|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
52-451 |
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 113681905 52 PLYMDFQATTPMDPRVLDAMLPY--QVNYYGNPHSRTHAYGWESESAMEKARKQVAGLIGADPREIVFTSGATESNNMSI 129
Cdd:PRK14012 4 PIYLDYSATTPVDPRVAEKMMPYltMDGTFGNPASRSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDNLAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 130 KGVARFYKAKKMHIITTQIEHKCVLDSCRVLETEGFDITYLPVKSNGLIDLKQLEDTIRPDTSLVSIMAINNEIGVKQPV 209
Cdd:PRK14012 84 KGAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVIQDI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 210 KEIGHLCRSKNVFFHTDAAQAVGKIPVDVTDWKVDLMSISAHKIYGPKGVGALFVRRRPRVRLEPLQSGGGQERGLRSGT 289
Cdd:PRK14012 164 AAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRLEAQMHGGGHERGMRSGT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 290 VPTPLAVGLGAACEIAQQELEYDHKRVSLLANRLVQKImSEIPDVVMNGDPDQRYPGCINLSFAYVEGESLLMALKDVAL 369
Cdd:PRK14012 244 LPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGI-KDIEEVYLNGDLEQRVPGNLNVSFNYVEGESLIMALKDLAV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 370 SSGSACTSASLEPSYVLRAIGADEDLAHSSIRFGIGRFTTEEEVDYTAEKCIHQVKRLREMSPLWEMVQEGIDLKSIKWT 449
Cdd:PRK14012 323 SSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGKLRELSPLWEMFKEGVDLNSIEWA 402
|
..
gi 113681905 450 QH 451
Cdd:PRK14012 403 HH 404
|
|
| IscS |
TIGR02006 |
cysteine desulfurase IscS; This model represents IscS, one of several cysteine desulfurases ... |
52-451 |
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: 657.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 52 PLYMDFQATTPMDPRVLDAMLPYQVNYYGNPHSRTHAYGWESESAMEKARKQVAGLIGADPREIVFTSGATESNNMSIKG 131
Cdd:TIGR02006 4 PIYLDYAATTPVDPRVAEKMMPYLTEKFGNPASRSHSFGWEAEEAVENARNQVAELIGADSREIVFTSGATESNNLAIKG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 132 VARFYKAKKMHIITTQIEHKCVLDSCRVLETEGFDITYLPVKSNGLIDLKQLEDTIRPDTSLVSIMAINNEIGVKQPVKE 211
Cdd:TIGR02006 84 IAHFYKSKGNHIITSKTEHKAVLDTCRYLEREGFEVTYLPPKSNGLIDLEELKAAIRDDTILVSIMHVNNEIGVIQDIAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 212 IGHLCRSKNVFFHTDAAQAVGKIPVDVTDWKVDLMSISAHKIYGPKGVGALFVRRRPRVRLEPLQSGGGQERGLRSGTVP 291
Cdd:TIGR02006 164 IGEICRERKVFFHVDAAQSVGKIPINVNELKVDLMSISGHKIYGPKGIGALYVRRKPRVRLEALIHGGGHERGMRSGTLP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 292 TPLAVGLGAACEIAQQELEYDHKRVSLLANRLVQKIMSeIPDVVMNGDPDQRYPGCINLSFAYVEGESLLMALKDVALSS 371
Cdd:TIGR02006 244 THQIVGMGEAFRIAKEEMAQDTAHVLALRDRLLNGIKS-IEEVYLNGDLEHRVPGNLNVSFNYVEGESLIMALKDLAVSS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 372 GSACTSASLEPSYVLRAIGADEDLAHSSIRFGIGRFTTEEEVDYTAEKCIHQVKRLREMSPLWEMVQEGIDLKSIKWTQH 451
Cdd:TIGR02006 323 GSACTSASLEPSYVLRALGINDELAHSSIRFTIGRFTTEEEIDYAVKLVKSAIDKLRELSPLWEMFKEGVDLNSIEWAAH 402
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
51-431 |
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: 642.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 51 RPLYMDFQATTPMDPRVLDAMLPYQVNYYGNPHSrTHAYGWESESAMEKARKQVAGLIGADPREIVFTSGATESNNMSIK 130
Cdd:COG1104 2 MMIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSS-LHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNLAIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 131 GVARFYKAKKMHIITTQIEHKCVLDSCRVLETEGFDITYLPVKSNGLIDLKQLEDTIRPDTSLVSIMAINNEIGVKQPVK 210
Cdd:COG1104 81 GAARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 211 EIGHLCRSKNVFFHTDAAQAVGKIPVDVTDWKVDLMSISAHKIYGPKGVGALFVRRrpRVRLEPLQSGGGQERGLRSGTV 290
Cdd:COG1104 161 EIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRK--GVRLEPLIHGGGQERGLRSGTE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 291 PTPLAVGLGAACEIAQQELEYDHKRVSLLANRLVQKIMSEIPDVVMNGDPDQRYPGCINLSFAYVEGESLLMAL--KDVA 368
Cdd:COG1104 239 NVPGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAAIPGVVINGDPENRLPNTLNFSFPGVEGEALLLALdlAGIA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 113681905 369 LSSGSACTSASLEPSYVLRAIGADEDLAHSSIRFGIGRFTTEEEVDYTAEKCIHQVKRLREMS 431
Cdd:COG1104 319 VSSGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARLRKLS 381
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
54-415 |
2.17e-115 |
|
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: 343.07 E-value: 2.17e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 54 YMDFQATTPMDPRVLDAMLPYQVNYYGNPHSRTHAYGWESESAMEKARKQVAGLIGA-DPREIVFTSGATESNNMSIKGV 132
Cdd:pfam00266 2 YLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINApSNDEIIFTSGTTEAINLVALSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 133 ARFYKAKKmHIITTQIEHKCVLDSCRVL-ETEGFDITYLPVKSNGLIDLKQLEDTIRPDTSLVSIMAINNEIGVKQPVKE 211
