|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
1-406 |
0e+00 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 820.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 1 MSFPVEKVRADFPVLTREVNGLPLAYLDSAASAQKPNQVVDAEAEFYRHGYAAVHRGIHTLSAEATQRMENVRTQLAAFL 80
Cdd:PRK09295 1 MTFSVEKVRADFPVLSREVNGLPLAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKQAALFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 81 NARSPEELVFVRGTTEGINLVANSWGNAQVHAGDNIIITQMEHHANIVPWQMLCERVGAQLRVIPLNADGTLQLEQLDLL 160
Cdd:PRK09295 81 NARSAEELVFVRGTTEGINLVANSWGNSNVRAGDNIIISEMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 161 LDDRTRLVAVTQVSNVLGTENPVAEIVDKAHQAGAKVLIDGAQAVMHHAVDVQALDCDFYVFSGHKLYGPTGIGVLYVKE 240
Cdd:PRK09295 161 FDERTRLLAITHVSNVLGTENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 241 EILQAMPPWEGGGSMIATVSLTEGTTYARAPWRFEAGTPNTGGIIGLGAAVSYVSAIGLDAIQEYEQLLMHYALAELASV 320
Cdd:PRK09295 241 ALLQEMPPWEGGGSMIATVSLTEGTTWAKAPWRFEAGTPNTGGIIGLGAALDYVSALGLNNIAEYEQNLMHYALSQLESV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 321 PDLTLYGPADRQGVIAFNLGKHHAYDVGSFLDNYGVAVRTGHHCAMPLMAFYQVPAMCRASLVMYNTTEEVDRLVAGLKR 400
Cdd:PRK09295 321 PDLTLYGPQNRLGVIAFNLGKHHAYDVGSFLDNYGIAVRTGHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVAGLQR 400
|
....*.
gi 544825110 401 IHQLLG 406
Cdd:PRK09295 401 IHRLLG 406
|
|
| sufS |
TIGR01979 |
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine ... |
6-406 |
0e+00 |
|
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine desulfurases involved in FeS cluster formation needed for nitrogen fixation among other vital functions. Many cysteine desulfurases are also active as selenocysteine lyase and/or cysteine sulfinate desulfinase. This subfamily is associated with the six-gene SUF system described in E. coli and Erwinia as an FeS cluster formation system during oxidative stress. The active site Cys is this subfamily resembles GHHC with one or both His conserved. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 131034 [Multi-domain] Cd Length: 403 Bit Score: 644.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 6 EKVRADFPVLTREVNGLPLAYLDSAASAQKPNQVVDAEAEFYRHGYAAVHRGIHTLSAEATQRMENVRTQLAAFLNARSP 85
Cdd:TIGR01979 1 KNIRADFPILKRKINGKPLVYLDSAATSQKPQQVIDAVAEYYRNSNANVHRGIHTLSVRATEAYEAVREKVAKFINAASD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 86 EELVFVRGTTEGINLVANSWGNAQVHAGDNIIITQMEHHANIVPWQMLCERVGAQLRVIPLNADGTLQLEQLDLLLDDRT 165
Cdd:TIGR01979 81 EEIVFTRGTTESINLVAYSWGDSNLKAGDEIVISEMEHHANIVPWQLLAERTGATLKFIPLDDDGTLDLDDLEKLLTEKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 166 RLVAVTQVSNVLGTENPVAEIVDKAHQAGAKVLIDGAQAVMHHAVDVQALDCDFYVFSGHKLYGPTGIGVLYVKEEILQA 245
Cdd:TIGR01979 161 KLVAITHVSNVLGTVNPVEEIAKLAHQVGAKVLVDGAQAVPHMPVDVQALDCDFYVFSGHKMYGPTGIGVLYGKEELLEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 246 MPPWEGGGSMIATVSLtEGTTYARAPWRFEAGTPNTGGIIGLGAAVSYVSAIGLDAIQEYEQLLMHYALAELASVPDLTL 325
Cdd:TIGR01979 241 MPPFLGGGEMIAEVSF-EETTYNEAPHKFEAGTPNIAGVIGLGAAIDYLEAIGLENIEAHEHELTAYALERLGEIPGLRI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 326 YGP---ADRQGVIAFNLGKHHAYDVGSFLDNYGVAVRTGHHCAMPLMAFYQVPAMCRASLVMYNTTEEVDRLVAGLKRIH 402
Cdd:TIGR01979 320 YGPrdaEDRGGIISFNVEGVHPHDVGTILDEEGIAVRSGHHCAQPLMRRFGVPATCRASFYIYNTEEDIDALVEALKKVR 399
|
....
gi 544825110 403 QLLG 406
Cdd:TIGR01979 400 KFFG 403
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
5-404 |
0e+00 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 590.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 5 VEKVRADFPVltrevNGLPLAYLDSAASAQKPNQVVDAEAEFYRHGYAAVHRGIHTLSAEATQRMENVRTQLAAFLNARS 84
Cdd:COG0520 2 VEAIRADFPV-----LGKPLVYLDNAATGQKPRPVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 85 PEELVFVRGTTEGINLVANSWGNaqVHAGDNIIITQMEHHANIVPWQMLCERVGAQLRVIPLNADGTLQLEQLDLLLDDR 164
Cdd:COG0520 77 PDEIIFTRGTTEAINLVAYGLGR--LKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDGELDLEALEALLTPR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 165 TRLVAVTQVSNVLGTENPVAEIVDKAHQAGAKVLIDGAQAVMHHAVDVQALDCDFYVFSGHKLYGPTGIGVLYVKEEILQ 244
Cdd:COG0520 155 TKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELLE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 245 AMPPWEGGGSMIATVSLtEGTTYARAPWRFEAGTPNTGGIIGLGAAVSYVSAIGLDAIQEYEQLLMHYALAELASVPDLT 324
Cdd:COG0520 235 ALPPFLGGGGMIEWVSF-DGTTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAIPGVR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 325 LYGPAD---RQGVIAFNLGKHHAYDVGSFLDNYGVAVRTGHHCAMPLMAFYQVPAMCRASLVMYNTTEEVDRLVAGLKRI 401
Cdd:COG0520 314 ILGPADpedRSGIVSFNVDGVHPHDVAALLDDEGIAVRAGHHCAQPLMRRLGVPGTVRASFHLYNTEEEIDRLVEALKKL 393
|
...
