|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
12-412 |
0e+00 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 716.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 12 PIYLDVQATAPMDPRVVDAMLPYMIND--FGNPHSRTHSYGWKAEEGVEQAREHVANLIKADPRDIIFTSGATESNNLAI 89
Cdd:PRK14012 4 PIYLDYSATTPVDPRVAEKMMPYLTMDgtFGNPASRSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDNLAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 90 KGVAKFRKQSGKnHIITLQTEHKCVLDSCRYLENEGFKVTYLPVDKGGMVDMEQLTQSITAETCLVSIMFVNNEIGVMQP 169
Cdd:PRK14012 84 KGAAHFYQKKGK-HIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVIQD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 170 IKQIGELCRSKGVYFHTDAAQATGKVPIDVNEMKIDLMSISAHKIYGPKGAGALYVRRRPRVRIEAQMSGGGQERGLRSG 249
Cdd:PRK14012 163 IAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRLEAQMHGGGHERGMRSG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 250 TVAAPLCIGLGEAAKIADKEMAMDKAHVERLSQMLINGISDkLPHIIRNGDARHAYPGCVNLSFAYVEGESLLMALKSIA 329
Cdd:PRK14012 243 TLPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGIKD-IEEVYLNGDLEQRVPGNLNVSFNYVEGESLIMALKDLA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 330 LSSGSACTSASLEPSYVLRAIGSEEDLAHSSIRFGLGRFTTDEEVKHTIDLCIRETNRLRDLSPLWEMVQEGIDLKSIQW 409
Cdd:PRK14012 322 VSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGKLRELSPLWEMFKEGVDLNSIEW 401
|
...
gi 25143064 410 TQH 412
Cdd:PRK14012 402 AHH 404
|
|
| IscS |
TIGR02006 |
cysteine desulfurase IscS; This model represents IscS, one of several cysteine desulfurases ... |
12-412 |
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: 646.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 12 PIYLDVQATAPMDPRVVDAMLPYMINDFGNPHSRTHSYGWKAEEGVEQAREHVANLIKADPRDIIFTSGATESNNLAIKG 91
Cdd:TIGR02006 4 PIYLDYAATTPVDPRVAEKMMPYLTEKFGNPASRSHSFGWEAEEAVENARNQVAELIGADSREIVFTSGATESNNLAIKG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 92 VAKFRKQSGkNHIITLQTEHKCVLDSCRYLENEGFKVTYLPVDKGGMVDMEQLTQSITAETCLVSIMFVNNEIGVMQPIK 171
Cdd:TIGR02006 84 IAHFYKSKG-NHIITSKTEHKAVLDTCRYLEREGFEVTYLPPKSNGLIDLEELKAAIRDDTILVSIMHVNNEIGVIQDIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 172 QIGELCRSKGVYFHTDAAQATGKVPIDVNEMKIDLMSISAHKIYGPKGAGALYVRRRPRVRIEAQMSGGGQERGLRSGTV 251
Cdd:TIGR02006 163 AIGEICRERKVFFHVDAAQSVGKIPINVNELKVDLMSISGHKIYGPKGIGALYVRRKPRVRLEALIHGGGHERGMRSGTL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 252 AAPLCIGLGEAAKIADKEMAMDKAHVERLSQMLINGISDkLPHIIRNGDARHAYPGCVNLSFAYVEGESLLMALKSIALS 331
Cdd:TIGR02006 243 PTHQIVGMGEAFRIAKEEMAQDTAHVLALRDRLLNGIKS-IEEVYLNGDLEHRVPGNLNVSFNYVEGESLIMALKDLAVS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 332 SGSACTSASLEPSYVLRAIGSEEDLAHSSIRFGLGRFTTDEEVKHTIDLCIRETNRLRDLSPLWEMVQEGIDLKSIQWTQ 411
Cdd:TIGR02006 322 SGSACTSASLEPSYVLRALGINDELAHSSIRFTIGRFTTEEEIDYAVKLVKSAIDKLRELSPLWEMFKEGVDLNSIEWAA 401
|
.
gi 25143064 412 H 412
Cdd:TIGR02006 402 H 402
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
11-392 |
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: 595.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 11 QPIYLDVQATAPMDPRVVDAMLPYMINDFGNPHSrTHSYGWKAEEGVEQAREHVANLIKADPRDIIFTSGATESNNLAIK 90
Cdd:COG1104 2 MMIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSS-LHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNLAIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 91 GVAKFRKQSGKnHIITLQTEHKCVLDSCRYLENEGFKVTYLPVDKGGMVDMEQLTQSITAETCLVSIMFVNNEIGVMQPI 170
Cdd:COG1104 81 GAARAYRKKGK-HIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 171 KQIGELCRSKGVYFHTDAAQATGKVPIDVNEMKIDLMSISAHKIYGPKGAGALYVRRrpRVRIEAQMSGGGQERGLRSGT 250
Cdd:COG1104 160 AEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRK--GVRLEPLIHGGGQERGLRSGT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 251 VAAPLCIGLGEAAKIADKEMAMDKAHVERLSQMLINGISDKLPHIIRNGDARHAYPGCVNLSFAYVEGESLLMAL--KSI 328
Cdd:COG1104 238 ENVPGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAAIPGVVINGDPENRLPNTLNFSFPGVEGEALLLALdlAGI 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25143064 329 ALSSGSACTSASLEPSYVLRAIGSEEDLAHSSIRFGLGRFTTDEEVKHTIDLCIRETNRLRDLS 392
Cdd:COG1104 318 AVSSGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARLRKLS 381
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
13-375 |
2.50e-105 |
|
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: 315.73 E-value: 2.50e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 13 IYLDVQATAPMDPRVVDAMLPYMINDFGNPHSRTHSYGWKAEEGVEQAREHVANLIKADPRD-IIFTSGATESNNLAIKG 91