Cdd:pfam00266 82 GRSLKPGD-EIVITEMEHHANLVPWQELaKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 212 IGHLCRSKNVFFHTDAAQAVGKIPVDVTDWKVDLMSISAHKIYGPKGVGALFVRRRPRVRLEPLQSGGG-------QERG 284
Cdd:pfam00266 161 IGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGmietvslQEST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 285 L-------RSGTVPTPLAVGLGAACE-IAQQELEYDHKRVSLLANRLVQKImSEIPDVVMNGdpDQRYPGCINLSFAYVE 356
Cdd:pfam00266 241 FadapwkfEAGTPNIAGIIGLGAALEyLSEIGLEAIEKHEHELAQYLYERL-LSLPGIRLYG--PERRASIISFNFKGVH 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 113681905 357 GESLLMALKD--VALSSGSACTsaslEPSYVLRAIgadedlaHSSIRFGIGRFTTEEEVDY 415
Cdd:pfam00266 318 PHDVATLLDEsgIAVRSGHHCA----QPLMVRLGL-------GGTVRASFYIYNTQEDVDR 367
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
54-414 |
2.07e-71 |
|
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: 230.05 E-value: 2.07e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 54 YMDFQATTPMDPRVLDAMLPYQVNYYGNPHSRTHAYGWESESAMEKARKQVAGLIGA-DPREIVFTSGATESNNMSIKGV 132
Cdd:cd06453 2 YLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINApSPDEIIFTRNTTEAINLVAYGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 133 ARFYKAKKmHIITTQIEHKCVLDSCRVL-ETEGFDITYLPVKSNGLIDLKQLEDTIRPDTSLVSIMAINNEIGVKQPVKE 211
Cdd:cd06453 82 GRANKPGD-EIVTSVMEHHSNIVPWQQLaERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPVKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 212 IGHLCRSKNVFFHTDAAQAVGKIPVDVTDWKVDLMSISAHKIYGPKGVGALFVRRRPRVRLEPLQSGGGQ-ERGLRSGTV 290
Cdd:cd06453 161 IGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMiEEVSFEETT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 291 PTPL-------------AVGLGAACE---------IAQQELEydhkrvslLANRLVQKiMSEIPDVVMNGDPDQRYPGci 348
Cdd:cd06453 241 YADLphkfeagtpniagAIGLGAAIDylekigmeaIAAHEHE--------LTAYALER-LSEIPGVRVYGDAEDRAGV-- 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113681905 349 nLSFAyVEG---ESLLMAL--KDVALSSGSACtsaslepsyvlrAIGADEDL-AHSSIRFGIGRFTTEEEVD 414
Cdd:cd06453 310 -VSFN-LEGihpHDVATILdqYGIAVRAGHHC------------AQPLMRRLgVPGTVRASFGLYNTEEEID 367
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
96-311 |
5.84e-18 |
|
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: 86.45 E-value: 5.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 96 AMEKARKQVAGLIGA-DPREIVFTSGATESNNMsikgVARFYKAKKMH----IITTQIEHKC--------------VLds 156
Cdd:NF041166 290 AYEGAREKVRRFIGApSVDEIIFVRGTTEAINL----VAKSWGRQNIGagdeIIVSHLEHHAnivpwqqlaqetgaKL-- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 157 cRVLetegfditylPVKSNGLIDLKQLEDTIRPDTSLVSIMAINNEIGVKQPVKEIGHLCRSKNVFFHTDAAQAVGKIPV 236
Cdd:NF041166 364 -RVI----------PVDDSGQILLDEYAKLLNPRTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPV 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 237 DV----TDWKVdlmsISAHKIYGPKGVGALFVRRRPRVRLEPLQSGGGQ------ERglrsgTV--PTPL---------- 294
Cdd:NF041166 433 DVqaldADFFV----FSGHKVFGPTGIGVVYGKRDLLEAMPPWQGGGNMiadvtfEK-----TVyqPAPNrfeagtgnia 503
|
250 260 270
....*....|....*....|....*....|
gi 113681905 295 -AVGLGAACE---------IAQQE---LEY 311
Cdd:NF041166 504 dAVGLGAALDyverigienIARYEhdlLEY 533
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
52-451 |
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 113681905 52 PLYMDFQATTPMDPRVLDAMLPY--QVNYYGNPHSRTHAYGWESESAMEKARKQVAGLIGADPREIVFTSGATESNNMSI 129
Cdd:PRK14012 4 PIYLDYSATTPVDPRVAEKMMPYltMDGTFGNPASRSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDNLAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 130 KGVARFYKAKKMHIITTQIEHKCVLDSCRVLETEGFDITYLPVKSNGLIDLKQLEDTIRPDTSLVSIMAINNEIGVKQPV 209
Cdd:PRK14012 84 KGAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVIQDI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 210 KEIGHLCRSKNVFFHTDAAQAVGKIPVDVTDWKVDLMSISAHKIYGPKGVGALFVRRRPRVRLEPLQSGGGQERGLRSGT 289
Cdd:PRK14012 164 AAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRLEAQMHGGGHERGMRSGT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 290 VPTPLAVGLGAACEIAQQELEYDHKRVSLLANRLVQKImSEIPDVVMNGDPDQRYPGCINLSFAYVEGESLLMALKDVAL 369
Cdd:PRK14012 244 LPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGI-KDIEEVYLNGDLEQRVPGNLNVSFNYVEGESLIMALKDLAV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 370 SSGSACTSASLEPSYVLRAIGADEDLAHSSIRFGIGRFTTEEEVDYTAEKCIHQVKRLREMSPLWEMVQEGIDLKSIKWT 449
Cdd:PRK14012 323 SSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGKLRELSPLWEMFKEGVDLNSIEWA 402
|
..
