|
Name |
Accession |
Description |
Interval |
E-value |
| 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: 559.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 1 MEVYADYAATTPVKPEVIDAMMEIYQSHFGNPSSIHSIGRDARKYLDQSRRTVAQLLGANPNEVIFTSGATESNNTAIKG 80
Cdd:COG1104 2 MMIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSSLHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNLAIKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 81 LVKANEQLGNHIITTKIEHHSVLHVYEQLEKEGYDVTYLDVDDTGAVDLDQLKETINDRTILVSIMFVNNEIGTVQNIYD 160
Cdd:COG1104 82 AARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQPIAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 161 IEDIIGDTHALFHIDAVQAIGHLDLDFHNFKIDTMSISAHKFGGPKGVGLLLVKEHTPIAYNQLGGEQETKRRAGTENLP 240
Cdd:COG1104 162 IAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRKGVRLEPLIHGGGQERGLRSGTENVP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 241 QIVGLTKALELAITNQDVNNVHLMNLKELFLVQLQERAIPFELNGSMTDSTGHILNIYFPFIDVETMLTLLDLAHVYVSS 320
Cdd:COG1104 242 GIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAAIPGVVINGDPENRLPNTLNFSFPGVEGEALLLALDLAGIAVSS 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 321 GSACTAGSTTPSHVLAAMFEDEERAKHSVRFSFNEQTTTQEIKYIVAEIHKIYHKFKEES 380
Cdd:COG1104 322 GSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARLRKLS 381
|
|
| FeS_nifS |
TIGR03402 |
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related ... |
3-380 |
6.61e-149 |
|
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: 425.87 E-value: 6.61e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 3 VYADYAATTPVKPEVIDAMMEIYQSHFGNPSSIHSIGRDARKYLDQSRRTVAQLLGANPNEVIFTSGATESNNTAIKGLV 82
Cdd:TIGR03402 1 IYLDNNATTRVDPEVLEAMLPYFTEYFGNPSSMHSFGGEVGKAVEEAREQVAKLLGAEPDEIIFTSGGTESDNTAIKSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 83 KANEQlGNHIITTKIEHHSVLHVYEQLEKEGYDVTYLDVDDTGAVDLDQLKETINDRTILVSIMFVNNEIGTVQNIYDIE 162
Cdd:TIGR03402 81 AAQPE-KRHIITTAVEHPAVLSLCQHLEKQGYKVTYLPVDEEGRLDLEELRAAITDDTALVSVMWANNETGTIFPIEEIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 163 DIIGDTHALFHIDAVQAIGHLDLDFHNFKIDTMSISAHKFGGPKGVGLLLVKEHTPIAYNQLGGEQETKRRAGTENLPQI 242
Cdd:TIGR03402 160 EIAKERGALFHTDAVQAVGKIPIDLKEMNIDMLSLSGHKLHGPKGVGALYIRKGTRFRPLLRGGHQERGRRAGTENVPGI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 243 VGLTKALELAITNQDVNNVHLMNLKELFLVQLQERaIPF-ELNGSMTDSTGHILNIYFPFIDVETMLTLLDLAHVYVSSG 321
Cdd:TIGR03402 240 VGLGKAAELATEHLEEENTRVRALRDRLEAGLLAR-IPDaRLNGDPTKRLPNTVNISFEYIEGEAILLLLDMEGICASSG 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 488435462 322 SACTAGSTTPSHVLAAMFEDEERAKHSVRFSFNEQTTTQEIKYIVAEIHKIYHKFKEES 380
Cdd:TIGR03402 319 SACTSGSLEPSHVLRAMGVPHTAAHGSIRFSLSRYNTEEDIDYVLEVLPPIIARLRAMS 377
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
3-362 |
3.24e-123 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 360.12 E-value: 3.24e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 3 VYADYAATTPVKPEVIDAMMEIYQSHFGNPSSI-HSIGRDARKYLDQSRRTVAQLLGANPNEVIFTSGATESNNTAIKGL 81
Cdd:PLN02651 1 LYLDMQATTPIDPRVLDAMLPFLIEHFGNPHSRtHLYGWESEDAVEKARAQVAALIGADPKEIIFTSGATESNNLAIKGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 82 VKANEQLGNHIITTKIEHHSVLHVYEQLEKEGYDVTYLDVDDTGAVDLDQLKETINDRTILVSIMFVNNEIGTVQNIYDI 161
Cdd:PLN02651 81 MHFYKDKKKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVEEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 162 EDIIGDTHALFHIDAVQAIGHLDLDFHNFKIDTMSISAHKFGGPKGVGLLLVKEHTPIAYNQL--GGEQETKRRAGTENL 239
Cdd:PLN02651 161 GELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRLEPLmsGGGQERGRRSGTENT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 240 PQIVGLTKALELAITNQDVNNVHLMNLKELFLVQLQERAIPFELNG--SMTDSTGHILNIYFPFIDVETML-TLLDLAhv 316
Cdd:PLN02651 241 PLVVGLGAACELAMKEMDYDEKHMKALRERLLNGLRAKLGGVRVNGprDPEKRYPGTLNLSFAYVEGESLLmGLKEVA-- 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 488435462 317 yVSSGSACTAGSTTPSHVLAAMFEDEERAKHSVRFSFNEQTTTQEI 362
Cdd:PLN02651 319 -VSSGSACTSASLEPSYVLRALGVPEEMAHGSLRLGVGRFTTEEEV 363
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
3-364 |
7.37e-81 |
|
