|
Name |
Accession |
Description |
Interval |
E-value |
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
1-378 |
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: 605.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 1 MERIYLDHAATSPTHPEVVEKMIPYMTETFGNPSSIHFYGRQTRHAVDEARRACARSIHANPNEIIFTSGGTEADNLALI 80
Cdd:COG1104 1 MMMIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSSLHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNLAIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 81 GVARANRHKGNHIITTQIEHHAILHTCELLEREGFEVTYLPVDETGRVQVSDIQKALTEETILVSIMFGNNEVGTMQPIA 160
Cdd:COG1104 81 GAARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 161 EIGKLLKEHQAYFHTDAVQAYGLVEIDVKEFGIDLLSISAHKINGPKGVGFLYAGADVKFEPLLIGGEQERKRRAGTENV 240
Cdd:COG1104 161 EIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRKGVRLEPLIHGGGQERGLRSGTENV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 241 PSIVGLQHAILLAEKTREQKNAQYEEFKDIMVSVFKNEDITFEVNGNLEYRLPHVLNISFTGMNIEPFLVNLDLAGIAVS 320
Cdd:COG1104 241 PGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAAIPGVVINGDPENRLPNTLNFSFPGVEGEALLLALDLAGIAVS 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 446362049 321 SGSACTAGSIDPSHVLVAMfGKDSDQIRSSVRFSFGLGNTKEQIEKAAYETVKIVKRL 378
Cdd:COG1104 321 SGSACSSGSLEPSHVLLAM-GLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARL 377
|
|
| FeS_nifS |
TIGR03402 |
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related ... |
4-378 |
5.89e-175 |
|
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: 491.74 E-value: 5.89e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 4 IYLDHAATSPTHPEVVEKMIPYMTETFGNPSSIHFYGRQTRHAVDEARRACARSIHANPNEIIFTSGGTEADNLALIGVA 83
Cdd:TIGR03402 1 IYLDNNATTRVDPEVLEAMLPYFTEYFGNPSSMHSFGGEVGKAVEEAREQVAKLLGAEPDEIIFTSGGTESDNTAIKSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 84 RANRHKgNHIITTQIEHHAILHTCELLEREGFEVTYLPVDETGRVQVSDIQKALTEETILVSIMFGNNEVGTMQPIAEIG 163
Cdd:TIGR03402 81 AAQPEK-RHIITTAVEHPAVLSLCQHLEKQGYKVTYLPVDEEGRLDLEELRAAITDDTALVSVMWANNETGTIFPIEEIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 164 KLLKEHQAYFHTDAVQAYGLVEIDVKEFGIDLLSISAHKINGPKGVGFLYAGADVKFEPLLIGGEQERKRRAGTENVPSI 243
Cdd:TIGR03402 160 EIAKERGALFHTDAVQAVGKIPIDLKEMNIDMLSLSGHKLHGPKGVGALYIRKGTRFRPLLRGGHQERGRRAGTENVPGI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 244 VGLQHAILLAEKTREQKNAQYEEFKDIMVSVFKNEDITFEVNGNLEYRLPHVLNISFTGMNIEPFLVNLDLAGIAVSSGS 323
Cdd:TIGR03402 240 VGLGKAAELATEHLEEENTRVRALRDRLEAGLLARIPDARLNGDPTKRLPNTVNISFEYIEGEAILLLLDMEGICASSGS 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 446362049 324 ACTAGSIDPSHVLVAMfGKDSDQIRSSVRFSFGLGNTKEQIEKAAYETVKIVKRL 378
Cdd:TIGR03402 320 ACTSGSLEPSHVLRAM-GVPHTAAHGSIRFSLSRYNTEEDIDYVLEVLPPIIARL 373
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
4-365 |
2.34e-140 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 403.65 E-value: 2.34e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 4 IYLDHAATSPTHPEVVEKMIPYMTETFGNPSSI-HFYGRQTRHAVDEARRACARSIHANPNEIIFTSGGTEADNLALIGV 82
Cdd:PLN02651 1 LYLDMQATTPIDPRVLDAMLPFLIEHFGNPHSRtHLYGWESEDAVEKARAQVAALIGADPKEIIFTSGATESNNLAIKGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 83 ARANRHKGNHIITTQIEHHAILHTCELLEREGFEVTYLPVDETGRVQVSDIQKALTEETILVSIMFGNNEVGTMQPIAEI 162
Cdd:PLN02651 81 MHFYKDKKKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVEEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 163 GKLLKEHQAYFHTDAVQAYGLVEIDVKEFGIDLLSISAHKINGPKGVGFLYA--GADVKFEPLLIGGEQERKRRAGTENV 240
Cdd:PLN02651 161 GELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVrrRPRVRLEPLMSGGGQERGRRSGTENT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 241 PSIVGLQHAILLAEKTREQKNAQYEEFKDIMVSVFKNEDITFEVNG--NLEYRLPHVLNISFTGMNIEPFLVNldLAGIA 318
Cdd:PLN02651 241 PLVVGLGAACELAMKEMDYDEKHMKALRERLLNGLRAKLGGVRVNGprDPEKRYPGTLNLSFAYVEGESLLMG--LKEVA 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 446362049 319 VSSGSACTAGSIDPSHVLVAMfGKDSDQIRSSVRFSFGLGNTKEQIE 365
Cdd:PLN02651 319 VSSGSACTSASLEPSYVLRAL-GVPEEMAHGSLRLGVGRFTTEEEVD 364
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
4-366 |
4.38e-96 |
|
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: 291.07 E-value: 4.38e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 4 IYLDHAATSPTHPEVVEKMIPYMTETFGNP-SSIHFYGRQTRHAVDEARRACARSIHANPN-EIIFTSGGTEADNLALIG 81
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVhRGVHTLGKEATQAYEEAREKVAEFINAPSNdEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 82 VARANRhKGNHIITTQIEHHAILHTCELL-EREGFEVTYLPVDETGRVQVSDIQKALTEETILVSIMFGNNEVGTMQPIA 160
Cdd:pfam00266 81 LGRSLK-PGDEIVITEMEHHANLVPWQELaKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 161 EIGKLLKEHQAYFHTDAVQAYGLVEIDVKEFGIDLLSISAHKINGPKGVGFLYA--GADVKFEPLLIGG----------- 227
