|
Name |
Accession |
Description |
Interval |
E-value |
| FeS_nifS |
TIGR03402 |
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related ... |
4-382 |
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: 629.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 4 VYLDNNATTRLDPMVLEAMMPFLTDFYGNPSSIHDFGIPAQAALERAHQQAAALLGAEyPSEIIFTSCATEATATAIASA 83
Cdd:TIGR03402 1 IYLDNNATTRVDPEVLEAMLPYFTEYFGNPSSMHSFGGEVGKAVEEAREQVAKLLGAE-PDEIIFTSGGTESDNTAIKSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 84 IALLPERREIITSVVEHPATLAACEHLERQGYRIHRIAVDSEGALDMAQFRAALSPRVALVSVMWANNETGVLFPIGEMA 163
Cdd:TIGR03402 80 LAAQPEKRHIITTAVEHPAVLSLCQHLEKQGYKVTYLPVDEEGRLDLEELRAAITDDTALVSVMWANNETGTIFPIEEIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 164 ELAHEQGALFHCDAVQVVGKIPIAVGQTRIDMLSCSAHKFHGPKGVGCLYLRRGTRFRPLLRGGHQEYGRRAGTENICGI 243
Cdd:TIGR03402 160 EIAKERGALFHTDAVQAVGKIPIDLKEMNIDMLSLSGHKLHGPKGVGALYIRKGTRFRPLLRGGHQERGRRAGTENVPGI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 244 VGMGAACELANIHLPGM-THIGQLRNRLEHRLLASVPSVMVMGGGQPRVPGTVNLAFEFIEGEAILLLLNQAGIAASSGS 322
Cdd:TIGR03402 240 VGLGKAAELATEHLEEEnTRVRALRDRLEAGLLARIPDARLNGDPTKRLPNTVNISFEYIEGEAILLLLDMEGICASSGS 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 323 ACTSGSLEPSHVMRAMNIPYTAAHGTIRFSLSRYTREKEIDYVVATLPPIIDRLRALSPY 382
Cdd:TIGR03402 320 ACTSGSLEPSHVLRAMGVPHTAAHGSIRFSLSRYNTEEDIDYVLEVLPPIIARLRAMSPF 379
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
1-380 |
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: 556.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 1 MKQVYLDNNATTRLDPMVLEAMMPFLTDFYGNPSSIHDFGIPAQAALERAHQQAAALLGAEyPSEIIF------------ 68
Cdd:COG1104 1 MMMIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSSLHSFGREARAALEEAREQVAALLGAD-PEEIIFtsggteannlai 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 69 --TSCATEatataiasaiallPERREIITSVVEHPATLAACEHLERQGYRIHRIAVDSEGALDMAQFRAALSPRVALVSV 146
Cdd:COG1104 80 kgAARAYR-------------KKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 147 MWANNETGVLFPIGEMAELAHEQGALFHCDAVQVVGKIPIAVGQTRIDMLSCSAHKFHGPKGVGCLYLRRGTRFRPLLRG 226
Cdd:COG1104 147 MHANNETGTIQPIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRKGVRLEPLIHG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 227 GHQEYGRRAGTENICGIVGMGAACELANIHLPG-MTHIGQLRNRLEHRLLASVPSVMVMGGGQPRVPGTVNLAFEFIEGE 305
Cdd:COG1104 227 GGQERGLRSGTENVPGIVGLGKAAELAAEELEEeAARLRALRDRLEEGLLAAIPGVVINGDPENRLPNTLNFSFPGVEGE 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575523325 306 AILLLLNQAGIAASSGSACTSGSLEPSHVMRAMNIPYTAAHGTIRFSLSRYTREKEIDYVVATLPPIIDRLRALS 380
Cdd:COG1104 307 ALLLALDLAGIAVSSGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARLRKLS 381
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
4-363 |
8.02e-134 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 387.86 E-value: 8.02e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 4 VYLDNNATTRLDPMVLEAMMPFLTDFYGNPSSI-HDFGIPAQAALERAHQQAAALLGAEyPSEIIFTSCATEATATAIAS 82
Cdd:PLN02651 1 LYLDMQATTPIDPRVLDAMLPFLIEHFGNPHSRtHLYGWESEDAVEKARAQVAALIGAD-PKEIIFTSGATESNNLAIKG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 83 AIALLPER-REIITSVVEHPATLAACEHLERQGYRIHRIAVDSEGALDMAQFRAALSPRVALVSVMWANNETGVLFPIGE 161
Cdd:PLN02651 80 VMHFYKDKkKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 162 MAELAHEQGALFHCDAVQVVGKIPIAVGQTRIDMLSCSAHKFHGPKGVGCLYLRRGTRFR--PLLRGGHQEYGRRAGTEN 239
Cdd:PLN02651 160 IGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRlePLMSGGGQERGRRSGTEN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 240 ICGIVGMGAACELANIHLPGM-THIGQLRNRLEHRLLASVPSVMVMGGGQP--RVPGTVNLAFEFIEGEAilLLLNQAGI 316
Cdd:PLN02651 240 TPLVVGLGAACELAMKEMDYDeKHMKALRERLLNGLRAKLGGVRVNGPRDPekRYPGTLNLSFAYVEGES--LLMGLKEV 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 575523325 317 AASSGSACTSGSLEPSHVMRAMNIPYTAAHGTIRFSLSRYTREKEID 363
Cdd:PLN02651 318 AVSSGSACTSASLEPSYVLRALGVPEEMAHGSLRLGVGRFTTEEEVD 364
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
4-365 |
9.56e-99 |
|
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: 298.39 E-value: 9.56e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 4 VYLDNNATTRLDPMVLEAMMPFLTDFYGNP-SSIHDFGIPAQAALERAHQQAAALLGAEYPSEIIFTSCATEATATAIAS 82