gi 113681905 450 QH 451
Cdd:PRK14012 403 HH 404
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
53-414 |
0e+00 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 681.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 53 LYMDFQATTPMDPRVLDAMLPYQVNYYGNPHSRTHAYGWESESAMEKARKQVAGLIGADPREIVFTSGATESNNMSIKGV 132
Cdd:PLN02651 1 LYLDMQATTPIDPRVLDAMLPFLIEHFGNPHSRTHLYGWESEDAVEKARAQVAALIGADPKEIIFTSGATESNNLAIKGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 133 ARFYKAKKMHIITTQIEHKCVLDSCRVLETEGFDITYLPVKSNGLIDLKQLEDTIRPDTSLVSIMAINNEIGVKQPVKEI 212
Cdd:PLN02651 81 MHFYKDKKKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVEEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 213 GHLCRSKNVFFHTDAAQAVGKIPVDVTDWKVDLMSISAHKIYGPKGVGALFVRRRPRVRLEPLQSGGGQERGLRSGTVPT 292
Cdd:PLN02651 161 GELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRLEPLMSGGGQERGRRSGTENT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 293 PLAVGLGAACEIAQQELEYDHKRVSLLANRLVQKIMSEIPDVVMNG--DPDQRYPGCINLSFAYVEGESLLMALKDVALS 370
Cdd:PLN02651 241 PLVVGLGAACELAMKEMDYDEKHMKALRERLLNGLRAKLGGVRVNGprDPEKRYPGTLNLSFAYVEGESLLMGLKEVAVS 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 113681905 371 SGSACTSASLEPSYVLRAIGADEDLAHSSIRFGIGRFTTEEEVD 414
Cdd:PLN02651 321 SGSACTSASLEPSYVLRALGVPEEMAHGSLRLGVGRFTTEEEVD 364
|
|
| IscS |
TIGR02006 |
cysteine desulfurase IscS; This model represents IscS, one of several cysteine desulfurases ... |
52-451 |
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: 657.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 52 PLYMDFQATTPMDPRVLDAMLPYQVNYYGNPHSRTHAYGWESESAMEKARKQVAGLIGADPREIVFTSGATESNNMSIKG 131
Cdd:TIGR02006 4 PIYLDYAATTPVDPRVAEKMMPYLTEKFGNPASRSHSFGWEAEEAVENARNQVAELIGADSREIVFTSGATESNNLAIKG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 132 VARFYKAKKMHIITTQIEHKCVLDSCRVLETEGFDITYLPVKSNGLIDLKQLEDTIRPDTSLVSIMAINNEIGVKQPVKE 211
Cdd:TIGR02006 84 IAHFYKSKGNHIITSKTEHKAVLDTCRYLEREGFEVTYLPPKSNGLIDLEELKAAIRDDTILVSIMHVNNEIGVIQDIAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 212 IGHLCRSKNVFFHTDAAQAVGKIPVDVTDWKVDLMSISAHKIYGPKGVGALFVRRRPRVRLEPLQSGGGQERGLRSGTVP 291
Cdd:TIGR02006 164 IGEICRERKVFFHVDAAQSVGKIPINVNELKVDLMSISGHKIYGPKGIGALYVRRKPRVRLEALIHGGGHERGMRSGTLP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 292 TPLAVGLGAACEIAQQELEYDHKRVSLLANRLVQKIMSeIPDVVMNGDPDQRYPGCINLSFAYVEGESLLMALKDVALSS 371
Cdd:TIGR02006 244 THQIVGMGEAFRIAKEEMAQDTAHVLALRDRLLNGIKS-IEEVYLNGDLEHRVPGNLNVSFNYVEGESLIMALKDLAVSS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 372 GSACTSASLEPSYVLRAIGADEDLAHSSIRFGIGRFTTEEEVDYTAEKCIHQVKRLREMSPLWEMVQEGIDLKSIKWTQH 451
Cdd:TIGR02006 323 GSACTSASLEPSYVLRALGINDELAHSSIRFTIGRFTTEEEIDYAVKLVKSAIDKLRELSPLWEMFKEGVDLNSIEWAAH 402
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
51-431 |
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: 642.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 51 RPLYMDFQATTPMDPRVLDAMLPYQVNYYGNPHSrTHAYGWESESAMEKARKQVAGLIGADPREIVFTSGATESNNMSIK 130
Cdd:COG1104 2 MMIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSS-LHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNLAIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 131 GVARFYKAKKMHIITTQIEHKCVLDSCRVLETEGFDITYLPVKSNGLIDLKQLEDTIRPDTSLVSIMAINNEIGVKQPVK 210
Cdd:COG1104 81 GAARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 211 EIGHLCRSKNVFFHTDAAQAVGKIPVDVTDWKVDLMSISAHKIYGPKGVGALFVRRrpRVRLEPLQSGGGQERGLRSGTV 290
Cdd:COG1104 161 EIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRK--GVRLEPLIHGGGQERGLRSGTE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 291 PTPLAVGLGAACEIAQQELEYDHKRVSLLANRLVQKIMSEIPDVVMNGDPDQRYPGCINLSFAYVEGESLLMAL--KDVA 368
Cdd:COG1104 239 NVPGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAAIPGVVINGDPENRLPNTLNFSFPGVEGEALLLALdlAGIA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 113681905 369 LSSGSACTSASLEPSYVLRAIGADEDLAHSSIRFGIGRFTTEEEVDYTAEKCIHQVKRLREMS 431
Cdd:COG1104 319 VSSGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARLRKLS 381
|
|
| FeS_nifS |
TIGR03402 |
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related ... |
54-433 |
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: 517.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 54 YMDFQATTPMDPRVLDAMLPYQVNYYGNPhSRTHAYGWESESAMEKARKQVAGLIGADPREIVFTSGATESNNMSIKGVA 133
Cdd:TIGR03402 2 YLDNNATTRVDPEVLEAMLPYFTEYFGNP-SSMHSFGGEVGKAVEEAREQVAKLLGAEPDEIIFTSGGTESDNTAIKSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 134 RFYKAKKmHIITTQIEHKCVLDSCRVLETEGFDITYLPVKSNGLIDLKQLEDTIRPDTSLVSIMAINNEIGVKQPVKEIG 213
