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Conserved domains on  [gi|2695378996|dbj|GMB70344.1|]
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cysteine desulfurase [Pectobacterium brasiliense]

Protein Classification

cysteine desulfurase( domain architecture ID 10793188)

cysteine desulfurase is a pyridoxal-5'-phoshate dependent enzyme that catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine

Graphical summary

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List of domain hits

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: 806.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996   1 MSYPIERVRADFPLLASEVNGQPLAYLDSAASAQKPHAVIDREAEFYRHEYAAVHRGIHTLSAQATSAMEAVREKVASFI 80
Cdd:PRK09295    1 MTFSVEKVRADFPVLSREVNGLPLAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKQAALFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996  81 NAASVEEIVFVRGTTEAINLVANSYGRTFIQPGDNLIITEMEHHANIVPWQMLAEARGVEVRVLPLAEDGSLDVAQLPGL 160
Cdd:PRK09295   81 NARSAEELVFVRGTTEGINLVANSWGNSNVRAGDNIIISEMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 161 LDERTRLLAVTQISNVLGALNPVKAMIAQAKAAGAVTLVDGAQSIMHQTVDVQDLDCDFFVFSGHKIYGPSGIGVLYGKR 240
Cdd:PRK09295  161 FDERTRLLAITHVSNVLGTENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 241 DLLQAMPPWEGGGAMIHQVSLRTGTTYADSPWRFEAGSPNTGGIMGLGAALDYVTALGREEIQRYESSLMQYALEALTQV 320
Cdd:PRK09295  241 ALLQEMPPWEGGGSMIATVSLTEGTTWAKAPWRFEAGTPNTGGIIGLGAALDYVSALGLNNIAEYEQNLMHYALSQLESV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 321 PDLTLYGPAERHGVIAFNLGQHHAYDVGSFLDRYGIAIRTGHHCAMPLMEHYGVPSMCRASLAVYTTREEIDRLVAGLQR 400
Cdd:PRK09295  321 PDLTLYGPQNRLGVIAFNLGKHHAYDVGSFLDNYGIAVRTGHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVAGLQR 400

                  ....*.
gi 2695378996 401 IHRLLG 406
Cdd:PRK09295  401 IHRLLG 406
 
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: 806.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996   1 MSYPIERVRADFPLLASEVNGQPLAYLDSAASAQKPHAVIDREAEFYRHEYAAVHRGIHTLSAQATSAMEAVREKVASFI 80
Cdd:PRK09295    1 MTFSVEKVRADFPVLSREVNGLPLAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKQAALFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996  81 NAASVEEIVFVRGTTEAINLVANSYGRTFIQPGDNLIITEMEHHANIVPWQMLAEARGVEVRVLPLAEDGSLDVAQLPGL 160
Cdd:PRK09295   81 NARSAEELVFVRGTTEGINLVANSWGNSNVRAGDNIIISEMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 161 LDERTRLLAVTQISNVLGALNPVKAMIAQAKAAGAVTLVDGAQSIMHQTVDVQDLDCDFFVFSGHKIYGPSGIGVLYGKR 240
Cdd:PRK09295  161 FDERTRLLAITHVSNVLGTENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 241 DLLQAMPPWEGGGAMIHQVSLRTGTTYADSPWRFEAGSPNTGGIMGLGAALDYVTALGREEIQRYESSLMQYALEALTQV 320
Cdd:PRK09295  241 ALLQEMPPWEGGGSMIATVSLTEGTTWAKAPWRFEAGTPNTGGIIGLGAALDYVSALGLNNIAEYEQNLMHYALSQLESV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 321 PDLTLYGPAERHGVIAFNLGQHHAYDVGSFLDRYGIAIRTGHHCAMPLMEHYGVPSMCRASLAVYTTREEIDRLVAGLQR 400
Cdd:PRK09295  321 PDLTLYGPQNRLGVIAFNLGKHHAYDVGSFLDNYGIAVRTGHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVAGLQR 400

                  ....*.
gi 2695378996 401 IHRLLG 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: 652.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996   6 ERVRADFPLLASEVNGQPLAYLDSAASAQKPHAVIDREAEFYRHEYAAVHRGIHTLSAQATSAMEAVREKVASFINAASV 85
Cdd:TIGR01979   1 KNIRADFPILKRKINGKPLVYLDSAATSQKPQQVIDAVAEYYRNSNANVHRGIHTLSVRATEAYEAVREKVAKFINAASD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996  86 EEIVFVRGTTEAINLVANSYGRTFIQPGDNLIITEMEHHANIVPWQMLAEARGVEVRVLPLAEDGSLDVAQLPGLLDERT 165
Cdd:TIGR01979  81 EEIVFTRGTTESINLVAYSWGDSNLKAGDEIVISEMEHHANIVPWQLLAERTGATLKFIPLDDDGTLDLDDLEKLLTEKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 166 RLLAVTQISNVLGALNPVKAMIAQAKAAGAVTLVDGAQSIMHQTVDVQDLDCDFFVFSGHKIYGPSGIGVLYGKRDLLQA 245
Cdd:TIGR01979 161 KLVAITHVSNVLGTVNPVEEIAKLAHQVGAKVLVDGAQAVPHMPVDVQALDCDFYVFSGHKMYGPTGIGVLYGKEELLEQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 246 MPPWEGGGAMIHQVSLRtGTTYADSPWRFEAGSPNTGGIMGLGAALDYVTALGREEIQRYESSLMQYALEALTQVPDLTL 325
Cdd:TIGR01979 241 MPPFLGGGEMIAEVSFE-ETTYNEAPHKFEAGTPNIAGVIGLGAAIDYLEAIGLENIEAHEHELTAYALERLGEIPGLRI 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 326 YGP---AERHGVIAFNLGQHHAYDVGSFLDRYGIAIRTGHHCAMPLMEHYGVPSMCRASLAVYTTREEIDRLVAGLQRIH 402
Cdd:TIGR01979 320 YGPrdaEDRGGIISFNVEGVHPHDVGTILDEEGIAVRSGHHCAQPLMRRFGVPATCRASFYIYNTEEDIDALVEALKKVR 399

                  ....
gi 2695378996 403 RLLG 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: 621.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996   5 IERVRADFPllaseVNGQPLAYLDSAASAQKPHAVIDREAEFYRHEYAAVHRGIHTLSAQATSAMEAVREKVASFINAAS 84
Cdd:COG0520     2 VEAIRADFP-----VLGKPLVYLDNAATGQKPRPVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAAS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996  85 VEEIVFVRGTTEAINLVANSYGRtfIQPGDNLIITEMEHHANIVPWQMLAEARGVEVRVLPLAEDGSLDVAQLPGLLDER 164
Cdd:COG0520    77 PDEIIFTRGTTEAINLVAYGLGR--LKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDGELDLEALEALLTPR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 165 TRLLAVTQISNVLGALNPVKAMIAQAKAAGAVTLVDGAQSIMHQTVDVQDLDCDFFVFSGHKIYGPSGIGVLYGKRDLLQ 244
Cdd:COG0520   155 TKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELLE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 245 AMPPWEGGGAMIHQVSLrTGTTYADSPWRFEAGSPNTGGIMGLGAALDYVTALGREEIQRYESSLMQYALEALTQVPDLT 324
Cdd:COG0520   235 ALPPFLGGGGMIEWVSF-DGTTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAIPGVR 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 325 LYGPA---ERHGVIAFNLGQHHAYDVGSFLDRYGIAIRTGHHCAMPLMEHYGVPSMCRASLAVYTTREEIDRLVAGLQRI 401
Cdd:COG0520   314 ILGPAdpeDRSGIVSFNVDGVHPHDVAALLDDEGIAVRAGHHCAQPLMRRLGVPGTVRASFHLYNTEEEIDRLVEALKKL 393