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: 251.78 E-value: 7.37e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 3 VYADYAATTPVKPEVIDAMMEIYQSHFGNP-SSIHSIGRDARKYLDQSRRTVAQLLGANPN-EVIFTSGATESNNTAIKG 80
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVhRGVHTLGKEATQAYEEAREKVAEFINAPSNdEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 81 LvKANEQLGNHIITTKIEHHSVLHVYEQLEK-EGYDVTYLDVDDTGAVDLDQLKETINDRTILVSIMFVNNEIGTVQNIY 159
Cdd:pfam00266 81 L-GRSLKPGDEIVITEMEHHANLVPWQELAKrTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 160 DIEDIIGDTHALFHIDAVQAIGHLDLDFHNFKIDTMSISAHKFGGPKGVGLLLVKEH--TPIAYNQLGG----------- 226
Cdd:pfam00266 160 EIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDllEKMPPLLGGGgmietvslqes 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 227 ---EQETKRRAGTENLPQIVGLTKALELaITNQDVNNV--HLMNLKELFLVQLQEraIP-FELNGSmtDSTGHILNIYFP 300
Cdd:pfam00266 240 tfaDAPWKFEAGTPNIAGIIGLGAALEY-LSEIGLEAIekHEHELAQYLYERLLS--LPgIRLYGP--ERRASIISFNFK 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488435462 301 FIDVETMLTLLDLAHVYVSSGSACtagsTTPSHVLAAMfedeeraKHSVRFSFNEQTTTQEIKY 364
Cdd:pfam00266 315 GVHPHDVATLLDESGIAVRSGHHC----AQPLMVRLGL-------GGTVRASFYIYNTQEDVDR 367
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
3-362 |
3.86e-57 |
|
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: 190.75 E-value: 3.86e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 3 VYADYAATTPVKPEVIDAMMEIYQSHFGNPS-SIHSIGRDA-RKYLDqSRRTVAQLLGA-NPNEVIFTSGATESNNTAIK 79
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHrGVHELSARAtDAYEA-AREKVARFINApSPDEIIFTRNTTEAINLVAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 80 GLVKANEQlGNHIITTKIEHHSVLHVYEQLEKE-GYDVTYLDVDDTGAVDLDQLKETINDRTILVSIMFVNNEIGTVQni 158
Cdd:cd06453 80 GLGRANKP-GDEIVTSVMEHHSNIVPWQQLAERtGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTIN-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 159 yDIEDIIGDTH---ALFHIDAVQAIGHLDLDFHNFKIDTMSISAHKFGGPKGVGLLLVKEH---TPIAYnQLGGE----- 227
Cdd:cd06453 157 -PVKEIGEIAHeagVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEElleEMPPY-GGGGEmieev 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 228 --QET-------KRRAGTENLPQIVGLTKALELaITNQDVNNV--HLMNLKELFLVQLqeRAIP-FELNGSMTDSTGhIL 295
Cdd:cd06453 235 sfEETtyadlphKFEAGTPNIAGAIGLGAAIDY-LEKIGMEAIaaHEHELTAYALERL--SEIPgVRVYGDAEDRAG-VV 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488435462 296 NIYFPFIDVETMLTLLDLAHVYVSSGSACtagsTTPSHvlaAMFEDEerakHSVRFSFNEQTTTQEI 362
Cdd:cd06453 311 SFNLEGIHPHDVATILDQYGIAVRAGHHC----AQPLM---RRLGVP----GTVRASFGLYNTEEEI 366
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
6-250 |
4.18e-21 |
|
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: 94.92 E-value: 4.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 6 DYAATTPvKPE-VIDAMMEIYQSHfgNpSSIHsigR----------DArkYLDqSRRTVAQLLGA-NPNEVIFTSGATES 73
Cdd:NF041166 250 DNAATTQ-KPQaVIDRLSYFYEHE--N-SNIH---RaahelaaratDA--YEG-AREKVRRFIGApSVDEIIFVRGTTEA 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 74 NNTAIKGLVKANEQLGNHIITTKIEHHSVLHVYEQL-EKEGYDVTYLDVDDTGAVDLDQLKETINDRTILVSIMFVNNEI 152
Cdd:NF041166 320 INLVAKSWGRQNIGAGDEIIVSHLEHHANIVPWQQLaQETGAKLRVIPVDDSGQILLDEYAKLLNPRTKLVSVTQVSNAL 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 153 GTVQniyDIEDIIgdthALFH-------IDAVQAIGH-------LDLDFHNFkidtmsiSAHKFGGPKGVGLLLVKEH-- 216
Cdd:NF041166 400 GTVT---PVKEII----ALAHragakvlVDGAQSVSHmpvdvqaLDADFFVF-------SGHKVFGPTGIGVVYGKRDll 465
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 488435462 217 --TPiAYnQLGGE-------QET-------KRRAGTENLPQIVGLTKALE 250
Cdd:NF041166 466 eaMP-PW-QGGGNmiadvtfEKTvyqpapnRFEAGTGNIADAVGLGAALD 513
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| 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: 559.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 1 MEVYADYAATTPVKPEVIDAMMEIYQSHFGNPSSIHSIGRDARKYLDQSRRTVAQLLGANPNEVIFTSGATESNNTAIKG 80
Cdd:COG1104 2 MMIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSSLHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNLAIKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 81 LVKANEQLGNHIITTKIEHHSVLHVYEQLEKEGYDVTYLDVDDTGAVDLDQLKETINDRTILVSIMFVNNEIGTVQNIYD 160