Cdd:TIGR03402 81 AAQPEKR-HIITTAVEHPAVLSLCQHLEKQGYKVTYLPVDEEGRLDLEELRAAITDDTALVSVMWANNETGTIFPIEEIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 214 HLCRSKNVFFHTDAAQAVGKIPVDVTDWKVDLMSISAHKIYGPKGVGALFVRRrpRVRLEPLQSGGGQERGLRSGTVPTP 293
Cdd:TIGR03402 160 EIAKERGALFHTDAVQAVGKIPIDLKEMNIDMLSLSGHKLHGPKGVGALYIRK--GTRFRPLLRGGHQERGRRAGTENVP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 294 LAVGLGAACEIAQQELEYDHKRVSLLANRLVQKIMSEIPDVVMNGDPDQRYPGCINLSFAYVEGESLLMAL--KDVALSS 371
Cdd:TIGR03402 238 GIVGLGKAAELATEHLEEENTRVRALRDRLEAGLLARIPDARLNGDPTKRLPNTVNISFEYIEGEAILLLLdmEGICASS 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113681905 372 GSACTSASLEPSYVLRAIGADEDLAHSSIRFGIGRFTTEEEVDYTAEKCIHQVKRLREMSPL 433
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 ... |
54-402 |
2.07e-154 |
|
cysteine desulfurase DndA; This model describes DndA, a protein related to IscS and part of a larger family of cysteine desulfurases. It is encoded, typically, divergently from a conserved, sparsely distributed operon for sulfur modification of DNA. This modification system is designated dnd, after the phenotype of DNA degradation during electrophoresis. The system is sporadically distributed in bacteria, much like some restriction enzyme operons. DndB is described as a putative ATPase. [DNA metabolism, Restriction/modification]
Pssm-ID: 163191 [Multi-domain] Cd Length: 353 Bit Score: 441.54 E-value: 2.07e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 54 YMDFQATTPMDPRVLDAMLPYQVNYYGNPHSRTHAYGWESESAMEKARKQVAGLIGADPREIVFTSGATESNNMSIKGVA 133
Cdd:TIGR03235 1 YLDHNATTPIDPAVAEAMLPWLLEEFGNPSSRTHEFGHNAKKAVERARKQVAEALGADTEEVIFTSGATESNNLAILGLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 134 RFYKAK-KMHIITTQIEHKCVLDSCRVLETEGFDITYLPVKSNGLIDLKQLEDTIRPDTSLVSIMAINNEIGVKQPVKEI 212
Cdd:TIGR03235 81 RAGEQKgKKHIITSAIEHPAVLEPIRALERNGFTVTYLPVDESGRIDVDELADAIRPDTLLVSIMHVNNETGSIQPIREI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 213 GHLCRSKNVFFHTDAAQAVGKIPVDVTDWKVDLMSISAHKIYGPKGVGALFVRRR--PRVRLEPLQSGGGQERGLRSGTV 290
Cdd:TIGR03235 161 AEVLEAHEAFFHVDAAQVVGKITVDLSADRIDLISCSGHKIYGPKGIGALVIRKRgkPKAPLKPIMFGGGQERGLRPGTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 291 PTPLAVGLGAACEIAQQELEYDHKRVSLLANRLVQKImsEIPDVVMNGDPDQRYPGCINLSFAYVEGESLLMALK-DVAL 369
Cdd:TIGR03235 241 PVHLIVGMGEAAEIARRNAQAWEVKLRAMRNQLRDAL--QTLGVKLNGDPAETIPHILNFSIDGVNSEALIVNLRaDAAV 318
|
330 340 350
....*....|....*....|....*....|...
gi 113681905 370 SSGSACTSASLEPSYVLRAIGADEDLAHSSIRF 402
Cdd:TIGR03235 319 STGSACSSSKYEPSHVLQAMGLDTDRARGAIRF 351
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
54-415 |
2.17e-115 |
|
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: 343.07 E-value: 2.17e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 54 YMDFQATTPMDPRVLDAMLPYQVNYYGNPHSRTHAYGWESESAMEKARKQVAGLIGA-DPREIVFTSGATESNNMSIKGV 132
Cdd:pfam00266 2 YLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINApSNDEIIFTSGTTEAINLVALSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 133 ARFYKAKKmHIITTQIEHKCVLDSCRVL-ETEGFDITYLPVKSNGLIDLKQLEDTIRPDTSLVSIMAINNEIGVKQPVKE 211
Cdd:pfam00266 82 GRSLKPGD-EIVITEMEHHANLVPWQELaKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 212 IGHLCRSKNVFFHTDAAQAVGKIPVDVTDWKVDLMSISAHKIYGPKGVGALFVRRRPRVRLEPLQSGGG-------QERG 284
Cdd:pfam00266 161 IGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGmietvslQEST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 285 L-------RSGTVPTPLAVGLGAACE-IAQQELEYDHKRVSLLANRLVQKImSEIPDVVMNGdpDQRYPGCINLSFAYVE 356
Cdd:pfam00266 241 FadapwkfEAGTPNIAGIIGLGAALEyLSEIGLEAIEKHEHELAQYLYERL-LSLPGIRLYG--PERRASIISFNFKGVH 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 113681905 357 GESLLMALKD--VALSSGSACTsaslEPSYVLRAIgadedlaHSSIRFGIGRFTTEEEVDY 415
Cdd:pfam00266 318 PHDVATLLDEsgIAVRSGHHCA----QPLMVRLGL-------GGTVRASFYIYNTQEDVDR 367
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
53-429 |
8.64e-104 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 313.59 E-value: 8.64e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 53 LYMDFQATTPMDPRVLDAMLPYQVNYYGNPHSrTHAYGWESESAMEKARKQVAGLIGADPREIVFTSGATESNNMSIKGV 132
Cdd:PRK02948 2 IYLDYAATTPMSKEALQTYQKAASQYFGNESS-LHDIGGTASSLLQVCRKTFAEMIGGEEQGIYFTSGGTESNYLAIQSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 133 ARFYKAKKMHIITTQIEHKCVLDSCRVLETEGFDITYLPVKSNGLIDLKQLEDTIRPDTSLVSIMAINNEIGVKQPVKEI 212
Cdd:PRK02948 81 LNALPQNKKHIITTPMEHASIHSYFQSLESQGYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQPIAEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 213 GHLCRSKNVFFHTDAAQAVGKIPVDVTDWKVDLMSISAHKIYGPKGVGALFVrrRPRVRLEPLQSGGGQERGLRSGTVPT 292