                  ...
gi 2695378996 402 HRL 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: 589.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996  26 YLDSAASAQKPHAVIDREAEFYRHEYAAVHRGIHTLSAQATSAMEAVREKVASFINAASVEEIVFVRGTTEAINLVANSY 105
Cdd:cd06453     2 YLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINAPSPDEIIFTRNTTEAINLVAYGL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 106 GRTFiQPGDNLIITEMEHHANIVPWQMLAEARGVEVRVLPLAEDGSLDVAQLPGLLDERTRLLAVTQISNVLGALNPVKA 185
Cdd:cd06453    82 GRAN-KPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPVKE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 186 MIAQAKAAGAVTLVDGAQSIMHQTVDVQDLDCDFFVFSGHKIYGPSGIGVLYGKRDLLQAMPPWEGGGAMIHQVSLrTGT 265
Cdd:cd06453   161 IGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMIEEVSF-EET 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 266 TYADSPWRFEAGSPNTGGIMGLGAALDYVTALGREEIQRYESSLMQYALEALTQVPDLTLYGPAERH-GVIAFNLGQHHA 344
Cdd:cd06453   240 TYADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEIPGVRVYGDAEDRaGVVSFNLEGIHP 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2695378996 345 YDVGSFLDRYGIAIRTGHHCAMPLMEHYGVPSMCRASLAVYTTREEIDRLVAGL 398
Cdd:cd06453   320 HDVATILDQYGIAVRAGHHCAQPLMRRLGVPGTVRASFGLYNTEEEIDALVEAL 373
f2_encap_cargo1 NF041166
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ...
5-401 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: 560.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996   5 IERVRADFPLLASEVNGQPLAYLDSAASAQKPHAVIDREAEFYRHEYAAVHRGIHTLSAQATSAMEAVREKVASFINAAS 84
Cdd:NF041166  227 VNAVRRDFPILQERVNGKPLVWFDNAATTQKPQAVIDRLSYFYEHENSNIHRAAHELAARATDAYEGAREKVRRFIGAPS 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996  85 VEEIVFVRGTTEAINLVANSYGRTFIQPGDNLIITEMEHHANIVPWQMLAEARGVEVRVLPLAEDGSLDVAQLPGLLDER 164
Cdd:NF041166  307 VDEIIFVRGTTEAINLVAKSWGRQNIGAGDEIIVSHLEHHANIVPWQQLAQETGAKLRVIPVDDSGQILLDEYAKLLNPR 386
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 165 TRLLAVTQISNVLGALNPVKAMIAQAKAAGAVTLVDGAQSIMHQTVDVQDLDCDFFVFSGHKIYGPSGIGVLYGKRDLLQ 244
Cdd:NF041166  387 TKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGIGVVYGKRDLLE 466
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 245 AMPPWEGGGAMIHQVSLrTGTTYADSPWRFEAGSPNTGGIMGLGAALDYVTALGREEIQRYESSLMQYALEALTQVPDLT 324
Cdd:NF041166  467 AMPPWQGGGNMIADVTF-EKTVYQPAPNRFEAGTGNIADAVGLGAALDYVERIGIENIARYEHDLLEYATAGLAEVPGLR 545
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2695378996 325 LYGPA-ERHGVIAFNLGQHHAYDVGSFLDRYGIAIRTGHHCAMPLMEHYGVPSMCRASLAVYTTREEIDRLVAGLQRI 401
Cdd:NF041166  546 LIGTAaDKASVLSFVLDGYSTEEVGKALNQEGIAVRSGHHCAQPILRRFGVEATVRPSLAFYNTCEEVDALVAVLRRL 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: 553.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996  26 YLDSAASAQKPHAVIDREAEFYRHEYAAVHRGIHTLSAQATSAMEAVREKVASFINAASVEEIVFVRGTTEAINLVANSY 105
Cdd:pfam00266   2 YLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAINLVALSL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 106 GRTFiQPGDNLIITEMEHHANIVPWQMLAEARGVEVRVLPLAEDGSLDVAQLPGLLDERTRLLAVTQISNVLGALNPVKA 185
Cdd:pfam00266  82 GRSL-KPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVPE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 186 MIAQAKAAGAVTLVDGAQSIMHQTVDVQDLDCDFFVFSGHKIYGPSGIGVLYGKRDLLQAMPPWEGGGAMIHQVSLRtGT 265
Cdd:pfam00266 161 IGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGMIETVSLQ-ES 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 266 TYADSPWRFEAGSPNTGGIMGLGAALDYVTALGREEIQRYESSLMQYALEALTQVPDLTLYGPAERHGVIAFNLGQHHAY 345
Cdd:pfam00266 240 TFADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPERRASIISFNFKGVHPH 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2695378996 346 DVGSFLDRYGIAIRTGHHCAMPLMEHYGVPSMCRASLAVYTTREEIDRL 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: 806.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996   1 MSYPIERVRADFPLLASEVNGQPLAYLDSAASAQKPHAVIDREAEFYRHEYAAVHRGIHTLSAQATSAMEAVREKVASFI 80
Cdd:PRK09295    1 MTFSVEKVRADFPVLSREVNGLPLAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKQAALFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996  81 NAASVEEIVFVRGTTEAINLVANSYGRTFIQPGDNLIITEMEHHANIVPWQMLAEARGVEVRVLPLAEDGSLDVAQLPGL 160
Cdd:PRK09295   81 NARSAEELVFVRGTTEGINLVANSWGNSNVRAGDNIIISEMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 161 LDERTRLLAVTQISNVLGALNPVKAMIAQAKAAGAVTLVDGAQSIMHQTVDVQDLDCDFFVFSGHKIYGPSGIGVLYGKR 240
Cdd:PRK09295  161 FDERTRLLAITHVSNVLGTENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 241 DLLQAMPPWEGGGAMIHQVSLRTGTTYADSPWRFEAGSPNTGGIMGLGAALDYVTALGREEIQRYESSLMQYALEALTQV 320
Cdd:PRK09295  241 ALLQEMPPWEGGGSMIATVSLTEGTTWAKAPWRFEAGTPNTGGIIGLGAALDYVSALGLNNIAEYEQNLMHYALSQLESV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 321 PDLTLYGPAERHGVIAFNLGQHHAYDVGSFLDRYGIAIRTGHHCAMPLMEHYGVPSMCRASLAVYTTREEIDRLVAGLQR 400
Cdd:PRK09295  321 PDLTLYGPQNRLGVIAFNLGKHHAYDVGSFLDNYGIAVRTGHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVAGLQR 400