gi 544825110 402 HQL 404
Cdd:COG0520 394 AEL 396
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
26-398 |
0e+00 |
|
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: 567.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 26 YLDSAASAQKPNQVVDAEAEFYRHGYAAVHRGIHTLSAEATQRMENVRTQLAAFLNARSPEELVFVRGTTEGINLVANSW 105
Cdd:cd06453 2 YLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINAPSPDEIIFTRNTTEAINLVAYGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 106 GNAQvHAGDNIIITQMEHHANIVPWQMLCERVGAQLRVIPLNADGTLQLEQLDLLLDDRTRLVAVTQVSNVLGTENPVAE 185
Cdd:cd06453 82 GRAN-KPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPVKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 186 IVDKAHQAGAKVLIDGAQAVMHHAVDVQALDCDFYVFSGHKLYGPTGIGVLYVKEEILQAMPPWEGGGSMIATVSLtEGT 265
Cdd:cd06453 161 IGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMIEEVSF-EET 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 266 TYARAPWRFEAGTPNTGGIIGLGAAVSYVSAIGLDAIQEYEQLLMHYALAELASVPDLTLYGPA-DRQGVIAFNLGKHHA 344
Cdd:cd06453 240 TYADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEIPGVRVYGDAeDRAGVVSFNLEGIHP 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 544825110 345 YDVGSFLDNYGVAVRTGHHCAMPLMAFYQVPAMCRASLVMYNTTEEVDRLVAGL 398
Cdd:cd06453 320 HDVATILDQYGIAVRAGHHCAQPLMRRLGVPGTVRASFGLYNTEEEIDALVEAL 373
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
3-401 |
0e+00 |
|
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: 527.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 3 FPVEKVRADFPVLTREVNGLPLAYLDSAASAQKPNQVVDAEAEFYRHGYAAVHRGIHTLSAEATQRMENVRTQLAAFLNA 82
Cdd:NF041166 225 FDVNAVRRDFPILQERVNGKPLVWFDNAATTQKPQAVIDRLSYFYEHENSNIHRAAHELAARATDAYEGAREKVRRFIGA 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 83 RSPEELVFVRGTTEGINLVANSWGNAQVHAGDNIIITQMEHHANIVPWQMLCERVGAQLRVIPLNADGTLQLEQLDLLLD 162
Cdd:NF041166 305 PSVDEIIFVRGTTEAINLVAKSWGRQNIGAGDEIIVSHLEHHANIVPWQQLAQETGAKLRVIPVDDSGQILLDEYAKLLN 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 163 DRTRLVAVTQVSNVLGTENPVAEIVDKAHQAGAKVLIDGAQAVMHHAVDVQALDCDFYVFSGHKLYGPTGIGVLYVKEEI 242
Cdd:NF041166 385 PRTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGIGVVYGKRDL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 243 LQAMPPWEGGGSMIATVSLtEGTTYARAPWRFEAGTPNTGGIIGLGAAVSYVSAIGLDAIQEYEQLLMHYALAELASVPD 322
Cdd:NF041166 465 LEAMPPWQGGGNMIADVTF-EKTVYQPAPNRFEAGTGNIADAVGLGAALDYVERIGIENIARYEHDLLEYATAGLAEVPG 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 323 LTLYGPA-DRQGVIAFNLGKHHAYDVGSFLDNYGVAVRTGHHCAMPLMAFYQVPAMCRASLVMYNTTEEVDRLVAGLKRI 401
Cdd:NF041166 544 LRLIGTAaDKASVLSFVLDGYSTEEVGKALNQEGIAVRSGHHCAQPILRRFGVEATVRPSLAFYNTCEEVDALVAVLRRL 623
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
26-394 |
0e+00 |
|
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: 521.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 26 YLDSAASAQKPNQVVDAEAEFYRHGYAAVHRGIHTLSAEATQRMENVRTQLAAFLNARSPEELVFVRGTTEGINLVANSW 105
Cdd:pfam00266 2 YLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAINLVALSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 106 GNAqVHAGDNIIITQMEHHANIVPWQMLCERVGAQLRVIPLNADGTLQLEQLDLLLDDRTRLVAVTQVSNVLGTENPVAE 185
Cdd:pfam00266 82 GRS-LKPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 186 IVDKAHQAGAKVLIDGAQAVMHHAVDVQALDCDFYVFSGHKLYGPTGIGVLYVKEEILQAMPPWEGGGSMIATVSLtEGT 265
Cdd:pfam00266 161 IGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGMIETVSL-QES 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 266 TYARAPWRFEAGTPNTGGIIGLGAAVSYVSAIGLDAIQEYEQLLMHYALAELASVPDLTLYGPADRQGVIAFNLGKHHAY 345
Cdd:pfam00266 240 TFADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPERRASIISFNFKGVHPH 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 544825110 346 DVGSFLDNYGVAVRTGHHCAMPLMAFYQVPAMCRASLVMYNTTEEVDRL 394
Cdd:pfam00266 320 DVATLLDESGIAVRSGHHCAQPLMVRLGLGGTVRASFYIYNTQEDVDRL 368
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
1-406 |
0e+00 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 820.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 1 MSFPVEKVRADFPVLTREVNGLPLAYLDSAASAQKPNQVVDAEAEFYRHGYAAVHRGIHTLSAEATQRMENVRTQLAAFL 80
