|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
58-457 |
0e+00 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 737.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 58 PLYMDVQATTPLDPRVLDAMLPYLIN--YYGNPHSRTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAI 135
Cdd:PRK14012 4 PIYLDYSATTPVDPRVAEKMMPYLTMdgTFGNPASRSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDNLAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 136 KGVARFYRSRKKHLITTQTEHKCVLDSCRSLEAEGFQVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPI 215
Cdd:PRK14012 84 KGAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVIQDI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 216 AEIGRICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRRPRVRVEALQSGGGQERGMRSGT 295
Cdd:PRK14012 164 AAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRLEAQMHGGGHERGMRSGT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 296 VPTPLVVGLGAACEVAQQEMEYDHKRISKLSERLIQNImKSLPDVVMNGDPKHHYPGCINLSFAYVEGESLLMALKDVAL 375
Cdd:PRK14012 244 LPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGI-KDIEEVYLNGDLEQRVPGNLNVSFNYVEGESLIMALKDLAV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 376 SSGSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVDYTVEKCIQHVKRLREMSPLWEMVQDGIDLKSIKWT 455
Cdd:PRK14012 323 SSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGKLRELSPLWEMFKEGVDLNSIEWA 402
|
..
gi 32307132 456 QH 457
Cdd:PRK14012 403 HH 404
|
|
| IscS |
TIGR02006 |
cysteine desulfurase IscS; This model represents IscS, one of several cysteine desulfurases ... |
58-457 |
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: 670.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 58 PLYMDVQATTPLDPRVLDAMLPYLINYYGNPHSRTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIKG 137
Cdd:TIGR02006 4 PIYLDYAATTPVDPRVAEKMMPYLTEKFGNPASRSHSFGWEAEEAVENARNQVAELIGADSREIVFTSGATESNNLAIKG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 138 VARFYRSRKKHLITTQTEHKCVLDSCRSLEAEGFQVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAE 217
Cdd:TIGR02006 84 IAHFYKSKGNHIITSKTEHKAVLDTCRYLEREGFEVTYLPPKSNGLIDLEELKAAIRDDTILVSIMHVNNEIGVIQDIAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 218 IGRICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRRPRVRVEALQSGGGQERGMRSGTVP 297
Cdd:TIGR02006 164 IGEICRERKVFFHVDAAQSVGKIPINVNELKVDLMSISGHKIYGPKGIGALYVRRKPRVRLEALIHGGGHERGMRSGTLP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 298 TPLVVGLGAACEVAQQEMEYDHKRISKLSERLIQNImKSLPDVVMNGDPKHHYPGCINLSFAYVEGESLLMALKDVALSS 377
Cdd:TIGR02006 244 THQIVGMGEAFRIAKEEMAQDTAHVLALRDRLLNGI-KSIEEVYLNGDLEHRVPGNLNVSFNYVEGESLIMALKDLAVSS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 378 GSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVDYTVEKCIQHVKRLREMSPLWEMVQDGIDLKSIKWTQH 457
Cdd:TIGR02006 323 GSACTSASLEPSYVLRALGINDELAHSSIRFTIGRFTTEEEIDYAVKLVKSAIDKLRELSPLWEMFKEGVDLNSIEWAAH 402
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
57-437 |
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: 636.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 57 RPLYMDVQATTPLDPRVLDAMLPYLINYYGNPHSrTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIK 136
Cdd:COG1104 2 MMIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSS-LHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNLAIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 137 GVARFYRSRKKHLITTQTEHKCVLDSCRSLEAEGFQVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIA 216
Cdd:COG1104 81 GAARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 217 EIGRICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRrpRVRVEALQSGGGQERGMRSGTV 296
Cdd:COG1104 161 EIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRK--GVRLEPLIHGGGQERGLRSGTE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 297 PTPLVVGLGAACEVAQQEMEYDHKRISKLSERLIQNIMKSLPDVVMNGDPKHHYPGCINLSFAYVEGESLLMAL--KDVA 374
Cdd:COG1104 239 NVPGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAAIPGVVINGDPENRLPNTLNFSFPGVEGEALLLALdlAGIA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32307132 375 LSSGSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVDYTVEKCIQHVKRLREMS 437
Cdd:COG1104 319 VSSGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARLRKLS 381
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
60-421 |
3.11e-110 |
|
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: 329.98 E-value: 3.11e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 60 YMDVQATTPLDPRVLDAMLPYLINYYGNPHSRTHAYGWESEAAMERARQQVASLIGA-DPREIIFTSGATESNNIAIKGV 138