                  ....*.
gi 2695378996 401 IHRLLG 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: 652.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996   6 ERVRADFPLLASEVNGQPLAYLDSAASAQKPHAVIDREAEFYRHEYAAVHRGIHTLSAQATSAMEAVREKVASFINAASV 85
Cdd:TIGR01979   1 KNIRADFPILKRKINGKPLVYLDSAATSQKPQQVIDAVAEYYRNSNANVHRGIHTLSVRATEAYEAVREKVAKFINAASD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996  86 EEIVFVRGTTEAINLVANSYGRTFIQPGDNLIITEMEHHANIVPWQMLAEARGVEVRVLPLAEDGSLDVAQLPGLLDERT 165
Cdd:TIGR01979  81 EEIVFTRGTTESINLVAYSWGDSNLKAGDEIVISEMEHHANIVPWQLLAERTGATLKFIPLDDDGTLDLDDLEKLLTEKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 166 RLLAVTQISNVLGALNPVKAMIAQAKAAGAVTLVDGAQSIMHQTVDVQDLDCDFFVFSGHKIYGPSGIGVLYGKRDLLQA 245
Cdd:TIGR01979 161 KLVAITHVSNVLGTVNPVEEIAKLAHQVGAKVLVDGAQAVPHMPVDVQALDCDFYVFSGHKMYGPTGIGVLYGKEELLEQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 246 MPPWEGGGAMIHQVSLRtGTTYADSPWRFEAGSPNTGGIMGLGAALDYVTALGREEIQRYESSLMQYALEALTQVPDLTL 325
Cdd:TIGR01979 241 MPPFLGGGEMIAEVSFE-ETTYNEAPHKFEAGTPNIAGVIGLGAAIDYLEAIGLENIEAHEHELTAYALERLGEIPGLRI 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 326 YGP---AERHGVIAFNLGQHHAYDVGSFLDRYGIAIRTGHHCAMPLMEHYGVPSMCRASLAVYTTREEIDRLVAGLQRIH 402
Cdd:TIGR01979 320 YGPrdaEDRGGIISFNVEGVHPHDVGTILDEEGIAVRSGHHCAQPLMRRFGVPATCRASFYIYNTEEDIDALVEALKKVR 399

                  ....
gi 2695378996 403 RLLG 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: 621.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996   5 IERVRADFPllaseVNGQPLAYLDSAASAQKPHAVIDREAEFYRHEYAAVHRGIHTLSAQATSAMEAVREKVASFINAAS 84
Cdd:COG0520     2 VEAIRADFP-----VLGKPLVYLDNAATGQKPRPVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAAS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996  85 VEEIVFVRGTTEAINLVANSYGRtfIQPGDNLIITEMEHHANIVPWQMLAEARGVEVRVLPLAEDGSLDVAQLPGLLDER 164
Cdd:COG0520    77 PDEIIFTRGTTEAINLVAYGLGR--LKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDGELDLEALEALLTPR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 165 TRLLAVTQISNVLGALNPVKAMIAQAKAAGAVTLVDGAQSIMHQTVDVQDLDCDFFVFSGHKIYGPSGIGVLYGKRDLLQ 244
Cdd:COG0520   155 TKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELLE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 245 AMPPWEGGGAMIHQVSLrTGTTYADSPWRFEAGSPNTGGIMGLGAALDYVTALGREEIQRYESSLMQYALEALTQVPDLT 324
Cdd:COG0520   235 ALPPFLGGGGMIEWVSF-DGTTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAIPGVR 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 325 LYGPA---ERHGVIAFNLGQHHAYDVGSFLDRYGIAIRTGHHCAMPLMEHYGVPSMCRASLAVYTTREEIDRLVAGLQRI 401
Cdd:COG0520   314 ILGPAdpeDRSGIVSFNVDGVHPHDVAALLDDEGIAVRAGHHCAQPLMRRLGVPGTVRASFHLYNTEEEIDRLVEALKKL 393

                  ...
gi 2695378996 402 HRL 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: 589.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996  26 YLDSAASAQKPHAVIDREAEFYRHEYAAVHRGIHTLSAQATSAMEAVREKVASFINAASVEEIVFVRGTTEAINLVANSY 105
Cdd:cd06453     2 YLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINAPSPDEIIFTRNTTEAINLVAYGL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 106 GRTFiQPGDNLIITEMEHHANIVPWQMLAEARGVEVRVLPLAEDGSLDVAQLPGLLDERTRLLAVTQISNVLGALNPVKA 185
Cdd:cd06453    82 GRAN-KPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPVKE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 186 MIAQAKAAGAVTLVDGAQSIMHQTVDVQDLDCDFFVFSGHKIYGPSGIGVLYGKRDLLQAMPPWEGGGAMIHQVSLrTGT 265
Cdd:cd06453   161 IGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMIEEVSF-EET 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 266 TYADSPWRFEAGSPNTGGIMGLGAALDYVTALGREEIQRYESSLMQYALEALTQVPDLTLYGPAERH-GVIAFNLGQHHA 344
Cdd:cd06453   240 TYADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEIPGVRVYGDAEDRaGVVSFNLEGIHP 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2695378996 345 YDVGSFLDRYGIAIRTGHHCAMPLMEHYGVPSMCRASLAVYTTREEIDRLVAGL 398
Cdd:cd06453   320 HDVATILDQYGIAVRAGHHCAQPLMRRLGVPGTVRASFGLYNTEEEIDALVEAL 373
f2_encap_cargo1 NF041166
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ...
5-401 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: 560.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996   5 IERVRADFPLLASEVNGQPLAYLDSAASAQKPHAVIDREAEFYRHEYAAVHRGIHTLSAQATSAMEAVREKVASFINAAS 84
Cdd:NF041166  227 VNAVRRDFPILQERVNGKPLVWFDNAATTQKPQAVIDRLSYFYEHENSNIHRAAHELAARATDAYEGAREKVRRFIGAPS 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996  85 VEEIVFVRGTTEAINLVANSYGRTFIQPGDNLIITEMEHHANIVPWQMLAEARGVEVRVLPLAEDGSLDVAQLPGLLDER 164
Cdd:NF041166  307 VDEIIFVRGTTEAINLVAKSWGRQNIGAGDEIIVSHLEHHANIVPWQQLAQETGAKLRVIPVDDSGQILLDEYAKLLNPR 386
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 165 TRLLAVTQISNVLGALNPVKAMIAQAKAAGAVTLVDGAQSIMHQTVDVQDLDCDFFVFSGHKIYGPSGIGVLYGKRDLLQ 244
Cdd:NF041166  387 TKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGIGVVYGKRDLLE 466
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 245 AMPPWEGGGAMIHQVSLrTGTTYADSPWRFEAGSPNTGGIMGLGAALDYVTALGREEIQRYESSLMQYALEALTQVPDLT 324
Cdd:NF041166  467 AMPPWQGGGNMIADVTF-EKTVYQPAPNRFEAGTGNIADAVGLGAALDYVERIGIENIARYEHDLLEYATAGLAEVPGLR 545
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2695378996 325 LYGPA-ERHGVIAFNLGQHHAYDVGSFLDRYGIAIRTGHHCAMPLMEHYGVPSMCRASLAVYTTREEIDRLVAGLQRI 401
Cdd:NF041166  546 LIGTAaDKASVLSFVLDGYSTEEVGKALNQEGIAVRSGHHCAQPILRRFGVEATVRPSLAFYNTCEEVDALVAVLRRL 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: 553.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996  26 YLDSAASAQKPHAVIDREAEFYRHEYAAVHRGIHTLSAQATSAMEAVREKVASFINAASVEEIVFVRGTTEAINLVANSY 105
Cdd:pfam00266   2 YLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAINLVALSL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 106 GRTFiQPGDNLIITEMEHHANIVPWQMLAEARGVEVRVLPLAEDGSLDVAQLPGLLDERTRLLAVTQISNVLGALNPVKA 185
Cdd:pfam00266  82 GRSL-KPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVPE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 186 MIAQAKAAGAVTLVDGAQSIMHQTVDVQDLDCDFFVFSGHKIYGPSGIGVLYGKRDLLQAMPPWEGGGAMIHQVSLRtGT 265
Cdd:pfam00266 161 IGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGMIETVSLQ-ES 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 266 TYADSPWRFEAGSPNTGGIMGLGAALDYVTALGREEIQRYESSLMQYALEALTQVPDLTLYGPAERHGVIAFNLGQHHAY 345
Cdd:pfam00266 240 TFADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPERRASIISFNFKGVHPH 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2695378996 346 DVGSFLDRYGIAIRTGHHCAMPLMEHYGVPSMCRASLAVYTTREEIDRL 394
Cdd:pfam00266 320 DVATLLDESGIAVRSGHHCAQPLMVRLGLGGTVRASFYIYNTQEDVDRL 368
PLN02855 PLN02855
Bifunctional selenocysteine lyase/cysteine desulfurase
6-399 2.63e-178