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVhRGVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 83 AIALLPERREIITSVVEHPATLAACEHLERQ-GYRIHRIAVDSEGALDMAQFRAALSPRVALVSVMWANNETGVLFPIGE 161
Cdd:pfam00266 81 LGRSLKPGDEIVITEMEHHANLVPWQELAKRtGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 162 MAELAHEQGALFHCDAVQVVGKIPIAVGQTRIDMLSCSAHKFHGPKGVGCLYLRR--GTRFRPLLRGGH-------QEYG 232
Cdd:pfam00266 161 IGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRdlLEKMPPLLGGGGmietvslQEST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 233 -------RRAGTENICGIVGMGAACE-LANIHLPGMT-HIGQLRNRLEHRLLaSVPSVMVMGGgqPRVPGTVNLAFEFIE 303
Cdd:pfam00266 241 fadapwkFEAGTPNIAGIIGLGAALEyLSEIGLEAIEkHEHELAQYLYERLL-SLPGIRLYGP--ERRASIISFNFKGVH 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 575523325 304 GEAILLLLNQAGIAASSGSACTsgslEPSHVMRAMnipytaaHGTIRFSLSRYTREKEIDYV 365
Cdd:pfam00266 318 PHDVATLLDESGIAVRSGHHCA----QPLMVRLGL-------GGTVRASFYIYNTQEDVDRL 368
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
4-369 |
4.63e-60 |
|
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: 198.84 E-value: 4.63e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 4 VYLDNNATTRLDPMVLEAMMPFLTDFYGNPS-SIHDFGIPAQAALERAHQQAAALLGAEYPSEIIFTSCATEATATAIAS 82
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHrGVHELSARATDAYEAAREKVARFINAPSPDEIIFTRNTTEAINLVAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 83 AIALLPERREIITSVVEHPATLAACEHL-ERQGYRIHRIAVDSEGALDMAQFRAALSPRVALVSVMWANNETGVLFPIGE 161
Cdd:cd06453 81 LGRANKPGDEIVTSVMEHHSNIVPWQQLaERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPVKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 162 MAELAHEQGALFHCDAVQVVGKIPIAVGQTRIDMLSCSAHKFHGPKGVGCLYLRRG--TRFRPLLRGGH----------- 228
Cdd:cd06453 161 IGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEEllEEMPPYGGGGEmieevsfeett 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 229 -QEYGRR--AGTENICGIVGMGAACE------LANIHlpgmTHIGQLRNRLEHRlLASVPSVMVMGGGQPRVpGTVNLAF 299
Cdd:cd06453 241 yADLPHKfeAGTPNIAGAIGLGAAIDylekigMEAIA----AHEHELTAYALER-LSEIPGVRVYGDAEDRA-GVVSFNL 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 300 EFIEGEAILLLLNQAGIAASSGSACTsgslepSHVMRAMNIPytaahGTIRFSLSRYTREKEIDYVVATL 369
Cdd:cd06453 315 EGIHPHDVATILDQYGIAVRAGHHCA------QPLMRRLGVP-----GTVRASFGLYNTEEEIDALVEAL 373
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
4-369 |
7.04e-13 |
|
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: 70.27 E-value: 7.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 4 VYLDNNATTRLDPMVLEAmmpfLTDFYG--NpSSIH-----------DfgipaqaALERAHQQAAALLGAEYPSEIIFTS 70
Cdd:NF041166 247 VWFDNAATTQKPQAVIDR----LSYFYEheN-SNIHraahelaaratD-------AYEGAREKVRRFIGAPSVDEIIFVR 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 71 CATeatataiasaiallpE----------RR------EIITSVVEHPAT------LAAcehleRQGYRIHRIAVDSEGAL 128
Cdd:NF041166 315 GTT---------------EainlvakswgRQnigagdEIIVSHLEHHANivpwqqLAQ-----ETGAKLRVIPVDDSGQI 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 129 DMAQFRAALSPRVALVSVMWANNETGVLFPIGEMAELAHEQGALFHCDAVQVVGKIPIAVGQTRIDMLSCSAHKFHGPKG 208
Cdd:NF041166 375 LLDEYAKLLNPRTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTG 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 209 VGCLYLRRGtrfrpLLR-------GGH------------QEYGRR--AGTENICGIVGMGAACE-LANIhlpGMTHIGql 266
Cdd:NF041166 455 IGVVYGKRD-----LLEamppwqgGGNmiadvtfektvyQPAPNRfeAGTGNIADAVGLGAALDyVERI---GIENIA-- 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 267 rnRLEHRLL-------ASVPSVmvmgggqpRVPGTV---------NLA-FEFIE-GEAilllLNQAGIAASSGSACTsgs 328
Cdd:NF041166 525 --RYEHDLLeyataglAEVPGL--------RLIGTAadkasvlsfVLDgYSTEEvGKA----LNQEGIAVRSGHHCA--- 587
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 575523325 329 lEPshVMRAMNIpytaaHGTIRFSLSRY-TREkEIDYVVATL 369
Cdd:NF041166 588 -QP--ILRRFGV-----EATVRPSLAFYnTCE-EVDALVAVL 620
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FeS_nifS |
TIGR03402 |
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related ... |
4-382 |