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNDeIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 92 VAkfRKQSGKNHIITLQTEHKCVLDSCRYLEN-EGFKVTYLPVDKGGMVDMEQLTQSITAETCLVSIMFVNNEIGVMQPI 170
Cdd:pfam00266 81 LG--RSLKPGDEIVITEMEHHANLVPWQELAKrTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 171 KQIGELCRSKGVYFHTDAAQATGKVPIDVNEMKIDLMSISAHKIYGPKGAGALYVRRRPRVRIEAQMSGGG-------QE 243
Cdd:pfam00266 159 PEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGmietvslQE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 244 RGL-------RSGTVAAPLCIGLGEAAK-IADKEMAMDKAHVERLSQMLINGIsDKLPHIIRNGDARHayPGCVNLSFAY 315
Cdd:pfam00266 239 STFadapwkfEAGTPNIAGIIGLGAALEyLSEIGLEAIEKHEHELAQYLYERL-LSLPGIRLYGPERR--ASIISFNFKG 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25143064 316 VEGESLLMAL--KSIALSSGSACTsaslEPSYVLRAIgseedlaHSSIRFGLGRFTTDEEVK 375
Cdd:pfam00266 316 VHPHDVATLLdeSGIAVRSGHHCA----QPLMVRLGL-------GGTVRASFYIYNTQEDVD 366
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
13-374 |
1.48e-61 |
|
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: 203.08 E-value: 1.48e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 13 IYLDVQATAPMDPRVVDAMLPYMINDFGNPHSRTHSYGWKAEEGVEQAREHVANLIKA-DPRDIIFTSGATESNNLAIKG 91
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINApSPDEIIFTRNTTEAINLVAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 92 VAKfRKQSGkNHIITLQTEHKCVLDSCRYLENE-GFKVTYLPVDKGGMVDMEQLTQSITAETCLVSIMFVNNEIGVMQPI 170
Cdd:cd06453 81 LGR-ANKPG-DEIVTSVMEHHSNIVPWQQLAERtGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 171 KQIGELCRSKGVYFHTDAAQATGKVPIDVNEMKIDLMSISAHKIYGPKGAGALYVRRRPRVRIEAQMSGGGQ-ERGLRSG 249
Cdd:cd06453 159 KEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMiEEVSFEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 250 TVAAPL-------------CIGLGEAAKIADKeMAMDK--AHVERLSQMLINGISDkLPHIIRNGDARHAYPGcvnLSFA 314
Cdd:cd06453 239 TTYADLphkfeagtpniagAIGLGAAIDYLEK-IGMEAiaAHEHELTAYALERLSE-IPGVRVYGDAEDRAGV---VSFN 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25143064 315 yVEG---ESLLMAL--KSIALSSGSACTsaslEPsyVLRAIGseedlAHSSIRFGLGRFTTDEEV 374
Cdd:cd06453 314 -LEGihpHDVATILdqYGIAVRAGHHCA----QP--LMRRLG-----VPGTVRASFGLYNTEEEI 366
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
58-227 |
6.33e-15 |
|
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: 76.43 E-value: 6.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 58 EQAREHVANLIKA-DPRDIIFTSGATESNNLaikgVAKfrkqS-GKNH------IITLQTEH-------------Kcvld 116
Cdd:NF041166 292 EGAREKVRRFIGApSVDEIIFVRGTTEAINL----VAK----SwGRQNigagdeIIVSHLEHhanivpwqqlaqeT---- 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 117 scryleneGFKVTYLPVDKGGMVDMEQLTQSITAETCLVSIMFVNNEIGVMQPIKQIGELCRSKGVYFHTDAAQATGKVP 196
Cdd:NF041166 360 --------GAKLRVIPVDDSGQILLDEYAKLLNPRTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMP 431
|
170 180 190
....*....|....*....|....*....|.
gi 25143064 197 IDVNEMKIDLMSISAHKIYGPKGAGALYVRR 227
Cdd:NF041166 432 VDVQALDADFFVFSGHKVFGPTGIGVVYGKR 462
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
12-412 |
0e+00 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 716.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 12 PIYLDVQATAPMDPRVVDAMLPYMIND--FGNPHSRTHSYGWKAEEGVEQAREHVANLIKADPRDIIFTSGATESNNLAI 89
Cdd:PRK14012 4 PIYLDYSATTPVDPRVAEKMMPYLTMDgtFGNPASRSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDNLAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 90 KGVAKFRKQSGKnHIITLQTEHKCVLDSCRYLENEGFKVTYLPVDKGGMVDMEQLTQSITAETCLVSIMFVNNEIGVMQP 169
Cdd:PRK14012 84 KGAAHFYQKKGK-HIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVIQD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 170 IKQIGELCRSKGVYFHTDAAQATGKVPIDVNEMKIDLMSISAHKIYGPKGAGALYVRRRPRVRIEAQMSGGGQERGLRSG 249
Cdd:PRK14012 163 IAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRLEAQMHGGGHERGMRSG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 250 TVAAPLCIGLGEAAKIADKEMAMDKAHVERLSQMLINGISDkLPHIIRNGDARHAYPGCVNLSFAYVEGESLLMALKSIA 329
Cdd:PRK14012 243 TLPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGIKD-IEEVYLNGDLEQRVPGNLNVSFNYVEGESLIMALKDLA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 330 LSSGSACTSASLEPSYVLRAIGSEEDLAHSSIRFGLGRFTTDEEVKHTIDLCIRETNRLRDLSPLWEMVQEGIDLKSIQW 409
Cdd:PRK14012 322 VSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGKLRELSPLWEMFKEGVDLNSIEW 401
|
...