Cdd:PRK09295 1 MTFSVEKVRADFPVLSREVNGLPLAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKQAALFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 81 NARSPEELVFVRGTTEGINLVANSWGNAQVHAGDNIIITQMEHHANIVPWQMLCERVGAQLRVIPLNADGTLQLEQLDLL 160
Cdd:PRK09295 81 NARSAEELVFVRGTTEGINLVANSWGNSNVRAGDNIIISEMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 161 LDDRTRLVAVTQVSNVLGTENPVAEIVDKAHQAGAKVLIDGAQAVMHHAVDVQALDCDFYVFSGHKLYGPTGIGVLYVKE 240
Cdd:PRK09295 161 FDERTRLLAITHVSNVLGTENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 241 EILQAMPPWEGGGSMIATVSLTEGTTYARAPWRFEAGTPNTGGIIGLGAAVSYVSAIGLDAIQEYEQLLMHYALAELASV 320
Cdd:PRK09295 241 ALLQEMPPWEGGGSMIATVSLTEGTTWAKAPWRFEAGTPNTGGIIGLGAALDYVSALGLNNIAEYEQNLMHYALSQLESV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 321 PDLTLYGPADRQGVIAFNLGKHHAYDVGSFLDNYGVAVRTGHHCAMPLMAFYQVPAMCRASLVMYNTTEEVDRLVAGLKR 400
Cdd:PRK09295 321 PDLTLYGPQNRLGVIAFNLGKHHAYDVGSFLDNYGIAVRTGHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVAGLQR 400
|
....*.
gi 544825110 401 IHQLLG 406
Cdd:PRK09295 401 IHRLLG 406
|
|
| sufS |
TIGR01979 |
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine ... |
6-406 |
0e+00 |
|
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine desulfurases involved in FeS cluster formation needed for nitrogen fixation among other vital functions. Many cysteine desulfurases are also active as selenocysteine lyase and/or cysteine sulfinate desulfinase. This subfamily is associated with the six-gene SUF system described in E. coli and Erwinia as an FeS cluster formation system during oxidative stress. The active site Cys is this subfamily resembles GHHC with one or both His conserved. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 131034 [Multi-domain] Cd Length: 403 Bit Score: 644.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 6 EKVRADFPVLTREVNGLPLAYLDSAASAQKPNQVVDAEAEFYRHGYAAVHRGIHTLSAEATQRMENVRTQLAAFLNARSP 85
Cdd:TIGR01979 1 KNIRADFPILKRKINGKPLVYLDSAATSQKPQQVIDAVAEYYRNSNANVHRGIHTLSVRATEAYEAVREKVAKFINAASD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 86 EELVFVRGTTEGINLVANSWGNAQVHAGDNIIITQMEHHANIVPWQMLCERVGAQLRVIPLNADGTLQLEQLDLLLDDRT 165
Cdd:TIGR01979 81 EEIVFTRGTTESINLVAYSWGDSNLKAGDEIVISEMEHHANIVPWQLLAERTGATLKFIPLDDDGTLDLDDLEKLLTEKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 166 RLVAVTQVSNVLGTENPVAEIVDKAHQAGAKVLIDGAQAVMHHAVDVQALDCDFYVFSGHKLYGPTGIGVLYVKEEILQA 245
Cdd:TIGR01979 161 KLVAITHVSNVLGTVNPVEEIAKLAHQVGAKVLVDGAQAVPHMPVDVQALDCDFYVFSGHKMYGPTGIGVLYGKEELLEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 246 MPPWEGGGSMIATVSLtEGTTYARAPWRFEAGTPNTGGIIGLGAAVSYVSAIGLDAIQEYEQLLMHYALAELASVPDLTL 325
Cdd:TIGR01979 241 MPPFLGGGEMIAEVSF-EETTYNEAPHKFEAGTPNIAGVIGLGAAIDYLEAIGLENIEAHEHELTAYALERLGEIPGLRI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 326 YGP---ADRQGVIAFNLGKHHAYDVGSFLDNYGVAVRTGHHCAMPLMAFYQVPAMCRASLVMYNTTEEVDRLVAGLKRIH 402
Cdd:TIGR01979 320 YGPrdaEDRGGIISFNVEGVHPHDVGTILDEEGIAVRSGHHCAQPLMRRFGVPATCRASFYIYNTEEDIDALVEALKKVR 399
|
....
gi 544825110 403 QLLG 406
Cdd:TIGR01979 400 KFFG 403
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
5-404 |
0e+00 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 590.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 5 VEKVRADFPVltrevNGLPLAYLDSAASAQKPNQVVDAEAEFYRHGYAAVHRGIHTLSAEATQRMENVRTQLAAFLNARS 84
Cdd:COG0520 2 VEAIRADFPV-----LGKPLVYLDNAATGQKPRPVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 85 PEELVFVRGTTEGINLVANSWGNaqVHAGDNIIITQMEHHANIVPWQMLCERVGAQLRVIPLNADGTLQLEQLDLLLDDR 164
Cdd:COG0520 77 PDEIIFTRGTTEAINLVAYGLGR--LKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDGELDLEALEALLTPR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 165 TRLVAVTQVSNVLGTENPVAEIVDKAHQAGAKVLIDGAQAVMHHAVDVQALDCDFYVFSGHKLYGPTGIGVLYVKEEILQ 244
Cdd:COG0520 155 TKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELLE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 245 AMPPWEGGGSMIATVSLtEGTTYARAPWRFEAGTPNTGGIIGLGAAVSYVSAIGLDAIQEYEQLLMHYALAELASVPDLT 324
Cdd:COG0520 235 ALPPFLGGGGMIEWVSF-DGTTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAIPGVR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 325 LYGPAD---RQGVIAFNLGKHHAYDVGSFLDNYGVAVRTGHHCAMPLMAFYQVPAMCRASLVMYNTTEEVDRLVAGLKRI 401
Cdd:COG0520 314 ILGPADpedRSGIVSFNVDGVHPHDVAALLDDEGIAVRAGHHCAQPLMRRLGVPGTVRASFHLYNTEEEIDRLVEALKKL 393
|
...