Cdd:pfam00266 160 EIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGrrDLLEKMPPLLGGGgmietvslqes 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 228 ---EQERKRRAGTENVPSIVGLQHAILLAEKTREQKNAQYE-EFKDIMVSVFKNEDItFEVNGNLeyRLPHVLNISFTGM 303
Cdd:pfam00266 240 tfaDAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEhELAQYLYERLLSLPG-IRLYGPE--RRASIISFNFKGV 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446362049 304 NIEPFLVNLDLAGIAVSSGSACTagsiDPSHVLVAMfgkdsdqiRSSVRFSFGLGNTKEQIEK 366
Cdd:pfam00266 317 HPHDVATLLDESGIAVRSGHHCA----QPLMVRLGL--------GGTVRASFYIYNTQEDVDR 367
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
4-368 |
1.65e-66 |
|
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: 215.02 E-value: 1.65e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 4 IYLDHAATSPTHPEVVEKMIPYMTETFGNPS-SIHFYGRQTRHAVDEARRACARSIHA-NPNEIIFTSGGTEADNLALIG 81
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHrGVHELSARATDAYEAAREKVARFINApSPDEIIFTRNTTEAINLVAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 82 VARANRhKGNHIITTQIEHHAILHTCELL-EREGFEVTYLPVDETGRVQVSDIQKALTEETILVSIMFGNNEVGTMQPIA 160
Cdd:cd06453 81 LGRANK-PGDEIVTSVMEHHSNIVPWQQLaERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 161 EIGKLLKEHQAYFHTDAVQAYGLVEIDVKEFGIDLLSISAHKINGPKGVGFLYA--GADVKFEPLLIGGEQER------- 231
Cdd:cd06453 160 EIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGkeELLEEMPPYGGGGEMIEevsfeet 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 232 -------KRRAGTENVPSIVGLQHAILLAEKT-------REQKNAQY--EEFKDI-MVSVFKNED-----ITFEVNGnle 289
Cdd:cd06453 240 tyadlphKFEAGTPNIAGAIGLGAAIDYLEKIgmeaiaaHEHELTAYalERLSEIpGVRVYGDAEdragvVSFNLEG--- 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446362049 290 yRLPHvlNISFTgmniepflvnLDLAGIAVSSGSACtagsidpSHVLVAMFGkdsdqIRSSVRFSFGLGNTKEQIEKAA 368
Cdd:cd06453 317 -IHPH--DVATI----------LDQYGIAVRAGHHC-------AQPLMRRLG-----VPGTVRASFGLYNTEEEIDALV 370
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
4-218 |
3.68e-20 |
|
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: 92.22 E-value: 3.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 4 IYLDHAATspTH-PEVVEKMIPYMTETfGNpSSIH-----FYGRQTrHAVDEARRACARSIHA-NPNEIIFTSGGTEADN 76
Cdd:NF041166 247 VWFDNAAT--TQkPQAVIDRLSYFYEH-EN-SNIHraaheLAARAT-DAYEGAREKVRRFIGApSVDEIIFVRGTTEAIN 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 77 LaligVA----RANRHKGNHIITTQIEHHA-ILHTCELLEREGFEVTYLPVDETGRVQVSDIQKALTEETILVSIMFGNN 151
Cdd:NF041166 322 L----VAkswgRQNIGAGDEIIVSHLEHHAnIVPWQQLAQETGAKLRVIPVDDSGQILLDEYAKLLNPRTKLVSVTQVSN 397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446362049 152 EVGTMQPIAEIgkllkehqayfhTDAVQAYG---LVE---------IDVKEFGIDLLSISAHKINGPKGVGFLYAGADV 218
Cdd:NF041166 398 ALGTVTPVKEI------------IALAHRAGakvLVDgaqsvshmpVDVQALDADFFVFSGHKVFGPTGIGVVYGKRDL 464
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
1-378 |
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: 605.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 1 MERIYLDHAATSPTHPEVVEKMIPYMTETFGNPSSIHFYGRQTRHAVDEARRACARSIHANPNEIIFTSGGTEADNLALI 80
Cdd:COG1104 1 MMMIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSSLHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNLAIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 81 GVARANRHKGNHIITTQIEHHAILHTCELLEREGFEVTYLPVDETGRVQVSDIQKALTEETILVSIMFGNNEVGTMQPIA 160
Cdd:COG1104 81 GAARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 161 EIGKLLKEHQAYFHTDAVQAYGLVEIDVKEFGIDLLSISAHKINGPKGVGFLYAGADVKFEPLLIGGEQERKRRAGTENV 240
Cdd:COG1104 161 EIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRKGVRLEPLIHGGGQERGLRSGTENV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 241 PSIVGLQHAILLAEKTREQKNAQYEEFKDIMVSVFKNEDITFEVNGNLEYRLPHVLNISFTGMNIEPFLVNLDLAGIAVS 320
Cdd:COG1104 241 PGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAAIPGVVINGDPENRLPNTLNFSFPGVEGEALLLALDLAGIAVS 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 446362049 321 SGSACTAGSIDPSHVLVAMfGKDSDQIRSSVRFSFGLGNTKEQIEKAAYETVKIVKRL 378
Cdd:COG1104 321 SGSACSSGSLEPSHVLLAM-GLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARL 377
|
|
| FeS_nifS |
TIGR03402 |
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related ... |
4-378 |
5.89e-175 |
|
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: 491.74 E-value: 5.89e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 4 IYLDHAATSPTHPEVVEKMIPYMTETFGNPSSIHFYGRQTRHAVDEARRACARSIHANPNEIIFTSGGTEADNLALIGVA 83
Cdd:TIGR03402 1 IYLDNNATTRVDPEVLEAMLPYFTEYFGNPSSMHSFGGEVGKAVEEAREQVAKLLGAEPDEIIFTSGGTESDNTAIKSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 84 RANRHKgNHIITTQIEHHAILHTCELLEREGFEVTYLPVDETGRVQVSDIQKALTEETILVSIMFGNNEVGTMQPIAEIG 163