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: 629.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 4 VYLDNNATTRLDPMVLEAMMPFLTDFYGNPSSIHDFGIPAQAALERAHQQAAALLGAEyPSEIIFTSCATEATATAIASA 83
Cdd:TIGR03402 1 IYLDNNATTRVDPEVLEAMLPYFTEYFGNPSSMHSFGGEVGKAVEEAREQVAKLLGAE-PDEIIFTSGGTESDNTAIKSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 84 IALLPERREIITSVVEHPATLAACEHLERQGYRIHRIAVDSEGALDMAQFRAALSPRVALVSVMWANNETGVLFPIGEMA 163
Cdd:TIGR03402 80 LAAQPEKRHIITTAVEHPAVLSLCQHLEKQGYKVTYLPVDEEGRLDLEELRAAITDDTALVSVMWANNETGTIFPIEEIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 164 ELAHEQGALFHCDAVQVVGKIPIAVGQTRIDMLSCSAHKFHGPKGVGCLYLRRGTRFRPLLRGGHQEYGRRAGTENICGI 243
Cdd:TIGR03402 160 EIAKERGALFHTDAVQAVGKIPIDLKEMNIDMLSLSGHKLHGPKGVGALYIRKGTRFRPLLRGGHQERGRRAGTENVPGI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 244 VGMGAACELANIHLPGM-THIGQLRNRLEHRLLASVPSVMVMGGGQPRVPGTVNLAFEFIEGEAILLLLNQAGIAASSGS 322
Cdd:TIGR03402 240 VGLGKAAELATEHLEEEnTRVRALRDRLEAGLLARIPDARLNGDPTKRLPNTVNISFEYIEGEAILLLLDMEGICASSGS 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 323 ACTSGSLEPSHVMRAMNIPYTAAHGTIRFSLSRYTREKEIDYVVATLPPIIDRLRALSPY 382
Cdd:TIGR03402 320 ACTSGSLEPSHVLRAMGVPHTAAHGSIRFSLSRYNTEEDIDYVLEVLPPIIARLRAMSPF 379
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
1-380 |
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: 556.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 1 MKQVYLDNNATTRLDPMVLEAMMPFLTDFYGNPSSIHDFGIPAQAALERAHQQAAALLGAEyPSEIIF------------ 68
Cdd:COG1104 1 MMMIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSSLHSFGREARAALEEAREQVAALLGAD-PEEIIFtsggteannlai 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 69 --TSCATEatataiasaiallPERREIITSVVEHPATLAACEHLERQGYRIHRIAVDSEGALDMAQFRAALSPRVALVSV 146
Cdd:COG1104 80 kgAARAYR-------------KKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 147 MWANNETGVLFPIGEMAELAHEQGALFHCDAVQVVGKIPIAVGQTRIDMLSCSAHKFHGPKGVGCLYLRRGTRFRPLLRG 226
Cdd:COG1104 147 MHANNETGTIQPIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRKGVRLEPLIHG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 227 GHQEYGRRAGTENICGIVGMGAACELANIHLPG-MTHIGQLRNRLEHRLLASVPSVMVMGGGQPRVPGTVNLAFEFIEGE 305
Cdd:COG1104 227 GGQERGLRSGTENVPGIVGLGKAAELAAEELEEeAARLRALRDRLEEGLLAAIPGVVINGDPENRLPNTLNFSFPGVEGE 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575523325 306 AILLLLNQAGIAASSGSACTSGSLEPSHVMRAMNIPYTAAHGTIRFSLSRYTREKEIDYVVATLPPIIDRLRALS 380
Cdd:COG1104 307 ALLLALDLAGIAVSSGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARLRKLS 381
|
|
| nifS_epsilon |
TIGR03403 |
cysteine desulfurase, NifS family, epsilon proteobacteria type; Members of this family are the ... |
4-380 |
4.58e-135 |
|
cysteine desulfurase, NifS family, epsilon proteobacteria type; Members of this family are the NifS-like cysteine desulfurase of the epsilon division of the Proteobacteria, similar to the NifS protein of nitrogen-fixing bacteria. Like NifS, and unlike IscS, this protein is found as part of a system of just two proteins, a cysteine desulfurase and a scaffold, for iron-sulfur cluster biosynthesis. This protein is called NifS by Olsen, et al. (), so we use this designation.
Pssm-ID: 132444 Cd Length: 382 Bit Score: 391.52 E-value: 4.58e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 4 VYLDNNATTRLDPMVLEAMMPFLTDFYGNPSSIHDFGIPAQAALERAHQQAAALLGAEYPSEIIFTSCATEAT---ATAI 80
Cdd:TIGR03403 1 VYLDNNATTMLDPKVKELMDPFFCDIYGNPNSLHQFGTATHPAIAEALDKLYKGINARDLDDIIITSCATESNnwvLKGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 81 ASAIALLPERREIITSVVEHPATLAACEHLERQGYRIHRIAVDSEGALDMAQFRAALSPRVALVSVMWANNETGVLFPIG 160
Cdd:TIGR03403 81 YFDEILKGGKNHIITTEVEHPAVRATCAFLESLGVEVTYLPINEQGTITAEQVREAITEKTALVSVMWANNETGMIFPIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 161 EMAELAHEQGALFHCDAVQVVGKIPIAVGQTRIDMLSCSAHKFHGPKGVGCLYLRRGTRFRPLLRGGHQEYGRRAGTENI 240
Cdd:TIGR03403 161 EIGEICKERGVLFHTDAVQAIGKIPVDVQKAGVDFLSFSAHKFHGPKGVGGLYIRKGVELTPLFHGGEHMGGRRSGTLNV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 241 CGIVGMGAACELANIHLP-GMTHIGQLRNRLEHRLLAsVPSVMVMGGGQPRVPGTVNLAFEFIEGEAILLLLNQAGIAAS 319