Cdd:pfam00266 2 YLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINApSNDEIIFTSGTTEAINLVALSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 139 ARFYRsRKKHLITTQTEHKCVLDSCRSL-EAEGFQVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAE 217
Cdd:pfam00266 82 GRSLK-PGDEIVITEMEHHANLVPWQELaKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 218 IGRICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRRPRVRVEALQSGGG-------QERG 290
Cdd:pfam00266 161 IGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGmietvslQEST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 291 M-------RSGTVPTPLVVGLGAACE-VAQQEMEYDHKRISKLSERLIQnIMKSLPDVVMNGDPKHhyPGCINLSFAYVE 362
Cdd:pfam00266 241 FadapwkfEAGTPNIAGIIGLGAALEyLSEIGLEAIEKHEHELAQYLYE-RLLSLPGIRLYGPERR--ASIISFNFKGVH 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32307132 363 GESLLMALKD--VALSSGSACTsaslEPSYVLRAIgtdedlaHSSIRFGIGRFTTEEEVDY 421
Cdd:pfam00266 318 PHDVATLLDEsgIAVRSGHHCA----QPLMVRLGL-------GGTVRASFYIYNTQEDVDR 367
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
60-420 |
2.95e-65 |
|
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: 214.25 E-value: 2.95e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 60 YMDVQATTPLDPRVLDAMLPYLINYYGNPHSRTHAYGWESEAAMERARQQVASLIGA-DPREIIFTSGATESNNIAIKGV 138
Cdd:cd06453 2 YLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINApSPDEIIFTRNTTEAINLVAYGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 139 ARfyrSRKK--HLITTQTEHKCVLDSCRSLEAE-GFQVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPI 215
Cdd:cd06453 82 GR---ANKPgdEIVTSVMEHHSNIVPWQQLAERtGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 216 AEIGRICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRRPRVRVEALQSGGG--------- 286
Cdd:cd06453 159 KEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEmieevsfee 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 287 ---QERGMR--SGTVPTPLVVGLGAACEVAQQE-MEYDHKRISKLSERLIQNiMKSLPDVVMNGDPKHHYPGcinLSFAy 360
Cdd:cd06453 239 ttyADLPHKfeAGTPNIAGAIGLGAAIDYLEKIgMEAIAAHEHELTAYALER-LSEIPGVRVYGDAEDRAGV---VSFN- 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32307132 361 VEG---ESLLMAL--KDVALSSGSACTsaslEPsyVLRAIGtdedlAHSSIRFGIGRFTTEEEVD 420
Cdd:cd06453 314 LEGihpHDVATILdqYGIAVRAGHHCA----QP--LMRRLG-----VPGTVRASFGLYNTEEEID 367
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
102-285 |
3.86e-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: 80.67 E-value: 3.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 102 AMERARQQVASLIGA-DPREIIFTSGATEsnniAIKGVARFYRsrKKHL------ITTQTEHK---------Cvldscrs 165
Cdd:NF041166 290 AYEGAREKVRRFIGApSVDEIIFVRGTTE----AINLVAKSWG--RQNIgagdeiIVSHLEHHanivpwqqlA------- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 166 lEAEGFQVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEIGRICssrkvyfH-------TDAAQAVG 238
Cdd:NF041166 357 -QETGAKLRVIPVDDSGQILLDEYAKLLNPRTKLVSVTQVSNALGTVTPVKEIIALA-------HragakvlVDGAQSVS 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 32307132 239 KIPLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRrprvrvEAL------QSGG 285
Cdd:NF041166 429 HMPVDVQALDADFFVFSGHKVFGPTGIGVVYGKR------DLLeamppwQGGG 475
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
58-457 |
0e+00 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 737.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 58 PLYMDVQATTPLDPRVLDAMLPYLIN--YYGNPHSRTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAI 135
Cdd:PRK14012 4 PIYLDYSATTPVDPRVAEKMMPYLTMdgTFGNPASRSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDNLAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 136 KGVARFYRSRKKHLITTQTEHKCVLDSCRSLEAEGFQVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPI 215
Cdd:PRK14012 84 KGAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVIQDI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 216 AEIGRICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRRPRVRVEALQSGGGQERGMRSGT 295
Cdd:PRK14012 164 AAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRLEAQMHGGGHERGMRSGT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 296 VPTPLVVGLGAACEVAQQEMEYDHKRISKLSERLIQNImKSLPDVVMNGDPKHHYPGCINLSFAYVEGESLLMALKDVAL 375
Cdd:PRK14012 244 LPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGI-KDIEEVYLNGDLEQRVPGNLNVSFNYVEGESLIMALKDLAV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 376 SSGSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVDYTVEKCIQHVKRLREMSPLWEMVQDGIDLKSIKWT 455
Cdd:PRK14012 323 SSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGKLRELSPLWEMFKEGVDLNSIEWA 402
|
..