Cdd:TIGR03402 81 AAQPEK-RHIITTAVEHPAVLSLCQHLEKQGYKVTYLPVDEEGRLDLEELRAAITDDTALVSVMWANNETGTIFPIEEIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 164 KLLKEHQAYFHTDAVQAYGLVEIDVKEFGIDLLSISAHKINGPKGVGFLYAGADVKFEPLLIGGEQERKRRAGTENVPSI 243
Cdd:TIGR03402 160 EIAKERGALFHTDAVQAVGKIPIDLKEMNIDMLSLSGHKLHGPKGVGALYIRKGTRFRPLLRGGHQERGRRAGTENVPGI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 244 VGLQHAILLAEKTREQKNAQYEEFKDIMVSVFKNEDITFEVNGNLEYRLPHVLNISFTGMNIEPFLVNLDLAGIAVSSGS 323
Cdd:TIGR03402 240 VGLGKAAELATEHLEEENTRVRALRDRLEAGLLARIPDARLNGDPTKRLPNTVNISFEYIEGEAILLLLDMEGICASSGS 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 446362049 324 ACTAGSIDPSHVLVAMfGKDSDQIRSSVRFSFGLGNTKEQIEKAAYETVKIVKRL 378
Cdd:TIGR03402 320 ACTSGSLEPSHVLRAM-GVPHTAAHGSIRFSLSRYNTEEDIDYVLEVLPPIIARL 373
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
4-365 |
2.34e-140 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 403.65 E-value: 2.34e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 4 IYLDHAATSPTHPEVVEKMIPYMTETFGNPSSI-HFYGRQTRHAVDEARRACARSIHANPNEIIFTSGGTEADNLALIGV 82
Cdd:PLN02651 1 LYLDMQATTPIDPRVLDAMLPFLIEHFGNPHSRtHLYGWESEDAVEKARAQVAALIGADPKEIIFTSGATESNNLAIKGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 83 ARANRHKGNHIITTQIEHHAILHTCELLEREGFEVTYLPVDETGRVQVSDIQKALTEETILVSIMFGNNEVGTMQPIAEI 162
Cdd:PLN02651 81 MHFYKDKKKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVEEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 163 GKLLKEHQAYFHTDAVQAYGLVEIDVKEFGIDLLSISAHKINGPKGVGFLYA--GADVKFEPLLIGGEQERKRRAGTENV 240
Cdd:PLN02651 161 GELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVrrRPRVRLEPLMSGGGQERGRRSGTENT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 241 PSIVGLQHAILLAEKTREQKNAQYEEFKDIMVSVFKNEDITFEVNG--NLEYRLPHVLNISFTGMNIEPFLVNldLAGIA 318
Cdd:PLN02651 241 PLVVGLGAACELAMKEMDYDEKHMKALRERLLNGLRAKLGGVRVNGprDPEKRYPGTLNLSFAYVEGESLLMG--LKEVA 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 446362049 319 VSSGSACTAGSIDPSHVLVAMfGKDSDQIRSSVRFSFGLGNTKEQIE 365
Cdd:PLN02651 319 VSSGSACTSASLEPSYVLRAL-GVPEEMAHGSLRLGVGRFTTEEEVD 364
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
4-378 |
4.66e-140 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 404.32 E-value: 4.66e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 4 IYLDHAATSPTHPEVVEKMIPYMT--ETFGNPSS-IHFYGRQTRHAVDEARRACARSIHANPNEIIFTSGGTEADNLALI 80
Cdd:PRK14012 5 IYLDYSATTPVDPRVAEKMMPYLTmdGTFGNPASrSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDNLAIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 81 GVARANRHKGNHIITTQIEHHAILHTCELLEREGFEVTYLPVDETGRVQVSDIQKALTEETILVSIMFGNNEVGTMQPIA 160
Cdd:PRK14012 85 GAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVIQDIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 161 EIGKLLKEHQAYFHTDAVQAYGLVEIDVKEFGIDLLSISAHKINGPKGVGFLYA--GADVKFEPLLIGGEQERKRRAGTE 238
Cdd:PRK14012 165 AIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVrrKPRVRLEAQMHGGGHERGMRSGTL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 239 NVPSIVGLQHAILLAEKTREQKNAQYEEFKDIMVSVFKNEDITFeVNGNLEYRLPHVLNISFTGMNIEPFLvnLDLAGIA 318
Cdd:PRK14012 245 PTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGIKDIEEVY-LNGDLEQRVPGNLNVSFNYVEGESLI--MALKDLA 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 319 VSSGSACTAGSIDPSHVLVAMfGKDSDQIRSSVRFSFGLGNTKEQIEKAAYETVKIVKRL 378
Cdd:PRK14012 322 VSSGSACTSASLEPSYVLRAL-GLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGKL 380
|
|
| DNA_S_dndA |
TIGR03235 |
cysteine desulfurase DndA; This model describes DndA, a protein related to IscS and part of a ... |
5-354 |
7.38e-133 |
|
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: 384.15 E-value: 7.38e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 5 YLDHAATSPTHPEVVEKMIPYMTETFGNPSSI-HFYGRQTRHAVDEARRACARSIHANPNEIIFTSGGTEADNLALIGVA 83
Cdd:TIGR03235 1 YLDHNATTPIDPAVAEAMLPWLLEEFGNPSSRtHEFGHNAKKAVERARKQVAEALGADTEEVIFTSGATESNNLAILGLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 84 RANRHKG-NHIITTQIEHHAILHTCELLEREGFEVTYLPVDETGRVQVSDIQKALTEETILVSIMFGNNEVGTMQPIAEI 162
Cdd:TIGR03235 81 RAGEQKGkKHIITSAIEHPAVLEPIRALERNGFTVTYLPVDESGRIDVDELADAIRPDTLLVSIMHVNNETGSIQPIREI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 163 GKLLKEHQAYFHTDAVQAYGLVEIDVKEFGIDLLSISAHKINGPKGVGFLYAGADVK----FEPLLIGGEQERKRRAGTE 238
Cdd:TIGR03235 161 AEVLEAHEAFFHVDAAQVVGKITVDLSADRIDLISCSGHKIYGPKGIGALVIRKRGKpkapLKPIMFGGGQERGLRPGTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 239 NVPSIVGLQHAILLAEKTREQKNAQYEEFKDIMVSVFKNEDITFevNGNLEYRLPHVLNISFTGMNIEPFLVNLDlAGIA 318
Cdd:TIGR03235 241 PVHLIVGMGEAAEIARRNAQAWEVKLRAMRNQLRDALQTLGVKL--NGDPAETIPHILNFSIDGVNSEALIVNLR-ADAA 317
|
330 340 350
....*....|....*....|....*....|....*.