Cdd:TIGR03403 241 PYIVAMGEAMRLANEYLDfEKSHVRRLRDRLEDALLE-LPDVFVVGDREHRVPNTILISIKGVEGEAMLWDLNKAGIAAS 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 575523325 320 SGSACTSGSLEPSHVMRAMNIPYTAAHGTIRFSLSRYTREKEIDYVVATLPPIIDRLRALS 380
Cdd:TIGR03403 320 TGSACASEDLEANPVMVAIGADKELAHTAIRLSLSRFTTEEEIDYTIEVFKKAVQRLRAIS 380
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
4-363 |
8.02e-134 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 387.86 E-value: 8.02e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 4 VYLDNNATTRLDPMVLEAMMPFLTDFYGNPSSI-HDFGIPAQAALERAHQQAAALLGAEyPSEIIFTSCATEATATAIAS 82
Cdd:PLN02651 1 LYLDMQATTPIDPRVLDAMLPFLIEHFGNPHSRtHLYGWESEDAVEKARAQVAALIGAD-PKEIIFTSGATESNNLAIKG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 83 AIALLPER-REIITSVVEHPATLAACEHLERQGYRIHRIAVDSEGALDMAQFRAALSPRVALVSVMWANNETGVLFPIGE 161
Cdd:PLN02651 80 VMHFYKDKkKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 162 MAELAHEQGALFHCDAVQVVGKIPIAVGQTRIDMLSCSAHKFHGPKGVGCLYLRRGTRFR--PLLRGGHQEYGRRAGTEN 239
Cdd:PLN02651 160 IGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRlePLMSGGGQERGRRSGTEN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 240 ICGIVGMGAACELANIHLPGM-THIGQLRNRLEHRLLASVPSVMVMGGGQP--RVPGTVNLAFEFIEGEAilLLLNQAGI 316
Cdd:PLN02651 240 TPLVVGLGAACELAMKEMDYDeKHMKALRERLLNGLRAKLGGVRVNGPRDPekRYPGTLNLSFAYVEGES--LLMGLKEV 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 575523325 317 AASSGSACTSGSLEPSHVMRAMNIPYTAAHGTIRFSLSRYTREKEID 363
Cdd:PLN02651 318 AVSSGSACTSASLEPSYVLRALGVPEEMAHGSLRLGVGRFTTEEEVD 364
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
4-383 |
6.01e-125 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 366.58 E-value: 6.01e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 4 VYLDNNATTRLDPMVLEAMMPFLT--DFYGNPSS-IHDFGIPAQAALERAHQQAAALLGAEyPSEIIFTSCATEATATAI 80
Cdd:PRK14012 5 IYLDYSATTPVDPRVAEKMMPYLTmdGTFGNPASrSHRFGWQAEEAVDIARNQIADLIGAD-PREIVFTSGATESDNLAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 81 ASAIALLPER-REIITSVVEHPATLAACEHLERQGYRIHRIAVDSEGALDMAQFRAALSPRVALVSVMWANNETGVLFPI 159
Cdd:PRK14012 84 KGAAHFYQKKgKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVIQDI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 160 GEMAELAHEQGALFHCDAVQVVGKIPIAVGQTRIDMLSCSAHKFHGPKGVGCLYLRRGTRFR--PLLRGGHQEYGRRAGT 237
Cdd:PRK14012 164 AAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRleAQMHGGGHERGMRSGT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 238 ENICGIVGMGAACELANIHLPG-MTHIGQLRNRLEHRLLaSVPSVMVMGGGQPRVPGTVNLAFEFIEGEAILLLLNQagI 316
Cdd:PRK14012 244 LPTHQIVGMGEAARIAKEEMATeNERIRALRDRLWNGIK-DIEEVYLNGDLEQRVPGNLNVSFNYVEGESLIMALKD--L 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575523325 317 AASSGSACTSGSLEPSHVMRAMNIPYTAAHGTIRFSLSRYTREKEIDYVVATLPPIIDRLRALSPYW 383
Cdd:PRK14012 321 AVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGKLRELSPLW 387
|
|
| DNA_S_dndA |
TIGR03235 |
cysteine desulfurase DndA; This model describes DndA, a protein related to IscS and part of a ... |
5-353 |
9.21e-103 |
|
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: 308.26 E-value: 9.21e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 5 YLDNNATTRLDPMVLEAMMPFLTDFYGNPSSI-HDFGIPAQAALERAHQQAAALLGAEyPSEIIFTSCATEATATAIASA 83
Cdd:TIGR03235 1 YLDHNATTPIDPAVAEAMLPWLLEEFGNPSSRtHEFGHNAKKAVERARKQVAEALGAD-TEEVIFTSGATESNNLAILGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 84 IALLPE--RREIITSVVEHPATLAACEHLERQGYRIHRIAVDSEGALDMAQFRAALSPRVALVSVMWANNETGVLFPIGE 161
Cdd:TIGR03235 80 ARAGEQkgKKHIITSAIEHPAVLEPIRALERNGFTVTYLPVDESGRIDVDELADAIRPDTLLVSIMHVNNETGSIQPIRE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 162 MAELAHEQGALFHCDAVQVVGKIPIAVGQTRIDMLSCSAHKFHGPKGVGCLYLRRG----TRFRPLLRGGHQEYGRRAGT 237
Cdd:TIGR03235 160 IAEVLEAHEAFFHVDAAQVVGKITVDLSADRIDLISCSGHKIYGPKGIGALVIRKRgkpkAPLKPIMFGGGQERGLRPGT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 238 ENICGIVGMGAACELANI-HLPGMTHIGQLRNRLEHRLlaSVPSVMVMGGGQPRVPGTVNLAFEFIEGEAILLLLNQAgI 316
Cdd:TIGR03235 240 LPVHLIVGMGEAAEIARRnAQAWEVKLRAMRNQLRDAL--QTLGVKLNGDPAETIPHILNFSIDGVNSEALIVNLRAD-A 316
|
330 340 350
....*....|....*....|....*....|....*..
