|
Name |
Accession |
Description |
Interval |
E-value |
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
24-389 |
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: 513.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 24 YLDSAATTQKPQVLLDALSHYYGHGAANVHRAQHLPGALATQAFEASRDKVAAWLNAADSRQIVFTHGATSALNLLAYGL 103
Cdd:pfam00266 2 YLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAINLVALSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 104 EYRFEAGDEIAISALEHHANLLPWQQLARRRGVRLVVLPLDEHGRIDLDQALQLIGPRTRLLAVSQLSNVLGTWQPLPAL 183
Cdd:pfam00266 82 GRSLKPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVPEI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 184 LSHARAQGALTVVDGAQGVVHGRHDVQQLGCDFYVFSSHKLYGPEGVGVLYGRPQALEQLRHWQFGGEMVQLADYQSASF 263
Cdd:pfam00266 162 GKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGMIETVSLQESTF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 264 RPAPLGFEAGTPPIAGVIGLGAILDYLASLDATAVAHHETSLHHSLLRGLGDREGIRILGTPQ-AALVSFVVEGVHNADI 342
Cdd:pfam00266 242 ADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPERrASIISFNFKGVHPHDV 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1321283129 343 AHLLTEQGIAVRAGHHCAMPLLKGLGLEGAIRVSLALYNDSDDLQRF 389
Cdd:pfam00266 322 ATLLDESGIAVRSGHHCAQPLMVRLGLGGTVRASFYIYNTQEDVDRL 368
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
4-395 |
0e+00 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 510.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 4 PSPWRADFPAIaalqRQHQTYLDSAATTQKPQVLLDALSHYYGHGAANVHRAQHLPGALATQAFEASRDKVAAWLNAADS 83
Cdd:COG0520 2 VEAIRADFPVL----GKPLVYLDNAATGQKPRPVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAASP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 84 RQIVFTHGATSALNLLAYGLEyRFEAGDEIAISALEHHANLLPWQQLARRRGVRLVVLPLDEHGRIDLDQALQLIGPRTR 163
Cdd:COG0520 78 DEIIFTRGTTEAINLVAYGLG-RLKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDGELDLEALEALLTPRTK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 164 LLAVSQLSNVLGTWQPLPALLSHARAQGALTVVDGAQGVVHGRHDVQQLGCDFYVFSSHKLYGPEGVGVLYGRPQALEQL 243
Cdd:COG0520 157 LVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELLEAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 244 RHWQFGGEMVQLADYQSASFRPAPLGFEAGTPPIAGVIGLGAILDYLASLDATAVAHHETSLHHSLLRGLGDREGIRILG 323
Cdd:COG0520 237 PPFLGGGGMIEWVSFDGTTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAIPGVRILG 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1321283129 324 TP----QAALVSFVVEGVHNADIAHLLTEQGIAVRAGHHCAMPLLKGLGLEGAIRVSLALYNDSDDLQRFFDALDQ 395
Cdd:COG0520 317 PAdpedRSGIVSFNVDGVHPHDVAALLDDEGIAVRAGHHCAQPLMRRLGVPGTVRASFHLYNTEEEIDRLVEALKK 392
|
|
| sufS |
TIGR01979 |
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine ... |
8-401 |
7.48e-174 |
|
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: 491.02 E-value: 7.48e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 8 RADFPAIAALQRQHQ-TYLDSAATTQKPQVLLDALSHYYGHGAANVHRAQHLPGALATQAFEASRDKVAAWLNAADSRQI 86
Cdd:TIGR01979 4 RADFPILKRKINGKPlVYLDSAATSQKPQQVIDAVAEYYRNSNANVHRGIHTLSVRATEAYEAVREKVAKFINAASDEEI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 87 VFTHGATSALNLLAYGL-EYRFEAGDEIAISALEHHANLLPWQQLARRRGVRLVVLPLDEHGRIDLDQALQLIGPRTRLL 165
Cdd:TIGR01979 84 VFTRGTTESINLVAYSWgDSNLKAGDEIVISEMEHHANIVPWQLLAERTGATLKFIPLDDDGTLDLDDLEKLLTEKTKLV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 166 AVSQLSNVLGTWQPLPALLSHARAQGALTVVDGAQGVVHGRHDVQQLGCDFYVFSSHKLYGPEGVGVLYGRPQALEQLRH 245