Cdd:PRK02948 161 GALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYI--NPQVRWKPVFPGTTHEKGFRPGTVNV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 293 PLAVGLGAACEIAQQELEYDHKRVSLLANRLVQKIMSEIPDVVMNGDPDQRYPGCINLSFAYVEGESLLMAL--KDVALS 370
Cdd:PRK02948 239 PGIAAFLTAAENILKNMQEESLRFKELRSYFLEQIQTLPLPIEVEGHSTSCLPHIIGVTIKGIEGQYTMLECnrRGIAIS 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 113681905 371 SGSACTSASLEPSYVLRAIGADEDLAHSSIRFGIGRFTTEEEVDYTaekcIHQVKRLRE 429
Cdd:PRK02948 319 TGSACQVGKQEPSKTMLAIGKTYEEAKQFVRFSFGQQTTKDQIDTT----IHALETIGN 373
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
51-430 |
4.76e-76 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 242.74 E-value: 4.76e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 51 RPL-YMDFQATTPMdPR-VLDAMLPYQVNYYGNPHSRTHAYGWESESAMEKARKQVAGLIGA-DPREIVFTSGATESNNM 127
Cdd:COG0520 14 KPLvYLDNAATGQK-PRpVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAaSPDEIIFTRGTTEAINL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 128 SIKGVARFykAKKMHIITTQIEHKCVLDSCRVL-ETEGFDITYLPVKSNGLIDLKQLEDTIRPDTSLVSIMAINNEIGVK 206
Cdd:COG0520 93 VAYGLGRL--KPGDEILITEMEHHSNIVPWQELaERTGAEVRVIPLDEDGELDLEALEALLTPRTKLVAVTHVSNVTGTV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 207 QPVKEIGHLCRSKNVFFHTDAAQAVGKIPVDVTDWKVDLMSISAHKIYGPKGVGALFVRRRPRVRLEPLQSGGG------ 280
Cdd:COG0520 171 NPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELLEALPPFLGGGGmiewvs 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 281 ------QERGLR--SGTVPTPLAVGLGAACEIAQQeLEYD--HKRVSLLANRLVQKiMSEIPDVVMNGDPDQRYPGCInL 350
Cdd:COG0520 251 fdgttyADLPRRfeAGTPNIAGAIGLGAAIDYLEA-IGMEaiEARERELTAYALEG-LAAIPGVRILGPADPEDRSGI-V 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 351 SFaYVEG---ESLLMALKD--VALSSGSACTsaslEPsyVLRAIGADedlahSSIRFGIGRFTTEEEVDYtaekCIHQVK 425
Cdd:COG0520 328 SF-NVDGvhpHDVAALLDDegIAVRAGHHCA----QP--LMRRLGVP-----GTVRASFHLYNTEEEIDR----LVEALK 391
|
....*
gi 113681905 426 RLREM 430
Cdd:COG0520 392 KLAEL 396
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
54-414 |
2.07e-71 |
|
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: 230.05 E-value: 2.07e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 54 YMDFQATTPMDPRVLDAMLPYQVNYYGNPHSRTHAYGWESESAMEKARKQVAGLIGA-DPREIVFTSGATESNNMSIKGV 132
Cdd:cd06453 2 YLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINApSPDEIIFTRNTTEAINLVAYGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 133 ARFYKAKKmHIITTQIEHKCVLDSCRVL-ETEGFDITYLPVKSNGLIDLKQLEDTIRPDTSLVSIMAINNEIGVKQPVKE 211
Cdd:cd06453 82 GRANKPGD-EIVTSVMEHHSNIVPWQQLaERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPVKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 212 IGHLCRSKNVFFHTDAAQAVGKIPVDVTDWKVDLMSISAHKIYGPKGVGALFVRRRPRVRLEPLQSGGGQ-ERGLRSGTV 290
Cdd:cd06453 161 IGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMiEEVSFEETT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 291 PTPL-------------AVGLGAACE---------IAQQELEydhkrvslLANRLVQKiMSEIPDVVMNGDPDQRYPGci 348
Cdd:cd06453 241 YADLphkfeagtpniagAIGLGAAIDylekigmeaIAAHEHE--------LTAYALER-LSEIPGVRVYGDAEDRAGV-- 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113681905 349 nLSFAyVEG---ESLLMAL--KDVALSSGSACtsaslepsyvlrAIGADEDL-AHSSIRFGIGRFTTEEEVD 414
Cdd:cd06453 310 -VSFN-LEGihpHDVATILdqYGIAVRAGHHC------------AQPLMRRLgVPGTVRASFGLYNTEEEID 367
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
51-415 |
8.90e-37 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 139.50 E-value: 8.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 51 RPL-YMDFQATTPMDPRVLDAMLPYQVNYYGNPHSRTHAYGWESESAMEKARKQVAGLIGA-DPREIVFTSGATESNNMs 128
Cdd:PLN02855 31 SKLvYLDNAATSQKPAAVLDALQDYYEEYNSNVHRGIHALSAKATDAYELARKKVAAFINAsTSREIVFTRNATEAINL- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 129 ikgVARFYKAKKM----HIITTQIEH-KCVLDSCRVLETEGFDITYLPVKSNGLIDLKQLEDTIRPDTSLVSIMAINNEI 203
Cdd:PLN02855 110 ---VAYTWGLANLkpgdEVILSVAEHhSNIVPWQLVAQKTGAVLKFVGLTPDEVLDVEQLKELLSEKTKLVATHHVSNVL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 204 GVKQPVKEIGHLCRSKNVFFHTDAAQAVGKIPVDVTDWKVDLMSISAHKIYGPKGVGALFVRRRPRVRLEPLQSGGG--- 280
Cdd:PLN02855 187 GSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLWGKSDLLESMPPFLGGGEmis 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 281 ---------QERGLR--SGTVPTPLAVGLGAAC----EIAQQEL-EYDHKrvslLANRLVQKiMSEIPDVVMNG----DP 340
Cdd:PLN02855 267 dvfldhstyAPPPSRfeAGTPAIGEAIGLGAAIdylsEIGMDRIhEYEVE----LGTYLYEK-LSSVPGVRIYGpkpsEG 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 341 DQRYPGCinlSFAyVEG------ESLLMALKDVALSSGSACTsaslEPSYvlRAIGADEDlAHSSIRFgigrFTTEEEVD 414
Cdd:PLN02855 342 VGRAALC---AFN-VEGihptdlSTFLDQQHGVAIRSGHHCA----QPLH--RYLGVNAS-ARASLYF----YNTKEEVD 406
|
.