gi 575523325 317 AASSGSACTSGSLEPSHVMRAMNIPYTAAHGTIRFSL 353
Cdd:TIGR03235 317 AVSTGSACSSSKYEPSHVLQAMGLDTDRARGAIRFSW 353
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
4-365 |
9.56e-99 |
|
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: 298.39 E-value: 9.56e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 4 VYLDNNATTRLDPMVLEAMMPFLTDFYGNP-SSIHDFGIPAQAALERAHQQAAALLGAEYPSEIIFTSCATEATATAIAS 82
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVhRGVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 83 AIALLPERREIITSVVEHPATLAACEHLERQ-GYRIHRIAVDSEGALDMAQFRAALSPRVALVSVMWANNETGVLFPIGE 161
Cdd:pfam00266 81 LGRSLKPGDEIVITEMEHHANLVPWQELAKRtGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 162 MAELAHEQGALFHCDAVQVVGKIPIAVGQTRIDMLSCSAHKFHGPKGVGCLYLRR--GTRFRPLLRGGH-------QEYG 232
Cdd:pfam00266 161 IGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRdlLEKMPPLLGGGGmietvslQEST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 233 -------RRAGTENICGIVGMGAACE-LANIHLPGMT-HIGQLRNRLEHRLLaSVPSVMVMGGgqPRVPGTVNLAFEFIE 303
Cdd:pfam00266 241 fadapwkFEAGTPNIAGIIGLGAALEyLSEIGLEAIEkHEHELAQYLYERLL-SLPGIRLYGP--ERRASIISFNFKGVH 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 575523325 304 GEAILLLLNQAGIAASSGSACTsgslEPSHVMRAMnipytaaHGTIRFSLSRYTREKEIDYV 365
Cdd:pfam00266 318 PHDVATLLDESGIAVRSGHHCA----QPLMVRLGL-------GGTVRASFYIYNTQEDVDRL 368
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
4-369 |
8.86e-84 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 260.43 E-value: 8.86e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 4 VYLDNNATTrldPMVLEAMMPFL---TDFYGNPSSIHDFGIPAQAALERAHQQAAALLGAEyPSEIIFTSCATEATATAI 80
Cdd:PRK02948 2 IYLDYAATT---PMSKEALQTYQkaaSQYFGNESSLHDIGGTASSLLQVCRKTFAEMIGGE-EQGIYFTSGGTESNYLAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 81 ASAIALLPER-REIITSVVEHPATLAACEHLERQGYRIHRIAVDSEGALDMAQFRAALSPRVALVSVMWANNETGVLFPI 159
Cdd:PRK02948 78 QSLLNALPQNkKHIITTPMEHASIHSYFQSLESQGYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQPI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 160 GEMAELAHEQGALFHCDAVQVVGKIPIAVGQTRIDMLSCSAHKFHGPKGVGCLYLRRGTRFRPLLRGGHQEYGRRAGTEN 239
Cdd:PRK02948 158 AEIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYINPQVRWKPVFPGTTHEKGFRPGTVN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 240 ICGIVGMGAACELANIHLPG-MTHIGQLRNRLEHRLLASVPSVMVMGGGQPRVPGTVNLAFEFIEGEAILLLLNQAGIAA 318
Cdd:PRK02948 238 VPGIAAFLTAAENILKNMQEeSLRFKELRSYFLEQIQTLPLPIEVEGHSTSCLPHIIGVTIKGIEGQYTMLECNRRGIAI 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 575523325 319 SSGSACTSGSLEPSHVMRAMNIPYTAAHGTIRFSLSRYTREKEIDYVVATL 369
Cdd:PRK02948 318 STGSACQVGKQEPSKTMLAIGKTYEEAKQFVRFSFGQQTTKDQIDTTIHAL 368
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
4-369 |
1.11e-64 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 211.54 E-value: 1.11e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 4 VYLDNNATTRLDPMVLEAMMPFLTDFYGNPS-SIHDFGIPAQAALERAHQQAAALLGAEYPSEIIF-------------- 68
Cdd:COG0520 17 VYLDNAATGQKPRPVIDAIRDYYEPYNANVHrGAHELSAEATDAYEAAREKVARFIGAASPDEIIFtrgtteainlvayg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 69 -TscateatataiasaiaLLPERREIITSVVEHPATLAACEHL-ERQGYRIHRIAVDSEGALDMAQFRAALSPRVALVSV 146
Cdd:COG0520 97 lG----------------RLKPGDEILITEMEHHSNIVPWQELaERTGAEVRVIPLDEDGELDLEALEALLTPRTKLVAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 147 MWANNETGVLFPIGEMAELAHEQGALFHCDAVQVVGKIPIAVGQTRIDMLSCSAHKFHGPKGVGCLYLRRGT--RFRPLL 224
Cdd:COG0520 161 THVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELleALPPFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 225 RGGH------------QEYGRR--AGTENICGIVGMGAACE------LANIHlpgmTHIGQLRNRLEHRlLASVPSVMVM 284
Cdd:COG0520 241 GGGGmiewvsfdgttyADLPRRfeAGTPNIAGAIGLGAAIDyleaigMEAIE----ARERELTAYALEG-LAAIPGVRIL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 285 GGGQPRVP-GTVNLAFEFIEGEAILLLLNQAGIAASSGSACTSGslepshVMRAMNIPytaahGTIRFSLSRYTREKEID 363
Cdd:COG0520 316 GPADPEDRsGIVSFNVDGVHPHDVAALLDDEGIAVRAGHHCAQP------LMRRLGVP-----GTVRASFHLYNTEEEID 384
|
....*.
