|
Name |
Accession |
Description |
Interval |
E-value |
| Bna5 |
COG3844 |
Kynureninase [Amino acid transport and metabolism]; |
1-416 |
0e+00 |
|
Kynureninase [Amino acid transport and metabolism];
Pssm-ID: 443054 [Multi-domain] Cd Length: 420 Bit Score: 665.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 1 MKTREEALALDRDDPLAPLREQFALP-AGVIYLDGNSLGAQPRAAAARAQQVIGAEWGEGLIRSWNTAGWFALPRRLGDR 79
Cdd:COG3844 2 ETTRAFARALDAADPLAAFRDRFHLPdDGVIYLDGNSLGLLPKAAAARLAEVLEEEWGELLIRGWNEAPWFDLPERLGDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 80 LAPLIGAADGEVAITDTISINLFKLLAAMLRHQarhaPKRRVIVSERSNFPTDLYIAQGLIAQLDRDYELRLID------ 153
Cdd:COG3844 82 LARLVGAAPGEVVVMDSTTVNLHKLLVAAYRPR----PGRTKILSEADNFPTDRYALEGQARLHGLDEELRLVEprdget 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 154 -DPADLPDALDDETAVAMITHVNYRTGYMHDMPSVTQTVRQAGALMLWDLAHSAGAVPVDLNGALADGAVGCTYKYLNGG 232
Cdd:COG3844 158 lRPEDIEAALDDDVALVLLSHVNYRTGQLFDMAAITAAAHAAGALVGWDLAHSAGAVPVDLHDWGVDFAVGCTYKYLNGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 233 PGSPAFVWVPKRHQRAFEQPLSGWWGHRAPFAMQPAFEPDPGIARFLCGTQPIVSMSMVECGLDVFAQTDMHAIRRKSLA 312
Cdd:COG3844 238 PGAPAFLYVHERHQDRLLQPLAGWWGHATPFAMEPGYEPAPGARRFQLGTPPILSMAALEASLDLFEEAGMDALRAKSLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 313 LTDAFVALVESRCAGQPLKLVTPRAHHQRGSQASFEHPHGYEVMQALIARGVIGDYREPRILRFGFTPLYTRFVDVWDAV 392
Cdd:COG3844 318 LTDYLIFLVEERLAPLGLELITPRDPARRGSQVSLRHPEAYAIFQALIERGVIGDFREPDVIRFGPTPLYTSFEDVWRAV 397
|
410 420
....*....|....*....|....
gi 490657658 393 ETLRDILDTEAWRAPEfATRAAVT 416
Cdd:COG3844 398 EILREILEEGEWEKFE-NERGAVT 420
|
|
| kynureninase |
TIGR01814 |
kynureninase; This model describes kynureninase, a pyridoxal-phosphate enzyme. Kynurinine is a ... |
7-400 |
6.26e-144 |
|
kynureninase; This model describes kynureninase, a pyridoxal-phosphate enzyme. Kynurinine is a Trp breakdown product and a precursor for NAD. In Chlamydia psittaci, an obligate intracellular pathogen, kynureninase makes anthranilate, a Trp precursor, from kynurenine. This counters the tryptophan hydrolysis that occurs in the host cell in response to the pathogen. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130873 [Multi-domain] Cd Length: 406 Bit Score: 415.67 E-value: 6.26e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 7 ALALDRDDPLAPLREQFALPAG-----VIYLDGNSLGAQPRAAAARAQQVIGaEWGEGLIRSWNT--AGWFALPRRLGDR 79
Cdd:TIGR01814 1 ALELDEADPLRALRDEFHLPKIgdenaVIYLDGNSLGLMPKAARNALKEELD-KWAKIAIRGHNTgkAPWFTLDESLLKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 80 LAplIGAADGEVAITDTISINLFKLLAAMLRHqarhAPKRRVIVSERSNFPTDLYIAQGLI-------------AQLDRD 146
