 109 MDLEDLEAAIrevgadiFPPTGLISL-ENTHNSAGGQVvslenLREIAALAREHGIPVHLDGARfanAAVALGVIVKEIT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 244 --IDLMSISGHK-LYGPkgVGAI------YIRRRPRVRveaLQSGGGqergMRSGTVPTplVVGLGAaCELAQQEMEYDH 314
Cdd:pfam01212 188 syADSVTMCLSKgLGAP--VGSVlagsddFIAKAIRQR---KYLGGG----LRQAGVLA--AAGLRA-LEEGVARLARDH 255
|
250
....*....|
gi 58618884 315 KRISKLAERL 324
Cdd:pfam01212 256 ATARRLAEGL 265
|
|
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
78-267 |
4.75e-08 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 55.64 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 78 NYYGNPHSRTHAYGWESEaAMERARQQVASLIGADPRE--IIFTSGATEsnniAIKGVAR-FYRSRKKHLVTTQTEHKCV 154
Cdd:PLN02724 61 NVYGNPHSQSDSSMRSSD-TIESARQQVLEYFNAPPSDyaCVFTSGATA----ALKLVGEtFPWSSESHFCYTLENHNSV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 155 L---------------------DSCRSLEAEGFRVTYLPVQKSGIIDLkELEAAIQPDTSLVSVMTVNNEIGVKQPIAEI 213
Cdd:PLN02724 136 LgireyalekgaaaiavdieeaANQPTNSQGSVVVKSRGLQRRNTSKL-QKREDDGEAYNLFAFPSECNFSGAKFPLDLV 214
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58618884 214 GQICSSRKLYFHT--------DAAQAVGKIPLDVNDMKIDLMSISGHKLYG-PKGVGAIYIRR 267
Cdd:PLN02724 215 KLIKDNQHSNFSKsgrwmvllDAAKGCGTSPPDLSRYPADFVVVSFYKIFGyPTGLGALLVRR 277
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
66-423 |
5.99e-06 |
|
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: 48.10 E-value: 5.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 66 PRVLDAMlpYLVNYygnphsRTHAYGwESEAAmERARQQVASLIGADprEIIFTSGATESNNIAIKGVARFYRSrkkhLV 145
Cdd:cd06502 12 PEMLEAM--AAANV------GDDVYG-EDPTT-AKLEARAAELFGKE--AALFVPSGTAANQLALAAHTQPGGS----VI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 146 TTQTEHKCvLDSCRSLEAEGfRVTYLPVQ-KSGIIDLKELEAAIQPD-------TSLVSVMTVNNEIGVKQP--IAEIGQ 215
Cdd:cd06502 76 CHETAHIY-TDEAGAPEFLS-GVKLLPVPgENGKLTPEDLEAAIRPRddihfppPSLVSLENTTEGGTVYPLdeLKAISA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 216 ICSSRKLYFHTDAAQ-----AVGKIPLDVNDMKIDLMSISGHK-LYGPkgVGAI------YIRRRPRVRVealQSGGgqe 283
Cdd:cd06502 154 LAKENGLPLHLDGARlanaaAALGVALKTYKSGVDSVSFCLSKgGGAP--VGAVvvgnrdFIARARRRRK---QAGG--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 284 rGMR-SGTVPTPLVVGLGAACELAQqeMEYDHKRISKLAERLiqkimKNLPDVVMNGDPkqhypgciNLSFAYVEGEsll 362
Cdd:cd06502 226 -GMRqSGFLAAAGLAALENDLWLRR--LRHDHEMARRLAEAL-----EELGGLESEVQT--------NIVLLDPVEA--- 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58618884 363 malkDVALSSGSACTSASLEPSYVLRAIGmdedlaHSSIRFGIGRFTTEEEVDYTVQKCIH 423
Cdd:cd06502 287 ----NAVFVELSKEAIERRGEGVLFYAWG------EGGVRFVTHWDTTEEDVDELLSALKA 337
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
161-325 |
6.74e-06 |
|
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.