gi 575523325 364 YVVATL 369
Cdd:COG0520 385 RLVEAL 390
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
4-369 |
4.63e-60 |
|
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: 198.84 E-value: 4.63e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 4 VYLDNNATTRLDPMVLEAMMPFLTDFYGNPS-SIHDFGIPAQAALERAHQQAAALLGAEYPSEIIFTSCATEATATAIAS 82
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHrGVHELSARATDAYEAAREKVARFINAPSPDEIIFTRNTTEAINLVAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 83 AIALLPERREIITSVVEHPATLAACEHL-ERQGYRIHRIAVDSEGALDMAQFRAALSPRVALVSVMWANNETGVLFPIGE 161
Cdd:cd06453 81 LGRANKPGDEIVTSVMEHHSNIVPWQQLaERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPVKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 162 MAELAHEQGALFHCDAVQVVGKIPIAVGQTRIDMLSCSAHKFHGPKGVGCLYLRRG--TRFRPLLRGGH----------- 228
Cdd:cd06453 161 IGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEEllEEMPPYGGGGEmieevsfeett 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 229 -QEYGRR--AGTENICGIVGMGAACE------LANIHlpgmTHIGQLRNRLEHRlLASVPSVMVMGGGQPRVpGTVNLAF 299
Cdd:cd06453 241 yADLPHKfeAGTPNIAGAIGLGAAIDylekigMEAIA----AHEHELTAYALER-LSEIPGVRVYGDAEDRA-GVVSFNL 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 300 EFIEGEAILLLLNQAGIAASSGSACTsgslepSHVMRAMNIPytaahGTIRFSLSRYTREKEIDYVVATL 369
Cdd:cd06453 315 EGIHPHDVATILDQYGIAVRAGHHCA------QPLMRRLGVP-----GTVRASFGLYNTEEEIDALVEAL 373
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
2-379 |
3.65e-40 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 147.59 E-value: 3.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 2 KQVYLDNNATTRLDPMVLEAMMPFLTDFYGN-PSSIHDFGIPAQAALERAHQQAAALLGAEYPSEIIFTSCATEATATAI 80
Cdd:PLN02855 32 KLVYLDNAATSQKPAAVLDALQDYYEEYNSNvHRGIHALSAKATDAYELARKKVAAFINASTSREIVFTRNATEAINLVA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 81 AS-AIALLPERREIITSVVEHPATLAACEHL-ERQGYRIHRIAVDSEGALDMAQFRAALSPRVALVSVMWANNETGVLFP 158
Cdd:PLN02855 112 YTwGLANLKPGDEVILSVAEHHSNIVPWQLVaQKTGAVLKFVGLTPDEVLDVEQLKELLSEKTKLVATHHVSNVLGSILP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 159 IGEMAELAHEQGALFHCDAVQVVGKIPIAVGQTRIDMLSCSAHKFHGPKGVGCLYLRRGTRFR--PLLRGG--------- 227
Cdd:PLN02855 192 VEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLWGKSDLLESmpPFLGGGemisdvfld 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 228 HQEYGR-----RAGTENICGIVGMGAACE-LANIhlpGMTHIGQLRNRLEHRL---LASVPSVMVMGggqPRVPGTVNLA 298
Cdd:PLN02855 272 HSTYAPppsrfEAGTPAIGEAIGLGAAIDyLSEI---GMDRIHEYEVELGTYLyekLSSVPGVRIYG---PKPSEGVGRA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 299 ------FEFIEGEAILLLLNQA-GIAASSGSACTsgslEPSHvmRAMNIPYTAahgtiRFSLSRYTREKEIDYVVATLPP 371
Cdd:PLN02855 346 alcafnVEGIHPTDLSTFLDQQhGVAIRSGHHCA----QPLH--RYLGVNASA-----RASLYFYNTKEEVDAFIHALKD 414
|
....*...
gi 575523325 372 IIDRLRAL 379
Cdd:PLN02855 415 TIAFFSSF 422
|
|
| am_tr_V_VC1184 |
TIGR01976 |
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of ... |
4-369 |
3.96e-33 |
|
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of probable pyridoxal phosphate-dependent enzymes in the aminotransferase class V family (pfam00266). The most closely related characterized proteins are active as cysteine desulfurases, selenocysteine lyases, or both; some are involved in FeS cofactor biosynthesis and are designated NifS. An active site Cys residue present in those sequences, in motifs resembling GHHC or GSAC, is not found in this family. The function of members of this family is unknown, but seems unlike to be as an aminotransferase. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 273906 [Multi-domain] Cd Length: 397 Bit Score: 127.95 E-value: 3.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 4 VYLDNNATTRLDPMVLEAMMPFLTDFYGNPSSIHDFGIPAQAALERAHQQAAALLGAeYPSEIIFTSCATEATATAIASA 83
Cdd:TIGR01976 19 VFFDNPAGTQIPQSVADAVSAALTRSNANRGGAYESSRRADQVVDDAREAVADLLNA-DPPEVVFGANATSLTFLLSRAI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 84 IALLPERREIITSVVEHPATLAACEHL-ERQGYRIHRIAVD-SEGALDMAQFRAALSPRVALVSVMWANNETGVLFPIGE 161
Cdd:TIGR01976 98 SRRWGPGDEVIVTRLDHEANISPWLQAaERAGAKVKWARVDeATGELHPDDLASLLSPRTRLVAVTAASNTLGSIVDLAA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 162 MAELAHEQGALFHCDAVQVVGKIPIAVGQTRIDMLSCSAHKFHGPKgVGCLYLR-------RGTRFRPLLRGGhqEYGRR 234
Cdd:TIGR01976 178 ITELVHAAGALVVVDAVHYAPHGLIDVQATGADFLTCSAYKFFGPH-MGILWGRpellmnlPPYKLTFSYDTG--PERFE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 235 AGTENICGIVGMGAACE-LANIH-----------LPGMTHIGQLRNRLEHRL---LASVPSVMVMGGGQP--RVPgTVNL 297
Cdd:TIGR01976 255 LGTPQYELLAGVVAAVDyLAGLGesangsrrerlVASFQAIDAYENRLAEYLlvgLSDLPGVTLYGVARLaaRVP-TVSF 333
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 575523325 298 AFEFIEGEAILLLLNQAGIAASSGSACTSGslepshVMRAMNIPytAAHGTIRFSLSRYTREKEIDYVVATL 369
Cdd:TIGR01976 334 TVHGLPPQRVVRRLADQGIDAWAGHFYAVR------LLRRLGLN--DEGGVVRVGLAHYNTAEEVDRLLEAL 397
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
4-372 |
1.54e-23 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 101.37 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 4 VYLDNNATTRLDPMVLEAMMPFLTDFYGN-PSSIHDFGIPAQAALERAHQQAAALLGAEYPSEIIFTSCATEATATAIAS 82