Cdd:TIGR01814 80 RL--VGAKEDEVVVMNTLTINLHLLLASFYKP----TPKRYKILLEAKAFPSDHYAIESQLqlhgltveesmvqIEPREE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 147 YELRLIDDPaDLPDALDDETAVAMITHVNYRTGYMHDMPSVTQTVRQAGALMLWDLAHSAGAVPVDLNGALADGAVGCTY 226
Cdd:TIGR01814 154 ETLRLEDIL-DTIEKNGDDIAVILLSGVQYYTGQLFDMAAITRAAHAKGALVGFDLAHAVGNVPLDLHDWGVDFACWCTY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 227 KYLNGGPGSPAFVWVPKRHQRAFEQPlsGWWGHRAP--FAMQPAFEPDPGiARFLCgTQPIVSMSMVECGLDVFAQTDMH 304
Cdd:TIGR01814 233 KYLNAGPGAGAFVHEKHAHTERPRLA--GWWGHARPtrFKMDNTLGLIPC-GFRIS-NPPILSVAALRGSLDIFDQAGME 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 305 AIRRKSLALTDAFVALVESRCAGQP-LKLVTPRAHHQRGSQASFEHP-HGYEVMQALIARGVIGDYREPRILRFGFTPLY 382
Cdd:TIGR01814 309 ALRKKSLLLTDYLEELIKARCGGPPvLTIITPRDHAQRGCQLSLTHPvPGKAVFQALIKRGVIGDKREPSVIRVAPVPLY 388
|
410
....*....|....*...
gi 490657658 383 TRFVDVWDAVETLRDILD 400
Cdd:TIGR01814 389 NTFVDVYDAVNVLEEILD 406
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
78-364 |
1.32e-09 |
|
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: 59.18 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 78 DRLAPLIGAADG-EVAITD--TISINLFkllAAMLRHQARhaPKRRVIVSE---RSNFPTDLYIAQgliaqlDRDYELRL 151
Cdd:pfam00266 50 EKVAEFINAPSNdEIIFTSgtTEAINLV---ALSLGRSLK--PGDEIVITEmehHANLVPWQELAK------RTGARVRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 152 ID-------DPADLPDALDDETAVAMITHVNYRTGYMHDMPSVTQTVRQAGALMLWDLAHSAGAVPVDLNGALADGAVGC 224
Cdd:pfam00266 119 LPldedgllDLDELEKLITPKTKLVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 225 TYKYLngGPGSPAFVWVPKRHQRAFEQPLSGwwG--------HRAPFAMQPafepdpgiARFLCGTQPIVSMSMVECGLD 296
Cdd:pfam00266 199 GHKLY--GPTGIGVLYGRRDLLEKMPPLLGG--GgmietvslQESTFADAP--------WKFEAGTPNIAGIIGLGAALE 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 297 VFAQTDMHAIRRKSLALTDAFVALVESrcagqpLKLVTPRAHHQRGSQASFEHP--HGYEVMQALIARGV 364
Cdd:pfam00266 267 YLSEIGLEAIEKHEHELAQYLYERLLS------LPGIRLYGPERRASIISFNFKgvHPHDVATLLDESGI 330
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
78-364 |
1.07e-08 |
|
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: 56.71 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 78 DRLAPLIGAAD-GEVAITD--TISINLfkLLAAMLRhqaRHAPKRRVIVSE---RSNFPTDLYIA--QGL---IAQLDRD 146
Cdd:cd06453 50 EKVARFINAPSpDEIIFTRntTEAINL--VAYGLGR---ANKPGDEIVTSVmehHSNIVPWQQLAerTGAklkVVPVDDD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 147 YELrlidDPADLPDALDDETAVAMITHVNYRTGYMHDMPSVTQTVRQAGALMLWDLAHSAGAVPVDLNgaladgAVGCTY 226
Cdd:cd06453 125 GQL----DLEALEKLLTERTKLVAVTHVSNVLGTINPVKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQ------DLGCDF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 227 ------KYLnGGPGSpAFVWVPKRHQRAFEQPLSGwwGHRAPFAMQPAFEPDPGIARFLCGTQPIVSMSMVECGLDVFAQ 300