Bifunctional selenocysteine lyase/cysteine desulfurase


Pssm-ID: 215460 [Multi-domain]  Cd Length: 424  Bit Score: 503.13  E-value: 2.63e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996   6 ERVRADFPLLASEVNGQPLAYLDSAASAQKPHAVIDREAEFYRHEYAAVHRGIHTLSAQATSAMEAVREKVASFINAASV 85
Cdd:PLN02855   15 AETRPDFPILDQTVNGSKLVYLDNAATSQKPAAVLDALQDYYEEYNSNVHRGIHALSAKATDAYELARKKVAAFINASTS 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996  86 EEIVFVRGTTEAINLVANSYGRTFIQPGDNLIITEMEHHANIVPWQMLAEARGVEVRVLPLAEDGSLDVAQLPGLLDERT 165
Cdd:PLN02855   95 REIVFTRNATEAINLVAYTWGLANLKPGDEVILSVAEHHSNIVPWQLVAQKTGAVLKFVGLTPDEVLDVEQLKELLSEKT 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 166 RLLAVTQISNVLGALNPVKAMIAQAKAAGAVTLVDGAQSIMHQTVDVQDLDCDFFVFSGHKIYGPSGIGVLYGKRDLLQA 245
Cdd:PLN02855  175 KLVATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLWGKSDLLES 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 246 MPPWEGGGAMIHQVSLrTGTTYADSPWRFEAGSPNTGGIMGLGAALDYVTALGREEIQRYESSLMQYALEALTQVPDLTL 325
Cdd:PLN02855  255 MPPFLGGGEMISDVFL-DHSTYAPPPSRFEAGTPAIGEAIGLGAAIDYLSEIGMDRIHEYEVELGTYLYEKLSSVPGVRI 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 326 YGPA-----ERHGVIAFNLGQHHAYDVGSFLD-RYGIAIRTGHHCAMPLMEHYGVPSMCRASLAVYTTREEIDRLVAGLQ 399
Cdd:PLN02855  334 YGPKpsegvGRAALCAFNVEGIHPTDLSTFLDqQHGVAIRSGHHCAQPLHRYLGVNASARASLYFYNTKEEVDAFIHALK 413
PRK10874 PRK10874
cysteine desulfurase CsdA;
9-405 4.29e-153

cysteine desulfurase CsdA;


Pssm-ID: 182799 [Multi-domain]  Cd Length: 401  Bit Score: 438.32  E-value: 4.29e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996   9 RADFPLLAsevngQPLAYLDSAASAQKPHAVIDREAEFYRHEYAAVHRGIHTLSAQATSAMEAVREKVASFINAASVEEI 88
Cdd:PRK10874   10 RAQFPALQ-----DAGVYLDSAATALKPQAVIEATQQFYSLSAGNVHRSQFAAAQRLTARYEAAREQVAQLLNAPDAKNI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996  89 VFVRGTTEAINLVANSYGRTFIQPGDNLIITEMEHHANIVPWQMLAEARGVEVRVLPLAEDGSLDVAQLPGLLDERTRLL 168
Cdd:PRK10874   85 VWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLVPWLMVAQQTGAKVVKLPLGADRLPDVDLLPELITPRTRIL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 169 AVTQISNVLGALNPVKAMIAQAKAAGAVTLVDGAQSIMHQTVDVQDLDCDFFVFSGHKIYGPSGIGVLYGKRDLLQAMPP 248
Cdd:PRK10874  165 ALGQMSNVTGGCPDLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMSP 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 249 WEGGGAMIHQVSLrTGTTYADSPWRFEAGSPNTGGIMGLGAALDYVTALGREEIQRYESSLMQYALEALTQVPDLTLYgP 328
Cdd:PRK10874  245 WQGGGKMLTEVSF-DGFTPQSAPWRFEAGTPNVAGVIGLSAALEWLADIDINQAESWSRSLATLAEDALAKLPGFRSF-R 322
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2695378996 329 AERHGVIAFNL-GQHHAyDVGSFLDRYGIAIRTGHHCAMPLMEHYGVPSMCRASLAVYTTREEIDRLVAGLQRIHRLL 405
Cdd:PRK10874  323 CQDSSLLAFDFaGVHHS-DLVTLLAEYGIALRAGQHCAQPLLAALGVTGTLRASFAPYNTQSDVDALVNAVDRALELL 399
FeS_syn_CsdA TIGR03392
cysteine desulfurase, catalytic subunit CsdA; Members of this protein family are CsdS. This ...
9-405 9.85e-140