gi 544825110 402 HQL 404
Cdd:COG0520 394 AEL 396
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
26-398 |
0e+00 |
|
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: 567.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 26 YLDSAASAQKPNQVVDAEAEFYRHGYAAVHRGIHTLSAEATQRMENVRTQLAAFLNARSPEELVFVRGTTEGINLVANSW 105
Cdd:cd06453 2 YLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINAPSPDEIIFTRNTTEAINLVAYGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 106 GNAQvHAGDNIIITQMEHHANIVPWQMLCERVGAQLRVIPLNADGTLQLEQLDLLLDDRTRLVAVTQVSNVLGTENPVAE 185
Cdd:cd06453 82 GRAN-KPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPVKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 186 IVDKAHQAGAKVLIDGAQAVMHHAVDVQALDCDFYVFSGHKLYGPTGIGVLYVKEEILQAMPPWEGGGSMIATVSLtEGT 265
Cdd:cd06453 161 IGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMIEEVSF-EET 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 266 TYARAPWRFEAGTPNTGGIIGLGAAVSYVSAIGLDAIQEYEQLLMHYALAELASVPDLTLYGPA-DRQGVIAFNLGKHHA 344
Cdd:cd06453 240 TYADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEIPGVRVYGDAeDRAGVVSFNLEGIHP 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 544825110 345 YDVGSFLDNYGVAVRTGHHCAMPLMAFYQVPAMCRASLVMYNTTEEVDRLVAGL 398
Cdd:cd06453 320 HDVATILDQYGIAVRAGHHCAQPLMRRLGVPGTVRASFGLYNTEEEIDALVEAL 373
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
3-401 |
0e+00 |
|
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: 527.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 3 FPVEKVRADFPVLTREVNGLPLAYLDSAASAQKPNQVVDAEAEFYRHGYAAVHRGIHTLSAEATQRMENVRTQLAAFLNA 82
Cdd:NF041166 225 FDVNAVRRDFPILQERVNGKPLVWFDNAATTQKPQAVIDRLSYFYEHENSNIHRAAHELAARATDAYEGAREKVRRFIGA 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 83 RSPEELVFVRGTTEGINLVANSWGNAQVHAGDNIIITQMEHHANIVPWQMLCERVGAQLRVIPLNADGTLQLEQLDLLLD 162
Cdd:NF041166 305 PSVDEIIFVRGTTEAINLVAKSWGRQNIGAGDEIIVSHLEHHANIVPWQQLAQETGAKLRVIPVDDSGQILLDEYAKLLN 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 163 DRTRLVAVTQVSNVLGTENPVAEIVDKAHQAGAKVLIDGAQAVMHHAVDVQALDCDFYVFSGHKLYGPTGIGVLYVKEEI 242
Cdd:NF041166 385 PRTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGIGVVYGKRDL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 243 LQAMPPWEGGGSMIATVSLtEGTTYARAPWRFEAGTPNTGGIIGLGAAVSYVSAIGLDAIQEYEQLLMHYALAELASVPD 322
Cdd:NF041166 465 LEAMPPWQGGGNMIADVTF-EKTVYQPAPNRFEAGTGNIADAVGLGAALDYVERIGIENIARYEHDLLEYATAGLAEVPG 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 323 LTLYGPA-DRQGVIAFNLGKHHAYDVGSFLDNYGVAVRTGHHCAMPLMAFYQVPAMCRASLVMYNTTEEVDRLVAGLKRI 401
Cdd:NF041166 544 LRLIGTAaDKASVLSFVLDGYSTEEVGKALNQEGIAVRSGHHCAQPILRRFGVEATVRPSLAFYNTCEEVDALVAVLRRL 623
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
26-394 |
0e+00 |
|
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: 521.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 26 YLDSAASAQKPNQVVDAEAEFYRHGYAAVHRGIHTLSAEATQRMENVRTQLAAFLNARSPEELVFVRGTTEGINLVANSW 105
Cdd:pfam00266 2 YLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAINLVALSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 106 GNAqVHAGDNIIITQMEHHANIVPWQMLCERVGAQLRVIPLNADGTLQLEQLDLLLDDRTRLVAVTQVSNVLGTENPVAE 185
Cdd:pfam00266 82 GRS-LKPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 186 IVDKAHQAGAKVLIDGAQAVMHHAVDVQALDCDFYVFSGHKLYGPTGIGVLYVKEEILQAMPPWEGGGSMIATVSLtEGT 265
Cdd:pfam00266 161 IGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGMIETVSL-QES 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 266 TYARAPWRFEAGTPNTGGIIGLGAAVSYVSAIGLDAIQEYEQLLMHYALAELASVPDLTLYGPADRQGVIAFNLGKHHAY 345
Cdd:pfam00266 240 TFADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPERRASIISFNFKGVHPH 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 544825110 346 DVGSFLDNYGVAVRTGHHCAMPLMAFYQVPAMCRASLVMYNTTEEVDRL 394
Cdd:pfam00266 320 DVATLLDESGIAVRSGHHCAQPLMVRLGLGGTVRASFYIYNTQEDVDRL 368
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
6-399 |
5.26e-171 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 484.64 E-value: 5.26e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 6 EKVRADFPVLTREVNGLPLAYLDSAASAQKPNQVVDAEAEFYRHGYAAVHRGIHTLSAEATQRMENVRTQLAAFLNARSP 85
Cdd:PLN02855 15 AETRPDFPILDQTVNGSKLVYLDNAATSQKPAAVLDALQDYYEEYNSNVHRGIHALSAKATDAYELARKKVAAFINASTS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 86 EELVFVRGTTEGINLVANSWGNAQVHAGDNIIITQMEHHANIVPWQMLCERVGAQLRVIPLNADGTLQLEQLDLLLDDRT 165