gi 25143064 410 TQH 412
Cdd:PRK14012 402 AHH 404
|
|
| IscS |
TIGR02006 |
cysteine desulfurase IscS; This model represents IscS, one of several cysteine desulfurases ... |
12-412 |
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: 646.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 12 PIYLDVQATAPMDPRVVDAMLPYMINDFGNPHSRTHSYGWKAEEGVEQAREHVANLIKADPRDIIFTSGATESNNLAIKG 91
Cdd:TIGR02006 4 PIYLDYAATTPVDPRVAEKMMPYLTEKFGNPASRSHSFGWEAEEAVENARNQVAELIGADSREIVFTSGATESNNLAIKG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 92 VAKFRKQSGkNHIITLQTEHKCVLDSCRYLENEGFKVTYLPVDKGGMVDMEQLTQSITAETCLVSIMFVNNEIGVMQPIK 171
Cdd:TIGR02006 84 IAHFYKSKG-NHIITSKTEHKAVLDTCRYLEREGFEVTYLPPKSNGLIDLEELKAAIRDDTILVSIMHVNNEIGVIQDIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 172 QIGELCRSKGVYFHTDAAQATGKVPIDVNEMKIDLMSISAHKIYGPKGAGALYVRRRPRVRIEAQMSGGGQERGLRSGTV 251
Cdd:TIGR02006 163 AIGEICRERKVFFHVDAAQSVGKIPINVNELKVDLMSISGHKIYGPKGIGALYVRRKPRVRLEALIHGGGHERGMRSGTL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 252 AAPLCIGLGEAAKIADKEMAMDKAHVERLSQMLINGISDkLPHIIRNGDARHAYPGCVNLSFAYVEGESLLMALKSIALS 331
Cdd:TIGR02006 243 PTHQIVGMGEAFRIAKEEMAQDTAHVLALRDRLLNGIKS-IEEVYLNGDLEHRVPGNLNVSFNYVEGESLIMALKDLAVS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 332 SGSACTSASLEPSYVLRAIGSEEDLAHSSIRFGLGRFTTDEEVKHTIDLCIRETNRLRDLSPLWEMVQEGIDLKSIQWTQ 411
Cdd:TIGR02006 322 SGSACTSASLEPSYVLRALGINDELAHSSIRFTIGRFTTEEEIDYAVKLVKSAIDKLRELSPLWEMFKEGVDLNSIEWAA 401
|
.
gi 25143064 412 H 412
Cdd:TIGR02006 402 H 402
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
13-374 |
0e+00 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 622.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 13 IYLDVQATAPMDPRVVDAMLPYMINDFGNPHSRTHSYGWKAEEGVEQAREHVANLIKADPRDIIFTSGATESNNLAIKGV 92
Cdd:PLN02651 1 LYLDMQATTPIDPRVLDAMLPFLIEHFGNPHSRTHLYGWESEDAVEKARAQVAALIGADPKEIIFTSGATESNNLAIKGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 93 AKFRKQSGKnHIITLQTEHKCVLDSCRYLENEGFKVTYLPVDKGGMVDMEQLTQSITAETCLVSIMFVNNEIGVMQPIKQ 172
Cdd:PLN02651 81 MHFYKDKKK-HVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 173 IGELCRSKGVYFHTDAAQATGKVPIDVNEMKIDLMSISAHKIYGPKGAGALYVRRRPRVRIEAQMSGGGQERGLRSGTVA 252
Cdd:PLN02651 160 IGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRLEPLMSGGGQERGRRSGTEN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 253 APLCIGLGEAAKIADKEMAMDKAHVERLSQMLINGISDKLPHIIRNG--DARHAYPGCVNLSFAYVEGESLLMALKSIAL 330
Cdd:PLN02651 240 TPLVVGLGAACELAMKEMDYDEKHMKALRERLLNGLRAKLGGVRVNGprDPEKRYPGTLNLSFAYVEGESLLMGLKEVAV 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 25143064 331 SSGSACTSASLEPSYVLRAIGSEEDLAHSSIRFGLGRFTTDEEV 374
Cdd:PLN02651 320 SSGSACTSASLEPSYVLRALGVPEEMAHGSLRLGVGRFTTEEEV 363
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
11-392 |
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: 595.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 11 QPIYLDVQATAPMDPRVVDAMLPYMINDFGNPHSrTHSYGWKAEEGVEQAREHVANLIKADPRDIIFTSGATESNNLAIK 90
Cdd:COG1104 2 MMIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSS-LHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNLAIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 91 GVAKFRKQSGKnHIITLQTEHKCVLDSCRYLENEGFKVTYLPVDKGGMVDMEQLTQSITAETCLVSIMFVNNEIGVMQPI 170
Cdd:COG1104 81 GAARAYRKKGK-HIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 171 KQIGELCRSKGVYFHTDAAQATGKVPIDVNEMKIDLMSISAHKIYGPKGAGALYVRRrpRVRIEAQMSGGGQERGLRSGT 250
Cdd:COG1104 160 AEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRK--GVRLEPLIHGGGQERGLRSGT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 251 VAAPLCIGLGEAAKIADKEMAMDKAHVERLSQMLINGISDKLPHIIRNGDARHAYPGCVNLSFAYVEGESLLMAL--KSI 328
Cdd:COG1104 238 ENVPGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAAIPGVVINGDPENRLPNTLNFSFPGVEGEALLLALdlAGI 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25143064 329 ALSSGSACTSASLEPSYVLRAIGSEEDLAHSSIRFGLGRFTTDEEVKHTIDLCIRETNRLRDLS 392
Cdd:COG1104 318 AVSSGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARLRKLS 381
|
|
| FeS_nifS |
TIGR03402 |
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related ... |
13-394 |
9.71e-174 |
|
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: 490.20 E-value: 9.71e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 13 IYLDVQATAPMDPRVVDAMLPYMINDFGNPhSRTHSYGWKAEEGVEQAREHVANLIKADPRDIIFTSGATESNNLAIKGV 92
Cdd:TIGR03402 1 IYLDNNATTRVDPEVLEAMLPYFTEYFGNP-SSMHSFGGEVGKAVEEAREQVAKLLGAEPDEIIFTSGGTESDNTAIKSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 93 AKFRKqsGKNHIITLQTEHKCVLDSCRYLENEGFKVTYLPVDKGGMVDMEQLTQSITAETCLVSIMFVNNEIGVMQPIKQ 172