Cdd:cd06453 195 lafsghKML-GPTGI-GVLYGKEELLEEMPPYGGG--GEMIEEVSFEETTYADLPHKFEAGTPNIAGAIGLGAAIDYLEK 270
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490657658 301 TDMHAIRRKSLALTDAFVAlvesRCAGQP-LKLVTPRAHhqRGSQASFE----HPHgyEVMQALIARGV 364
Cdd:cd06453 271 IGMEAIAAHEHELTAYALE----RLSEIPgVRVYGDAED--RAGVVSFNlegiHPH--DVATILDQYGI 331
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
79-255 |
3.46e-05 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 45.42 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 79 RLAPLIGAADGEVAITD--TISINLFKLLAAMLRHQarhapKRRVIVSERSNFPTDL----YIAQGLIaqldrDYELRLI 152
Cdd:PLN02651 51 QVAALIGADPKEIIFTSgaTESNNLAIKGVMHFYKD-----KKKHVITTQTEHKCVLdscrHLQQEGF-----EVTYLPV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 153 D-----DPADLPDALDDETAVAMITHVNYRTGYMHDMPSVTQTVRQAGALMLWDLAHSAGAVPVDLNGALADGAVGCTYK 227
Cdd:PLN02651 121 KsdglvDLDELAAAIRPDTALVSVMAVNNEIGVIQPVEEIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHK 200
|
170 180
....*....|....*....|....*...
gi 490657658 228 YlnGGPGSPAFVWVPKRHQRAFEQPLSG 255
Cdd:PLN02651 201 I--YGPKGVGALYVRRRPRVRLEPLMSG 226
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Bna5 |
COG3844 |
Kynureninase [Amino acid transport and metabolism]; |
1-416 |
0e+00 |
|
Kynureninase [Amino acid transport and metabolism];
Pssm-ID: 443054 [Multi-domain] Cd Length: 420 Bit Score: 665.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 1 MKTREEALALDRDDPLAPLREQFALP-AGVIYLDGNSLGAQPRAAAARAQQVIGAEWGEGLIRSWNTAGWFALPRRLGDR 79
Cdd:COG3844 2 ETTRAFARALDAADPLAAFRDRFHLPdDGVIYLDGNSLGLLPKAAAARLAEVLEEEWGELLIRGWNEAPWFDLPERLGDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 80 LAPLIGAADGEVAITDTISINLFKLLAAMLRHQarhaPKRRVIVSERSNFPTDLYIAQGLIAQLDRDYELRLID------ 153
Cdd:COG3844 82 LARLVGAAPGEVVVMDSTTVNLHKLLVAAYRPR----PGRTKILSEADNFPTDRYALEGQARLHGLDEELRLVEprdget 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 154 -DPADLPDALDDETAVAMITHVNYRTGYMHDMPSVTQTVRQAGALMLWDLAHSAGAVPVDLNGALADGAVGCTYKYLNGG 232
Cdd:COG3844 158 lRPEDIEAALDDDVALVLLSHVNYRTGQLFDMAAITAAAHAAGALVGWDLAHSAGAVPVDLHDWGVDFAVGCTYKYLNGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 233 PGSPAFVWVPKRHQRAFEQPLSGWWGHRAPFAMQPAFEPDPGIARFLCGTQPIVSMSMVECGLDVFAQTDMHAIRRKSLA 312
Cdd:COG3844 238 PGAPAFLYVHERHQDRLLQPLAGWWGHATPFAMEPGYEPAPGARRFQLGTPPILSMAALEASLDLFEEAGMDALRAKSLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 313 LTDAFVALVESRCAGQPLKLVTPRAHHQRGSQASFEHPHGYEVMQALIARGVIGDYREPRILRFGFTPLYTRFVDVWDAV 392
Cdd:COG3844 318 LTDYLIFLVEERLAPLGLELITPRDPARRGSQVSLRHPEAYAIFQALIERGVIGDFREPDVIRFGPTPLYTSFEDVWRAV 397
|
410 420
....*....|....*....|....