gi 32307132 456 QH 457
Cdd:PRK14012 403 HH 404
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
59-420 |
0e+00 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 682.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 59 LYMDVQATTPLDPRVLDAMLPYLINYYGNPHSRTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIKGV 138
Cdd:PLN02651 1 LYLDMQATTPIDPRVLDAMLPFLIEHFGNPHSRTHLYGWESEDAVEKARAQVAALIGADPKEIIFTSGATESNNLAIKGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 139 ARFYRSRKKHLITTQTEHKCVLDSCRSLEAEGFQVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEI 218
Cdd:PLN02651 81 MHFYKDKKKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVEEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 219 GRICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRRPRVRVEALQSGGGQERGMRSGTVPT 298
Cdd:PLN02651 161 GELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRLEPLMSGGGQERGRRSGTENT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 299 PLVVGLGAACEVAQQEMEYDHKRISKLSERLIQNIMKSLPDVVMNG--DPKHHYPGCINLSFAYVEGESLLMALKDVALS 376
Cdd:PLN02651 241 PLVVGLGAACELAMKEMDYDEKHMKALRERLLNGLRAKLGGVRVNGprDPEKRYPGTLNLSFAYVEGESLLMGLKEVAVS 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 32307132 377 SGSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVD 420
Cdd:PLN02651 321 SGSACTSASLEPSYVLRALGVPEEMAHGSLRLGVGRFTTEEEVD 364
|
|
| IscS |
TIGR02006 |
cysteine desulfurase IscS; This model represents IscS, one of several cysteine desulfurases ... |
58-457 |
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: 670.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 58 PLYMDVQATTPLDPRVLDAMLPYLINYYGNPHSRTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIKG 137
Cdd:TIGR02006 4 PIYLDYAATTPVDPRVAEKMMPYLTEKFGNPASRSHSFGWEAEEAVENARNQVAELIGADSREIVFTSGATESNNLAIKG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 138 VARFYRSRKKHLITTQTEHKCVLDSCRSLEAEGFQVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAE 217
Cdd:TIGR02006 84 IAHFYKSKGNHIITSKTEHKAVLDTCRYLEREGFEVTYLPPKSNGLIDLEELKAAIRDDTILVSIMHVNNEIGVIQDIAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 218 IGRICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRRPRVRVEALQSGGGQERGMRSGTVP 297
Cdd:TIGR02006 164 IGEICRERKVFFHVDAAQSVGKIPINVNELKVDLMSISGHKIYGPKGIGALYVRRKPRVRLEALIHGGGHERGMRSGTLP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 298 TPLVVGLGAACEVAQQEMEYDHKRISKLSERLIQNImKSLPDVVMNGDPKHHYPGCINLSFAYVEGESLLMALKDVALSS 377
Cdd:TIGR02006 244 THQIVGMGEAFRIAKEEMAQDTAHVLALRDRLLNGI-KSIEEVYLNGDLEHRVPGNLNVSFNYVEGESLIMALKDLAVSS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 378 GSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVDYTVEKCIQHVKRLREMSPLWEMVQDGIDLKSIKWTQH 457
Cdd:TIGR02006 323 GSACTSASLEPSYVLRALGINDELAHSSIRFTIGRFTTEEEIDYAVKLVKSAIDKLRELSPLWEMFKEGVDLNSIEWAAH 402
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
57-437 |
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: 636.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 57 RPLYMDVQATTPLDPRVLDAMLPYLINYYGNPHSrTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIK 136
Cdd:COG1104 2 MMIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSS-LHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNLAIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 137 GVARFYRSRKKHLITTQTEHKCVLDSCRSLEAEGFQVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIA 216
Cdd:COG1104 81 GAARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 217 EIGRICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRrpRVRVEALQSGGGQERGMRSGTV 296
Cdd:COG1104 161 EIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRK--GVRLEPLIHGGGQERGLRSGTE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 297 PTPLVVGLGAACEVAQQEMEYDHKRISKLSERLIQNIMKSLPDVVMNGDPKHHYPGCINLSFAYVEGESLLMAL--KDVA 374
Cdd:COG1104 239 NVPGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAAIPGVVINGDPENRLPNTLNFSFPGVEGEALLLALdlAGIA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32307132 375 LSSGSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVDYTVEKCIQHVKRLREMS 437
Cdd:COG1104 319 VSSGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARLRKLS 381
|
|
| FeS_nifS |
TIGR03402 |
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related ... |
60-439 |
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: 527.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 60 YMDVQATTPLDPRVLDAMLPYLINYYGNPhSRTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIKGVA 139
Cdd:TIGR03402 2 YLDNNATTRVDPEVLEAMLPYFTEYFGNP-SSMHSFGGEVGKAVEEAREQVAKLLGAEPDEIIFTSGGTESDNTAIKSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 140 RFYRSrKKHLITTQTEHKCVLDSCRSLEAEGFQVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEIG 219
Cdd:TIGR03402 81 AAQPE-KRHIITTAVEHPAVLSLCQHLEKQGYKVTYLPVDEEGRLDLEELRAAITDDTALVSVMWANNETGTIFPIEEIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 220 RICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRrpRVRVEALQSGGGQERGMRSGTVPTP 299
Cdd:TIGR03402 160 EIAKERGALFHTDAVQAVGKIPIDLKEMNIDMLSLSGHKLHGPKGVGALYIRK--GTRFRPLLRGGHQERGRRAGTENVP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 300 LVVGLGAACEVAQQEMEYDHKRISKLSERLIQNIMKSLPDVVMNGDPKHHYPGCINLSFAYVEGESLLMAL--KDVALSS 377
Cdd:TIGR03402 238 GIVGLGKAAELATEHLEEENTRVRALRDRLEAGLLARIPDARLNGDPTKRLPNTVNISFEYIEGEAILLLLdmEGICASS 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32307132 378 GSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVDYTVEKCIQHVKRLREMSPL 439
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 ... |
60-408 |
2.16e-156 |
|
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: 446.94 E-value: 2.16e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 60 YMDVQATTPLDPRVLDAMLPYLINYYGNPHSRTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIKGVA 139
Cdd:TIGR03235 1 YLDHNATTPIDPAVAEAMLPWLLEEFGNPSSRTHEFGHNAKKAVERARKQVAEALGADTEEVIFTSGATESNNLAILGLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 140 RFY-RSRKKHLITTQTEHKCVLDSCRSLEAEGFQVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEI 218
Cdd:TIGR03235 81 RAGeQKGKKHIITSAIEHPAVLEPIRALERNGFTVTYLPVDESGRIDVDELADAIRPDTLLVSIMHVNNETGSIQPIREI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 219 GRICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRR--PRVRVEALQSGGGQERGMRSGTV 296
Cdd:TIGR03235 161 AEVLEAHEAFFHVDAAQVVGKITVDLSADRIDLISCSGHKIYGPKGIGALVIRKRgkPKAPLKPIMFGGGQERGLRPGTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 297 PTPLVVGLGAACEVAQQEMEYDHKRISKLSERLIQNIMKslPDVVMNGDPKHHYPGCINLSFAYVEGESLLMALK-DVAL 375
Cdd:TIGR03235 241 PVHLIVGMGEAAEIARRNAQAWEVKLRAMRNQLRDALQT--LGVKLNGDPAETIPHILNFSIDGVNSEALIVNLRaDAAV 318
|
330 340 350
....*....|....*....|....*....|...