Cdd:TIGR03402 80 LAAQP--EKRHIITTAVEHPAVLSLCQHLEKQGYKVTYLPVDEEGRLDLEELRAAITDDTALVSVMWANNETGTIFPIEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 173 IGELCRSKGVYFHTDAAQATGKVPIDVNEMKIDLMSISAHKIYGPKGAGALYVRRrpRVRIEAQMSGGGQERGLRSGTVA 252
Cdd:TIGR03402 158 IGEIAKERGALFHTDAVQAVGKIPIDLKEMNIDMLSLSGHKLHGPKGVGALYIRK--GTRFRPLLRGGHQERGRRAGTEN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 253 APLCIGLGEAAKIADKEMAMDKAHVERLSQMLINGISDKLPHIIRNGDARHAYPGCVNLSFAYVEGESLLMAL--KSIAL 330
Cdd:TIGR03402 236 VPGIVGLGKAAELATEHLEEENTRVRALRDRLEAGLLARIPDARLNGDPTKRLPNTVNISFEYIEGEAILLLLdmEGICA 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25143064 331 SSGSACTSASLEPSYVLRAIGSEEDLAHSSIRFGLGRFTTDEEVKHTIDLCIRETNRLRDLSPL 394
Cdd:TIGR03402 316 SSGSACTSGSLEPSHVLRAMGVPHTAAHGSIRFSLSRYNTEEDIDYVLEVLPPIIARLRAMSPF 379
|
|
| DNA_S_dndA |
TIGR03235 |
cysteine desulfurase DndA; This model describes DndA, a protein related to IscS and part of a ... |
14-365 |
1.87e-152 |
|
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: 435.38 E-value: 1.87e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 14 YLDVQATAPMDPRVVDAMLPYMINDFGNPHSRTHSYGWKAEEGVEQAREHVANLIKADPRDIIFTSGATESNNLAIKGVA 93
Cdd:TIGR03235 1 YLDHNATTPIDPAVAEAMLPWLLEEFGNPSSRTHEFGHNAKKAVERARKQVAEALGADTEEVIFTSGATESNNLAILGLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 94 KFRKQSGKNHIITLQTEHKCVLDSCRYLENEGFKVTYLPVDKGGMVDMEQLTQSITAETCLVSIMFVNNEIGVMQPIKQI 173
Cdd:TIGR03235 81 RAGEQKGKKHIITSAIEHPAVLEPIRALERNGFTVTYLPVDESGRIDVDELADAIRPDTLLVSIMHVNNETGSIQPIREI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 174 GELCRSKGVYFHTDAAQATGKVPIDVNEMKIDLMSISAHKIYGPKGAGALYVRRR--PRVRIEAQMSGGGQERGLRSGTV 251
Cdd:TIGR03235 161 AEVLEAHEAFFHVDAAQVVGKITVDLSADRIDLISCSGHKIYGPKGIGALVIRKRgkPKAPLKPIMFGGGQERGLRPGTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 252 AAPLCIGLGEAAKIADKEMAMDKAHVERLSQMLINGIsdKLPHIIRNGDARHAYPGCVNLSFAYVEGESLLMALKS-IAL 330
Cdd:TIGR03235 241 PVHLIVGMGEAAEIARRNAQAWEVKLRAMRNQLRDAL--QTLGVKLNGDPAETIPHILNFSIDGVNSEALIVNLRAdAAV 318
|
330 340 350
....*....|....*....|....*....|....*
gi 25143064 331 SSGSACTSASLEPSYVLRAIGSEEDLAHSSIRFGL 365
Cdd:TIGR03235 319 STGSACSSSKYEPSHVLQAMGLDTDRARGAIRFSW 353
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
13-375 |
2.50e-105 |
|
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: 315.73 E-value: 2.50e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 13 IYLDVQATAPMDPRVVDAMLPYMINDFGNPHSRTHSYGWKAEEGVEQAREHVANLIKADPRD-IIFTSGATESNNLAIKG 91
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNDeIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 92 VAkfRKQSGKNHIITLQTEHKCVLDSCRYLEN-EGFKVTYLPVDKGGMVDMEQLTQSITAETCLVSIMFVNNEIGVMQPI 170
Cdd:pfam00266 81 LG--RSLKPGDEIVITEMEHHANLVPWQELAKrTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 171 KQIGELCRSKGVYFHTDAAQATGKVPIDVNEMKIDLMSISAHKIYGPKGAGALYVRRRPRVRIEAQMSGGG-------QE 243
Cdd:pfam00266 159 PEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGmietvslQE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 244 RGL-------RSGTVAAPLCIGLGEAAK-IADKEMAMDKAHVERLSQMLINGIsDKLPHIIRNGDARHayPGCVNLSFAY 315
Cdd:pfam00266 239 STFadapwkfEAGTPNIAGIIGLGAALEyLSEIGLEAIEKHEHELAQYLYERL-LSLPGIRLYGPERR--ASIISFNFKG 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25143064 316 VEGESLLMAL--KSIALSSGSACTsaslEPSYVLRAIgseedlaHSSIRFGLGRFTTDEEVK 375
Cdd:pfam00266 316 VHPHDVATLLdeSGIAVRSGHHCA----QPLMVRLGL-------GGTVRASFYIYNTQEDVD 366
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
13-379 |
9.59e-99 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 299.34 E-value: 9.59e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 13 IYLDVQATAPMDPRVVDAMLPYMINDFGNPHSrTHSYGWKAEEGVEQAREHVANLIKADPRDIIFTSGATESNNLAIKGV 92
Cdd:PRK02948 2 IYLDYAATTPMSKEALQTYQKAASQYFGNESS-LHDIGGTASSLLQVCRKTFAEMIGGEEQGIYFTSGGTESNYLAIQSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 93 AKFRKQsGKNHIITLQTEHKCVLDSCRYLENEGFKVTYLPVDKGGMVDMEQLTQSITAETCLVSIMFVNNEIGVMQPIKQ 172
Cdd:PRK02948 81 LNALPQ-NKKHIITTPMEHASIHSYFQSLESQGYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQPIAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 173 IGELCRSKGVYFHTDAAQATGKVPIDVNEMKIDLMSISAHKIYGPKGAGALYVrrRPRVRIEAQMSGGGQERGLRSGTVA 252
Cdd:PRK02948 160 IGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYI--NPQVRWKPVFPGTTHEKGFRPGTVN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 253 APLCIGLGEAAKIADKEMAMDKAHVERLSQMLINGISDK-LPhIIRNGDARHAYPGCVNLSFAYVEGESLLMAL--KSIA 329
Cdd:PRK02948 238 VPGIAAFLTAAENILKNMQEESLRFKELRSYFLEQIQTLpLP-IEVEGHSTSCLPHIIGVTIKGIEGQYTMLECnrRGIA 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 25143064 330 LSSGSACTSASLEPSYVLRAIGSEEDLAHSSIRFGLGRFTTDEEVKHTID 379
Cdd:PRK02948 317 ISTGSACQVGKQEPSKTMLAIGKTYEEAKQFVRFSFGQQTTKDQIDTTIH 366