Cdd:COG1104 82 AARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQPIAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 161 IEDIIGDTHALFHIDAVQAIGHLDLDFHNFKIDTMSISAHKFGGPKGVGLLLVKEHTPIAYNQLGGEQETKRRAGTENLP 240
Cdd:COG1104 162 IAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRKGVRLEPLIHGGGQERGLRSGTENVP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 241 QIVGLTKALELAITNQDVNNVHLMNLKELFLVQLQERAIPFELNGSMTDSTGHILNIYFPFIDVETMLTLLDLAHVYVSS 320
Cdd:COG1104 242 GIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAAIPGVVINGDPENRLPNTLNFSFPGVEGEALLLALDLAGIAVSS 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 321 GSACTAGSTTPSHVLAAMFEDEERAKHSVRFSFNEQTTTQEIKYIVAEIHKIYHKFKEES 380
Cdd:COG1104 322 GSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARLRKLS 381
|
|
| FeS_nifS |
TIGR03402 |
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related ... |
3-380 |
6.61e-149 |
|
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: 425.87 E-value: 6.61e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 3 VYADYAATTPVKPEVIDAMMEIYQSHFGNPSSIHSIGRDARKYLDQSRRTVAQLLGANPNEVIFTSGATESNNTAIKGLV 82
Cdd:TIGR03402 1 IYLDNNATTRVDPEVLEAMLPYFTEYFGNPSSMHSFGGEVGKAVEEAREQVAKLLGAEPDEIIFTSGGTESDNTAIKSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 83 KANEQlGNHIITTKIEHHSVLHVYEQLEKEGYDVTYLDVDDTGAVDLDQLKETINDRTILVSIMFVNNEIGTVQNIYDIE 162
Cdd:TIGR03402 81 AAQPE-KRHIITTAVEHPAVLSLCQHLEKQGYKVTYLPVDEEGRLDLEELRAAITDDTALVSVMWANNETGTIFPIEEIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 163 DIIGDTHALFHIDAVQAIGHLDLDFHNFKIDTMSISAHKFGGPKGVGLLLVKEHTPIAYNQLGGEQETKRRAGTENLPQI 242
Cdd:TIGR03402 160 EIAKERGALFHTDAVQAVGKIPIDLKEMNIDMLSLSGHKLHGPKGVGALYIRKGTRFRPLLRGGHQERGRRAGTENVPGI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 243 VGLTKALELAITNQDVNNVHLMNLKELFLVQLQERaIPF-ELNGSMTDSTGHILNIYFPFIDVETMLTLLDLAHVYVSSG 321
Cdd:TIGR03402 240 VGLGKAAELATEHLEEENTRVRALRDRLEAGLLAR-IPDaRLNGDPTKRLPNTVNISFEYIEGEAILLLLDMEGICASSG 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 488435462 322 SACTAGSTTPSHVLAAMFEDEERAKHSVRFSFNEQTTTQEIKYIVAEIHKIYHKFKEES 380
Cdd:TIGR03402 319 SACTSGSLEPSHVLRAMGVPHTAAHGSIRFSLSRYNTEEDIDYVLEVLPPIIARLRAMS 377
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
3-362 |
3.24e-123 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 360.12 E-value: 3.24e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 3 VYADYAATTPVKPEVIDAMMEIYQSHFGNPSSI-HSIGRDARKYLDQSRRTVAQLLGANPNEVIFTSGATESNNTAIKGL 81
Cdd:PLN02651 1 LYLDMQATTPIDPRVLDAMLPFLIEHFGNPHSRtHLYGWESEDAVEKARAQVAALIGADPKEIIFTSGATESNNLAIKGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 82 VKANEQLGNHIITTKIEHHSVLHVYEQLEKEGYDVTYLDVDDTGAVDLDQLKETINDRTILVSIMFVNNEIGTVQNIYDI 161
Cdd:PLN02651 81 MHFYKDKKKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVEEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 162 EDIIGDTHALFHIDAVQAIGHLDLDFHNFKIDTMSISAHKFGGPKGVGLLLVKEHTPIAYNQL--GGEQETKRRAGTENL 239
Cdd:PLN02651 161 GELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRLEPLmsGGGQERGRRSGTENT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 240 PQIVGLTKALELAITNQDVNNVHLMNLKELFLVQLQERAIPFELNG--SMTDSTGHILNIYFPFIDVETML-TLLDLAhv 316
Cdd:PLN02651 241 PLVVGLGAACELAMKEMDYDEKHMKALRERLLNGLRAKLGGVRVNGprDPEKRYPGTLNLSFAYVEGESLLmGLKEVA-- 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 488435462 317 yVSSGSACTAGSTTPSHVLAAMFEDEERAKHSVRFSFNEQTTTQEI 362
Cdd:PLN02651 319 -VSSGSACTSASLEPSYVLRALGVPEEMAHGSLRLGVGRFTTEEEV 363
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
3-380 |
7.73e-123 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 360.41 E-value: 7.73e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 3 VYADYAATTPVKPEVIDAMMEIYQSH--FGNPSS-IHSIGRDARKYLDQSRRTVAQLLGANPNEVIFTSGATESNNTAIK 79
Cdd:PRK14012 5 IYLDYSATTPVDPRVAEKMMPYLTMDgtFGNPASrSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDNLAIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 80 GLVKANEQLGNHIITTKIEHHSVLHVYEQLEKEGYDVTYLDVDDTGAVDLDQLKETINDRTILVSIMFVNNEIGTVQNIY 159
Cdd:PRK14012 85 GAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVIQDIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 160 DIEDIIGDTHALFHIDAVQAIGHLDLDFHNFKIDTMSISAHKFGGPKGVGLLLV--KEHTPIAYNQLGGEQETKRRAGTE 237