Cdd:PLN02855 95 REIVFTRNATEAINLVAYTWGLANLKPGDEVILSVAEHHSNIVPWQLVAQKTGAVLKFVGLTPDEVLDVEQLKELLSEKT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 166 RLVAVTQVSNVLGTENPVAEIVDKAHQAGAKVLIDGAQAVMHHAVDVQALDCDFYVFSGHKLYGPTGIGVLYVKEEILQA 245
Cdd:PLN02855 175 KLVATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLWGKSDLLES 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 246 MPPWEGGGSMIATVSLtEGTTYARAPWRFEAGTPNTGGIIGLGAAVSYVSAIGLDAIQEYEQLLMHYALAELASVPDLTL 325
Cdd:PLN02855 255 MPPFLGGGEMISDVFL-DHSTYAPPPSRFEAGTPAIGEAIGLGAAIDYLSEIGMDRIHEYEVELGTYLYEKLSSVPGVRI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 326 YGPADRQGV-----IAFNLGKHHAYDVGSFLD-NYGVAVRTGHHCAMPLMAFYQVPAMCRASLVMYNTTEEVDRLVAGLK 399
Cdd:PLN02855 334 YGPKPSEGVgraalCAFNVEGIHPTDLSTFLDqQHGVAIRSGHHCAQPLHRYLGVNASARASLYFYNTKEEVDAFIHALK 413
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
1-405 |
1.30e-136 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 396.33 E-value: 1.30e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 1 MSFPVEKVRADFPVLTRevnglPLAYLDSAASAQKPNQVVDAEAEFYRHGYAAVHRGIHTLSAEATQRMENVRTQLAAFL 80
Cdd:PRK10874 2 NVFNPAQFRAQFPALQD-----AGVYLDSAATALKPQAVIEATQQFYSLSAGNVHRSQFAAAQRLTARYEAAREQVAQLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 81 NARSPEELVFVRGTTEGINLVANSWGNAQVHAGDNIIITQMEHHANIVPWQMLCERVGAQLRVIPLNADGTLQLEQLDLL 160
Cdd:PRK10874 77 NAPDAKNIVWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLVPWLMVAQQTGAKVVKLPLGADRLPDVDLLPEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 161 LDDRTRLVAVTQVSNVLGTENPVAEIVDKAHQAGAKVLIDGAQAVMHHAVDVQALDCDFYVFSGHKLYGPTGIGVLYVKE 240
Cdd:PRK10874 157 ITPRTRILALGQMSNVTGGCPDLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 241 EILQAMPPWEGGGSMIATVSLtEGTTYARAPWRFEAGTPNTGGIIGLGAAVSYVSAIGLDAIQEYEQLLMHYALAELASV 320
Cdd:PRK10874 237 ELLEAMSPWQGGGKMLTEVSF-DGFTPQSAPWRFEAGTPNVAGVIGLSAALEWLADIDINQAESWSRSLATLAEDALAKL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 321 PDLTLYGPADrQGVIAFNL-GKHHAyDVGSFLDNYGVAVRTGHHCAMPLMAFYQVPAMCRASLVMYNTTEEVDRLVAGLK 399
Cdd:PRK10874 316 PGFRSFRCQD-SSLLAFDFaGVHHS-DLVTLLAEYGIALRAGQHCAQPLLAALGVTGTLRASFAPYNTQSDVDALVNAVD 393
|
....*.
gi 544825110 400 RIHQLL 405
Cdd:PRK10874 394 RALELL 399
|
|
| FeS_syn_CsdA |
TIGR03392 |
cysteine desulfurase, catalytic subunit CsdA; Members of this protein family are CsdS. This ... |
3-405 |
1.59e-127 |
|
cysteine desulfurase, catalytic subunit CsdA; Members of this protein family are CsdS. This protein, found Escherichia coli, Yersinia pestis, Photorhabdus luminescens, and related species, and related to SufS, works together with and physically interacts with CsdE (a paralog of SufE). CsdA has cysteine desulfurase activity that is enhanced by CsdE, a sulfur acceptor protein. This gene pair, although involved in FeS cluster biosynthesis, is not found next to other such genes as are its paralogs from the Suf or Isc systems. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 274558 [Multi-domain] Cd Length: 398 Bit Score: 373.40 E-value: 1.59e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 3 FPVEKVRADFPVLTREvnglpLAYLDSAASAQKPNQVVDAEAEFYRHGYAAVHRGIHTLSAEATQRMENVRTQLAAFLNA 82
Cdd:TIGR03392 1 FNPAQFRRQFPALQDA-----TVYLDSAATALKPQAVIDATQQFYRLSSGTVHRSQHQEAQSLTARYEAAREQVAQLLNA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 83 RSPEELVFVRGTTEGINLVANSWGNAQVHAGDNIIITQMEHHANIVPWQMLCERVGAQLRVIPLNADGTLQLEQLDLLLD 162
Cdd:TIGR03392 76 PDAENIVWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLIPWLMVAQQTGAKVVKLPIGADLLPDIDQLPELLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 163 DRTRLVAVTQVSNVLGTENPVAEIVDKAHQAGAKVLIDGAQAVMHHAVDVQALDCDFYVFSGHKLYGPTGIGVLYVKEEI 242
Cdd:TIGR03392 156 PRTRILALGQMSNVTGGCPDLARAITLAHQYGCVVVVDGAQGVVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKTEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 243 LQAMPPWEGGGSMIATVSLTEGTTYArAPWRFEAGTPNTGGIIGLGAAVSYVSAIGLDAIQEYEQLLMHYALAELASVPD 322
Cdd:TIGR03392 236 LEAMPPWQGGGKMLSHVSFDGFTPQA-VPWRFEAGTPNIAGVIGLSAALEWLADIDINAAESWSVSLATLAEEALAQLPG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 323 LTLYGPADrQGVIAFNLGKHHAYDVGSFLDNYGVAVRTGHHCAMPLMAFYQVPAMCRASLVMYNTTEEVDRLVAGLKRIH 402
Cdd:TIGR03392 315 FRSFRCQG-SSLLAFDFAGVHHSDLVTLLAEQGIALRAGQHCAQPLMAALGVSGTLRASFAPYNTQQDVDALVNAVGRAL 393
|
...