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: 404.22  E-value: 9.85e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996   9 RADFPLLAsevngQPLAYLDSAASAQKPHAVIDREAEFYRHEYAAVHRGIHTLSAQATSAMEAVREKVASFINAASVEEI 88
Cdd:TIGR03392   7 RRQFPALQ-----DATVYLDSAATALKPQAVIDATQQFYRLSSGTVHRSQHQEAQSLTARYEAAREQVAQLLNAPDAENI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996  89 VFVRGTTEAINLVANSYGRTFIQPGDNLIITEMEHHANIVPWQMLAEARGVEVRVLPLAEDGSLDVAQLPGLLDERTRLL 168
Cdd:TIGR03392  82 VWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLIPWLMVAQQTGAKVVKLPIGADLLPDIDQLPELLTPRTRIL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 169 AVTQISNVLGALNPVKAMIAQAKAAGAVTLVDGAQSIMHQTVDVQDLDCDFFVFSGHKIYGPSGIGVLYGKRDLLQAMPP 248
Cdd:TIGR03392 162 ALGQMSNVTGGCPDLARAITLAHQYGCVVVVDGAQGVVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKTELLEAMPP 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 249 WEGGGAMIHQVSLrTGTTYADSPWRFEAGSPNTGGIMGLGAALDYVTALGREEIQRYESSLMQYALEALTQVPDLTLYGP 328
Cdd:TIGR03392 242 WQGGGKMLSHVSF-DGFTPQAVPWRFEAGTPNIAGVIGLSAALEWLADIDINAAESWSVSLATLAEEALAQLPGFRSFRC 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2695378996 329 AERhGVIAFNLGQHHAYDVGSFLDRYGIAIRTGHHCAMPLMEHYGVPSMCRASLAVYTTREEIDRLVAGLQRIHRLL 405
Cdd:TIGR03392 321 QGS-SLLAFDFAGVHHSDLVTLLAEQGIALRAGQHCAQPLMAALGVSGTLRASFAPYNTQQDVDALVNAVGRALELL 396
am_tr_V_VC1184 TIGR01976
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of ...
3-398 1.11e-82

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: 258.53  E-value: 1.11e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996   3 YPIERVRADFPLLASEVngqpLAYLDSAASAQKPHAVIDREAEFYRHEYAavHRGIHTLSAQATSAM-EAVREKVASFIN 81
Cdd:TIGR01976   1 FDVEAVRGQFPALADGD----RVFFDNPAGTQIPQSVADAVSAALTRSNA--NRGGAYESSRRADQVvDDAREAVADLLN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996  82 AASvEEIVFVRGTTEAINLVANSYGRTFiQPGDNLIITEMEHHANIVPWQMLAEARGVEVRVLPL-AEDGSLDVAQLPGL 160
Cdd:TIGR01976  75 ADP-PEVVFGANATSLTFLLSRAISRRW-GPGDEVIVTRLDHEANISPWLQAAERAGAKVKWARVdEATGELHPDDLASL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 161 LDERTRLLAVTQISNVLGALNPVKAMIAQAKAAGAVTLVDGAQSIMHQTVDVQDLDCDFFVFSGHKIYGPSgIGVLYGKR 240
Cdd:TIGR01976 153 LSPRTRLVAVTAASNTLGSIVDLAAITELVHAAGALVVVDAVHYAPHGLIDVQATGADFLTCSAYKFFGPH-MGILWGRP 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 241 DLLQAMPPWegggamihqvslRTGTTYADSPWRFEAGSPNTGGIMGLGAALDYVTALGREE--------------IQRYE 306
Cdd:TIGR01976 232 ELLMNLPPY------------KLTFSYDTGPERFELGTPQYELLAGVVAAVDYLAGLGESAngsrrerlvasfqaIDAYE 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 307 SSLMQYALEALTQVPDLTLYG---PAERHGVIAFNLGQHHAYDVGSFLDRYGIAIRTGHHCAMPLMEHYGVPS---MCRA 380
Cdd:TIGR01976 300 NRLAEYLLVGLSDLPGVTLYGvarLAARVPTVSFTVHGLPPQRVVRRLADQGIDAWAGHFYAVRLLRRLGLNDeggVVRV 379
                         410
                  ....*....|....*...
gi 2695378996 381 SLAVYTTREEIDRLVAGL 398
Cdd:TIGR01976 380 GLAHYNTAEEVDRLLEAL 397
NifS COG1104
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ...
26-401 8.31e-62

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: 203.74  E-value: 8.31e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996  26 YLDSAASAQKPHAVIDREAEFYRHEYaavhrG----IHTLSAQATSAMEAVREKVASFINAASvEEIVFVRGTTEAINLV 101
Cdd:COG1104     5 YLDNAATTPVDPEVLEAMLPYLTEYF-----GnpssLHSFGREARAALEEAREQVAALLGADP-EEIIFTSGGTEANNLA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 102 ANSYGRTFIQPGDNLIITEMEHHA--NIVPWqmlAEARGVEVRVLPLAEDGSLDVAQLPGLLDERTRLLAVTQISNVLGA 179
Cdd:COG1104    79 IKGAARAYRKKGKHIITSAIEHPAvlETARF---LEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 180 LNPVKAMIAQAKAAGAVTLVDGAQSIMHQTVDVQDLDCDFFVFSGHKIYGPSGIGVLYGKRDlLQAMPPWEGGGamiHQV 259
Cdd:COG1104   156 IQPIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRKG-VRLEPLIHGGG---QER 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 260 SLRTGTtyadspwrfeagsPNTGGIMGLGAALDYVTALGREEIQRYeSSLMQYALEALTQ-VPDLTLYGPAERH--GVIA 336
Cdd:COG1104   232 GLRSGT-------------ENVPGIVGLGKAAELAAEELEEEAARL-RALRDRLEEGLLAaIPGVVINGDPENRlpNTLN 297
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2695378996 337 FNLGQHHAYDVGSFLDRYGIAIRTGHHC------------AMPLMEHYGVPSMcRASLAVYTTREEIDRLVAGLQRI 401
Cdd:COG1104   298 FSFPGVEGEALLLALDLAGIAVSSGSACssgslepshvllAMGLDEELAHGSI-RFSLGRFTTEEEIDRAIEALKEI 373
PLN02651 PLN02651
cysteine desulfurase
26-392 1.84e-35