Cdd:PRK14012 165 AIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVrrKPRVRLEAQMHGGGHERGMRSGTL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 238 NLPQIVGLTKALELAITNQDVNNVHLMNLKELFLVQLQEraipFE---LNGSMTDSTGHILNIYFPFIDVET-MLTLLDL 313
Cdd:PRK14012 245 PTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGIKD----IEevyLNGDLEQRVPGNLNVSFNYVEGESlIMALKDL 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488435462 314 AhvyVSSGSACTAGSTTPSHVLAAMFEDEERAKHSVRFSFNEQTTTQEIKYIVAEIHKIYHKFKEES 380
Cdd:PRK14012 321 A---VSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGKLRELS 384
|
|
| DNA_S_dndA |
TIGR03235 |
cysteine desulfurase DndA; This model describes DndA, a protein related to IscS and part of a ... |
4-352 |
1.48e-116 |
|
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: 342.55 E-value: 1.48e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 4 YADYAATTPVKPEVIDAMMEIYQSHFGNPSSI-HSIGRDARKYLDQSRRTVAQLLGANPNEVIFTSGATESNNTAIKGLV 82
Cdd:TIGR03235 1 YLDHNATTPIDPAVAEAMLPWLLEEFGNPSSRtHEFGHNAKKAVERARKQVAEALGADTEEVIFTSGATESNNLAILGLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 83 KANEQLG-NHIITTKIEHHSVLHVYEQLEKEGYDVTYLDVDDTGAVDLDQLKETINDRTILVSIMFVNNEIGTVQNIYDI 161
Cdd:TIGR03235 81 RAGEQKGkKHIITSAIEHPAVLEPIRALERNGFTVTYLPVDESGRIDVDELADAIRPDTLLVSIMHVNNETGSIQPIREI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 162 EDIIGDTHALFHIDAVQAIGHLDLDFHNFKIDTMSISAHKFGGPKGVGLLLVKEH-------TPIAYnqlGGEQETKRRA 234
Cdd:TIGR03235 161 AEVLEAHEAFFHVDAAQVVGKITVDLSADRIDLISCSGHKIYGPKGIGALVIRKRgkpkaplKPIMF---GGGQERGLRP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 235 GTENLPQIVGLTKALELAITNQDVNNVHLMNLKELFLVQLQerAIPFELNGSMTDSTGHILNIYFPFIDVETMLTLLDlA 314
Cdd:TIGR03235 238 GTLPVHLIVGMGEAAEIARRNAQAWEVKLRAMRNQLRDALQ--TLGVKLNGDPAETIPHILNFSIDGVNSEALIVNLR-A 314
|
330 340 350
....*....|....*....|....*....|....*...
gi 488435462 315 HVYVSSGSACTAGSTTPSHVLAAMFEDEERAKHSVRFS 352
Cdd:TIGR03235 315 DAAVSTGSACSSSKYEPSHVLQAMGLDTDRARGAIRFS 352
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
3-380 |
9.30e-99 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 298.18 E-value: 9.30e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 3 VYADYAATTPVKPEVIDAMMEIYQSHFGNPSSIHSIGRDARKYLDQSRRTVAQLLGANPNEVIFTSGATESNNTAIKGLV 82
Cdd:PRK02948 2 IYLDYAATTPMSKEALQTYQKAASQYFGNESSLHDIGGTASSLLQVCRKTFAEMIGGEEQGIYFTSGGTESNYLAIQSLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 83 KANEQLGNHIITTKIEHHSVLHVYEQLEKEGYDVTYLDVDDTGAVDLDQLKETINDRTILVSIMFVNNEIGTVQNIYDIE 162
Cdd:PRK02948 82 NALPQNKKHIITTPMEHASIHSYFQSLESQGYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQPIAEIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 163 DIIGDTHALFHIDAVQAIGHLDLDFHNFKIDTMSISAHKFGGPKGVGLLLVKEHTPiaYNQL--GGEQETKRRAGTENLP 240
Cdd:PRK02948 162 ALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYINPQVR--WKPVfpGTTHEKGFRPGTVNVP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 241 QIVGLTKALELAITNQDVNNVHLMNLKELFLVQLQERAIPFELNGSMTDSTGHILNIYFPFIdvETMLTLLDL--AHVYV 318
Cdd:PRK02948 240 GIAAFLTAAENILKNMQEESLRFKELRSYFLEQIQTLPLPIEVEGHSTSCLPHIIGVTIKGI--EGQYTMLECnrRGIAI 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488435462 319 SSGSACTAGSTTPSHVLAAMFEDEERAKHSVRFSFNEQTTTQEIKYIVAEIHKIYHKFKEES 380
Cdd:PRK02948 318 STGSACQVGKQEPSKTMLAIGKTYEEAKQFVRFSFGQQTTKDQIDTTIHALETIGNQFYRGV 379
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
3-364 |
7.37e-81 |
|
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: 251.78 E-value: 7.37e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 3 VYADYAATTPVKPEVIDAMMEIYQSHFGNP-SSIHSIGRDARKYLDQSRRTVAQLLGANPN-EVIFTSGATESNNTAIKG 80
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVhRGVHTLGKEATQAYEEAREKVAEFINAPSNdEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 81 LvKANEQLGNHIITTKIEHHSVLHVYEQLEK-EGYDVTYLDVDDTGAVDLDQLKETINDRTILVSIMFVNNEIGTVQNIY 159
Cdd:pfam00266 81 L-GRSLKPGDEIVITEMEHHANLVPWQELAKrTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 160 DIEDIIGDTHALFHIDAVQAIGHLDLDFHNFKIDTMSISAHKFGGPKGVGLLLVKEH--TPIAYNQLGG----------- 226
Cdd:pfam00266 160 EIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDllEKMPPLLGGGgmietvslqes 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 227 ---EQETKRRAGTENLPQIVGLTKALELaITNQDVNNV--HLMNLKELFLVQLQEraIP-FELNGSmtDSTGHILNIYFP 300