gi 446362049 319 VSSGSACTAGSIDPSHVLVAMFGkDSDQIRSSVRFS 354
Cdd:TIGR03235 318 VSTGSACSSSKYEPSHVLQAMGL-DTDRARGAIRFS 352
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
4-366 |
6.63e-110 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 326.69 E-value: 6.63e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 4 IYLDHAATSPTHPEVVEKMIPYMTETFGNPSSIHFYGRQTRHAVDEARRACARSIHANPNEIIFTSGGTEADNLALIGVA 83
Cdd:PRK02948 2 IYLDYAATTPMSKEALQTYQKAASQYFGNESSLHDIGGTASSLLQVCRKTFAEMIGGEEQGIYFTSGGTESNYLAIQSLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 84 RANRHKGNHIITTQIEHHAILHTCELLEREGFEVTYLPVDETGRVQVSDIQKALTEETILVSIMFGNNEVGTMQPIAEIG 163
Cdd:PRK02948 82 NALPQNKKHIITTPMEHASIHSYFQSLESQGYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQPIAEIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 164 KLLKEHQAYFHTDAVQAYGLVEIDVKEFGIDLLSISAHKINGPKGVGFLYAGADVKFEPLLIGGEQERKRRAGTENVPSI 243
Cdd:PRK02948 162 ALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYINPQVRWKPVFPGTTHEKGFRPGTVNVPGI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 244 VGLQHAILLAEKTREQKNAQYEEFKDIMVSVFKNEDITFEVNGNLEYRLPHVLNISFTGmnIEPFLVNLDL--AGIAVSS 321
Cdd:PRK02948 242 AAFLTAAENILKNMQEESLRFKELRSYFLEQIQTLPLPIEVEGHSTSCLPHIIGVTIKG--IEGQYTMLECnrRGIAIST 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 446362049 322 GSACTAGSIDPSHVLVAMfGKDSDQIRSSVRFSFGLGNTKEQIEK 366
Cdd:PRK02948 320 GSACQVGKQEPSKTMLAI-GKTYEEAKQFVRFSFGQQTTKDQIDT 363
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
4-366 |
4.38e-96 |
|
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: 291.07 E-value: 4.38e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 4 IYLDHAATSPTHPEVVEKMIPYMTETFGNP-SSIHFYGRQTRHAVDEARRACARSIHANPN-EIIFTSGGTEADNLALIG 81
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVhRGVHTLGKEATQAYEEAREKVAEFINAPSNdEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 82 VARANRhKGNHIITTQIEHHAILHTCELL-EREGFEVTYLPVDETGRVQVSDIQKALTEETILVSIMFGNNEVGTMQPIA 160
Cdd:pfam00266 81 LGRSLK-PGDEIVITEMEHHANLVPWQELaKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 161 EIGKLLKEHQAYFHTDAVQAYGLVEIDVKEFGIDLLSISAHKINGPKGVGFLYA--GADVKFEPLLIGG----------- 227
Cdd:pfam00266 160 EIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGrrDLLEKMPPLLGGGgmietvslqes 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 228 ---EQERKRRAGTENVPSIVGLQHAILLAEKTREQKNAQYE-EFKDIMVSVFKNEDItFEVNGNLeyRLPHVLNISFTGM 303
Cdd:pfam00266 240 tfaDAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEhELAQYLYERLLSLPG-IRLYGPE--RRASIISFNFKGV 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446362049 304 NIEPFLVNLDLAGIAVSSGSACTagsiDPSHVLVAMfgkdsdqiRSSVRFSFGLGNTKEQIEK 366
Cdd:pfam00266 317 HPHDVATLLDESGIAVRSGHHCA----QPLMVRLGL--------GGTVRASFYIYNTQEDVDR 367
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
4-378 |
6.57e-70 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 224.63 E-value: 6.57e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 4 IYLDHAATSPTHPEVVEKMIPYMTETFGNPS-SIHFYGRQTRHAVDEARRACARSIHAN-PNEIIFTSGGTEADNLALIG 81
Cdd:COG0520 17 VYLDNAATGQKPRPVIDAIRDYYEPYNANVHrGAHELSAEATDAYEAAREKVARFIGAAsPDEIIFTRGTTEAINLVAYG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 82 VARANrhKGNHIITTQIEHHAILHTC-ELLEREGFEVTYLPVDETGRVQVSDIQKALTEETILVSIMFGNNEVGTMQPIA 160
Cdd:COG0520 97 LGRLK--PGDEILITEMEHHSNIVPWqELAERTGAEVRVIPLDEDGELDLEALEALLTPRTKLVAVTHVSNVTGTVNPVK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 161 EIGKLLKEHQAYFHTDAVQAYGLVEIDVKEFGIDLLSISAHKINGPKGVGFLYAGADV--KFEPLLIGGEQ--------- 229