gi 32307132 376 SSGSACTSASLEPSYVLRAIGTDEDLAHSSIRF 408
Cdd:TIGR03235 319 STGSACSSSKYEPSHVLQAMGLDTDRARGAIRF 351
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
60-421 |
3.11e-110 |
|
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: 329.98 E-value: 3.11e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 60 YMDVQATTPLDPRVLDAMLPYLINYYGNPHSRTHAYGWESEAAMERARQQVASLIGA-DPREIIFTSGATESNNIAIKGV 138
Cdd:pfam00266 2 YLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINApSNDEIIFTSGTTEAINLVALSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 139 ARFYRsRKKHLITTQTEHKCVLDSCRSL-EAEGFQVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAE 217
Cdd:pfam00266 82 GRSLK-PGDEIVITEMEHHANLVPWQELaKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 218 IGRICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRRPRVRVEALQSGGG-------QERG 290
Cdd:pfam00266 161 IGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGmietvslQEST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 291 M-------RSGTVPTPLVVGLGAACE-VAQQEMEYDHKRISKLSERLIQnIMKSLPDVVMNGDPKHhyPGCINLSFAYVE 362
Cdd:pfam00266 241 FadapwkfEAGTPNIAGIIGLGAALEyLSEIGLEAIEKHEHELAQYLYE-RLLSLPGIRLYGPERR--ASIISFNFKGVH 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32307132 363 GESLLMALKD--VALSSGSACTsaslEPSYVLRAIgtdedlaHSSIRFGIGRFTTEEEVDY 421
Cdd:pfam00266 318 PHDVATLLDEsgIAVRSGHHCA----QPLMVRLGL-------GGTVRASFYIYNTQEDVDR 367
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
59-423 |
9.94e-107 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 321.68 E-value: 9.94e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 59 LYMDVQATTPLDPRVLDAMLPYLINYYGNPHSrTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIKGV 138
Cdd:PRK02948 2 IYLDYAATTPMSKEALQTYQKAASQYFGNESS-LHDIGGTASSLLQVCRKTFAEMIGGEEQGIYFTSGGTESNYLAIQSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 139 ARFYRSRKKHLITTQTEHKCVLDSCRSLEAEGFQVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEI 218
Cdd:PRK02948 81 LNALPQNKKHIITTPMEHASIHSYFQSLESQGYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQPIAEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 219 GRICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKIYGPKGVGAIYIrrRPRVRVEALQSGGGQERGMRSGTVPT 298
Cdd:PRK02948 161 GALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYI--NPQVRWKPVFPGTTHEKGFRPGTVNV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 299 PLVVGLGAACEVAQQEMEYDHKRISKLSERLIQNI-MKSLPdVVMNGDPKHHYPGCINLSFAYVEGESLLMAL--KDVAL 375
Cdd:PRK02948 239 PGIAAFLTAAENILKNMQEESLRFKELRSYFLEQIqTLPLP-IEVEGHSTSCLPHIIGVTIKGIEGQYTMLECnrRGIAI 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 32307132 376 SSGSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVDYTV 423
Cdd:PRK02948 318 STGSACQVGKQEPSKTMLAIGKTYEEAKQFVRFSFGQQTTKDQIDTTI 365
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
54-436 |
9.53e-71 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 229.26 E-value: 9.53e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 54 PVL-RPL-YMDVQATTPLdPR-VLDAMLPYLINYYGNPHSRTHAYGWESEAAMERARQQVASLIGA-DPREIIFTSGATE 129
Cdd:COG0520 10 PVLgKPLvYLDNAATGQK-PRpVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAaSPDEIIFTRGTTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 130 SNNIAIKGVARFyrSRKKHLITTQTEHKCVLDSCRSLEAE-GFQVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNE 208
Cdd:COG0520 89 AINLVAYGLGRL--KPGDEILITEMEHHSNIVPWQELAERtGAEVRVIPLDEDGELDLEALEALLTPRTKLVAVTHVSNV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 209 IGVKQPIAEIGRICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRRPRVRVEALQSGGG-- 286
Cdd:COG0520 167 TGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELLEALPPFLGGGGmi 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 287 ----------QERGMR--SGTVPTPLVVGLGAACEVAQQ-EMEYDHKRISKLSERLIQNiMKSLPDVVMNGDPKHHYPGC 353
Cdd:COG0520 247 ewvsfdgttyADLPRRfeAGTPNIAGAIGLGAAIDYLEAiGMEAIEARERELTAYALEG-LAAIPGVRILGPADPEDRSG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 354 InLSFaYVEG---ESLLMALKD--VALSSGSACTsaslEPsyVLRAIGTDedlahSSIRFGIGRFTTEEEVDYTVEkciq 428
Cdd:COG0520 326 I-VSF-NVDGvhpHDVAALLDDegIAVRAGHHCA----QP--LMRRLGVP-----GTVRASFHLYNTEEEIDRLVE---- 388
|
....*...