gi 113681905 415 Y 415
Cdd:PLN02855 407 A 407
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
52-343 |
3.34e-30 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 121.01 E-value: 3.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 52 PL-YMDFQATTPMDPRVLDAMLPYQVNYYGNPHSRTHAYGWESESAMEKARKQVAGLIGA-DPREIVFTSGATESNNMsi 129
Cdd:PRK09295 23 PLaYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKQAALFINArSAEELVFVRGTTEGINL-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 130 kgVARFYKAKKMH----IITTQIEHKCVLDSCRVL-ETEGFDITYLPVKSNGLIDLKQLEDTIRPDTSLVSIMAINNEIG 204
Cdd:PRK09295 101 --VANSWGNSNVRagdnIIISEMEHHANIVPWQMLcARVGAELRVIPLNPDGTLQLETLPALFDERTRLLAITHVSNVLG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 205 VKQPVKEIGHLCRSKNVFFHTDAAQAVGKIPVDVTDWKVDLMSISAHKIYGPKGVGALFVRRRPRVRLEPLQSGGGQERG 284
Cdd:PRK09295 179 TENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKEALLQEMPPWEGGGSMIAT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 285 L---------------RSGTVPTPLAVGLGAACE---------IAQQEleydhkrVSLLANRLVQkiMSEIPDVVMNGdP 340
Cdd:PRK09295 259 VsltegttwakapwrfEAGTPNTGGIIGLGAALDyvsalglnnIAEYE-------QNLMHYALSQ--LESVPDLTLYG-P 328
|
...
gi 113681905 341 DQR 343
Cdd:PRK09295 329 QNR 331
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
54-388 |
2.06e-26 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 110.13 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 54 YMDfQATTPMDPR-VLDAMLPYQVNYYGNPHSRTHAYGWESESAMEKARKQVAGLIGA-DPREIVFTSGATESNNMSIKG 131
Cdd:PRK10874 22 YLD-SAATALKPQaVIEATQQFYSLSAGNVHRSQFAAAQRLTARYEAAREQVAQLLNApDAKNIVWTRGTTESINLVAQS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 132 VARFYKAKKMHIITTQIEHKCVLDS-CRVLETEGFDITYLPVKSNGLIDLKQLEDTIRPDTSLVSIMAINNEIGVKQPVK 210
Cdd:PRK10874 101 YARPRLQPGDEIIVSEAEHHANLVPwLMVAQQTGAKVVKLPLGADRLPDVDLLPELITPRTRILALGQMSNVTGGCPDLA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 211 EIGHLCRSKNVFFHTDAAQAVGKIPVDVTDWKVDLMSISAHKIYGPKGVGALFVRRRPRVRLEPLQSGGGQER-----GL 285
Cdd:PRK10874 181 RAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMSPWQGGGKMLTevsfdGF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 286 RSGTVP------TP-LA--VGLGAACE-IAQQELEYDHKRVSLLANrLVQKIMSEIPdvvmnGDPDQRYPGCINLSF--A 353
Cdd:PRK10874 261 TPQSAPwrfeagTPnVAgvIGLSAALEwLADIDINQAESWSRSLAT-LAEDALAKLP-----GFRSFRCQDSSLLAFdfA 334
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 113681905 354 YVEGESL--LMALKDVALSSGSACTS---ASLEPSYVLRA 388
Cdd:PRK10874 335 GVHHSDLvtLLAEYGIALRAGQHCAQpllAALGVTGTLRA 374
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
96-311 |
5.84e-18 |
|
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: 86.45 E-value: 5.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 96 AMEKARKQVAGLIGA-DPREIVFTSGATESNNMsikgVARFYKAKKMH----IITTQIEHKC--------------VLds 156
Cdd:NF041166 290 AYEGAREKVRRFIGApSVDEIIFVRGTTEAINL----VAKSWGRQNIGagdeIIVSHLEHHAnivpwqqlaqetgaKL-- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 157 cRVLetegfditylPVKSNGLIDLKQLEDTIRPDTSLVSIMAINNEIGVKQPVKEIGHLCRSKNVFFHTDAAQAVGKIPV 236
Cdd:NF041166 364 -RVI----------PVDDSGQILLDEYAKLLNPRTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPV 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 237 DV----TDWKVdlmsISAHKIYGPKGVGALFVRRRPRVRLEPLQSGGGQ------ERglrsgTV--PTPL---------- 294
Cdd:NF041166 433 DVqaldADFFV----FSGHKVFGPTGIGVVYGKRDLLEAMPPWQGGGNMiadvtfEK-----TVyqPAPNrfeagtgnia 503
|
250 260 270
....*....|....*....|....*....|