Cdd:COG0520 175 EIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELleALPPFLGGGGMiewvsfdgt 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 230 -----ERKRRAGTENVPSIVGLQHAILLAEK-------TREQKNAQY--EEFKDImvsvfknEDITFEVNGNLEYRLPhv 295
Cdd:COG0520 255 tyadlPRRFEAGTPNIAGAIGLGAAIDYLEAigmeaieARERELTAYalEGLAAI-------PGVRILGPADPEDRSG-- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 296 lNISFTGMNIEPFLVN--LDLAGIAVSSGSACTagsidpsHVLVAMFGkdsdqIRSSVRFSFGLGNTKEQIEKAAyETVK 373
Cdd:COG0520 326 -IVSFNVDGVHPHDVAalLDDEGIAVRAGHHCA-------QPLMRRLG-----VPGTVRASFHLYNTEEEIDRLV-EALK 391
|
....*
gi 446362049 374 IVKRL 378
Cdd:COG0520 392 KLAEL 396
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
4-368 |
1.65e-66 |
|
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: 215.02 E-value: 1.65e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 4 IYLDHAATSPTHPEVVEKMIPYMTETFGNPS-SIHFYGRQTRHAVDEARRACARSIHA-NPNEIIFTSGGTEADNLALIG 81
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHrGVHELSARATDAYEAAREKVARFINApSPDEIIFTRNTTEAINLVAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 82 VARANRhKGNHIITTQIEHHAILHTCELL-EREGFEVTYLPVDETGRVQVSDIQKALTEETILVSIMFGNNEVGTMQPIA 160
Cdd:cd06453 81 LGRANK-PGDEIVTSVMEHHSNIVPWQQLaERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 161 EIGKLLKEHQAYFHTDAVQAYGLVEIDVKEFGIDLLSISAHKINGPKGVGFLYA--GADVKFEPLLIGGEQER------- 231
Cdd:cd06453 160 EIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGkeELLEEMPPYGGGGEMIEevsfeet 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 232 -------KRRAGTENVPSIVGLQHAILLAEKT-------REQKNAQY--EEFKDI-MVSVFKNED-----ITFEVNGnle 289
Cdd:cd06453 240 tyadlphKFEAGTPNIAGAIGLGAAIDYLEKIgmeaiaaHEHELTAYalERLSEIpGVRVYGDAEdragvVSFNLEG--- 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446362049 290 yRLPHvlNISFTgmniepflvnLDLAGIAVSSGSACtagsidpSHVLVAMFGkdsdqIRSSVRFSFGLGNTKEQIEKAA 368
Cdd:cd06453 317 -IHPH--DVATI----------LDQYGIAVRAGHHC-------AQPLMRRLG-----VPGTVRASFGLYNTEEEIDALV 370
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
4-365 |
3.36e-34 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 131.02 E-value: 3.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 4 IYLDHAATSPTHPEVVEKMIPYMTETFGN-PSSIHFYGRQTRHAVDEARRACARSIHA-NPNEIIFTSGGTEADNLALIG 81
Cdd:PLN02855 34 VYLDNAATSQKPAAVLDALQDYYEEYNSNvHRGIHALSAKATDAYELARKKVAAFINAsTSREIVFTRNATEAINLVAYT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 82 VARANRHKGNHIITTQIEHHAILHTCELL-EREGFEVTYLPVDETGRVQVSDIQKALTEETILVSIMFGNNEVGTMQPIA 160
Cdd:PLN02855 114 WGLANLKPGDEVILSVAEHHSNIVPWQLVaQKTGAVLKFVGLTPDEVLDVEQLKELLSEKTKLVATHHVSNVLGSILPVE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 161 EIGKLLKEHQAYFHTDAVQAYGLVEIDVKEFGIDLLSISAHKINGPKGVGFLYAGADV--KFEPLLIGGE---------- 228
Cdd:PLN02855 194 DIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLWGKSDLleSMPPFLGGGEmisdvfldhs 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 229 --QERKRR--AGTENVPSIVGLQHAILLAEKTREQKNAQYEEfkdimvsvfkneditfEVNGNLEYRLPHVLNI------ 298
Cdd:PLN02855 274 tyAPPPSRfeAGTPAIGEAIGLGAAIDYLSEIGMDRIHEYEV----------------ELGTYLYEKLSSVPGVriygpk 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 299 -----------SFTGMNIEPFLVN--LDLA-GIAVSSGSACTagsiDPSHVLVAmfgkdsdqIRSSVRFSFGLGNTKEQI 364
Cdd:PLN02855 338 psegvgraalcAFNVEGIHPTDLStfLDQQhGVAIRSGHHCA----QPLHRYLG--------VNASARASLYFYNTKEEV 405
|
.