Cdd:pfam00266 240 tfaDAPWKFEAGTPNIAGIIGLGAALEY-LSEIGLEAIekHEHELAQYLYERLLS--LPgIRLYGP--ERRASIISFNFK 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488435462 301 FIDVETMLTLLDLAHVYVSSGSACtagsTTPSHVLAAMfedeeraKHSVRFSFNEQTTTQEIKY 364
Cdd:pfam00266 315 GVHPHDVATLLDESGIAVRSGHHC----AQPLMVRLGL-------GGTVRASFYIYNTQEDVDR 367
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
3-372 |
1.64e-61 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 202.68 E-value: 1.64e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 3 VYADYAATTPvKPE-VIDAMMEIYQSHFGNPS-SIHSIGRDARKYLDQSRRTVAQLLGAN-PNEVIFTSGATESNNTAIK 79
Cdd:COG0520 17 VYLDNAATGQ-KPRpVIDAIRDYYEPYNANVHrGAHELSAEATDAYEAAREKVARFIGAAsPDEIIFTRGTTEAINLVAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 80 GLVKANEqlGNHIITTKIEHHSVLHVYEQLEKE-GYDVTYLDVDDTGAVDLDQLKETINDRTILVSIMFVNNEIGTVQNI 158
Cdd:COG0520 96 GLGRLKP--GDEILITEMEHHSNIVPWQELAERtGAEVRVIPLDEDGELDLEALEALLTPRTKLVAVTHVSNVTGTVNPV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 159 YDIEDIIGDTHALFHIDAVQAIGHLDLDFHNFKIDTMSISAHKFGGPKGVGLLLVKEHtpiAYNQL-----GGE------ 227
Cdd:COG0520 174 KEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRE---LLEALppflgGGGmiewvs 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 228 ------QETKRR--AGTENLPQIVGLTKALELaITNQDVNNV--HLMNLKELFLVQLQEraIP-FELNGSM-TDSTGHIL 295
Cdd:COG0520 251 fdgttyADLPRRfeAGTPNIAGAIGLGAAIDY-LEAIGMEAIeaRERELTAYALEGLAA--IPgVRILGPAdPEDRSGIV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 296 NIYFPFIDVETMLTLLDLAHVYVSSGSACtagsTTPSHvlaamfedeeRAKH---SVRFSFNEQTTTQEIKYIVAEIHKI 372
Cdd:COG0520 328 SFNVDGVHPHDVAALLDDEGIAVRAGHHC----AQPLM----------RRLGvpgTVRASFHLYNTEEEIDRLVEALKKL 393
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
3-362 |
3.86e-57 |
|
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: 190.75 E-value: 3.86e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 3 VYADYAATTPVKPEVIDAMMEIYQSHFGNPS-SIHSIGRDA-RKYLDqSRRTVAQLLGA-NPNEVIFTSGATESNNTAIK 79
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHrGVHELSARAtDAYEA-AREKVARFINApSPDEIIFTRNTTEAINLVAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 80 GLVKANEQlGNHIITTKIEHHSVLHVYEQLEKE-GYDVTYLDVDDTGAVDLDQLKETINDRTILVSIMFVNNEIGTVQni 158
Cdd:cd06453 80 GLGRANKP-GDEIVTSVMEHHSNIVPWQQLAERtGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTIN-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 159 yDIEDIIGDTH---ALFHIDAVQAIGHLDLDFHNFKIDTMSISAHKFGGPKGVGLLLVKEH---TPIAYnQLGGE----- 227
Cdd:cd06453 157 -PVKEIGEIAHeagVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEElleEMPPY-GGGGEmieev 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 228 --QET-------KRRAGTENLPQIVGLTKALELaITNQDVNNV--HLMNLKELFLVQLqeRAIP-FELNGSMTDSTGhIL 295
Cdd:cd06453 235 sfEETtyadlphKFEAGTPNIAGAIGLGAAIDY-LEKIGMEAIaaHEHELTAYALERL--SEIPgVRVYGDAEDRAG-VV 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488435462 296 NIYFPFIDVETMLTLLDLAHVYVSSGSACtagsTTPSHvlaAMFEDEerakHSVRFSFNEQTTTQEI 362
Cdd:cd06453 311 SFNLEGIHPHDVATILDQYGIAVRAGHHC----AQPLM---RRLGVP----GTVRASFGLYNTEEEI 366
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
3-211 |
4.32e-32 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 125.24 E-value: 4.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 3 VYADYAATTPVKPEVIDAMMEIYQSHFGN-PSSIHSIGRDARKYLDQSRRTVAQLLGA-NPNEVIFTSGATESNNTAIKG 80
Cdd:PLN02855 34 VYLDNAATSQKPAAVLDALQDYYEEYNSNvHRGIHALSAKATDAYELARKKVAAFINAsTSREIVFTRNATEAINLVAYT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 81 LVKANEQLGNHIITTKIEHHSVLhVYEQL--EKEGYDVTYLDVDDTGAVDLDQLKETINDRTILVSIMFVNNEIGTVQNI 158
Cdd:PLN02855 114 WGLANLKPGDEVILSVAEHHSNI-VPWQLvaQKTGAVLKFVGLTPDEVLDVEQLKELLSEKTKLVATHHVSNVLGSILPV 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488435462 159 YDIEDIIGDTHALFHIDAVQAIGHLDLDFHNFKIDTMSISAHKFGGPKGVGLL 211
Cdd:PLN02855 193 EDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFL 245
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
3-371 |
1.19e-25 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 106.66 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 3 VYADYAATTpVKPE-VIDAMMEIYQSHFGN-PSSIHSIGRDARKYLDQSRRTVAQLLGAN-PNEVIFTSGATESNNTAIK 79