cysteine desulfurase


Pssm-ID: 178257 [Multi-domain]  Cd Length: 364  Bit Score: 133.63  E-value: 1.84e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996  26 YLDSAASAQKPHAVIDREAEFYRHEYAAVHRGIHTLSAQATSAMEAVREKVASFINAASvEEIVFVRGTTEAINLVANSY 105
Cdd:PLN02651    2 YLDMQATTPIDPRVLDAMLPFLIEHFGNPHSRTHLYGWESEDAVEKARAQVAALIGADP-KEIIFTSGATESNNLAIKGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 106 GRTFIQPGDNLIITEMEHHANIVPWQMLaEARGVEVRVLPLAEDGSLDVAQLPGLLDERTRLLAVTQISNVLGALNPVKA 185
Cdd:PLN02651   81 MHFYKDKKKHVITTQTEHKCVLDSCRHL-QQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVEE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 186 MIAQAKAAGAVTLVDGAQSIMHQTVDVQDLDCDFFVFSGHKIYGPSGIGVLYGKRDLLQAMPPWEGGGAMIHqvSLRTGT 265
Cdd:PLN02651  160 IGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRLEPLMSGGGQER--GRRSGT 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 266 TyadspwrfeagspNTGGIMGLGAAldyvTALGREEIQRYESSL------MQYALEAltQVPDLTLYGPAERHGVIAFNL 339
Cdd:PLN02651  238 E-------------NTPLVVGLGAA----CELAMKEMDYDEKHMkalrerLLNGLRA--KLGGVRVNGPRDPEKRYPGTL 298
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2695378996 340 GQHHAY-DVGSFLDRY-GIAIRTGHHC------------AMPLMEHYGVPSMcRASLAVYTTREEID 392
Cdd:PLN02651  299 NLSFAYvEGESLLMGLkEVAVSSGSACtsaslepsyvlrALGVPEEMAHGSL-RLGVGRFTTEEEVD 364
PRK14012 PRK14012
IscS subfamily cysteine desulfurase;
59-392 1.89e-30

IscS subfamily cysteine desulfurase;


Pssm-ID: 184450 [Multi-domain]  Cd Length: 404  Bit Score: 120.82  E-value: 1.89e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996  59 HTLSAQATSAMEAVREKVASFINAASvEEIVFVRGTTEAINL----VANSYGRTfiqpGDNLIITEMEHHANIVPWQMLa 134
Cdd:PRK14012   41 HRFGWQAEEAVDIARNQIADLIGADP-REIVFTSGATESDNLaikgAAHFYQKK----GKHIITSKTEHKAVLDTCRQL- 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 135 EARGVEVRVLPLAEDGSLDVAQLPGLLDERTRLLAVTQISNVLGALNPVKAMIAQAKAAGAVTLVDGAQSIMHQTVDVQD 214
Cdd:PRK14012  115 EREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVIQDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSK 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 215 LDCDFFVFSGHKIYGPSGIGVLYGKRD----LLQAMppwEGGGamiHQVSLRTGTTyadspwrfeagspNTGGIMGLGAA 290
Cdd:PRK14012  195 LKVDLMSFSAHKIYGPKGIGALYVRRKprvrLEAQM---HGGG---HERGMRSGTL-------------PTHQIVGMGEA 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 291 LDYVTALGREEIQRYEsSLMQYALEALTQVPDLTLYGPAERHgvIAFNLGQHHAYDVGSFL-----DrygIAIRTGHHC- 364
Cdd:PRK14012  256 ARIAKEEMATENERIR-ALRDRLWNGIKDIEEVYLNGDLEQR--VPGNLNVSFNYVEGESLimalkD---LAVSSGSACt 329
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2695378996 365 -----------AMPL---MEHygvpSMCRASLAVYTTREEID 392
Cdd:PRK14012  330 saslepsyvlrALGLndeLAH----SSIRFSLGRFTTEEEID 367
PRK02948 PRK02948
IscS subfamily cysteine desulfurase;
26-401 3.47e-24

IscS subfamily cysteine desulfurase;


Pssm-ID: 179511 [Multi-domain]  Cd Length: 381  Bit Score: 102.89  E-value: 3.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996  26 YLDSAASAQkphavIDREA-EFYRH---EYAAVHRGIHTLSAQATSAMEAVREKVASFINAASvEEIVFVRGTTEAINLV 101
Cdd:PRK02948    3 YLDYAATTP-----MSKEAlQTYQKaasQYFGNESSLHDIGGTASSLLQVCRKTFAEMIGGEE-QGIYFTSGGTESNYLA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 102 ANSYGRTFIQPGDNLIITEMEHHANIVPWQMLaEARGVEVRVLPLAEDGSLDVAQLPGLLDERTRLLAVTQISNVLGALN 181
Cdd:PRK02948   77 IQSLLNALPQNKKHIITTPMEHASIHSYFQSL-ESQGYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 182 PVKAMIAQAKAAGAVTLVDGAQSIMHQTVDVQDLDCDFFVFSGHKIYGPSGIGVLYGKRDLlqampPWEgggamihqvSL 261
Cdd:PRK02948  156 PIAEIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYINPQV-----RWK---------PV 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 262 RTGTTYADSpwrFEAGSPNTGGIMGLGAALDYVTALGREEIQRYEsSLMQYALEaltQVPDLTLYGPAERHGviafnlGQ 341
Cdd:PRK02948  222 FPGTTHEKG---FRPGTVNVPGIAAFLTAAENILKNMQEESLRFK-ELRSYFLE---QIQTLPLPIEVEGHS------TS 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 342 HHAYDVGSFL------------DRYGIAIRTGHHCAMPLMEhygvPS---------------MCRASLAVYTTREEIDRL 394
Cdd:PRK02948  289 CLPHIIGVTIkgiegqytmlecNRRGIAISTGSACQVGKQE----PSktmlaigktyeeakqFVRFSFGQQTTKDQIDTT 364

                  ....*..
gi 2695378996 395 VAGLQRI 401
Cdd:PRK02948  365 IHALETI 371
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
69-239 1.33e-15

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: 73.96  E-value: 1.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996  69 MEAVREKVASFINAaSVEEIVFVRGTTEAINLVANSYGrtfiQPGDNLIITEMEHHANIVPWQMLAEARGVEVRVLPlAE 148
Cdd:cd01494     2 LEELEEKLARLLQP-GNDKAVFVPSGTGANEAALLALL----GPGDEVIVDANGHGSRYWVAAELAGAKPVPVPVDD-AG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 149 DGSLDVAQLP-GLLDERTRLLAVTQISNVLGALNPVKAMIAQAKAAGAVTLVDGAQSIMHQTVDVQDLD---CDFFVFSG 224
Cdd:cd01494    76 YGGLDVAILEeLKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPeggADVVTFSL 155
                         170
                  ....*....|....*
gi 2695378996 225 HKIYGPSGIGVLYGK 239
Cdd:cd01494   156 HKNLGGEGGGVVIVK 170
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
70-400 5.07e-09

Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 57.35  E-value: 5.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996  70 EAVREKVASFIN-----AASVEEIVFVRGTTEAINLVAnsygRTFIQPGDNLIITEmehhanivP-WQM---LAEARGVE 140
Cdd:cd00609    39 PELREAIAEWLGrrggvDVPPEEIVVTNGAQEALSLLL----RALLNPGDEVLVPD--------PtYPGyeaAARLAGAE 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 141 VRVLPLAEDGS--LDVAQLPGLLDERTRLLAVTQISNVLGALNP---VKAMIAQAKAAGAVTLVDGA-------QSIMHQ 208
Cdd:cd00609   107 VVPVPLDEEGGflLDLELLEAAKTPKTKLLYLNNPNNPTGAVLSeeeLEELAELAKKHGILIISDEAyaelvydGEPPPA 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 209 TVDVQDLDCDFFVFSGHKIYGPSG--IGVLYGKRDLLqamppwegggamIHQVSLRtgttyadspWRFEAGSPNTGGIMG 286
Cdd:cd00609   187 LALLDAYERVIVLRSFSKTFGLPGlrIGYLIAPPEEL------------LERLKKL---------LPYTTSGPSTLSQAA 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 287 LGAALDYVTALGREEIQRYESSlMQYALEALTQVPDLTLYGPAerhgvIAFNL-----GQHHAYDVGSFLDRYGIAIRTG 361
Cdd:cd00609   246 AAAALDDGEEHLEELRERYRRR-RDALLEALKELGPLVVVKPS-----GGFFLwldlpEGDDEEFLERLLLEAGVVVRPG 319
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 2695378996 362 HHCAMPLMEHYgvpsmcRASLAvyTTREEIDRLVAGLQR 400
Cdd:cd00609   320 SAFGEGGEGFV------RLSFA--TPEEELEEALERLAE 350
PucG COG0075
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ...
130-361 2.82e-08

Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 439845 [Multi-domain]  Cd Length: 376  Bit Score: 55.10  E-value: 2.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 130 WQMLAEARGVEVRVLPLAEDGSLDVAQLpglldeRTRLLAVTQISNVL--------GALNPVKAMIAQAKAAGAVTLVDG 201
Cdd:COG0075    89 WAEIAERYGAEVVVLEVPWGEAVDPEEV------EEALAADPDIKAVAvvhnetstGVLNPLEEIGALAKEHGALLIVDA 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 202 AQSIMHQTVDVQDLDCDFFVFSGHK-IYGPSGIGVLYGKRDLLQAMppwegggamiHQVSLRtgTTYAD-SPWR--FEAG 277
Cdd:COG0075   163 VSSLGGVPLDMDEWGIDVVVSGSQKcLMLPPGLAFVAVSERALEAI----------EARKLP--SYYLDlKLWLkyWEKG 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 278 S----PNTGGIMGLGAALDYVTALGREE-IQRYE--SSLMQYALEALtqvpDLTLYGPAER--HGVIAFNLGQHHAYD-- 346
Cdd:COG0075   231 QtpytPPVSLLYALREALDLILEEGLENrFARHRrlAEALRAGLEAL----GLELFAEEEYrsPTVTAVRVPEGVDAAal 306
                         250
                  ....*....|....*
gi 2695378996 347 VGSFLDRYGIAIRTG 361
Cdd:COG0075   307 RKRLKERYGIEIAGG 321
SepCysS cd06452
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ...
74-236 2.37e-07

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: 52.39  E-value: 2.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996  74 EKVASFINAASVEeivFVRGTTEAINLVANSYGrtfiQPGDNLIITEMEHHANIVPwqmlAEARGVEVRVLPLAEDGS-- 151
Cdd:cd06452    51 HDLAEFLGMDEAR---VTPGAREGKFAVMHSLC----EKGDWVVVDGLAHYTSYVA----AERAGLNVREVPNTGHPEyh 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 152 LDVAQLPGLLDERTR-------LLAVTQISNVLGALNPVKAMIAQAKAAGAVTLVDGAQSIMHQTVDVQDLDCDFFVFSG 224
Cdd:cd06452   120 ITPEGYAEVIEEVKDefgkppaLALLTHVDGNYGNLHDAKKIAKVCHEYGVPLLLNGAYTVGRMPVSGKELGADFIVGSG 199
                         170
                  ....*....|...
gi 2695378996 225 HKIYGPSG-IGVL 236
Cdd:cd06452   200 HKSMAASApIGVL 212
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
71-246 3.48e-07

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 51.92  E-value: 3.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996  71 AVREKVASFINA------ASVEEIVFVRGTTEAINLVAnsygRTFIQPGDNLIITEMEH--HANIvpwqmlAEARGVEVR 142
Cdd:pfam00155  43 ELREALAKFLGRspvlklDREAAVVFGSGAGANIEALI----FLLANPGDAILVPAPTYasYIRI------ARLAGGEVV 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 143 VLPL--AEDGSLDVAQLPGLLDERTRLLAVTQISNVLGALNP---VKAMIAQAKAAGAVTLVD--------GAQSIMHQT 209
Cdd:pfam00155 113 RYPLydSNDFHLDFDALEAALKEKPKVVLHTSPHNPTGTVATleeLEKLLDLAKEHNILLLVDeayagfvfGSPDAVATR 192
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2695378996 210 VDVQDLDCDFFVFSGHKIYGPSG--IGVLYGKRDLLQAM 246
Cdd:pfam00155 193 ALLAEGPNLLVVGSFSKAFGLAGwrVGYILGNAAVISQL 231
PRK09331 PRK09331
Sep-tRNA:Cys-tRNA synthetase; Provisional
74-236 4.48e-06

Sep-tRNA:Cys-tRNA synthetase; Provisional


Pssm-ID: 236469  Cd Length: 387  Bit Score: 48.39  E-value: 4.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996  74 EKVASFINaasVEEIVFVRGTTEAINLVANSYGrtfiQPGDNLIITEMEHHANIVPwqmlAEARGVEVRVLPLAEDGS-- 151
Cdd:PRK09331   70 EDLAEFLG---MDEARVTHGAREGKFAVMHSLC----KKGDYVVLDGLAHYTSYVA----AERAGLNVREVPKTGYPEyk 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 152 LDVAQLPGLLDERTR-------LLAVTQISNVLGALNPVKAMIAQAKAAGAVTLVDGAQSIMHQTVDVQDLDCDFFVFSG 224
Cdd:PRK09331  139 ITPEAYAEKIEEVKEetgkppaLALLTHVDGNYGNLADAKKVAKVAHEYGIPFLLNGAYTVGRMPVDGKKLGADFIVGSG 218
                         170
                  ....*....|...
gi 2695378996 225 HKIYGPSG-IGVL 236
Cdd:PRK09331  219 HKSMAASApSGVL 231
PRK13479 PRK13479
2-aminoethylphosphonate--pyruvate transaminase; Provisional
133-245 1.73e-05