gi 32307132 429 HVKRLREM 436
Cdd:COG0520 389 ALKKLAEL 396
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
60-420 |
2.95e-65 |
|
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: 214.25 E-value: 2.95e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 60 YMDVQATTPLDPRVLDAMLPYLINYYGNPHSRTHAYGWESEAAMERARQQVASLIGA-DPREIIFTSGATESNNIAIKGV 138
Cdd:cd06453 2 YLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINApSPDEIIFTRNTTEAINLVAYGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 139 ARfyrSRKK--HLITTQTEHKCVLDSCRSLEAE-GFQVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPI 215
Cdd:cd06453 82 GR---ANKPgdEIVTSVMEHHSNIVPWQQLAERtGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 216 AEIGRICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRRPRVRVEALQSGGG--------- 286
Cdd:cd06453 159 KEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEmieevsfee 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 287 ---QERGMR--SGTVPTPLVVGLGAACEVAQQE-MEYDHKRISKLSERLIQNiMKSLPDVVMNGDPKHHYPGcinLSFAy 360
Cdd:cd06453 239 ttyADLPHKfeAGTPNIAGAIGLGAAIDYLEKIgMEAIAAHEHELTAYALER-LSEIPGVRVYGDAEDRAGV---VSFN- 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32307132 361 VEG---ESLLMAL--KDVALSSGSACTsaslEPsyVLRAIGtdedlAHSSIRFGIGRFTTEEEVD 420
Cdd:cd06453 314 LEGihpHDVATILdqYGIAVRAGHHCA----QP--LMRRLG-----VPGTVRASFGLYNTEEEID 367
|
|
| sufS |
TIGR01979 |
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine ... |
60-433 |
7.61e-44 |
|
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: 158.59 E-value: 7.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 60 YMDVQATTpLDPR-VLDAMLPYLINYYGNPHSRTHAYGWESEAAMERARQQVASLIGA-DPREIIFTSGATESNNIAIKG 137
Cdd:TIGR01979 21 YLDSAATS-QKPQqVIDAVAEYYRNSNANVHRGIHTLSVRATEAYEAVREKVAKFINAaSDEEIVFTRGTTESINLVAYS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 138 VARFYRSRKKHLITTQTEHKCVLDSCRSL-EAEGFQVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIA 216
Cdd:TIGR01979 100 WGDSNLKAGDEIVISEMEHHANIVPWQLLaERTGATLKFIPLDDDGTLDLDDLEKLLTEKTKLVAITHVSNVLGTVNPVE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 217 EIGRICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRRPRVRVEALQSGGG---------- 286
Cdd:TIGR01979 180 EIAKLAHQVGAKVLVDGAQAVPHMPVDVQALDCDFYVFSGHKMYGPTGIGVLYGKEELLEQMPPFLGGGEmiaevsfeet 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 287 --QERGMR--SGTVPTPLVVGLGAACE-VAQQEMEYDHKRISKLSERLIQNIMKsLPDVVMNG-DPKHHYPGCINLSFAY 360
Cdd:TIGR01979 260 tyNEAPHKfeAGTPNIAGVIGLGAAIDyLEAIGLENIEAHEHELTAYALERLGE-IPGLRIYGpRDAEDRGGIISFNVEG 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32307132 361 VEGESLLMALKD--VALSSGSACTsaslEPsyVLRAIGtdedlAHSSIRFGIGRFTTEEEVDYTVEKcIQHVKRL 433
Cdd:TIGR01979 339 VHPHDVGTILDEegIAVRSGHHCA----QP--LMRRFG-----VPATCRASFYIYNTEEDIDALVEA-LKKVRKF 401
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
40-424 |
2.86e-33 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 129.87 E-value: 2.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 40 SAVPADTAAAPEVGPVLRP--------------LYMDVQATTPLDPRVLDAMLPYLINYYGNPHSRTHAYGWESEAAMER 105
Cdd:PLN02855 1 SSAPAASAASVSLGAETRPdfpildqtvngsklVYLDNAATSQKPAAVLDALQDYYEEYNSNVHRGIHALSAKATDAYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 106 ARQQVASLIGA-DPREIIFTSGATEsnniAIKGVARFY-RSRKK---HLITTQTEHKCVLDSCRSLEAE-GFQVTYLPVQ 179
Cdd:PLN02855 81 ARKKVAAFINAsTSREIVFTRNATE----AINLVAYTWgLANLKpgdEVILSVAEHHSNIVPWQLVAQKtGAVLKFVGLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 180 KSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEIGRICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKI 259
Cdd:PLN02855 157 PDEVLDVEQLKELLSEKTKLVATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 260 YGPKGVGAIYirrrprVRVEALQS-----GGGQergM-------RSGTVPTPL-----------VVGLGAACEVAQQ-EM 315
Cdd:PLN02855 237 CGPTGIGFLW------GKSDLLESmppflGGGE---MisdvfldHSTYAPPPSrfeagtpaigeAIGLGAAIDYLSEiGM 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 316 EYDHKRISKLSERLIQNiMKSLPDVVMNGDPKHHYPGCINLSFAYVEG------ESLLMALKDVALSSGSACTsaslEPS 389