Cdd:PRK09295 25 AYLDSAASAQKPSQVIDAEAEFYRHGYAAvHRGIHTLSAQATEKMENVRKQAALFINARSAEELVFVRGTTEGINLVANS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 83 -AIALLPERREIITSVVEHPATLAACEHL-ERQGYRIHRIAVDSEGALDMAQFRAALSPRVALVSVMWANNETGVLFPIG 160
Cdd:PRK09295 105 wGNSNVRAGDNIIISEMEHHANIVPWQMLcARVGAELRVIPLNPDGTLQLETLPALFDERTRLLAITHVSNVLGTENPLA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 161 EMAELAHEQGALFHCDAVQVVGKIPIAVGQTRIDMLSCSAHKFHGPKGVGCLYLRR------------GTRFRPLLRGGH 228
Cdd:PRK09295 185 EMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKEallqemppweggGSMIATVSLTEG 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 229 QEYGR-----RAGTENICGIVGMGAACELANIHlpGMTHIGQLRNRLEH---RLLASVPSVMVMGggqPRVPGTVnLAFE 300
Cdd:PRK09295 265 TTWAKapwrfEAGTPNTGGIIGLGAALDYVSAL--GLNNIAEYEQNLMHyalSQLESVPDLTLYG---PQNRLGV-IAFN 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 575523325 301 FIEGEA--ILLLLNQAGIAASSGSACTSGslepshVMRAMNIPytaahGTIRFSLSRYTREKEIDYVVATLPPI 372
Cdd:PRK09295 339 LGKHHAydVGSFLDNYGIAVRTGHHCAMP------LMAYYNVP-----AMCRASLAMYNTHEEVDRLVAGLQRI 401
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
4-367 |
6.82e-23 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 99.34 E-value: 6.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 4 VYLDNnATTRLDPmvlEAMMPFLTDFYGNPS-----SIHDFGIPAQAALERAHQQAAALLGAEYPSEIIFT--SCATEAT 76
Cdd:PRK10874 21 VYLDS-AATALKP---QAVIEATQQFYSLSAgnvhrSQFAAAQRLTARYEAAREQVAQLLNAPDAKNIVWTrgTTESINL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 77 ATAIASAIALLPERrEIITSVVEHPATLAACEHLERQ-GYRIHRIAVDSEGALDMAQFRAALSPRVALVSVMWANNETGV 155
Cdd:PRK10874 97 VAQSYARPRLQPGD-EIIVSEAEHHANLVPWLMVAQQtGAKVVKLPLGADRLPDVDLLPELITPRTRILALGQMSNVTGG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 156 LFPIGEMAELAHEQGALFHCDAVQVVGKIPIAVGQTRIDMLSCSAHKFHGPKGVGCLYLRRG--TRFRPLLRGGH----- 228
Cdd:PRK10874 176 CPDLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKSEllEAMSPWQGGGKmltev 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 229 -------QEYGRR--AGTENICGIVGMGAACE-LANIHLPGM-THIGQLRNRLEHRlLASVPsvmvmGGGQPRVPGTVNL 297
Cdd:PRK10874 256 sfdgftpQSAPWRfeAGTPNVAGVIGLSAALEwLADIDINQAeSWSRSLATLAEDA-LAKLP-----GFRSFRCQDSSLL 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 575523325 298 AFEF--IEGEAILLLLNQAGIAASSGSACTsgslEPshVMRAMNIPytaahGTIRFSLSRYTREKEIDYVVA 367
Cdd:PRK10874 330 AFDFagVHHSDLVTLLAEYGIALRAGQHCA----QP--LLAALGVT-----GTLRASFAPYNTQSDVDALVN 390
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
4-369 |
7.04e-13 |
|
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: 70.27 E-value: 7.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 4 VYLDNNATTRLDPMVLEAmmpfLTDFYG--NpSSIH-----------DfgipaqaALERAHQQAAALLGAEYPSEIIFTS 70
Cdd:NF041166 247 VWFDNAATTQKPQAVIDR----LSYFYEheN-SNIHraahelaaratD-------AYEGAREKVRRFIGAPSVDEIIFVR 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 71 CATeatataiasaiallpE----------RR------EIITSVVEHPAT------LAAcehleRQGYRIHRIAVDSEGAL 128
Cdd:NF041166 315 GTT---------------EainlvakswgRQnigagdEIIVSHLEHHANivpwqqLAQ-----ETGAKLRVIPVDDSGQI 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 129 DMAQFRAALSPRVALVSVMWANNETGVLFPIGEMAELAHEQGALFHCDAVQVVGKIPIAVGQTRIDMLSCSAHKFHGPKG 208
Cdd:NF041166 375 LLDEYAKLLNPRTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTG 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 209 VGCLYLRRGtrfrpLLR-------GGH------------QEYGRR--AGTENICGIVGMGAACE-LANIhlpGMTHIGql 266
Cdd:NF041166 455 IGVVYGKRD-----LLEamppwqgGGNmiadvtfektvyQPAPNRfeAGTGNIADAVGLGAALDyVERI---GIENIA-- 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 267 rnRLEHRLL-------ASVPSVmvmgggqpRVPGTV---------NLA-FEFIE-GEAilllLNQAGIAASSGSACTsgs 328
Cdd:NF041166 525 --RYEHDLLeyataglAEVPGL--------RLIGTAadkasvlsfVLDgYSTEEvGKA----LNQEGIAVRSGHHCA--- 587
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 575523325 329 lEPshVMRAMNIpytaaHGTIRFSLSRY-TREkEIDYVVATL 369
Cdd:NF041166 588 -QP--ILRRFGV-----EATVRPSLAFYnTCE-EVDALVAVL 620
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
86-215 |
5.11e-10 |
|
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: 58.16 E-value: 5.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 86 LLPERREIITSVVEHPATLAAceHLERQGYRIHRIAVD--SEGALDMAQFR-AALSPRVALVSVMWANNETGVLFPIGEM 162
Cdd:cd01494 37 LLGPGDEVIVDANGHGSRYWV--AAELAGAKPVPVPVDdaGYGGLDVAILEeLKAKPNVALIVITPNTTSGGVLVPLKEI 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 575523325 163 AELAHEQGALFHCDAVQVVGKIPIA---VGQTRIDMLSCSAHKFHGPKGVGCLYLR 215
Cdd:cd01494 115 RKIAKEYGILLLVDAASAGGASPAPgvlIPEGGADVVTFSLHKNLGGEGGGVVIVK 170
|
|
| PRK04366 |
PRK04366 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPB; |
89-176 |
1.64e-09 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPB;
Pssm-ID: 235292 Cd Length: 481 Bit Score: 59.36 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 89 ERREIITSVVEH---PATLAACehlerqGYRIHRIAVDSEGALDMAQFRAALSPRVAlvSVMWANNETGVLFP--IGEMA 163
Cdd:PRK04366 160 KRTEVIVPDSAHgtnPASAAMA------GFKVVEIPSNEDGLVDLEALKAAVGEDTA--ALMLTNPNTLGLFErnILEIA 231
|
90
....*....|...