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
7-379 |
8.39e-62 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 204.60 E-value: 8.39e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 7 PGSPQP-IYLDVQATAPMdPR-VVDAMLPYMINDFGNPHSRTHSYGWKAEEGVEQAREHVANLIKA-DPRDIIFTSGATE 83
Cdd:COG0520 10 PVLGKPlVYLDNAATGQK-PRpVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAaSPDEIIFTRGTTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 84 SNNLAIKGVAKFRKqsgKNHIITLQTEHKCVLDSCRYL-ENEGFKVTYLPVDKGGMVDMEQLTQSITAETCLVSIMFVNN 162
Cdd:COG0520 89 AINLVAYGLGRLKP---GDEILITEMEHHSNIVPWQELaERTGAEVRVIPLDEDGELDLEALEALLTPRTKLVAVTHVSN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 163 EIGVMQPIKQIGELCRSKGVYFHTDAAQATGKVPIDVNEMKIDLMSISAHKIYGPKGAGALYVRRRPRVRIEAQMSGGG- 241
Cdd:COG0520 166 VTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELLEALPPFLGGGGm 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 242 -----------QERGLR--SGTVAAPLCIGLGEAAKIADkEMAMDK--AHVERLSQMLINGISdKLPHIIRNGDARHAYP 306
Cdd:COG0520 246 iewvsfdgttyADLPRRfeAGTPNIAGAIGLGAAIDYLE-AIGMEAieARERELTAYALEGLA-AIPGVRILGPADPEDR 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25143064 307 GCVnLSFaYVEG------ESLLMALKsIALSSGSACTsaslEPsyVLRAIGseedlAHSSIRFGLGRFTTDEEVKHTID 379
Cdd:COG0520 324 SGI-VSF-NVDGvhphdvAALLDDEG-IAVRAGHHCA----QP--LMRRLG-----VPGTVRASFHLYNTEEEIDRLVE 388
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
13-374 |
1.48e-61 |
|
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: 203.08 E-value: 1.48e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 13 IYLDVQATAPMDPRVVDAMLPYMINDFGNPHSRTHSYGWKAEEGVEQAREHVANLIKA-DPRDIIFTSGATESNNLAIKG 91
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINApSPDEIIFTRNTTEAINLVAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 92 VAKfRKQSGkNHIITLQTEHKCVLDSCRYLENE-GFKVTYLPVDKGGMVDMEQLTQSITAETCLVSIMFVNNEIGVMQPI 170
Cdd:cd06453 81 LGR-ANKPG-DEIVTSVMEHHSNIVPWQQLAERtGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 171 KQIGELCRSKGVYFHTDAAQATGKVPIDVNEMKIDLMSISAHKIYGPKGAGALYVRRRPRVRIEAQMSGGGQ-ERGLRSG 249
Cdd:cd06453 159 KEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMiEEVSFEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 250 TVAAPL-------------CIGLGEAAKIADKeMAMDK--AHVERLSQMLINGISDkLPHIIRNGDARHAYPGcvnLSFA 314
Cdd:cd06453 239 TTYADLphkfeagtpniagAIGLGAAIDYLEK-IGMEAiaAHEHELTAYALERLSE-IPGVRVYGDAEDRAGV---VSFN 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25143064 315 yVEG---ESLLMAL--KSIALSSGSACTsaslEPsyVLRAIGseedlAHSSIRFGLGRFTTDEEV 374
Cdd:cd06453 314 -LEGihpHDVATILdqYGIAVRAGHHCA----QP--LMRRLG-----VPGTVRASFGLYNTEEEI 366
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
13-242 |
8.47e-32 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 124.77 E-value: 8.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 13 IYLDVQATApMDPR-VVDAMLPYMINDFGNPHSRTHSYGWKAEEGVEQAREHVANLIKA-DPRDIIFTSGATESNNLAIK 90
Cdd:PRK10874 21 VYLDSAATA-LKPQaVIEATQQFYSLSAGNVHRSQFAAAQRLTARYEAAREQVAQLLNApDAKNIVWTRGTTESINLVAQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 91 GVAKFRKQSGkNHIITLQTEHKCVLdsCRYL---ENEGFKVTYLPVDKGGMVDMEQLTQSITAETCLVSIMFVNNEIGVM 167
Cdd:PRK10874 100 SYARPRLQPG-DEIIVSEAEHHANL--VPWLmvaQQTGAKVVKLPLGADRLPDVDLLPELITPRTRILALGQMSNVTGGC 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25143064 168 QPIKQIGELCRSKGVYFHTDAAQATGKVPIDVNEMKIDLMSISAHKIYGPKGAGALYVRRrprvRIEAQMS---GGGQ 242
Cdd:PRK10874 177 PDLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKS----ELLEAMSpwqGGGK 250
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
13-337 |
3.13e-30 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 120.62 E-value: 3.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 13 IYLDVQATAPMDPRVVDAMLPY--MINdfGNPHSRTHSYGWKAEEGVEQAREHVANLIKA-DPRDIIFTSGATESNNLAI 89
Cdd:PLN02855 34 VYLDNAATSQKPAAVLDALQDYyeEYN--SNVHRGIHALSAKATDAYELARKKVAAFINAsTSREIVFTRNATEAINLVA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 90 K--GVAKFrkQSGKNHIITLQTEHKCVLDSCRYLENEGFKVTYLPVDKGGMVDMEQLTQSITAETCLVSIMFVNNEIGVM 167
Cdd:PLN02855 112 YtwGLANL--KPGDEVILSVAEHHSNIVPWQLVAQKTGAVLKFVGLTPDEVLDVEQLKELLSEKTKLVATHHVSNVLGSI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 168 QPIKQIGELCRSKGVYFHTDAAQATGKVPIDVNEMKIDLMSISAHKIYGPKGAGALYVRRRPRVRIEAQMSGGG------ 241
Cdd:PLN02855 190 LPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLWGKSDLLESMPPFLGGGEmisdvf 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 242 ------QERGLR--SGTVAAPLCIGLGEAA---------KIADKEMAMDKAHVERLSQmlINGISDKLPhiiRNGDARHA 304
Cdd:PLN02855 270 ldhstyAPPPSRfeAGTPAIGEAIGLGAAIdylseigmdRIHEYEVELGTYLYEKLSS--VPGVRIYGP---KPSEGVGR 344
|
330 340 350
....*....|....*....|....*....|....*....