Pssm-ID: 99744 [Multi-domain] Cd Length: 356 Bit Score: 48.06 E-value: 6.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 161 LEAEGFRVTYLPVQKSGIIDLKELEAAI-QPDTSLVSVMTVNNEIGVKQPIAEIGQICSSRKLYFHTDAAQAVGKIPLDV 239
Cdd:cd06451 93 AERYGADVDVVEKPWGEAVSPEEIAEALeQHDIKAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVDAVSSLGGEPFRM 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 240 NDMKIDLMSISGHK-LYGPKGVGAIYIRRRPRVRVEALQSGGG------------QERGMRSGTVPTPLVVGLGAACELA 306
Cdd:cd06451 173 DEWGVDVAYTGSQKaLGAPPGLGPIAFSERALERIKKKTKPKGfyfdlllllkywGEGYSYPHTPPVNLLYALREALDLI 252
|
170 180
....*....|....*....|
gi 58618884 307 QQE-MEYDHKRISKLAERLI 325
Cdd:cd06451 253 LEEgLENRWARHRRLAKALR 272
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
63-337 |
1.32e-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: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 63 PLDPRVLDAMLpyLVNYYGNPHSRTHAYGweseaaMERARQQVASLIG------ADPREIIFTSGATEsnniAIKGVARF 136
Cdd:cd00609 11 PPPPEVLEALA--AAALRAGLLGYYPDPG------LPELREAIAEWLGrrggvdVPPEEIVVTNGAQE----ALSLLLRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 137 YRSRKKHLVTTQ---TEHKcvldscRSLEAEGFRVTYLPVQKSGII--DLKELEAAIQPDTSLVSVMTVNNEIGV---KQ 208
Cdd:cd00609 79 LLNPGDEVLVPDptyPGYE------AAARLAGAEVVPVPLDEEGGFllDLELLEAAKTPKTKLLYLNNPNNPTGAvlsEE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 209 PIAEIGQICSSRKLY---------FHTDAAQAvgkIPLDVNDMKIDLMSISGH-KLYGPKG--VGAIYIrrRPRVRVEAL 276
Cdd:cd00609 153 ELEELAELAKKHGILiisdeayaeLVYDGEPP---PALALLDAYERVIVLRSFsKTFGLPGlrIGYLIA--PPEELLERL 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58618884 277 QSgggqERGMRSGTVPTPLVVGLGAACELAQQEMEYDHKRISKLAERLIQKIMKNLPDVVM 337
Cdd:cd00609 228 KK----LLPYTTSGPSTLSQAAAAAALDDGEEHLEELRERYRRRRDALLEALKELGPLVVV 284
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
117-278 |
1.74e-03 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 40.48 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 117 IFTSGATESNNIAIKGV-ARFYRSRKKH--------------LVTTQTEHKCVLdscRSLEAEGFRVTYLPVQKSGIIDL 181
Cdd:pfam00282 106 VLQPGSSESNLLALLAArTKWIKRMKAAgkpadssgilaklvAYTSDQAHSSIE---KAALYGGVKLREIPSDDNGKMRG 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 182 KELEAAIQPDTSLVSV-MTVNNEIGVK-----QPIAEIGQICSSRKLYFHTDAAQAVGKI------PLDVNDMKIDLMSI 249
Cdd:pfam00282 183 MDLEKAIEEDKENGLIpFFVVATLGTTgsgafDDLQELGDICAKHNLWLHVDAAYGGSAFicpefrHWLFGIERADSITF 262
|
170 180 190
....*....|....*....|....*....|
gi 58618884 250 SGHKLYG-PKGVGAIYIRRRprvrvEALQS 278
Cdd:pfam00282 263 NPHKWMLvLLDCSAVWVKDK-----EALQQ 287
|
|
| PRK05939 |
PRK05939 |
cystathionine gamma-synthase family protein; |
160-227 |
2.34e-03 |
|
cystathionine gamma-synthase family protein;
Pssm-ID: 235650 [Multi-domain] Cd Length: 397 Bit Score: 40.06 E-value: 2.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58618884 160 SLEAEGFRVTYLPVqksgiIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEIGQICSSRKLYFHTD 227
Cdd:PRK05939 105 TLRGLGVEVTMVDA-----TDVQNVAAAIRPNTRMVFVETIANPGTQVADLAGIGALCRERGLLYVVD 167
|
|
| GDC-P |
cd00613 |
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ... |
133-261 |
6.23e-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: 38.75 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 133 VARFYRSRKKHLV--TTQTEHKCVLDSCrsLEAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPI 210
Cdd:cd00613 101 AIRAYHKRNKVLVpdSAHPTNPAVARTR--GEPLGIEVVEVPSDEGGTVDLEALKEEVSEEVAALMVQYPNTLGVFEDLI 178
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 58618884 211 AEIGQICSSRKLYFHTDAA--QAVGKIPldVNDMKIDLMSISGHKLYGPKGVG 261
Cdd:cd00613 179 KEIADIAHSAGALVYVDGDnlNLTGLKP--PGEYGADIVVGNLQKTGVPHGGG 229
|
|
| PLN02721 |
PLN02721 |
threonine aldolase |
171-326 |
7.07e-03 |
|
threonine aldolase
Pssm-ID: 178323 [Multi-domain] Cd Length: 353 Bit Score: 38.52 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 171 LPVQKSGIIDLKELEAAIQPD-------TSLVSVMTVNNEIGVK----QPIAEIGQICSSRKLYFHTDAAQ------AVG 233
Cdd:PLN02721 110 VKNNEDGTMDLDAIEAAIRPKgddhfptTRLICLENTHANCGGRclsvEYTDKVGELAKRHGLKLHIDGARifnasvALG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58618884 234 kIPLDVNDMKIDLMSISGHK-LYGPKG---VG-AIYIRRRPRVRvEALqsGGgqerGMRSGTVptplvvgLGAACELAQQ 308
Cdd:PLN02721 190 -VPVHRLVKAADSVSVCLSKgLGAPVGsviVGsKSFIRKAKRLR-KTL--GG----GMRQVGV-------LAAAALVALQ 254
|
170 180
....*....|....*....|..
gi 58618884 309 EM----EYDHKRISKLAERLIQ 326
Cdd:PLN02721 255 ENvpklEDDHKKAKLLAEGLNQ 276
|
|
| |