Cdd:TIGR01979 164 AITHVSNVLGTVNPVEEIAKLAHQVGAKVLVDGAQAVPHMPVDVQALDCDFYVFSGHKMYGPTGIGVLYGKEELLEQMPP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 246 WQFGGEMVQLADYQSASFRPAPLGFEAGTPPIAGVIGLGAILDYLASLDATAVAHHETSLHHSLLRGLGDREGIRILGT- 324
Cdd:TIGR01979 244 FLGGGEMIAEVSFEETTYNEAPHKFEAGTPNIAGVIGLGAAIDYLEAIGLENIEAHEHELTAYALERLGEIPGLRIYGPr 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 325 ---PQAALVSFVVEGVHNADIAHLLTEQGIAVRAGHHCAMPLLKGLGLEGAIRVSLALYNDSDDLQRFFDALDQGLELLR 401
Cdd:TIGR01979 324 daeDRGGIISFNVEGVHPHDVGTILDEEGIAVRSGHHCAQPLMRRFGVPATCRASFYIYNTEEDIDALVEALKKVRKFFG 403
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
23-393 |
1.53e-171 |
|
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: 483.89 E-value: 1.53e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 23 TYLDSAATTQKPQVLLDALSHYYGHGAANVHRAQHLPGALATQAFEASRDKVAAWLNAADSRQIVFTHGATSALNLLAYG 102
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINAPSPDEIIFTRNTTEAINLVAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 103 LEYRFEAGDEIAISALEHHANLLPWQQLARRRGVRLVVLPLDEHGRIDLDQALQLIGPRTRLLAVSQLSNVLGTWQPLPA 182
Cdd:cd06453 81 LGRANKPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPVKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 183 LLSHARAQGALTVVDGAQGVVHGRHDVQQLGCDFYVFSSHKLYGPEGVGVLYGRPQALEQLRHWQFGGEMVQLADYQSAS 262
Cdd:cd06453 161 IGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMIEEVSFEETT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 263 FRPAPLGFEAGTPPIAGVIGLGAILDYLASLDATAVAHHETSLHHSLLRGLGDREGIRILGTPQ--AALVSFVVEGVHNA 340
Cdd:cd06453 241 YADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEIPGVRVYGDAEdrAGVVSFNLEGIHPH 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1321283129 341 DIAHLLTEQGIAVRAGHHCAMPLLKGLGLEGAIRVSLALYNDSDDLQRFFDAL 393
Cdd:cd06453 321 DVATILDQYGIAVRAGHHCAQPLMRRLGVPGTVRASFGLYNTEEEIDALVEAL 373
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
2-400 |
1.97e-142 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 410.97 E-value: 1.97e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 2 FQPSPWRADFPAIaalqRQHQTYLDSAATTQKPQVLLDALSHYYGHGAANVHRAQHLPGALATQAFEASRDKVAAWLNAA 81
Cdd:PRK10874 4 FNPAQFRAQFPAL----QDAGVYLDSAATALKPQAVIEATQQFYSLSAGNVHRSQFAAAQRLTARYEAAREQVAQLLNAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 82 DSRQIVFTHGATSALNLLAYG-LEYRFEAGDEIAISALEHHANLLPWQQLARRRGVRLVVLPLDEHGRIDLDQALQLIGP 160
Cdd:PRK10874 80 DAKNIVWTRGTTESINLVAQSyARPRLQPGDEIIVSEAEHHANLVPWLMVAQQTGAKVVKLPLGADRLPDVDLLPELITP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 161 RTRLLAVSQLSNVLGTWQPLPALLSHARAQGALTVVDGAQGVVHGRHDVQQLGCDFYVFSSHKLYGPEGVGVLYGRPQAL 240
Cdd:PRK10874 160 RTRILALGQMSNVTGGCPDLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKSELL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 241 EQLRHWQFGGEMVQLADYQSASFRPAPLGFEAGTPPIAGVIGLGAILDYLASLDATAVAHHETSLHHSLLRGLGDREGIR 320
Cdd:PRK10874 240 EAMSPWQGGGKMLTEVSFDGFTPQSAPWRFEAGTPNVAGVIGLSAALEWLADIDINQAESWSRSLATLAEDALAKLPGFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 321 ILGTPQAALVSFVVEGVHNADIAHLLTEQGIAVRAGHHCAMPLLKGLGLEGAIRVSLALYNDSDDLQRFFDALDQGLELL 400
Cdd:PRK10874 320 SFRCQDSSLLAFDFAGVHHSDLVTLLAEYGIALRAGQHCAQPLLAALGVTGTLRASFAPYNTQSDVDALVNAVDRALELL 399