gi 544825110 403 QLL 405
Cdd:TIGR03392 394 ELL 396
|
|
| am_tr_V_VC1184 |
TIGR01976 |
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of ... |
3-398 |
5.39e-70 |
|
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: 225.79 E-value: 5.39e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 3 FPVEKVRADFPVLTREVnglpLAYLDSAASAQKPNQVVDAEAE-FYRHGyaaVHRGIHTLSAEATQRM-ENVRTQLAAFL 80
Cdd:TIGR01976 1 FDVEAVRGQFPALADGD----RVFFDNPAGTQIPQSVADAVSAaLTRSN---ANRGGAYESSRRADQVvDDAREAVADLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 81 NARSPEeLVFVRGTTEGINLVANS----WGnaqvhAGDNIIITQMEHHANIVPWQMLCERVGAQLRVIPLN-ADGTLQLE 155
Cdd:TIGR01976 74 NADPPE-VVFGANATSLTFLLSRAisrrWG-----PGDEVIVTRLDHEANISPWLQAAERAGAKVKWARVDeATGELHPD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 156 QLDLLLDDRTRLVAVTQVSNVLGTENPVAEIVDKAHQAGAKVLIDGAQAVMHHAVDVQALDCDFYVFSGHKLYGPTgIGV 235
Cdd:TIGR01976 148 DLASLLSPRTRLVAVTAASNTLGSIVDLAAITELVHAAGALVVVDAVHYAPHGLIDVQATGADFLTCSAYKFFGPH-MGI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 236 LYVKEEILQAMPPWEgggsmiatvsltEGTTYARAPWRFEAGTPNTGGIIGLGAAVSYVSAIGLD--------------A 301
Cdd:TIGR01976 227 LWGRPELLMNLPPYK------------LTFSYDTGPERFELGTPQYELLAGVVAAVDYLAGLGESangsrrerlvasfqA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 302 IQEYEQLLMHYALAELASVPDLTLYG---PADRQGVIAFNLGKHHAYDVGSFLDNYGVAVRTGHHCAMPLM---AFYQVP 375
Cdd:TIGR01976 295 IDAYENRLAEYLLVGLSDLPGVTLYGvarLAARVPTVSFTVHGLPPQRVVRRLADQGIDAWAGHFYAVRLLrrlGLNDEG 374
|
410 420
....*....|....*....|...
gi 544825110 376 AMCRASLVMYNTTEEVDRLVAGL 398
Cdd:TIGR01976 375 GVVRVGLAHYNTAEEVDRLLEAL 397
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
26-401 |
1.36e-48 |
|
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: 169.07 E-value: 1.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 26 YLDSAASAQKPNQVVDAEAEFYRHGYaavhrG----IHTLSAEATQRMENVRTQLAAFLNARsPEELVFVRGTTEGINLV 101
Cdd:COG1104 5 YLDNAATTPVDPEVLEAMLPYLTEYF-----GnpssLHSFGREARAALEEAREQVAALLGAD-PEEIIFTSGGTEANNLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 102 ANSWGNAQVHAGDNIIITQMEHHANIVPWQMLcERVGAQLRVIPLNADGTLQLEQLDLLLDDRTRLVAVTQVSNVLGTEN 181
Cdd:COG1104 79 IKGAARAYRKKGKHIITSAIEHPAVLETARFL-EKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 182 PVAEIVDKAHQAGAKVLIDGAQAVMHHAVDVQALDCDFYVFSGHKLYGPTGIGVLYVKEEIlQAMPPWEGGGSmiatvsl 261
Cdd:COG1104 158 PIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRKGV-RLEPLIHGGGQ------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 262 tEGTtyarapWRfeAGTPNTGGIIGLGAAVSYVSAiGLDAIQEYEQLLMHYALAEL-ASVPDLTLYGPADRQ--GVIAFN 338
Cdd:COG1104 230 -ERG------LR--SGTENVPGIVGLGKAAELAAE-ELEEEAARLRALRDRLEEGLlAAIPGVVINGDPENRlpNTLNFS 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544825110 339 LGKHHAYDVGSFLDNYGVAVRTGHHCA----MP---LMAFYQVPAMCRASLVM----YNTTEEVDRLVAGLKRI 401
Cdd:COG1104 300 FPGVEGEALLLALDLAGIAVSSGSACSsgslEPshvLLAMGLDEELAHGSIRFslgrFTTEEEIDRAIEALKEI 373
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
26-392 |
8.14e-27 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 110.13 E-value: 8.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 26 YLDSAASAQKPNQVVDAEAEFYRHGYAAVHRGIHTLSAEATQRMENVRTQLAAFLNArSPEELVFVRGTTEGINL----V 101
Cdd:PLN02651 2 YLDMQATTPIDPRVLDAMLPFLIEHFGNPHSRTHLYGWESEDAVEKARAQVAALIGA-DPKEIIFTSGATESNNLaikgV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 102 ANSWGNAQVHagdnIIITQMEHHANIVPWQMLcERVGAQLRVIPLNADGTLQLEQLDLLLDDRTRLVAVTQVSNVLGTEN 181
Cdd:PLN02651 81 MHFYKDKKKH----VITTQTEHKCVLDSCRHL-QQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 182 PVAEIVDKAHQAGAKVLIDGAQAVMHHAVDVQALDCDFYVFSGHKLYGPTGIGVLYVKEEILQAMPP-WEGGGSmiatvs 260