gi 25143064 305 YPGCvnlSFAyVEG------ESLLMALKSIALSSGSACT 337
Cdd:PLN02855 345 AALC---AFN-VEGihptdlSTFLDQQHGVAIRSGHHCA 379
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
11-227 |
4.61e-26 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 108.69 E-value: 4.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 11 QPI-YLDVQATAPMDPRVVDAMLPYMINDFGNPHSRTHSYGWKAEEGVEQAREHVANLIKA-DPRDIIFTSGATESNNLA 88
Cdd:PRK09295 22 LPLaYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKQAALFINArSAEELVFVRGTTEGINLV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 89 IKGVAKFRKQSGKNHIITLQTEHKCVLDSCRYLENEGFKVTYLPVDKGGMVDMEQLTQSITAETCLVSIMFVNNEIGVMQ 168
Cdd:PRK09295 102 ANSWGNSNVRAGDNIIISEMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPALFDERTRLLAITHVSNVLGTEN 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 25143064 169 PIKQIGELCRSKGVYFHTDAAQATGKVPIDVNEMKIDLMSISAHKIYGPKGAGALYVRR 227
Cdd:PRK09295 182 PLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKE 240
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
58-227 |
6.33e-15 |
|
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: 76.43 E-value: 6.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 58 EQAREHVANLIKA-DPRDIIFTSGATESNNLaikgVAKfrkqS-GKNH------IITLQTEH-------------Kcvld 116
Cdd:NF041166 292 EGAREKVRRFIGApSVDEIIFVRGTTEAINL----VAK----SwGRQNigagdeIIVSHLEHhanivpwqqlaqeT---- 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 117 scryleneGFKVTYLPVDKGGMVDMEQLTQSITAETCLVSIMFVNNEIGVMQPIKQIGELCRSKGVYFHTDAAQATGKVP 196
Cdd:NF041166 360 --------GAKLRVIPVDDSGQILLDEYAKLLNPRTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMP 431
|
170 180 190
....*....|....*....|....*....|.
gi 25143064 197 IDVNEMKIDLMSISAHKIYGPKGAGALYVRR 227
Cdd:NF041166 432 VDVQALDADFFVFSGHKVFGPTGIGVVYGKR 462
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
57-226 |
1.49e-12 |
|
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: 65.48 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 57 VEQAREHVANLIKADPRDIIFTSGATESNNLAIKGVAKFRKqsgknHIITLQTEHKCVLDScrYLENEGFKVTYLPVDKG 136
Cdd:cd01494 2 LEELEEKLARLLQPGNDKAVFVPSGTGANEAALLALLGPGD-----EVIVDANGHGSRYWV--AAELAGAKPVPVPVDDA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 137 GMVDMEQLT---QSITAETCLVSIMFVNNEIGVMQPIKQIGELCRSKGVYFHTDAAQATGKVP---IDVNEMKIDLMSIS 210
Cdd:cd01494 75 GYGGLDVAIleeLKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPapgVLIPEGGADVVTFS 154
|
170
....*....|....*.
gi 25143064 211 AHKIYGPKGAGALYVR 226
Cdd:cd01494 155 LHKNLGGEGGGVVIVK 170
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
64-226 |
4.86e-12 |
|
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: 66.84 E-value: 4.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 64 VANLIKADPRDI--IFTSGATESNNLAIKgVAKFRKQS----------GKNHIITLQTEHKCVLDSCRYLENegfKVTYL 131
Cdd:cd06450 47 LAKLFGLPSEDAdgVFTSGGSESNLLALL-AARDRARKrlkagggrgiDKLVIVCSDQAHVSVEKAAAYLDV---KVRLV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 132 PVDKGGMVDMEQLTQSI--TAETCLVSIMFV----NNEIGVMQPIKQIGELCRSKGVYFHTDAAQATGKVPIDVNEMKID 205
Cdd:cd06450 123 PVDEDGRMDPEALEAAIdeDKAEGLNPIMVVatagTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDF 202
|
170 180
....*....|....*....|....*....