Cdd:PLN02855 308 DRIHEYEVELGTYLYEK-LSSVPGVRIYGPKPSEGVGRAALCAFNVEGihptdlSTFLDQQHGVAIRSGHHCA----QPL 382
|
410 420 430
....*....|....*....|....*....|....*
gi 32307132 390 YvlRAIGTDEDlAHSSIRFgigrFTTEEEVDYTVE 424
Cdd:PLN02855 383 H--RYLGVNAS-ARASLYF----YNTKEEVDAFIH 410
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
54-309 |
3.53e-25 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 106.76 E-value: 3.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 54 PVL------RPL-YMDVQATTPLDPRVLDAMLPYLINYYGNPHSRTHAYGWESEAAMERARQQVASLIGA-DPREIIFTS 125
Cdd:PRK09295 13 PVLsrevngLPLaYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKQAALFINArSAEELVFVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 126 GATESNNIAIKGVARFYRSRKKHLITTQTEHKCVLDSCRSL-EAEGFQVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMT 204
Cdd:PRK09295 93 GTTEGINLVANSWGNSNVRAGDNIIISEMEHHANIVPWQMLcARVGAELRVIPLNPDGTLQLETLPALFDERTRLLAITH 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 205 VNNEIGVKQPIAEIgrICSSRK--VYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRrprvrvEALQ 282
Cdd:PRK09295 173 VSNVLGTENPLAEM--IALAHQhgAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKE------ALLQ 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 32307132 283 S-----GGGQ-------ERGM---------RSGTVPTPLVVGLGAACE 309
Cdd:PRK09295 245 EmppweGGGSmiatvslTEGTtwakapwrfEAGTPNTGGIIGLGAALD 292
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
60-316 |
2.02e-24 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 104.35 E-value: 2.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 60 YMDvQATTPLDPR-VLDAMLPYLINYYGNPHSRTHAYGWESEAAMERARQQVASLIGA-DPREIIFTSGATESNNIAIKG 137
Cdd:PRK10874 22 YLD-SAATALKPQaVIEATQQFYSLSAGNVHRSQFAAAQRLTARYEAAREQVAQLLNApDAKNIVWTRGTTESINLVAQS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 138 VARFYRSRKKHLITTQTEHKCVLDSCRSL-EAEGFQVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIA 216
Cdd:PRK10874 101 YARPRLQPGDEIIVSEAEHHANLVPWLMVaQQTGAKVVKLPLGADRLPDVDLLPELITPRTRILALGQMSNVTGGCPDLA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 217 EIGRICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRRPRVRVEALQSGGGQER-----GM 291
Cdd:PRK10874 181 RAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMSPWQGGGKMLTevsfdGF 260
|
250 260 270
....*....|....*....|....*....|....*
gi 32307132 292 RSGTVP------TPL---VVGLGAACE-VAQQEME 316
Cdd:PRK10874 261 TPQSAPwrfeagTPNvagVIGLSAALEwLADIDIN 295
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
102-285 |
3.86e-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: 80.67 E-value: 3.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 102 AMERARQQVASLIGA-DPREIIFTSGATEsnniAIKGVARFYRsrKKHL------ITTQTEHK---------Cvldscrs 165
Cdd:NF041166 290 AYEGAREKVRRFIGApSVDEIIFVRGTTE----AINLVAKSWG--RQNIgagdeiIVSHLEHHanivpwqqlA------- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 166 lEAEGFQVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEIGRICssrkvyfH-------TDAAQAVG 238
Cdd:NF041166 357 -QETGAKLRVIPVDDSGQILLDEYAKLLNPRTKLVSVTQVSNALGTVTPVKEIIALA-------HragakvlVDGAQSVS 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 32307132 239 KIPLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRrprvrvEAL------QSGG 285
Cdd:NF041166 429 HMPVDVQALDADFFVFSGHKVFGPTGIGVVYGKR------DLLeamppwQGGG 475
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
100-271 |
5.76e-14 |
|
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: 69.72 E-value: 5.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 100 EAAMERARQqvASLIGADprEIIFTSGATESNNIAIKgvarFYRSRKKHLITTQTEHKCVLDScrSLEAEGFQVTYLPVQ 179
Cdd:cd01494 3 EELEEKLAR--LLQPGND--KAVFVPSGTGANEAALL----ALLGPGDEVIVDANGHGSRYWV--AAELAGAKPVPVPVD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 180 KS--GIIDLKELE-AAIQPDTSLVSVMTVNNEIGVKQPIAEIGRICSSRKVYFHTDAAQAVGKIP---LDVNDMKIDLMS 253
Cdd:cd01494 73 DAgyGGLDVAILEeLKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPapgVLIPEGGADVVT 152
|
170
....*....|....*...