gi 446362049 365 E 365
Cdd:PLN02855 406 D 406
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
4-266 |
2.55e-29 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 117.16 E-value: 2.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 4 IYLDHAATSPTHPEVVEKMIP-YMTETFGNPSSIHFYGRQTRHAVDEARRACARSIHA-NPNEIIFTSGGTEADNLALIG 81
Cdd:PRK09295 25 AYLDSAASAQKPSQVIDAEAEfYRHGYAAVHRGIHTLSAQATEKMENVRKQAALFINArSAEELVFVRGTTEGINLVANS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 82 VARANRHKGNHIITTQIEHHA-ILHTCELLEREGFEVTYLPVDETGRVQVSDIQKALTEETILVSIMFGNNEVGTMQPIA 160
Cdd:PRK09295 105 WGNSNVRAGDNIIISEMEHHAnIVPWQMLCARVGAELRVIPLNPDGTLQLETLPALFDERTRLLAITHVSNVLGTENPLA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 161 EIGKLLKEHQAYFHTDAVQAYGLVEIDVKEFGIDLLSISAHKINGPKGVGFLYA--------------GADVKFEPLLIG 226
Cdd:PRK09295 185 EMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVkeallqemppweggGSMIATVSLTEG 264
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446362049 227 ---GEQERKRRAGTENVPSIVGLQHAILLAEKTREQKNAQYEE 266
Cdd:PRK09295 265 ttwAKAPWRFEAGTPNTGGIIGLGAALDYVSALGLNNIAEYEQ 307
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
4-365 |
2.79e-21 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 94.33 E-value: 2.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 4 IYLDHAATSPTHPEVVEKMIPYMTETFGN-PSSIHFYGRQTRHAVDEARRACARSIHAN-PNEIIFTSGGTEADNLALIG 81
Cdd:PRK10874 21 VYLDSAATALKPQAVIEATQQFYSLSAGNvHRSQFAAAQRLTARYEAAREQVAQLLNAPdAKNIVWTRGTTESINLVAQS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 82 VARANRHKGNHIITTQIEHHAILHTCELL-EREGFEVTYLPVDETGRVQVSDIQKALTEETILVSIMFGNNEVGTMQPIA 160
Cdd:PRK10874 101 YARPRLQPGDEIIVSEAEHHANLVPWLMVaQQTGAKVVKLPLGADRLPDVDLLPELITPRTRILALGQMSNVTGGCPDLA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 161 EIGKLLKEHQAYFHTDAVQayGLVE--IDVKEFGIDLLSISAHKINGPKGVGFLYAGADV--KFEPLLIGG--------- 227
Cdd:PRK10874 181 RAITLAHQAGMVVMVDGAQ--GAVHfpADVQALDIDFYAFSGHKLYGPTGIGVLYGKSELleAMSPWQGGGkmltevsfd 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 228 ---EQERKRR--AGTENVPSIVGL----------------QHAILLAEKTrEQKNAQYEEFKdimvsvfkneditfevng 286
Cdd:PRK10874 259 gftPQSAPWRfeAGTPNVAGVIGLsaalewladidinqaeSWSRSLATLA-EDALAKLPGFR------------------ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 287 nlEYRLPH--VLNISFTGMNiEPFLVNLdLA--GIAVSSGSACTAgsidPshvLVAMFGkdsdqIRSSVRFSFGLGNTKE 362
Cdd:PRK10874 320 --SFRCQDssLLAFDFAGVH-HSDLVTL-LAeyGIALRAGQHCAQ----P---LLAALG-----VTGTLRASFAPYNTQS 383
|
...
gi 446362049 363 QIE 365
Cdd:PRK10874 384 DVD 386
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
4-218 |
3.68e-20 |
|
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: 92.22 E-value: 3.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 4 IYLDHAATspTH-PEVVEKMIPYMTETfGNpSSIH-----FYGRQTrHAVDEARRACARSIHA-NPNEIIFTSGGTEADN 76
Cdd:NF041166 247 VWFDNAAT--TQkPQAVIDRLSYFYEH-EN-SNIHraaheLAARAT-DAYEGAREKVRRFIGApSVDEIIFVRGTTEAIN 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 77 LaligVA----RANRHKGNHIITTQIEHHA-ILHTCELLEREGFEVTYLPVDETGRVQVSDIQKALTEETILVSIMFGNN 151
Cdd:NF041166 322 L----VAkswgRQNIGAGDEIIVSHLEHHAnIVPWQQLAQETGAKLRVIPVDDSGQILLDEYAKLLNPRTKLVSVTQVSN 397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446362049 152 EVGTMQPIAEIgkllkehqayfhTDAVQAYG---LVE---------IDVKEFGIDLLSISAHKINGPKGVGFLYAGADV 218
Cdd:NF041166 398 ALGTVTPVKEI------------IALAHRAGakvLVDgaqsvshmpVDVQALDADFFVFSGHKVFGPTGIGVVYGKRDL 464
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
66-212 |
8.34e-13 |
|
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: 69.48 E-value: 8.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 66 IFTSGGTEAdNL-ALIgVAR------ANRHKGNH------IITTQIEHHAILHTCELLereGFE---VTYLPVDETGRVQ 129
Cdd:COG0076 129 VFTSGGTEA-NLlALL-AARdralarRVRAEGLPgaprprIVVSEEAHSSVDKAARLL---GLGrdaLRKVPVDEDGRMD 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 130 VSDIQKALTE------ETILVSIMFGNNEVGTMQPIAEIGKLLKEHQAYFHTDAvqAYG---LVEIDVKEF--GIDL--- 195
Cdd:COG0076 204 PDALEAAIDEdraaglNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDA--AYGgfaLPSPELRHLldGIERads 281
|
170
....*....|....*...