gi 25143064 206 ----LMSISA--HKiYG--PKGAGALYVR 226
Cdd:cd06450 203 gierVDSISVdpHK-YGlvPLGCSAVLVR 230
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
76-228 |
1.33e-11 |
|
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: 66.01 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 76 IFTSGATESNNLAIKgVAK--FRKQSGKNH---------IITLQTEHKCVLDSCRYLENEGFKVTYLPVDKGGMVDMEQL 144
Cdd:COG0076 129 VFTSGGTEANLLALL-AARdrALARRVRAEglpgaprprIVVSEEAHSSVDKAARLLGLGRDALRKVPVDEDGRMDPDAL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 145 TQSITA--ETCLVSIMFV----NNEIGVMQPIKQIGELCRSKGVYFHTDAA-------QATGKVPIDvnemKIDL---MS 208
Cdd:COG0076 208 EAAIDEdrAAGLNPIAVVatagTTNTGAIDPLAEIADIAREHGLWLHVDAAyggfalpSPELRHLLD----GIERadsIT 283
|
170 180
....*....|....*....|..
gi 25143064 209 ISAHKiYG--PKGAGALYVRRR 228
Cdd:COG0076 284 VDPHK-WLyvPYGCGAVLVRDP 304
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
125-288 |
1.58e-09 |
|
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: 59.23 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 125 GFKVTYLPVDKGGMVDMEQLTQSITAETcLVSIMFVNNE--IGVMQPIKQIGELCRSKGVYFHTDAAQATGKVPIDVNEM 202
Cdd:cd06451 97 GADVDVVEKPWGEAVSPEEIAEALEQHD-IKAVTLTHNEtsTGVLNPLEGIGALAKKHDALLIVDAVSSLGGEPFRMDEW 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 203 KIDLMSISAHKIYG-PKGAGALYVRRRPRVRIEAQMS-----------GGGQERGLRS-GTVAAPLCIGLGEAAKIADKE 269
Cdd:cd06451 176 GVDVAYTGSQKALGaPPGLGPIAFSERALERIKKKTKpkgfyfdllllLKYWGEGYSYpHTPPVNLLYALREALDLILEE 255
|
170 180
....*....|....*....|.
gi 25143064 270 mAMDK--AHVERLSQMLINGI 288
Cdd:cd06451 256 -GLENrwARHRRLAKALREGL 275
|
|
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
11-253 |
4.45e-08 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 55.26 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 11 QPIYLD-VQATAPMDPRVVDAMLPYMINDFGNPHSRTHSyGWKAEEGVEQAREHVANLIKADPRD--IIFTSGATEsnnl 87
Cdd:PLN02724 34 GVVYLDhAGATLYSESQLEAALADFSSNVYGNPHSQSDS-SMRSSDTIESARQQVLEYFNAPPSDyaCVFTSGATA---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 88 AIKGVAK-FRKQSGKNHIITLQTeHKCVLDSCRYLENEGFKVTYL--------PVDKGGMVDME------------QLTQ 146
Cdd:PLN02724 109 ALKLVGEtFPWSSESHFCYTLEN-HNSVLGIREYALEKGAAAIAVdieeaanqPTNSQGSVVVKsrglqrrntsklQKRE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 147 SITAETCLVSIMFVNNEIGVMQPIKQIGELCRSKGVYFHT--------DAAQATGKVPIDVNEMKIDLMSISAHKIYG-P 217
Cdd:PLN02724 188 DDGEAYNLFAFPSECNFSGAKFPLDLVKLIKDNQHSNFSKsgrwmvllDAAKGCGTSPPDLSRYPADFVVVSFYKIFGyP 267
|
250 260 270
....*....|....*....|....*....|....*.
gi 25143064 218 KGAGALYVRRRPRVRIEAQMSGGgqerglrsGTVAA 253
Cdd:PLN02724 268 TGLGALLVRRDAAKLLKKKYFGG--------GTVAA 295
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
48-283 |
6.08e-06 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 47.60 E-value: 6.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 48 SYGwkAEEGVEQAREHVANLIKADPrdIIFTSGATESNNLAIKGVAKfRKQSgknhIITLQTEHKCvLDSCRYL-ENEGF 126
Cdd:pfam01212 27 VYG--GDPTVNRLEDRVAELFGKEA--ALFVPSGTAANQLALMAHCQ-RGDE----VICGEPAHIH-FDETGGHaELGGV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 127 KVTYLPVDKGGMVDMEQL-------TQSITAETCLVSIMFVNNEIG----VMQPIKQIGELCRSKGVYFHTDAAQ---AT 192
Cdd:pfam01212 97 QPRPLDGDEAGNMDLEDLeaairevGADIFPPTGLISLENTHNSAGgqvvSLENLREIAALAREHGIPVHLDGARfanAA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 193 GKVPIDVNEMK--IDLMSISahkiyGPKGAGAL----------YVRRRPRVRieaQMSGGgqerGLR-SGTVAAPLCIGL 259
Cdd:pfam01212 177 VALGVIVKEITsyADSVTMC-----LSKGLGAPvgsvlagsddFIAKAIRQR---KYLGG----GLRqAGVLAAAGLRAL 244
|
250 260
....*....|....*....|....