gi 32307132 254 ISGHKIYGPKGVGAIYIR 271
Cdd:cd01494 153 FSLHKNLGGEGGGVVIVK 170
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
101-273 |
5.16e-12 |
|
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: 67.55 E-value: 5.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 101 AAMER-ARQQVASLIGADPREI-IFTSGATESNNIAIKgVARFY----RSRKKHL--------ITTQTEHKCVLDSCRSL 166
Cdd:COG0076 106 TELEReVVRWLADLLGLPEGAGgVFTSGGTEANLLALL-AARDRalarRVRAEGLpgaprpriVVSEEAHSSVDKAARLL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 167 EAEGFQVTYLPVQKSGIIDLKELEAAIQPDTS-------LV-SVMTVNneIGVKQPIAEIGRICSSRKVYFHTDAA---- 234
Cdd:COG0076 185 GLGRDALRKVPVDEDGRMDPDALEAAIDEDRAaglnpiaVVaTAGTTN--TGAIDPLAEIADIAREHGLWLHVDAAyggf 262
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 32307132 235 --------QAVGKIPLdvndmkIDLMSISGHKiYG--PKGVGAIYIRRR 273
Cdd:COG0076 263 alpspelrHLLDGIER------ADSITVDPHK-WLyvPYGCGAVLVRDP 304
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
66-271 |
1.72e-10 |
|
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: 62.22 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 66 TTPLDPRVLDAMLPYLINYYGNPHSRTHAYgweseAAMErarQQV----ASLIGADPREI--IFTSGATESNNIAIKGVA 139
Cdd:cd06450 7 TTMDPPALLLEMLTSAKNAIDFTWDESPAA-----TEME---AEVvnwlAKLFGLPSEDAdgVFTSGGSESNLLALLAAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 140 RFYRSRKKH----------LITTQTEHKCVLDSCRSLEAEgfqVTYLPVQKSGIIDLKELEAAIQPD------TSLVSVM 203
Cdd:cd06450 79 DRARKRLKAgggrgidklvIVCSDQAHVSVEKAAAYLDVK---VRLVPVDEDGRMDPEALEAAIDEDkaeglnPIMVVAT 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32307132 204 TVNNEIGVKQPIAEIGRICSSRKVYFHTDAAQAVGKIPLDVNDMKI------DLMSISGHKiYG--PKGVGAIYIR 271
Cdd:cd06450 156 AGTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDfgiervDSISVDPHK-YGlvPLGCSAVLVR 230
|
|
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
38-272 |
2.62e-10 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 62.58 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 38 PQSAVPADTAAAPEVGPVLRPLYMDVQATTPLDPRVLDAMLP-YLINYYGNPHSRTHAYGWESEaAMERARQQVASLIGA 116
Cdd:PLN02724 15 PDGPKPIDELRATEFARLKGVVYLDHAGATLYSESQLEAALAdFSSNVYGNPHSQSDSSMRSSD-TIESARQQVLEYFNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 117 DPRE--IIFTSGATEsnniAIKGVAR-FYRSRKKHLITTQTEHKCVL---------------------DSCRSLEAEGFQ 172
Cdd:PLN02724 94 PPSDyaCVFTSGATA----ALKLVGEtFPWSSESHFCYTLENHNSVLgireyalekgaaaiavdieeaANQPTNSQGSVV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 173 VTYLPVQKSGIIDLkELEAAIQPDTSLVSVMTVNNEIGVKQPIAEIGRICSSRKVYFHT--------DAAQAVGKIPLDV 244
Cdd:PLN02724 170 VKSRGLQRRNTSKL-QKREDDGEAYNLFAFPSECNFSGAKFPLDLVKLIKDNQHSNFSKsgrwmvllDAAKGCGTSPPDL 248
|
250 260
....*....|....*....|....*....