gi 446362049 196 LSISAHK-INGPKGVGFL 212
Cdd:COG0076 282 ITVDPHKwLYVPYGCGAV 299
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
54-212 |
1.25e-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: 68.38 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 54 CARSIHANPNEI--IFTSGGTEADNLALIGVARANRHKGNH----------IITTQIEHHAILHTCELLEREgfeVTYLP 121
Cdd:cd06450 47 LAKLFGLPSEDAdgVFTSGGSESNLLALLAARDRARKRLKAgggrgidklvIVCSDQAHVSVEKAAAYLDVK---VRLVP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 122 VDETGRVQVSDIQKALTEE------TILVSIMFGNNEVGTMQPIAEIGKLLKEHQAYFHTDAvqAYG-----LVEIDVKE 190
Cdd:cd06450 124 VDEDGRMDPEALEAAIDEDkaeglnPIMVVATAGTTDTGAIDPLEEIADLAEKYDLWLHVDA--AYGgfllpFPEPRHLD 201
|
170 180
....*....|....*....|....*.
gi 446362049 191 FGI---DLLSISAHKING-PKGVGFL 212
Cdd:cd06450 202 FGIervDSISVDPHKYGLvPLGCSAV 227
|
|
| PucG |
COG0075 |
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ... |
107-212 |
2.05e-11 |
|
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: 64.73 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 107 CELLEREGFEVTYLPVDETGRVQVSDIQKALTEETILVSIMFGNNEV--GTMQPIAEIGKLLKEHQAYFHTDAVQAYGLV 184
Cdd:COG0075 90 AEIAERYGAEVVVLEVPWGEAVDPEEVEEALAADPDIKAVAVVHNETstGVLNPLEEIGALAKEHGALLIVDAVSSLGGV 169
|
90 100
....*....|....*....|....*....
gi 446362049 185 EIDVKEFGIDLLSISAHK-INGPKGVGFL 212
Cdd:COG0075 170 PLDMDEWGIDVVVSGSQKcLMLPPGLAFV 198
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
47-213 |
1.61e-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: 59.32 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 47 VDEARRACARSIHANPNEIIFTSGGTEADNLALIGVARanrhKGNHIITTQIEHHAilHTCELLEREGFEVTYLPVDETG 126
Cdd:cd01494 2 LEELEEKLARLLQPGNDKAVFVPSGTGANEAALLALLG----PGDEVIVDANGHGS--RYWVAAELAGAKPVPVPVDDAG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 127 RVQVSD---IQKALTEETILVSIMFGNNEVGTMQPIAEIGKLLKEHQAYFHTDAVQAYGLV---EIDVKEFGIDLLSISA 200
Cdd:cd01494 76 YGGLDVailEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASpapGVLIPEGGADVVTFSL 155
|
170
....*....|...
gi 446362049 201 HKINGPKGVGFLY 213
Cdd:cd01494 156 HKNLGGEGGGVVI 168
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
108-212 |
9.05e-10 |
|
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: 59.61 E-value: 9.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 108 ELLEREGFEVTYLPVDETGRVQVSDIQKALTEETI-LVSIMFGNNEVGTMQPIAEIGKLLKEHQAYFHTDAVQAYGLVEI 186
Cdd:cd06451 91 DMAERYGADVDVVEKPWGEAVSPEEIAEALEQHDIkAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVDAVSSLGGEPF 170
|
90 100
....*....|....*....|....*..
gi 446362049 187 DVKEFGIDLLSISAHK-INGPKGVGFL 212
Cdd:cd06451 171 RMDEWGVDVAYTGSQKaLGAPPGLGPI 197
|
|
| PRK13479 |
PRK13479 |
2-aminoethylphosphonate--pyruvate transaminase; Provisional |
103-214 |
9.17e-10 |
|
2-aminoethylphosphonate--pyruvate transaminase; Provisional
Pssm-ID: 184076 [Multi-domain] Cd Length: 368 Bit Score: 59.54 E-value: 9.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 103 ILHTCELLEREgfeVTYLPVDETGRVQVSDIQKALTEETILVSIMFGNNEVGT--MQPIAEIGKLLKEHQAYFHTDAVQA 180
Cdd:PRK13479 95 IAQIAEYLGIA---HVVLDTGEDEPPDAAEVEAALAADPRITHVALVHCETTTgiLNPLDEIAAVAKRHGKRLIVDAMSS 171
|
90 100 110
....*....|....*....|....*....|....*
gi 446362049 181 YGLVEIDVKEFGIDLLSISAHK-INGPKGVGFLYA 214
Cdd:PRK13479 172 FGAIPIDIAELGIDALISSANKcIEGVPGFGFVIA 206
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
13-368 |
3.74e-07 |
|
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.
Pssm-ID: 99734 [Multi-domain] Cd Length: 350 Bit Score: 51.57 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 13 PTHPEVVEKMIpymteTFGNPSSIHFYGRQTRHavDEARRACA------RSIHANPNEIIFTSGGTEADNLALIGVARAn 86
Cdd:cd00609 11 PPPPEVLEALA-----AAALRAGLLGYYPDPGL--PELREAIAewlgrrGGVDVPPEEIVVTNGAQEALSLLLRALLNP- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 87 rhkGNHIITTQIEHHAILHTCELLereGFEVTYLPVDETGRVQVS--DIQKALTEETILVSIMFGNNEVGTMQP---IAE 161
Cdd:cd00609 83 ---GDEVLVPDPTYPGYEAAARLA---GAEVVPVPLDEEGGFLLDleLLEAAKTPKTKLLYLNNPNNPTGAVLSeeeLEE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 162 IGKLLKEHQAY---------FHTDAVQAYGLVEIDVKEFGIDLLSISahKINGPKG--VGFLYAGadvkfEPLLIggEQE 230
Cdd:cd00609 157 LAELAKKHGILiisdeayaeLVYDGEPPPALALLDAYERVIVLRSFS--KTFGLPGlrIGYLIAP-----PEELL--ERL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 231 RKRRAGTENVPSIVGlQHAILLAEKT------------REQKNAQYEEFKDIMVSVFKNEDITFevngnleyrlpHVLnI 298
Cdd:cd00609 228 KKLLPYTTSGPSTLS-QAAAAAALDDgeehleelreryRRRRDALLEALKELGPLVVVKPSGGF-----------FLW-L 294
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446362049 299 SFTGMNIEPFLVN-LDLAGIAVSSGSACtaGSIDPSHvlvamfgkdsdqirssVRFSFglGNTKEQIEKAA 368
Cdd:cd00609 295 DLPEGDDEEFLERlLLEAGVVVRPGSAF--GEGGEGF----------------VRLSF--ATPEEELEEAL 345
|
|
| ARO8 |
COG1167 |
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ... |
44-142 |
1.82e-06 |
|
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain [Transcription, Amino acid transport and metabolism]; DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 440781 [Multi-domain] Cd Length: 471 Bit Score: 49.83 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 44 RHAVdeARRACARSIHANPNEIIFTSGGTEADNLALIGVARAnrhkGNHIITTQIEHHAILHtceLLEREGFEVTYLPVD 123
Cdd:COG1167 154 REAI--ARYLARRGVPASPDQILITSGAQQALDLALRALLRP----GDTVAVESPTYPGALA---ALRAAGLRLVPVPVD 224
|
90
....*....|....*....