gi 25143064 260 GEAAKIADKEMAMDKAHVERLSQM 283
Cdd:pfam01212 245 EEGVARLARDHATARRLAEGLELL 268
|
|
| PRK07324 |
PRK07324 |
transaminase; Validated |
48-210 |
1.16e-05 |
|
transaminase; Validated
Pssm-ID: 235989 Cd Length: 373 Bit Score: 47.24 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 48 SYGWKaeEGVEQAREHVANLIK-ADPRDIIFTSGATESNNLAIKGVAKfrkqsGKNHIITlqtehkcVLDSCRYL----E 122
Cdd:PRK07324 57 TYGWI--EGSPEFKEAVASLYQnVKPENILQTNGATGANFLVLYALVE-----PGDHVIS-------VYPTYQQLydipE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 123 NEGFKVTYLPV--DKGGMVDMEQLTQSITAETCLVSIMFVNNEIG-VMQP--IKQIGELCRSKG-------VYFHTDAAQ 190
Cdd:PRK07324 123 SLGAEVDYWQLkeENGWLPDLDELRRLVRPNTKLICINNANNPTGaLMDRayLEEIVEIARSVDayvlsdeVYRPLDEDG 202
|
170 180
....*....|....*....|
gi 25143064 191 ATGKVpIDVNEMKIDLMSIS 210
Cdd:PRK07324 203 STPSI-ADLYEKGISTNSMS 221
|
|
| PRK04366 |
PRK04366 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPB; |
125-232 |
5.52e-05 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPB;
Pssm-ID: 235292 Cd Length: 481 Bit Score: 45.10 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 125 GFKVTYLPVDKGGMVDMEQLTQSITAETClvSIMFVN-NEIGVMQP-IKQIGELCRSKGVYFHTDAAQAT---GKV-PID 198
Cdd:PRK04366 182 GFKVVEIPSNEDGLVDLEALKAAVGEDTA--ALMLTNpNTLGLFERnILEIAEIVHEAGGLLYYDGANLNailGKArPGD 259
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 25143064 199 vneMKIDLMSISAHKIY-------GPkGAGALYVRRR-------PRVR 232
Cdd:PRK04366 260 ---MGFDVVHLNLHKTFstphgggGP-GSGPVGVKEElapflpvPVVE 303
|
|
| GDC-P |
cd00613 |
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ... |
91-221 |
1.08e-04 |
|
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine cleavage system P-proteins EC:1.4.4.2 from bacterial, mammalian and plant sources. The P protein is part of the glycine decarboxylase multienzyme complex EC:2.1.2.10 (GDC) also annotated as glycine cleavage system or glycine synthase. GDC consists of four proteins P, H, L and T. The reaction catalysed by this protein is: Glycine + lipoylprotein <=> S-aminomethyldihydrolipoylprotein + CO2. Alpha-beta-type dimers associate to form an alpha(2)beta(2) tetramer, where the alpha- and beta-subunits are structurally similar and appear to have arisen by gene duplication and subsequent divergence with a loss of one active site. The members of this CD are widely dispersed among all three forms of cellular life.
Pssm-ID: 99737 [Multi-domain] Cd Length: 398 Bit Score: 44.14 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 91 GVAKFRKQSGKNHIITLQTEHKCVLDSCR-YLENEGFKVTYLPVDKGGMVDMEQLTQSITAETclVSIMFVN-NEIGVM- 167
Cdd:cd00613 98 GLAAIRAYHKRNKVLVPDSAHPTNPAVARtRGEPLGIEVVEVPSDEGGTVDLEALKEEVSEEV--AALMVQYpNTLGVFe 175
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 25143064 168 QPIKQIGELCRSKGVYFHTDAA--QATGKVPidVNEMKIDLMSISAHKIYGPKGAG 221
Cdd:cd00613 176 DLIKEIADIAHSAGALVYVDGDnlNLTGLKP--PGEYGADIVVGNLQKTGVPHGGG 229
|
|
| PRK13479 |
PRK13479 |
2-aminoethylphosphonate--pyruvate transaminase; Provisional |
165-227 |
1.20e-04 |
|
2-aminoethylphosphonate--pyruvate transaminase; Provisional
Pssm-ID: 184076 [Multi-domain] Cd Length: 368 Bit Score: 43.75 E-value: 1.20e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25143064 165 GVMQPIKQIGELCRSKGVYFHTDAAQATGKVPIDVNEMKIDLMSISAHK-IYGPKGAGALYVRR 227
Cdd:PRK13479 145 GILNPLDEIAAVAKRHGKRLIVDAMSSFGAIPIDIAELGIDALISSANKcIEGVPGFGFVIARR 208
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
76-238 |
5.86e-03 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 38.55 E-value: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 76 IFTSGATESNNLAIKGvAKFR-----KQSGKNH----------IITLQTEHKCVLDSCRYLeneGFKVTYLPVDKGGMVD 140
Cdd:pfam00282 106 VLQPGSSESNLLALLA-ARTKwikrmKAAGKPAdssgilaklvAYTSDQAHSSIEKAALYG---GVKLREIPSDDNGKMR 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 141 MEQLTQSITA--ETCLVsIMFVNNEIGV-----MQPIKQIGELCRSKGVYFHTDAAQATGKV------PIDVNEMKIDLM 207
Cdd:pfam00282 182 GMDLEKAIEEdkENGLI-PFFVVATLGTtgsgaFDDLQELGDICAKHNLWLHVDAAYGGSAFicpefrHWLFGIERADSI 260
|
170 180 190
....*....|....*....|....*....|..
gi 25143064 208 SISAHKIYG-PKGAGALYVRRRPRVRIEAQMS 238
Cdd:pfam00282 261 TFNPHKWMLvLLDCSAVWVKDKEALQQAFQFN 292
|
|
| PRK00451 |
PRK00451 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPA; |
100-184 |
6.09e-03 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
Pssm-ID: 234769 [Multi-domain] Cd Length: 447 Bit Score: 38.58 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 100 GKNHII---TLQTEHKCVLDScrYLENEGFKVTYLPVDKgGMVDMEQLTQSITAETCLVsIMFVNNEIGVMQPIKQIGEL 176
Cdd:PRK00451 153 KRKKVLvsgAVHPEYREVLKT--YLKGQGIEVVEVPYED-GVTDLEALEAAVDDDTAAV-VVQYPNFFGVIEDLEEIAEI 228
|
....*...
gi 25143064 177 CRSKGVYF 184
Cdd:PRK00451 229 AHAGGALF 236
|
|
| PRK09331 |
PRK09331 |
Sep-tRNA:Cys-tRNA synthetase; Provisional |
154-213 |
9.45e-03 |
|
Sep-tRNA:Cys-tRNA synthetase; Provisional
Pssm-ID: 236469 Cd Length: 387 Bit Score: 37.99 E-value: 9.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143064 154 LVSIMFVNNEIGVMQPIKQIGELCRSKGVYFHTDAAQATGKVPIDVNEMKIDLMSISAHK 213
Cdd:PRK09331 161 LALLTHVDGNYGNLADAKKVAKVAHEYGIPFLLNGAYTVGRMPVDGKKLGADFIVGSGHK 220
|
|
| |