gi 32307132 245 NDMKIDLMSISGHKIYG-PKGVGAIYIRR 272
Cdd:PLN02724 249 SRYPADFVVVSFYKIFGyPTGLGALLVRR 277
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
71-426 |
3.02e-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: 48.87 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 71 PRVLDAMlpYLINYygnphsRTHAYGwESEAAmERARQQVASLIGADprEIIFTSGATESNNIAIKGVARFYRSrkkhLI 150
Cdd:cd06502 12 PEMLEAM--AAANV------GDDVYG-EDPTT-AKLEARAAELFGKE--AALFVPSGTAANQLALAAHTQPGGS----VI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 151 TTQTEHKCvLDSCRSLEAEGfQVTYLPVQ-KSGIIDLKELEAAIQPD-------TSLVSVMTVNNEIGVKQP--IAEIGR 220
Cdd:cd06502 76 CHETAHIY-TDEAGAPEFLS-GVKLLPVPgENGKLTPEDLEAAIRPRddihfppPSLVSLENTTEGGTVYPLdeLKAISA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 221 ICSSRKVYFHTDAAQ-----AVGKIPLDVNDMKIDLMSISGHKiYGPKGVGAI------YIRRRPRVRVealQSGGgqer 289
Cdd:cd06502 154 LAKENGLPLHLDGARlanaaAALGVALKTYKSGVDSVSFCLSK-GGGAPVGAVvvgnrdFIARARRRRK---QAGG---- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 290 GMRSGTVptplvvgLGAACEVAQQEMEY------DHKRISKLSERLiqnimKSLPDVVMNGDPkhhypgciNLSFAYVEG 363
Cdd:cd06502 226 GMRQSGF-------LAAAGLAALENDLWlrrlrhDHEMARRLAEAL-----EELGGLESEVQT--------NIVLLDPVE 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32307132 364 EsllmalkDVALSSGSACTSASLEPSYVLRAIGtdedlaHSSIRFGIGRFTTEEEVDYTVEKC 426
Cdd:cd06502 286 A-------NAVFVELSKEAIERRGEGVLFYAWG------EGGVRFVTHWDTTEEDVDELLSAL 335
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
166-277 |
1.09e-04 |
|
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: 44.20 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 166 LEAEGFQVTYLPVQKSGIIDLKELEAAI-QPDTSLVSVMTVNNEIGVKQPIAEIGRICSSRKVYFHTDAAQAVGKIPLDV 244
Cdd:cd06451 93 AERYGADVDVVEKPWGEAVSPEEIAEALeQHDIKAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVDAVSSLGGEPFRM 172
|
90 100 110
....*....|....*....|....*....|....
gi 32307132 245 NDMKIDLMSISGHKIYG-PKGVGAIYIRRRPRVR 277
Cdd:cd06451 173 DEWGVDVAYTGSQKALGaPPGLGPIAFSERALER 206
|
|
| PRK07324 |
PRK07324 |
transaminase; Validated |
95-255 |
2.66e-03 |
|
transaminase; Validated
Pssm-ID: 235989 Cd Length: 373 Bit Score: 39.92 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 95 YGWeSEAAmERARQQVASLI-GADPREIIFTSGATESNNIAIKGVArfyrSRKKHLITTQTEHKCVLDSCRSLeaeGFQV 173
Cdd:PRK07324 58 YGW-IEGS-PEFKEAVASLYqNVKPENILQTNGATGANFLVLYALV----EPGDHVISVYPTYQQLYDIPESL---GAEV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 174 TYLPVQKSG--IIDLKELEAAIQPDTSLVSVMTVNNEIG------VKQPIAEIGRICS----SRKVYFHTDAAQAVGKIp 241
Cdd:PRK07324 129 DYWQLKEENgwLPDLDELRRLVRPNTKLICINNANNPTGalmdraYLEEIVEIARSVDayvlSDEVYRPLDEDGSTPSI- 207
|
170
....*....|....
gi 32307132 242 LDVNDMKIDLMSIS 255
Cdd:PRK07324 208 ADLYEKGISTNSMS 221
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
68-342 |
5.26e-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: 38.86 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 68 PLDPRVLDAMLPYLINyygnphSRTHAYGweSEAAMERARQQVASLIG------ADPREIIFTSGATEsnniAIKGVARF 141
Cdd:cd00609 11 PPPPEVLEALAAAALR------AGLLGYY--PDPGLPELREAIAEWLGrrggvdVPPEEIVVTNGAQE----ALSLLLRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 142 YRSRKKHLITTQ---TEHKcvldscRSLEAEGFQVTYLPVQKSGII--DLKELEAAIQPDTSLVSVMTVNNEIGV---KQ 213
Cdd:cd00609 79 LLNPGDEVLVPDptyPGYE------AAARLAGAEVVPVPLDEEGGFllDLELLEAAKTPKTKLLYLNNPNNPTGAvlsEE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307132 214 PIAEIGRICSSRKVY---------FHTDAAQAvgkIPLDVNDMKIDLMSISGH-KIYGPKG--VGAIYIrrRPRVRVEAL 281
Cdd:cd00609 153 ELEELAELAKKHGILiisdeayaeLVYDGEPP---PALALLDAYERVIVLRSFsKTFGLPGlrIGYLIA--PPEELLERL 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32307132 282 QSgggqERGMRSGTVPTPLVVGLGAACEVAQQEMEYDHKRISKLSERLIQNIMKSLPDVVM 342
Cdd:cd00609 228 KK----LLPYTTSGPSTLSQAAAAAALDDGEEHLEELRERYRRRRDALLEALKELGPLVVV 284
|
|
| PRK05939 |
PRK05939 |
cystathionine gamma-synthase family protein; |
165-232 |
7.34e-03 |
|
cystathionine gamma-synthase family protein;
Pssm-ID: 235650 [Multi-domain] Cd Length: 397 Bit Score: 38.52 E-value: 7.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32307132 165 SLEAEGFQVTYLPVqksgiIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEIGRICSSRKVYFHTD 232
Cdd:PRK05939 105 TLRGLGVEVTMVDA-----TDVQNVAAAIRPNTRMVFVETIANPGTQVADLAGIGALCRERGLLYVVD 167
|
|
| |