gi 446362049 124 ETGrVQVSDIQKALTEETI 142
Cdd:COG1167 225 EDG-LDLDALEAALRRHRP 242
|
|
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
4-212 |
1.58e-05 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 47.17 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 4 IYLDHA-ATSPTHPEVVEKMIPYMTETFGNPSSIHFYGRQTRHAVDEARRACARSIHANPNE--IIFTSGGTEAdnLALI 80
Cdd:PLN02724 36 VYLDHAgATLYSESQLEAALADFSSNVYGNPHSQSDSSMRSSDTIESARQQVLEYFNAPPSDyaCVFTSGATAA--LKLV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 81 GVARANRHKGNHIITTQiEHHAILHTCEL-LEREG--------------------FEVTYLPVDETGRVQVSdiQKALTE 139
Cdd:PLN02724 114 GETFPWSSESHFCYTLE-NHNSVLGIREYaLEKGAaaiavdieeaanqptnsqgsVVVKSRGLQRRNTSKLQ--KREDDG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 140 ETI-LVSIMFGNNEVGTMQPIaEIGKLLKEHQAYFHT---------DAVQAYGLVEIDVKEFGIDLLSISAHKING-PKG 208
Cdd:PLN02724 191 EAYnLFAFPSECNFSGAKFPL-DLVKLIKDNQHSNFSksgrwmvllDAAKGCGTSPPDLSRYPADFVVVSFYKIFGyPTG 269
|
....
gi 446362049 209 VGFL 212
Cdd:PLN02724 270 LGAL 273
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
66-202 |
3.57e-04 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 42.40 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 66 IFTSGGTEADNLALIGvARAN-------RHKGNH--------IITTQIEHHAILHTCELLEreGFEVTYLPVDETGRVQV 130
Cdd:pfam00282 106 VLQPGSSESNLLALLA-ARTKwikrmkaAGKPADssgilaklVAYTSDQAHSSIEKAALYG--GVKLREIPSDDNGKMRG 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 131 SDIQKALTEE-----TIL-VSIMFGNNEVGTMQPIAEIGKLLKEHQAYFHTDAVQAYGLV---EIDVKEFGIDL---LSI 198
Cdd:pfam00282 183 MDLEKAIEEDkenglIPFfVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAYGGSAFicpEFRHWLFGIERadsITF 262
|
....
gi 446362049 199 SAHK 202
Cdd:pfam00282 263 NPHK 266
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
65-270 |
5.95e-04 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 41.43 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 65 IIFTSGGTEADNLALigvaRANRHKGNHIITTQiEHHAILHTCE-LLEREGFEVTYLPVDETGRVQVSDIQKALTE---- 139
Cdd:pfam01212 50 ALFVPSGTAANQLAL----MAHCQRGDEVICGE-PAHIHFDETGgHAELGGVQPRPLDGDEAGNMDLEDLEAAIREvgad 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 140 ---ETILVSIMFGNNEVG----TMQPIAEIGKLLKEHQAYFHTD------AVQAYGlveIDVKEF--GIDLLSISAHKiN 204
Cdd:pfam01212 125 ifpPTGLISLENTHNSAGgqvvSLENLREIAALAREHGIPVHLDgarfanAAVALG---VIVKEItsYADSVTMCLSK-G 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446362049 205 GPKGVGFLYAGAD------VKFEPLLIGGeqerKRRAGTENVPSIVGLQHAILLAEktREQKNAQ--YEEFKDI 270
Cdd:pfam01212 201 LGAPVGSVLAGSDdfiakaIRQRKYLGGG----LRQAGVLAAAGLRALEEGVARLA--RDHATARrlAEGLELL 268
|
|
| PRK07324 |
PRK07324 |
transaminase; Validated |
59-199 |
4.84e-03 |
|
transaminase; Validated
Pssm-ID: 235989 Cd Length: 373 Bit Score: 38.77 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446362049 59 HANPNEIIFTSGGTEADNLALIGVARAnrhkGNHIIT---TQIEHHAIlhtcelLEREGFEVTYLPVDETGRV--QVSDI 133
Cdd:PRK07324 77 NVKPENILQTNGATGANFLVLYALVEP----GDHVISvypTYQQLYDI------PESLGAEVDYWQLKEENGWlpDLDEL 146
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446362049 134 QKALTEETILVSIMFGNNEVGT------MQPIAEIGkllKEHQAYFHTDAV-----QAYGLVEI-DVKEFGIDLLSIS 199
Cdd:PRK07324 147 RRLVRPNTKLICINNANNPTGAlmdrayLEEIVEIA---RSVDAYVLSDEVyrpldEDGSTPSIaDLYEKGISTNSMS 221
|
|
| |