gi 113681905 295 -AVGLGAACE---------IAQQE---LEY 311
Cdd:NF041166 504 dAVGLGAALDyverigienIARYEhdlLEY 533
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
97-265 |
3.32e-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: 67.41 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 97 MEKARKQVAGLIGADPREIVFTSGATESNNMSIKGVARfykaKKMHIITTQIEHKCVLDScrVLETEGFDITYLPVKSN- 175
Cdd:cd01494 2 LEELEEKLARLLQPGNDKAVFVPSGTGANEAALLALLG----PGDEVIVDANGHGSRYWV--AAELAGAKPVPVPVDDAg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 176 -GLIDLKQLEDTIRPD-TSLVSIMAINNEIGVKQPVKEIGHLCRSKNVFFHTDAAQAVGKIP---VDVTDWKVDLMSISA 250
Cdd:cd01494 76 yGGLDVAILEELKAKPnVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPapgVLIPEGGADVVTFSL 155
|
170
....*....|....*
gi 113681905 251 HKIYGPKGVGALFVR 265
Cdd:cd01494 156 HKNLGGEGGGVVIVK 170
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
95-267 |
3.30e-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: 67.93 E-value: 3.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 95 SAMEK-ARKQVAGLIGADPREI-VFTSGATESNNMSIKgVARFYK------------AKKMHIITTQIEHKCVLDSCRVL 160
Cdd:COG0076 106 TELEReVVRWLADLLGLPEGAGgVFTSGGTEANLLALL-AARDRAlarrvraeglpgAPRPRIVVSEEAHSSVDKAARLL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 161 ETEGFDITYLPVKSNGLIDLKQLEDTIRPDTSLVS-IMAI-----NNEIGVKQPVKEIGHLCRSKNVFFHTDAA------ 228
Cdd:COG0076 185 GLGRDALRKVPVDEDGRMDPDALEAAIDEDRAAGLnPIAVvatagTTNTGAIDPLAEIADIAREHGLWLHVDAAyggfal 264
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 113681905 229 ------QAVGKIPvdvtdwKVDLMSISAHKiYG--PKGVGALFVRRR 267
Cdd:COG0076 265 pspelrHLLDGIE------RADSITVDPHK-WLyvPYGCGAVLVRDP 304
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
58-265 |
3.08e-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: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 58 QATTPMDPRVLDA-MLPYQVNYYGNPhsrthaygWESESAMEKARKQV----AGLIGADPREI--VFTSGATESNNMSIK 130
Cdd:cd06450 4 GFVTTMDPPALLLeMLTSAKNAIDFT--------WDESPAATEMEAEVvnwlAKLFGLPSEDAdgVFTSGGSESNLLALL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 131 gVARFYKAKKMH-----------IITTQIEHKCVLDSCRVLETEgfdITYLPVKSNGLIDLKQLEDTIRPDTS--LVSIM 197
Cdd:cd06450 76 -AARDRARKRLKagggrgidklvIVCSDQAHVSVEKAAAYLDVK---VRLVPVDEDGRMDPEALEAAIDEDKAegLNPIM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 198 AI----NNEIGVKQPVKEIGHLCRSKNVFFHTDAAQAVGKIPVDVTDWK------VDLMSISAHKiYG--PKGVGALFVR 265
Cdd:cd06450 152 VVatagTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLdfgierVDSISVDPHK-YGlvPLGCSAVLVR 230
|
|
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
53-280 |
1.36e-09 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 60.27 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 53 LYMDFQATTPMDPRVLDAMLP-YQVNYYGNPHSRTHAyGWESESAMEKARKQVAGLIGADPRE--IVFTSGATES----- 124
Cdd:PLN02724 36 VYLDHAGATLYSESQLEAALAdFSSNVYGNPHSQSDS-SMRSSDTIESARQQVLEYFNAPPSDyaCVFTSGATAAlklvg 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 125 ----------------NNMSIKGVARFYKAKKMHIITTQIEHKCVLDSCRVLEtegFDITYLPVKSNGLIDLKQLEDtir 188
Cdd:PLN02724 115 etfpwsseshfcytleNHNSVLGIREYALEKGAAAIAVDIEEAANQPTNSQGS---VVVKSRGLQRRNTSKLQKRED--- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 189 pDTSLVSIMAINNEI---GVKQP------VKEIGHL--CRSKNVFFHTDAAQAVGKIPVDVTDWKVDLMSISAHKIYG-P 256
Cdd:PLN02724 189 -DGEAYNLFAFPSECnfsGAKFPldlvklIKDNQHSnfSKSGRWMVLLDAAKGCGTSPPDLSRYPADFVVVSFYKIFGyP 267
|
250 260
....*....|....*....|....