2-aminoethylphosphonate--pyruvate transaminase; Provisional


Pssm-ID: 184076 [Multi-domain]  Cd Length: 368  Bit Score: 46.44  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 133 LAEARGVEVRVLPLAEDGSLDVAQLPGLLDERTRL--LAVTQISNVLGALNPVKAMIAQAKAAGAVTLVDGAQSIMHQTV 210
Cdd:PRK13479   98 IAEYLGIAHVVLDTGEDEPPDAAEVEAALAADPRIthVALVHCETTTGILNPLDEIAAVAKRHGKRLIVDAMSSFGAIPI 177
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2695378996 211 DVQDLDCDFFVFSGHK-IYGPSGIGVLYGKRDLLQA 245
Cdd:PRK13479  178 DIAELGIDALISSANKcIEGVPGFGFVIARRSELEA 213
PRK07324 PRK07324
transaminase; Validated
70-200 2.27e-04

transaminase; Validated


Pssm-ID: 235989  Cd Length: 373  Bit Score: 43.00  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996  70 EAVREKVASFINAASVEEIVFVRGTTEAINLVANsygrTFIQPGDNLIitemehhaNIVP-WQML---AEARGVEVRVLP 145
Cdd:PRK07324   65 PEFKEAVASLYQNVKPENILQTNGATGANFLVLY----ALVEPGDHVI--------SVYPtYQQLydiPESLGAEVDYWQ 132
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 146 LAED-GSL-DVAQLPGLLDERTRLLAVTQISNVLGALNPV---KAMIAQAKAAGAVTLVD 200
Cdd:PRK07324  133 LKEEnGWLpDLDELRRLVRPNTKLICINNANNPTGALMDRaylEEIVEIARSVDAYVLSD 192
GcvP1 COG0403
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport ...
134-199 4.86e-04

Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport and metabolism]; Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain is part of the Pathway/BioSystem: Glycine cleavage


Pssm-ID: 440172 [Multi-domain]  Cd Length: 442  Bit Score: 41.94  E-value: 4.86e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2695378996 134 AEARGVEVRVLPLaEDGSLDVAQLPGLLDERTrLLAVTQISNVLGALNPVKAMIAQAKAAGAVTLV 199
Cdd:COG0403   176 AEPLGIEVVEVPD-EDGVTDLEALKALLDDDV-AGVLVQYPNFFGVIEDLRAIAEAAHAAGALVIV 239
PRK00451 PRK00451
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
134-199 9.05e-04

aminomethyl-transferring glycine dehydrogenase subunit GcvPA;


Pssm-ID: 234769 [Multi-domain]  Cd Length: 447  Bit Score: 41.28  E-value: 9.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2695378996 134 AEARGVEVRVLPLaEDGSLDVAQLPGLLDERTRLLAVtQISNVLGALNPVKAMIAQAKAAGAVTLV 199
Cdd:PRK00451  175 LKGQGIEVVEVPY-EDGVTDLEALEAAVDDDTAAVVV-QYPNFFGVIEDLEEIAEIAHAGGALFIV 238
PRK06225 PRK06225
pyridoxal phosphate-dependent aminotransferase;
87-246 1.51e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235749 [Multi-domain]  Cd Length: 380  Bit Score: 40.51  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996  87 EIVFVRGTTEAINLVAnsygRTFIQPGDNLIITEmehhanivP-WQML---AEARGVEVRVLPL---AEDGSLDVAQLPG 159
Cdd:PRK06225   85 EALITAGATESLYLVM----RAFLSPGDNAVTPD--------PgYLIIdnfASRFGAEVIEVPIyseECNYKLTPELVKE 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 160 LLDERTRLLAVTQISNVLGA---LNPVKAMIAQAKAAGA-----VTLVDGAQSimHQTVDVQDLDCDFFVFSGHKIYGPS 231
Cdd:PRK06225  153 NMDENTRLIYLIDPLNPLGSsytEEEIKEFAEIARDNDAfllhdCTYRDFARE--HTLAAEYAPEHTVTSYSFSKIFGMA 230
                         170
                  ....*....|....*..
gi 2695378996 232 G--IGVLYGKRDLLQAM 246
Cdd:PRK06225  231 GlrIGAVVATPDLIEVV 247
tyr_amTase_E TIGR01264
tyrosine aminotransferase, eukaryotic; This model describes tyrosine aminotransferase as found ...
65-179 2.43e-03

tyrosine aminotransferase, eukaryotic; This model describes tyrosine aminotransferase as found in animals and Trypanosoma cruzi. It is the first enzyme of a pathway of tyrosine degradation via homogentisate. Several plant enzyme designated as probable tyrosine aminotransferases are very closely related to an experimentally demonstrated nicotianamine aminotransferase, an enzyme in a siderophore (iron uptake chelator) biosynthesis pathway. These plant sequences are excluded from the model seed and score between the trusted an noise cutoffs. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273529 [Multi-domain]  Cd Length: 401  Bit Score: 39.77  E-value: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996  65 ATSAMEAVREKVASFINAASVEEIVFVRGTTEAINL----VANsygrtfiqPGDNLIITemehHANIVPWQMLAEARGVE 140
Cdd:TIGR01264  75 ALSAREAIASYYHNPDGPIEADDVVLCSGCSHAIEMciaaLAN--------AGQNILVP----RPGFPLYETLAESMGIE 142
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2695378996 141 VRVLPLAEDGS--LDVAQLPGLLDERTRLLAVTQISNVLGA 179
Cdd:TIGR01264 143 VKLYNLLPDKSweIDLKQLESLIDEKTAALIVNNPSNPCGS 183
PRK09105 PRK09105
pyridoxal phosphate-dependent aminotransferase;
134-246 4.61e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 181651  Cd Length: 370  Bit Score: 38.87  E-value: 4.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 134 AEARGVEVRVLPLAEDGSLDV-AQLPGllDERTRLLAVTQISNVLGALNPvKAMIAQA---KAAGAVTLVDGAQ---SIM 206
Cdd:PRK09105  136 ADAQGAPVAKVPLRADGAHDVkAMLAA--DPNAGLIYICNPNNPTGTVTP-RADIEWLlanKPAGSVLLVDEAYihfSDA 212
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2695378996 207 HQTVDVQDLDCDFFV---FSghKIYGPSGI--GVLYGKRDLLQAM 246
Cdd:PRK09105  213 PSVVDLVAQRKDLIVlrtFS--KLYGMAGMrlGLAAARPDLLAKL 255
GDC-P cd00613
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ...
131-202 5.44e-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: 38.75  E-value: 5.44e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2695378996 131 QMLAEARGVEVRVLPLAEDGSLDVAQLPGLLDERTRLLAVTQiSNVLGAL-NPVKAMIAQAKAAGAVTLVDGA 202
Cdd:cd00613   126 RTRGEPLGIEVVEVPSDEGGTVDLEALKEEVSEEVAALMVQY-PNTLGVFeDLIKEIADIAHSAGALVYVDGD 197
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
109-205 7.04e-03

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: 38.43  E-value: 7.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2695378996 109 FIQPGDNLIITEMEHHANIvpWQMLAEARGVEVRVLPLAEDGSLDVAQLPGLLDERT-RLLAVTQISNVLGALNPVKAMI 187
Cdd:cd06451    70 LLEPGDKVLVGVNGVFGDR--WADMAERYGADVDVVEKPWGEAVSPEEIAEALEQHDiKAVTLTHNETSTGVLNPLEGIG 147
                          90
                  ....*....|....*...
gi 2695378996 188 AQAKAAGAVTLVDGAQSI 205
Cdd:cd06451   148 ALAKKHDALLIVDAVSSL 165
 
Blast search parameters
Data Source: Live blast search RID = SWMRR88V013
User Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01   Maximum number of hits: 500

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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