gi 490657658 393 ETLRDILDTEAWRAPEfATRAAVT 416
Cdd:COG3844 398 EILREILEEGEWEKFE-NERGAVT 420
|
|
| kynureninase |
TIGR01814 |
kynureninase; This model describes kynureninase, a pyridoxal-phosphate enzyme. Kynurinine is a ... |
7-400 |
6.26e-144 |
|
kynureninase; This model describes kynureninase, a pyridoxal-phosphate enzyme. Kynurinine is a Trp breakdown product and a precursor for NAD. In Chlamydia psittaci, an obligate intracellular pathogen, kynureninase makes anthranilate, a Trp precursor, from kynurenine. This counters the tryptophan hydrolysis that occurs in the host cell in response to the pathogen. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130873 [Multi-domain] Cd Length: 406 Bit Score: 415.67 E-value: 6.26e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 7 ALALDRDDPLAPLREQFALPAG-----VIYLDGNSLGAQPRAAAARAQQVIGaEWGEGLIRSWNT--AGWFALPRRLGDR 79
Cdd:TIGR01814 1 ALELDEADPLRALRDEFHLPKIgdenaVIYLDGNSLGLMPKAARNALKEELD-KWAKIAIRGHNTgkAPWFTLDESLLKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 80 LAplIGAADGEVAITDTISINLFKLLAAMLRHqarhAPKRRVIVSERSNFPTDLYIAQGLI-------------AQLDRD 146
Cdd:TIGR01814 80 RL--VGAKEDEVVVMNTLTINLHLLLASFYKP----TPKRYKILLEAKAFPSDHYAIESQLqlhgltveesmvqIEPREE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 147 YELRLIDDPaDLPDALDDETAVAMITHVNYRTGYMHDMPSVTQTVRQAGALMLWDLAHSAGAVPVDLNGALADGAVGCTY 226
Cdd:TIGR01814 154 ETLRLEDIL-DTIEKNGDDIAVILLSGVQYYTGQLFDMAAITRAAHAKGALVGFDLAHAVGNVPLDLHDWGVDFACWCTY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 227 KYLNGGPGSPAFVWVPKRHQRAFEQPlsGWWGHRAP--FAMQPAFEPDPGiARFLCgTQPIVSMSMVECGLDVFAQTDMH 304
Cdd:TIGR01814 233 KYLNAGPGAGAFVHEKHAHTERPRLA--GWWGHARPtrFKMDNTLGLIPC-GFRIS-NPPILSVAALRGSLDIFDQAGME 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 305 AIRRKSLALTDAFVALVESRCAGQP-LKLVTPRAHHQRGSQASFEHP-HGYEVMQALIARGVIGDYREPRILRFGFTPLY 382
Cdd:TIGR01814 309 ALRKKSLLLTDYLEELIKARCGGPPvLTIITPRDHAQRGCQLSLTHPvPGKAVFQALIKRGVIGDKREPSVIRVAPVPLY 388
|
410
....*....|....*...
gi 490657658 383 TRFVDVWDAVETLRDILD 400
Cdd:TIGR01814 389 NTFVDVYDAVNVLEEILD 406
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
78-364 |
1.08e-18 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 87.12 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 78 DRLAPLIGAAD-GEVAITD--TISINLfklLAAMLrhqARHAPKRRVIVSER---SNFPTDLYIAQGLIAQL-----DRD 146
Cdd:COG0520 66 EKVARFIGAASpDEIIFTRgtTEAINL---VAYGL---GRLKPGDEILITEMehhSNIVPWQELAERTGAEVrviplDED 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 147 YELrlidDPADLPDALDDETAVAMITHVNYRTGYMHDMPSVTQTVRQAGALMLWDLAHSAGAVPVDLNGALADGAVGCTY 226
Cdd:COG0520 140 GEL----DLEALEALLTPRTKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGH 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 227 KYlnGGPGSPAFVWVPKRHQRAFEQPLSGwwGHRAPFAMQPAFEPDPGIARFLCGTQPIVSMSMVECGLDVFAQTDMHAI 306
Cdd:COG0520 216 KL--YGPTGIGVLYGKRELLEALPPFLGG--GGMIEWVSFDGTTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAI 291