Cdd:PRK10874 21 VYLDSAATA-LKPQaVIEATQQFYSLSAGNvHRSQFAAAQRLTARYEAAREQVAQLLNAPdAKNIVWTRGTTESINLVAQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 80 GLVKANEQLGNHIITTKIEHHS----VLHVYEQLekeGYDVTYLDVDDTGAVDLDQLKETINDRTILVSIMFVNNEIGTV 155
Cdd:PRK10874 100 SYARPRLQPGDEIIVSEAEHHAnlvpWLMVAQQT---GAKVVKLPLGADRLPDVDLLPELITPRTRILALGQMSNVTGGC 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 156 QniyDIEDIIGDTH---ALFHIDAVQAIGHLDLDFHNFKIDTMSISAHKFGGPKGVGLL-----LVKEHTPIaynQLGG- 226
Cdd:PRK10874 177 P---DLARAITLAHqagMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLygkseLLEAMSPW---QGGGk 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 227 -----------EQETKRR--AGTENLPQIVGLTKALE-LAITNQDVNNVHLMNLKELFLVQLQERA--IPFELNGSMTDS 290
Cdd:PRK10874 251 mltevsfdgftPQSAPWRfeAGTPNVAGVIGLSAALEwLADIDINQAESWSRSLATLAEDALAKLPgfRSFRCQDSSLLA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 291 tghilniyFPFIDVETMltllDLAHVYVSSGSACTAGSTTPSHVLAAMfedeeRAKHSVRFSFNEQTTTQEIKYIVAEIH 370
Cdd:PRK10874 331 --------FDFAGVHHS----DLVTLLAEYGIALRAGQHCAQPLLAAL-----GVTGTLRASFAPYNTQSDVDALVNAVD 393
|
.
gi 488435462 371 K 371
Cdd:PRK10874 394 R 394
|
|
| am_tr_V_VC1184 |
TIGR01976 |
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of ... |
3-205 |
4.44e-24 |
|
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: 102.14 E-value: 4.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 3 VYADYAATTPVKPEVIDAMMEIYQSHFGNPSSIHSIGRDARKYLDQSRRTVAQLLGANPNEVIFTSGATesnnTAIKGLV 82
Cdd:TIGR01976 19 VFFDNPAGTQIPQSVADAVSAALTRSNANRGGAYESSRRADQVVDDAREAVADLLNADPPEVVFGANAT----SLTFLLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 83 KANEQ---LGNHIITTKIEHHSVLHVYEQL-EKEGYDVTYLDVD-DTGAVDLDQLKETINDRTILVSIMFVNNEIGTVQN 157
Cdd:TIGR01976 95 RAISRrwgPGDEVIVTRLDHEANISPWLQAaERAGAKVKWARVDeATGELHPDDLASLLSPRTRLVAVTAASNTLGSIVD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488435462 158 IYDIEDIIGDTHALFHIDAVQAIGHLDLDFHNFKIDTMSISAHKFGGP 205
Cdd:TIGR01976 175 LAAITELVHAAGALVVVDAVHYAPHGLIDVQATGADFLTCSAYKFFGP 222
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
3-215 |
6.35e-24 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 102.14 E-value: 6.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 3 VYADYAATTPVKPEVIDAMMEIYQS-----HFGnpssIHSIGRDARKYLDQSRRTVAQLLGA-NPNEVIFTSGATESNNT 76
Cdd:PRK09295 25 AYLDSAASAQKPSQVIDAEAEFYRHgyaavHRG----IHTLSAQATEKMENVRKQAALFINArSAEELVFVRGTTEGINL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 77 AIKGLVKANEQLGNHIITTKIEHHSVLHVYEQL-EKEGYDVTYLDVDDTGAVDLDQLKETINDRTILVSIMFVNNEIGTV 155
Cdd:PRK09295 101 VANSWGNSNVRAGDNIIISEMEHHANIVPWQMLcARVGAELRVIPLNPDGTLQLETLPALFDERTRLLAITHVSNVLGTE 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488435462 156 QniyDIEDIIGDTHAL---FHIDAVQAIGHLDLDFHNFKIDTMSISAHKFGGPKGVGLLLVKE 215
Cdd:PRK09295 181 N---PLAEMIALAHQHgakVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKE 240
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
6-250 |
4.18e-21 |
|
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: 94.92 E-value: 4.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 6 DYAATTPvKPE-VIDAMMEIYQSHfgNpSSIHsigR----------DArkYLDqSRRTVAQLLGA-NPNEVIFTSGATES 73
Cdd:NF041166 250 DNAATTQ-KPQaVIDRLSYFYEHE--N-SNIH---RaahelaaratDA--YEG-AREKVRRFIGApSVDEIIFVRGTTEA 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 74 NNTAIKGLVKANEQLGNHIITTKIEHHSVLHVYEQL-EKEGYDVTYLDVDDTGAVDLDQLKETINDRTILVSIMFVNNEI 152
Cdd:NF041166 320 INLVAKSWGRQNIGAGDEIIVSHLEHHANIVPWQQLaQETGAKLRVIPVDDSGQILLDEYAKLLNPRTKLVSVTQVSNAL 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 153 GTVQniyDIEDIIgdthALFH-------IDAVQAIGH-------LDLDFHNFkidtmsiSAHKFGGPKGVGLLLVKEH-- 216
Cdd:NF041166 400 GTVT---PVKEII----ALAHragakvlVDGAQSVSHmpvdvqaLDADFFVF-------SGHKVFGPTGIGVVYGKRDll 465
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 488435462 217 --TPiAYnQLGGE-------QET-------KRRAGTENLPQIVGLTKALE 250
Cdd:NF041166 466 eaMP-PW-QGGGNmiadvtfEKTvyqpapnRFEAGTGNIADAVGLGAALD 513
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
50-214 |
1.28e-12 |
|
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).
Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 65.48 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 50 RRTVAQLLGANPNEVIFTSGATESNNTAIKGLVKAneqlGNHIITTKIEHHSVLHVYEqlEKEGYDVTYLDVDDTGAVDL 129
Cdd:cd01494 6 EEKLARLLQPGNDKAVFVPSGTGANEAALLALLGP----GDEVIVDANGHGSRYWVAA--ELAGAKPVPVPVDDAGYGGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 130 D--QLKETIN-DRTILVSIMFVNNEIGTVQNIYDIEDIIGDTHALFHIDAVQAIGHLDLDFH---NFKIDTMSISAHKFG 203
Cdd:cd01494 80 DvaILEELKAkPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVlipEGGADVVTFSLHKNL 159
|
170
....*....|.
gi 488435462 204 GPKGVGLLLVK 214
Cdd:cd01494 160 GGEGGGVVIVK 170
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
53-214 |
1.01e-08 |
|
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: 56.44 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 53 VAQLLGANPNEV--IFTSGATESNNTAIKGL-------VKANEQLGNH---IITTKIEHHSVlhvyeqlEKEGY----DV 116
Cdd:cd06450 47 LAKLFGLPSEDAdgVFTSGGSESNLLALLAArdrarkrLKAGGGRGIDklvIVCSDQAHVSV-------EKAAAyldvKV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 117 TYLDVDDTGAVDLDQLKETIND------RTILVSIMFVNNEIGTVQNIYDIEDiIGDTHAL-FHIDAvqAIG-------- 181
Cdd:cd06450 120 RLVPVDEDGRMDPEALEAAIDEdkaeglNPIMVVATAGTTDTGAIDPLEEIAD-LAEKYDLwLHVDA--AYGgfllpfpe 196
|
170 180 190
....*....|....*....|....*....|....
gi 488435462 182 HLDLDFHNFKIDTMSISAHKFGG-PKGVGLLLVK 214
Cdd:cd06450 197 PRHLDFGIERVDSISVDPHKYGLvPLGCSAVLVR 230
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
50-215 |
2.17e-08 |
|
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: 55.61 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 50 RRTV---AQLLGANPN-EVIFTSGATESN--------NTAIKGLVKANEQLGNH---IITTKIEHHSVlhvyeqlEK--- 111
Cdd:COG0076 110 REVVrwlADLLGLPEGaGGVFTSGGTEANllallaarDRALARRVRAEGLPGAPrprIVVSEEAHSSV-------DKaar 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 112 ----EGYDVTYLDVDDTGAVDLDQLKETIND------RTILV-----SIMFvnneiGTVQNIYDIEDIIGDTHALFHIDA 176
Cdd:COG0076 183 llglGRDALRKVPVDEDGRMDPDALEAAIDEdraaglNPIAVvatagTTNT-----GAIDPLAEIADIAREHGLWLHVDA 257
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488435462 177 vqAIG----------HLdLDfhnfKI---DTMSISAHKFGG-PKGVGLLLVKE 215
Cdd:COG0076 258 --AYGgfalpspelrHL-LD----GIeraDSITVDPHKWLYvPYGCGAVLVRD 303
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
11-215 |
4.97e-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: 54.22 E-value: 4.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 11 TPVKPEVIDAMmeiyqshfgNPSSIHSIGRDARKYLDQSRRTVAQLLGANPNEV-IFTSGATESNNTAIKGLVKAneqlG 89
Cdd:cd06451 8 SNVPPRVLKAM---------NRPMLGHRSPEFLALMDEILEGLRYVFQTENGLTfLLSGSGTGAMEAALSNLLEP----G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 90 NHIITTKIEHHSVLHVyEQLEKEGYDVTYLDVDDTGAVDLDQLKETINDRTIlVSIMFVNNEIGT-VQNiyDIEDIIGDT 168
Cdd:cd06451 75 DKVLVGVNGVFGDRWA-DMAERYGADVDVVEKPWGEAVSPEEIAEALEQHDI-KAVTLTHNETSTgVLN--PLEGIGALA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488435462 169 H---ALFHIDAVQAIGHLDLDFHNFKIDTMSISAHK-FGGPKGVGLLLVKE 215
Cdd:cd06451 151 KkhdALLIVDAVSSLGGEPFRMDEWGVDVAYTGSQKaLGAPPGLGPIAFSE 201
|
|
| PRK07324 |
PRK07324 |
transaminase; Validated |
50-155 |
3.08e-07 |
|
transaminase; Validated
Pssm-ID: 235989 Cd Length: 373 Bit Score: 51.86 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 50 RRTVAQLL-GANPNEVIFTSGATESNNTAIKGLVKAneqlGNHIIttkiehhSVLHVYEQL----EKEGYDVTYLDVDDT 124
Cdd:PRK07324 68 KEAVASLYqNVKPENILQTNGATGANFLVLYALVEP----GDHVI-------SVYPTYQQLydipESLGAEVDYWQLKEE 136
|
90 100 110
....*....|....*....|....*....|...
