|
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
|
|
|