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490657658 307 RRKSLALTDAFVAlvesRCAGQP-LKLVTPRAHHQRGSQASFE----HPHgyEVMQALIARGV 364
Cdd:COG0520 292 EARERELTAYALE----GLAAIPgVRILGPADPEDRSGIVSFNvdgvHPH--DVAALLDDEGI 348
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
78-364 |
1.32e-09 |
|
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: 59.18 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 78 DRLAPLIGAADG-EVAITD--TISINLFkllAAMLRHQARhaPKRRVIVSE---RSNFPTDLYIAQgliaqlDRDYELRL 151
Cdd:pfam00266 50 EKVAEFINAPSNdEIIFTSgtTEAINLV---ALSLGRSLK--PGDEIVITEmehHANLVPWQELAK------RTGARVRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 152 ID-------DPADLPDALDDETAVAMITHVNYRTGYMHDMPSVTQTVRQAGALMLWDLAHSAGAVPVDLNGALADGAVGC 224
Cdd:pfam00266 119 LPldedgllDLDELEKLITPKTKLVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 225 TYKYLngGPGSPAFVWVPKRHQRAFEQPLSGwwG--------HRAPFAMQPafepdpgiARFLCGTQPIVSMSMVECGLD 296
Cdd:pfam00266 199 GHKLY--GPTGIGVLYGRRDLLEKMPPLLGG--GgmietvslQESTFADAP--------WKFEAGTPNIAGIIGLGAALE 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 297 VFAQTDMHAIRRKSLALTDAFVALVESrcagqpLKLVTPRAHHQRGSQASFEHP--HGYEVMQALIARGV 364
Cdd:pfam00266 267 YLSEIGLEAIEKHEHELAQYLYERLLS------LPGIRLYGPERRASIISFNFKgvHPHDVATLLDESGI 330
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
78-364 |
1.07e-08 |
|
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: 56.71 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 78 DRLAPLIGAAD-GEVAITD--TISINLfkLLAAMLRhqaRHAPKRRVIVSE---RSNFPTDLYIA--QGL---IAQLDRD 146
Cdd:cd06453 50 EKVARFINAPSpDEIIFTRntTEAINL--VAYGLGR---ANKPGDEIVTSVmehHSNIVPWQQLAerTGAklkVVPVDDD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 147 YELrlidDPADLPDALDDETAVAMITHVNYRTGYMHDMPSVTQTVRQAGALMLWDLAHSAGAVPVDLNgaladgAVGCTY 226
Cdd:cd06453 125 GQL----DLEALEKLLTERTKLVAVTHVSNVLGTINPVKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQ------DLGCDF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 227 ------KYLnGGPGSpAFVWVPKRHQRAFEQPLSGwwGHRAPFAMQPAFEPDPGIARFLCGTQPIVSMSMVECGLDVFAQ 300
Cdd:cd06453 195 lafsghKML-GPTGI-GVLYGKEELLEEMPPYGGG--GEMIEEVSFEETTYADLPHKFEAGTPNIAGAIGLGAAIDYLEK 270
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490657658 301 TDMHAIRRKSLALTDAFVAlvesRCAGQP-LKLVTPRAHhqRGSQASFE----HPHgyEVMQALIARGV 364
Cdd:cd06453 271 IGMEAIAAHEHELTAYALE----RLSEIPgVRVYGDAED--RAGVVSFNlegiHPH--DVATILDQYGI 331
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
79-219 |
5.88e-06 |
|
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: 48.12 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 79 RLAPLIGAADGEVAITD--TISINL-FKLLAAMLRHQARHapkrrVIVS--------------ERSNF-----PTDlyiA 136
Cdd:COG1104 53 QVAALLGADPEEIIFTSggTEANNLaIKGAARAYRKKGKH-----IITSaiehpavletarflEKEGFevtylPVD---E 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 137 QGLIaqldrdyelrlidDPADLPDALDDETAVAMITHVNYRTGYMHDMPSVTQTVRQAGALMLWDLAHSAGAVPVDLNGA 216
Cdd:COG1104 125 DGRV-------------DLEALEAALRPDTALVSVMHANNETGTIQPIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKEL 191
|
...