gi 575523325 164 ELAHEQGALFHCD 176
Cdd:PRK04366 232 EIVHEAGGLLYYD 244
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
108-210 |
7.31e-08 |
|
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: 53.83 E-value: 7.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 108 EHLERQGYRIHRIAVDSEGALDMAQFRAALS-PRVALVSVMWANNETGVLFPIGEMAELAHEQGALFHCDAVQVVGKIPI 186
Cdd:cd06451 91 DMAERYGADVDVVEKPWGEAVSPEEIAEALEqHDIKAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVDAVSSLGGEPF 170
|
90 100
....*....|....*....|....*
gi 575523325 187 AVGQTRID-MLSCSAHKFHGPKGVG 210
Cdd:cd06451 171 RMDEWGVDvAYTGSQKALGAPPGLG 195
|
|
| PucG |
COG0075 |
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ... |
107-210 |
3.51e-06 |
|
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG is part of the Pathway/BioSystem: Serine biosynthesis
Pssm-ID: 439845 [Multi-domain] Cd Length: 376 Bit Score: 48.55 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 107 CEHLERQGYRIHRIAVDSEGALDMAQFRAALS--PRVALVSVmwANNET--GVLFPIGEMAELAHEQGALFHCDAVQVVG 182
Cdd:COG0075 90 AEIAERYGAEVVVLEVPWGEAVDPEEVEEALAadPDIKAVAV--VHNETstGVLNPLEEIGALAKEHGALLIVDAVSSLG 167
|
90 100
....*....|....*....|....*....
gi 575523325 183 KIPIAVGQTRIDMLSCSAHK-FHGPKGVG 210
Cdd:COG0075 168 GVPLDMDEWGIDVVVSGSQKcLMLPPGLA 196
|
|
| GDC-P |
cd00613 |
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ... |
99-177 |
4.47e-06 |
|
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: 48.38 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 99 EHPATLAACehLERQGYRIHRIAVDSEGALDMAQFRAALSPRVALVSVMWANNEtGVLFP-IGEMAELAHEQGALFHCDA 177
Cdd:cd00613 120 TNPAVARTR--GEPLGIEVVEVPSDEGGTVDLEALKEEVSEEVAALMVQYPNTL-GVFEDlIKEIADIAHSAGALVYVDG 196
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
89-225 |
4.45e-05 |
|
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: 45.21 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 89 ERREIITSVVEHPATLAACEHL--ERQGyrIHRIAVDSEGALDMAQFRAALSP------RVALV-----SVmwannETGV 155
Cdd:COG0076 163 PRPRIVVSEEAHSSVDKAARLLglGRDA--LRKVPVDEDGRMDPDALEAAIDEdraaglNPIAVvatagTT-----NTGA 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 156 LFPIGEMAELAHEQGALFHCDAvqvvgkipiAVG------------QTRIDM---LSCSAHK-FHGPKGVGCLYLRRGTR 219
Cdd:COG0076 236 IDPLAEIADIAREHGLWLHVDA---------AYGgfalpspelrhlLDGIERadsITVDPHKwLYVPYGCGAVLVRDPEL 306
|
....*.
gi 575523325 220 FRPLLR 225
Cdd:COG0076 307 LREAFS 312
|
|
| PRK13479 |
PRK13479 |
2-aminoethylphosphonate--pyruvate transaminase; Provisional |
110-202 |
4.46e-04 |
|
2-aminoethylphosphonate--pyruvate transaminase; Provisional
Pssm-ID: 184076 [Multi-domain] Cd Length: 368 Bit Score: 42.21 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 110 LERQGYRIHRIAVDSEGALDMAQFRAALS--PRVALVSVMWANNETGVLFPIGEMAELAHEQGALFHCDAVQVVGKIPIA 187
Cdd:PRK13479 99 AEYLGIAHVVLDTGEDEPPDAAEVEAALAadPRITHVALVHCETTTGILNPLDEIAAVAKRHGKRLIVDAMSSFGAIPID 178
|
90
....*....|....*
gi 575523325 188 VGQTRIDMLSCSAHK 202
Cdd:PRK13479 179 IAELGIDALISSANK 193
|
|
| PRK00451 |
PRK00451 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPA; |
88-189 |
1.34e-03 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
Pssm-ID: 234769 [Multi-domain] Cd Length: 447 Bit Score: 40.51 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523325 88 PERREIITSVVEHpatlaacehlerQGYRIHRIAVDsEGALDMAQFRAALSPRVALVSVmwAN-NETGVLFPIGEMAELA 166
Cdd:PRK00451 165 PEYREVLKTYLKG------------QGIEVVEVPYE-DGVTDLEALEAAVDDDTAAVVV--QYpNFFGVIEDLEEIAEIA 229
|
90 100
....*....|....*....|...
gi 575523325 167 HEQGALFhcdavqVVGKIPIAVG 189
Cdd:PRK00451 230 HAGGALF------IVGVDPVSLG 246
|
|
| |