Cdd:PLN02651 156 PVEEIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRLEPlMSGGGQ------ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 261 ltEGTtyarapwrFEAGTPNTGGIIGLGAAVSYvsaigldAIQEYEQLLMHY-ALAE------LASVPDLTLYGPADRQG 333
Cdd:PLN02651 230 --ERG--------RRSGTENTPLVVGLGAACEL-------AMKEMDYDEKHMkALRErllnglRAKLGGVRVNGPRDPEK 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544825110 334 VIAFNLGKHHAY-DVGSFLDNY-GVAVRTGHHCAMP-LMAFYQVPAM----------CRASLVMYNTTEEVD 392
Cdd:PLN02651 293 RYPGTLNLSFAYvEGESLLMGLkEVAVSSGSACTSAsLEPSYVLRALgvpeemahgsLRLGVGRFTTEEEVD 364
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
22-290 |
1.70e-20 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 92.31 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 22 LPLaYLDSAASAQKPNQVVDAEAEFYRHG--YAAVHRGIHTLSAEATQRMENVRTQLAAFLNArSPEELVFVRGTTEGIN 99
Cdd:PRK14012 3 LPI-YLDYSATTPVDPRVAEKMMPYLTMDgtFGNPASRSHRFGWQAEEAVDIARNQIADLIGA-DPREIVFTSGATESDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 100 L----VANSWGNAqvhaGDNIIITQMEHHANIVPWQMLcERVGAQLRVIPLNADGTLQLEQLDLLLDDRTRLVAVTQVSN 175
Cdd:PRK14012 81 LaikgAAHFYQKK----GKHIITSKTEHKAVLDTCRQL-EREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 176 VLGTENPVAEIVDKAHQAGAKVLIDGAQAVMHHAVDVQALDCDFYVFSGHKLYGPTGIGVLYV-KEEILQAMPPWEGGGs 254
Cdd:PRK14012 156 EIGVIQDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVrRKPRVRLEAQMHGGG- 234
|
250 260 270
....*....|....*....|....*....|....*.
gi 544825110 255 miatvsltegttYARApwrFEAGTPNTGGIIGLGAA 290
Cdd:PRK14012 235 ------------HERG---MRSGTLPTHQIVGMGEA 255
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
26-401 |
9.30e-14 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 72.07 E-value: 9.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 26 YLDSAASAQKPNQVVDAEAEFYRHgYAAVHRGIHTLSAEATQRMENVRTQLAAFLNARSpEELVFVRGTTEGINLVANSW 105
Cdd:PRK02948 3 YLDYAATTPMSKEALQTYQKAASQ-YFGNESSLHDIGGTASSLLQVCRKTFAEMIGGEE-QGIYFTSGGTESNYLAIQSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 106 GNAQVHAGDNIIITQMEHHANIVPWQMLcERVGAQLRVIPLNADGTLQLEQLDLLLDDRTRLVAVTQVSNVLGTENPVAE 185
Cdd:PRK02948 81 LNALPQNKKHIITTPMEHASIHSYFQSL-ESQGYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQPIAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 186 IVDKAHQAGAKVLIDGAQAVMHHAVDVQALDCDFYVFSGHKLYGPTGIGVLYVKEEIlqampPWEgggsmiatvSLTEGT 265
Cdd:PRK02948 160 IGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYINPQV-----RWK---------PVFPGT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 266 TYARApwrFEAGTPNTGGIIGLGAAVSYVSAIGLDAIQEYEQLLMHYalaeLASVPDLTLygPADRQGVIAFNLgkhhAY 345
Cdd:PRK02948 226 THEKG---FRPGTVNVPGIAAFLTAAENILKNMQEESLRFKELRSYF----LEQIQTLPL--PIEVEGHSTSCL----PH 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 346 DVGSFLDNY------------GVAVRTGHHCAmplmAFYQVP--AM-------------CRASLVMYNTTEEVDRLVAGL 398
Cdd:PRK02948 293 IIGVTIKGIegqytmlecnrrGIAISTGSACQ----VGKQEPskTMlaigktyeeakqfVRFSFGQQTTKDQIDTTIHAL 368
|
...
gi 544825110 399 KRI 401
Cdd:PRK02948 369 ETI 371
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
69-239 |
6.08e-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: 57.78 E-value: 6.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 69 MENVRTQLAAFLNArSPEELVFVRGTTEGINLVANSWGNAqvhaGDNIIITQMEHHANIvpWQMLcERVGAQLRVIPLNA 148
Cdd:cd01494 2 LEELEEKLARLLQP-GNDKAVFVPSGTGANEAALLALLGP----GDEVIVDANGHGSRY--WVAA-ELAGAKPVPVPVDD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 149 DGTLQLEQLDLLLDDRTRLVA--VTQVSNVLGT-ENPVAEIVDKAHQAGAKVLIDGAQAVMHHAVDVQALD---CDFYVF 222
Cdd:cd01494 74 AGYGGLDVAILEELKAKPNVAliVITPNTTSGGvLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPeggADVVTF 153
|
170
....*....|....*..