gi 490657658 217 LAD 219
Cdd:COG1104 192 GVD 194
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
79-255 |
3.46e-05 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 45.42 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 79 RLAPLIGAADGEVAITD--TISINLFKLLAAMLRHQarhapKRRVIVSERSNFPTDL----YIAQGLIaqldrDYELRLI 152
Cdd:PLN02651 51 QVAALIGADPKEIIFTSgaTESNNLAIKGVMHFYKD-----KKKHVITTQTEHKCVLdscrHLQQEGF-----EVTYLPV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 153 D-----DPADLPDALDDETAVAMITHVNYRTGYMHDMPSVTQTVRQAGALMLWDLAHSAGAVPVDLNGALADGAVGCTYK 227
Cdd:PLN02651 121 KsdglvDLDELAAAIRPDTALVSVMAVNNEIGVIQPVEEIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHK 200
|
170 180
....*....|....*....|....*...
gi 490657658 228 YlnGGPGSPAFVWVPKRHQRAFEQPLSG 255
Cdd:PLN02651 201 I--YGPKGVGALYVRRRPRVRLEPLMSG 226
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
154-214 |
5.29e-05 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 44.93 E-value: 5.29e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490657658 154 DPADLPDALDDETAVAMITHVNYRTGYMHDMPSVTQTVRQAGALMLWDLAHSAGAVPVDLN 214
Cdd:PRK14012 133 DLEKLEAAMRDDTILVSIMHVNNEIGVIQDIAAIGEICRERGIIFHVDAAQSVGKVPIDLS 193
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
154-234 |
8.77e-05 |
|
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.
Pssm-ID: 99744 [Multi-domain] Cd Length: 356 Bit Score: 44.20 E-value: 8.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490657658 154 DPADLPDALDDETAVA-MITHVNYRTGYMHDMPSVTQTVRQAGALMLWDLAHSAGAVPVDLNGALADGAVGCTYKYLNGG 232
Cdd:cd06451 112 SPEEIAEALEQHDIKAvTLTHNETSTGVLNPLEGIGALAKKHDALLIVDAVSSLGGEPFRMDEWGVDVAYTGSQKALGAP 191
|
..
gi 490657658 233 PG 234
Cdd:cd06451 192 PG 193
|
|
| SepCysS |
cd06452 |
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ... |
157-227 |
2.87e-04 |
|
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Cys-tRNA(Cys) is produced by O-phosphoseryl-tRNA synthetase which ligates O-phosphoserine (Sep) to tRNA(Cys), and Sep-tRNA:Cys-tRNA synthase (SepCysS) converts Sep-tRNA(Cys) to Cys-tRNA(Cys), in methanogenic archaea. SepCysS forms a dimer, each monomer is composed of a large and small domain; the larger, a typical pyridoxal 5'-phosphate (PLP)-dependent-like enzyme fold. In the active site of each monomer, PLP is covalently bound to a conserved Lys residue near the dimer interface.
Pssm-ID: 99745 Cd Length: 361 Bit Score: 42.76 E-value: 2.87e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490657658 157 DLPDALDDETAVAMITHVNYRTGYMHDMPSVTQTVRQAGALMLWDLAHSAGAVPVDLNGALADGAVGCTYK 227
Cdd:cd06452 131 EVKDEFGKPPALALLTHVDGNYGNLHDAKKIAKVCHEYGVPLLLNGAYTVGRMPVSGKELGADFIVGSGHK 201
|
|
| PRK09331 |
PRK09331 |
Sep-tRNA:Cys-tRNA synthetase; Provisional |
167-227 |
1.29e-03 |
|
Sep-tRNA:Cys-tRNA synthetase; Provisional
Pssm-ID: 236469 Cd Length: 387 Bit Score: 40.68 E-value: 1.29e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490657658 167 AVAMITHVNYRTGYMHDMPSVTQTVRQAGALMLWDLAHSAGAVPVDLNGALADGAVGCTYK 227
Cdd:PRK09331 160 ALALLTHVDGNYGNLADAKKVAKVAHEYGIPFLLNGAYTVGRMPVDGKKLGADFIVGSGHK 220
|
|
| |