gi 488435462 125 GAV--DLDQLKETINDRTILVSIMFVNNEIGTV 155
Cdd:PRK07324 137 NGWlpDLDELRRLVRPNTKLICINNANNPTGAL 169
|
|
| tyr_nico_aTase |
TIGR01265 |
tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal ... |
12-155 |
2.32e-04 |
|
tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal phosphate-dependent enzymes includes known examples of both tyrosine aminotransferase from animals and nicotianamine aminotransferase from barley.
Pssm-ID: 188123 Cd Length: 403 Bit Score: 42.71 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 12 PVKPEVIDAMMEIYQSHFGN---PSSIHSIGRDA-RKYLdqSRRTVAQLlgaNPNEVIFTSGATESNNTAIKGLVKAneq 87
Cdd:TIGR01265 48 RTDPEAEEAVKDALRSGKFNgyaPSVGALAAREAvAEYL--SSDLPGKL---TADDVVLTSGCSQAIEICIEALANP--- 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 88 lGNHIITTK--IEHHSVLHVYEQLEKEGYDvtyLDVDDTGAVDLDQLKETINDRTILVSIMFVNNEIGTV 155
Cdd:TIGR01265 120 -GANILVPRpgFPLYDTRAAFSGLEVRLYD---LLPEKDWEIDLDGLESLADEKTVAIVVINPSNPCGSV 185
|
|
| PLN02409 |
PLN02409 |
serine--glyoxylate aminotransaminase |
89-211 |
2.41e-04 |
|
serine--glyoxylate aminotransaminase
Pssm-ID: 178031 [Multi-domain] Cd Length: 401 Bit Score: 42.82 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 89 GNHIITTKIEHHSVLhVYEQLEKEGYDVTYLDVDDTGAVDLDQLKETI-NDRTILVSIMF-VNNE--IGTVQNIYDIEDI 164
Cdd:PLN02409 84 GDKVVSFRIGQFSLL-WIDQMQRLNFDVDVVESPWGQGADLDILKSKLrQDTNHKIKAVCvVHNEtsTGVTNDLAGVRKL 162
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 488435462 165 IGD--THALFHIDAVQAIGHLDLDFHNFKID-TMSISAHKFGGPKGVGLL 211
Cdd:PLN02409 163 LDCaqHPALLLVDGVSSIGALDFRMDEWGVDvALTGSQKALSLPTGLGIV 212
|
|
| PRK02769 |
PRK02769 |
histidine decarboxylase; Provisional |
30-217 |
6.52e-04 |
|
histidine decarboxylase; Provisional
Pssm-ID: 235068 [Multi-domain] Cd Length: 380 Bit Score: 41.57 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 30 GNPSSIHSIGRDARKYLDQSRRTVAQLLGANPNEV--IFTSGATESNntaIKGLVKANEQLGNHII-TTKIEHHSVLHVY 106
Cdd:PRK02769 51 GDPYSKSNYPLNSFDFERDVMNFFAELFKIPFNESwgYITNGGTEGN---LYGCYLARELFPDGTLyYSKDTHYSVSKIA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 107 EQLEKEGYDVTYLDvddTGAVDLDQLKETINDRTILVSIMFVNneIGT-----VQNIYDIEDI-----IGDTHalFHIDA 176
Cdd:PRK02769 128 RLLRIKSRVITSLP---NGEIDYDDLISKIKENKNQPPIIFAN--IGTtmtgaIDNIKEIQEIlkkigIDDYY--IHADA 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488435462 177 vqAIGHLDLDF------HNFK--IDTMSISAHKF-GGPKGVGLLLVKEHT 217
Cdd:PRK02769 201 --ALSGMILPFvnnpppFSFAdgIDSIAISGHKFiGSPMPCGIVLAKKKY 248
|
|
| GDC-P |
cd00613 |
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ... |
98-216 |
5.65e-03 |
|
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: 38.37 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488435462 98 EHHSVLHVYeqLEKEGYDVTYLDVDDTGAVDLDQLKETINDRTilVSIMFVN-NEIGTV-QNIYDIEDIIGDTHALFHID 175
Cdd:cd00613 120 TNPAVARTR--GEPLGIEVVEVPSDEGGTVDLEALKEEVSEEV--AALMVQYpNTLGVFeDLIKEIADIAHSAGALVYVD 195
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 488435462 176 A-------VQAIGHldldfhnFKIDTMSISAHKFGGPKG-----VGLLLVKEH 216
Cdd:cd00613 196 GdnlnltgLKPPGE-------YGADIVVGNLQKTGVPHGgggpgAGFFAVKKE 241
|
|
| |