gi 544825110 223 SGHKLYGPTGIGVLYVK 239
Cdd:cd01494 154 SLHKNLGGEGGGVVIVK 170
|
|
| SepCysS |
cd06452 |
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ... |
74-241 |
8.95e-09 |
|
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Cys-tRNA(Cys) is produced by O-phosphoseryl-tRNA synthetase which ligates O-phosphoserine (Sep) to tRNA(Cys), and Sep-tRNA:Cys-tRNA synthase (SepCysS) converts Sep-tRNA(Cys) to Cys-tRNA(Cys), in methanogenic archaea. SepCysS forms a dimer, each monomer is composed of a large and small domain; the larger, a typical pyridoxal 5'-phosphate (PLP)-dependent-like enzyme fold. In the active site of each monomer, PLP is covalently bound to a conserved Lys residue near the dimer interface.
Pssm-ID: 99745 Cd Length: 361 Bit Score: 56.63 E-value: 8.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 74 TQLAAFLNArspEELVFVRGTTEGINLVANSWgnaqVHAGDNIIITQMEHHANIVPwqmlCERVGAQLRVIP-------- 145
Cdd:cd06452 51 HDLAEFLGM---DEARVTPGAREGKFAVMHSL----CEKGDWVVVDGLAHYTSYVA----AERAGLNVREVPntghpeyh 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 146 LNADGTLQLEQLDLLLDDRTRLVA-VTQVSNVLGTENPVAEIVDKAHQAGAKVLIDGAQAVMHHAVDVQALDCDFYVFSG 224
Cdd:cd06452 120 ITPEGYAEVIEEVKDEFGKPPALAlLTHVDGNYGNLHDAKKIAKVCHEYGVPLLLNGAYTVGRMPVSGKELGADFIVGSG 199
|
170
....*....|....*...
gi 544825110 225 HKLYGPTG-IGVLYVKEE 241
Cdd:cd06452 200 HKSMAASApIGVLATTEE 217
|
|
| PRK09331 |
PRK09331 |
Sep-tRNA:Cys-tRNA synthetase; Provisional |
76-241 |
2.66e-08 |
|
Sep-tRNA:Cys-tRNA synthetase; Provisional
Pssm-ID: 236469 Cd Length: 387 Bit Score: 55.32 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 76 LAAFLNArspEELVFVRGTTEGINLVANSWGNAqvhaGDNIIITQMEHHANIVPwqmlCERVGAQLRVIP--------LN 147
Cdd:PRK09331 72 LAEFLGM---DEARVTHGAREGKFAVMHSLCKK----GDYVVLDGLAHYTSYVA----AERAGLNVREVPktgypeykIT 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 148 ADGTLQLEQLDLLLDDRTRLVA-VTQVSNVLGTENPVAEIVDKAHQAGAKVLIDGAQAVMHHAVDVQALDCDFYVFSGHK 226
Cdd:PRK09331 141 PEAYAEKIEEVKEETGKPPALAlLTHVDGNYGNLADAKKVAKVAHEYGIPFLLNGAYTVGRMPVDGKKLGADFIVGSGHK 220
|
170
....*....|....*.
gi 544825110 227 LYGPTG-IGVLYVKEE 241
Cdd:PRK09331 221 SMAASApSGVLATTEE 236
|
|
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
181-339 |
1.08e-04 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 44.47 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 181 NPVAEIVDKAHQAGAK-----VLIDGAQAVMHHAVDVQALDCDFYVFSGHKLYG-PTGIGVLYVKEEILQAM-PPWEGGG 253
Cdd:PLN02724 212 DLVKLIKDNQHSNFSKsgrwmVLLDAAKGCGTSPPDLSRYPADFVVVSFYKIFGyPTGLGALLVRRDAAKLLkKKYFGGG 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825110 254 SMIATVSLTEGTT-YARAPWRFEAGTPNTGGIIGLGAAVSYVSAIGLDAIQEYEQLLMHYALAELAS------VPDLTLY 326
Cdd:PLN02724 292 TVAASIADIDFVKrRERVEQRFEDGTISFLSIAALRHGFKLLNRLTISAIAMHTWALTHYVANSLRNlkhgngAPVCVLY 371
|
170 180
....*....|....*....|
gi 544825110 327 GPAD------RQG-VIAFNL 339
Cdd:PLN02724 372 GNHTfklefhIQGpIVTFNL 391
|
|
| AdSS |
cd03108 |
adenylosuccinate synthetase; Adenylosuccinate synthetase (AdSS) catalyzes the first step in ... |
183-235 |
3.37e-03 |
|
adenylosuccinate synthetase; Adenylosuccinate synthetase (AdSS) catalyzes the first step in the de novo biosynthesis of AMP. IMP and L-aspartate are conjugated in a two-step reaction accompanied by the hydrolysis of GTP to GDP in the presence of Mg2+. In the first step, the r-phosphate group of GTP is transferred to the 6-oxygen atom of IMP. An aspartate then displaces this 6-phosphate group to form the product adenylosuccinate. Because of its critical role in purine biosynthesis, AdSS is a target of antibiotics, herbicides and antitumor drugs.
Pssm-ID: 349762 Cd Length: 316 Bit Score: 39.02 E-value: 3.37e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 544825110 183 VAEIVDKAHQAGAKVLIDGAQAVMhhavdvqaLDCDF----YVFSGHKL--YGPTGIGV 235
Cdd:cd03108 155 TVELLNEALKAGKKVLFEGAQGTL--------LDIDFgtypYVTSSNTTagGVCTGLGI 205
|
|
| |