gi 113681905 257 KGVGALFVRRRPRVRLEPLQSGGG 280
Cdd:PLN02724 268 TGLGALLVRRDAAKLLKKKYFGGG 291
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
104-323 |
4.98e-08 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 54.14 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 104 VAGLIGADprEIVFTSGATESNNMSIKGVARFYKAkkmhIITTQIEHKCvLDSCRVLET-EGFDITYLPVKSNGLIDLKQ 182
Cdd:pfam01212 41 VAELFGKE--AALFVPSGTAANQLALMAHCQRGDE----VICGEPAHIH-FDETGGHAElGGVQPRPLDGDEAGNMDLED 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 183 LEDTIRPD-------TSLVSiMAINNEIGVKQPV-----KEIGHLCRSKNVFFHTD------AAQAVGKIPVDVTDWkVD 244
Cdd:pfam01212 114 LEAAIREVgadifppTGLIS-LENTHNSAGGQVVslenlREIAALAREHGIPVHLDgarfanAAVALGVIVKEITSY-AD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 245 LMSISAHKIYGpKGVGAL------FVRRRPRVRlepLQSGGgqerGLRSGTVPTplAVGLGaACEIAQQELEYDHKRVSL 318
Cdd:pfam01212 192 SVTMCLSKGLG-APVGSVlagsddFIAKAIRQR---KYLGG----GLRQAGVLA--AAGLR-ALEEGVARLARDHATARR 260
|
....*
gi 113681905 319 LANRL 323
Cdd:pfam01212 261 LAEGL 265
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
60-422 |
5.03e-07 |
|
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: 51.56 E-value: 5.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 60 TTPMdPRVLDAMlpYQVNYygnphsRTHAYGwESEsAMEKARKQVAGLIGADprEIVFTSGATESNNMSIKGVARFYKA- 138
Cdd:cd06502 8 TGPT-PEMLEAM--AAANV------GDDVYG-EDP-TTAKLEARAAELFGKE--AALFVPSGTAANQLALAAHTQPGGSv 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 139 ---KKMHIITtqieHKC----VLDSCRVLETEGfditylpvkSNGLIDLKQLEDTIRPD-------TSLVSiMAINNEIG 204
Cdd:cd06502 75 ichETAHIYT----DEAgapeFLSGVKLLPVPG---------ENGKLTPEDLEAAIRPRddihfppPSLVS-LENTTEGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 205 VKQPVKE---IGHLCRSKNVFFHTDAAQ---AVGKIPVDVTDWK--VDLMSISahkiyGPKG----VGAL------FVRR 266
Cdd:cd06502 141 TVYPLDElkaISALAKENGLPLHLDGARlanAAAALGVALKTYKsgVDSVSFC-----LSKGggapVGAVvvgnrdFIAR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 267 RPRVRlepLQSGGgqerGLRSGTVptplavgLGAACEIAQQE------LEYDHKRVSLLANRLvqkimSEIPDVVMNGDP 340
Cdd:cd06502 216 ARRRR---KQAGG----GMRQSGF-------LAAAGLAALENdlwlrrLRHDHEMARRLAEAL-----EELGGLESEVQT 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 341 dqrypgciNLSFAYVEGEsllmalkDVALSSGSACTSASLEPSYVLRAIGadedlaHSSIRFGIGRFTTEEEVDYTAEKC 420
Cdd:cd06502 277 --------NIVLLDPVEA-------NAVFVELSKEAIERRGEGVLFYAWG------EGGVRFVTHWDTTEEDVDELLSAL 335
|
..
gi 113681905 421 IH 422
Cdd:cd06502 336 KA 337
|
|
| PLN02721 |
PLN02721 |
threonine aldolase |
170-325 |
5.41e-05 |
|
threonine aldolase
Pssm-ID: 178323 [Multi-domain] Cd Length: 353 Bit Score: 45.06 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 170 LPVKSNGLIDLKQLEDTIRPD-------TSLVSIMAINNEIGVK----QPVKEIGHLCRSKNVFFHTDAAQ------AVG 232
Cdd:PLN02721 110 VKNNEDGTMDLDAIEAAIRPKgddhfptTRLICLENTHANCGGRclsvEYTDKVGELAKRHGLKLHIDGARifnasvALG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 233 kIPVDVTDWKVDLMSISAHKIYG-PKG---VG-ALFVRRRPRVRleplQSGGGqerGLRSGTVptplavgLGAACEIAQQ 307
Cdd:PLN02721 190 -VPVHRLVKAADSVSVCLSKGLGaPVGsviVGsKSFIRKAKRLR----KTLGG---GMRQVGV-------LAAAALVALQ 254
|
170 180
....*....|....*....|..
gi 113681905 308 E----LEYDHKRVSLLANRLVQ 325
Cdd:PLN02721 255 EnvpkLEDDHKKAKLLAEGLNQ 276
|
|
| PRK13479 |
PRK13479 |
2-aminoethylphosphonate--pyruvate transaminase; Provisional |
158-285 |
8.32e-04 |
|
2-aminoethylphosphonate--pyruvate transaminase; Provisional
Pssm-ID: 184076 [Multi-domain] Cd Length: 368 Bit Score: 41.44 E-value: 8.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 158 RVLETEGFDITYLPVKSNGLIDLKQLEDTIRPDTSLVSIMAINNEI--GVKQPVKEIGHLCRSKNVFFHTDAAQAVGKIP 235
Cdd:PRK13479 97 QIAEYLGIAHVVLDTGEDEPPDAAEVEAALAADPRITHVALVHCETttGILNPLDEIAAVAKRHGKRLIVDAMSSFGAIP 176
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 113681905 236 VDVTDWKVDLMSISAHK-IYGPKGVGALFVRRrprvrlEPLQSGGGQERGL 285
Cdd:PRK13479 177 IDIAELGIDALISSANKcIEGVPGFGFVIARR------SELEACKGNSRSL 221
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
164-273 |
8.68e-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: 41.51 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113681905 164 GFDITYLPVKSNGLIDLKQLEDTIR-PDTSLVSIMAINNEIGVKQPVKEIGHLCRSKNVFFHTDAAQAVGKIPVDVTDWK 242
Cdd:cd06451 97 GADVDVVEKPWGEAVSPEEIAEALEqHDIKAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVDAVSSLGGEPFRMDEWG 176
|
90 100 110
....*....|....*....|....*....|..
gi 113681905 243 VDLMSISAHKIYG-PKGVGALFVRRRPRVRLE 273
Cdd:cd06451 177 VDVAYTGSQKALGaPPGLGPIAFSERALERIK 208
|
|
| |