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
8-393 |
1.41e-132 |
|
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: 393.84 E-value: 1.41e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 8 RADFPAIAALQRQHQ-TYLDSAATTQKPQVLLDALSHYYGHGAANVHRAQHLPGALATQAFEASRDKVAAWLNAADSRQI 86
Cdd:NF041166 231 RRDFPILQERVNGKPlVWFDNAATTQKPQAVIDRLSYFYEHENSNIHRAAHELAARATDAYEGAREKVRRFIGAPSVDEI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 87 VFTHGATSALNLLA--YGlEYRFEAGDEIAISALEHHANLLPWQQLARRRGVRLVVLPLDEHGRIDLDQALQLIGPRTRL 164
Cdd:NF041166 311 IFVRGTTEAINLVAksWG-RQNIGAGDEIIVSHLEHHANIVPWQQLAQETGAKLRVIPVDDSGQILLDEYAKLLNPRTKL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 165 LAVSQLSNVLGTWQPLPALLSHARAQGALTVVDGAQGVVHGRHDVQQLGCDFYVFSSHKLYGPEGVGVLYGRPQALEQLR 244
Cdd:NF041166 390 VSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGIGVVYGKRDLLEAMP 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 245 HWQFGGEMVQLADYQSASFRPAPLGFEAGTPPIAGVIGLGAILDYLASLDATAVAHHEtslhHSLL----RGLGDREGIR 320
Cdd:NF041166 470 PWQGGGNMIADVTFEKTVYQPAPNRFEAGTGNIADAVGLGAALDYVERIGIENIARYE----HDLLeyatAGLAEVPGLR 545
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1321283129 321 ILGTPQ--AALVSFVVEGVHNADIAHLLTEQGIAVRAGHHCAMPLLKGLGLEGAIRVSLALYNDSDDLQRFFDAL 393
Cdd:NF041166 546 LIGTAAdkASVLSFVLDGYSTEEVGKALNQEGIAVRSGHHCAQPILRRFGVEATVRPSLAFYNTCEEVDALVAVL 620
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
24-389 |
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: 513.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 24 YLDSAATTQKPQVLLDALSHYYGHGAANVHRAQHLPGALATQAFEASRDKVAAWLNAADSRQIVFTHGATSALNLLAYGL 103
Cdd:pfam00266 2 YLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAINLVALSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 104 EYRFEAGDEIAISALEHHANLLPWQQLARRRGVRLVVLPLDEHGRIDLDQALQLIGPRTRLLAVSQLSNVLGTWQPLPAL 183
Cdd:pfam00266 82 GRSLKPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVPEI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 184 LSHARAQGALTVVDGAQGVVHGRHDVQQLGCDFYVFSSHKLYGPEGVGVLYGRPQALEQLRHWQFGGEMVQLADYQSASF 263
Cdd:pfam00266 162 GKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGMIETVSLQESTF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 264 RPAPLGFEAGTPPIAGVIGLGAILDYLASLDATAVAHHETSLHHSLLRGLGDREGIRILGTPQ-AALVSFVVEGVHNADI 342
Cdd:pfam00266 242 ADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPERrASIISFNFKGVHPHDV 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1321283129 343 AHLLTEQGIAVRAGHHCAMPLLKGLGLEGAIRVSLALYNDSDDLQRF 389
Cdd:pfam00266 322 ATLLDESGIAVRSGHHCAQPLMVRLGLGGTVRASFYIYNTQEDVDRL 368
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
4-395 |
0e+00 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 510.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 4 PSPWRADFPAIaalqRQHQTYLDSAATTQKPQVLLDALSHYYGHGAANVHRAQHLPGALATQAFEASRDKVAAWLNAADS 83
Cdd:COG0520 2 VEAIRADFPVL----GKPLVYLDNAATGQKPRPVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAASP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 84 RQIVFTHGATSALNLLAYGLEyRFEAGDEIAISALEHHANLLPWQQLARRRGVRLVVLPLDEHGRIDLDQALQLIGPRTR 163
Cdd:COG0520 78 DEIIFTRGTTEAINLVAYGLG-RLKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDGELDLEALEALLTPRTK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 164 LLAVSQLSNVLGTWQPLPALLSHARAQGALTVVDGAQGVVHGRHDVQQLGCDFYVFSSHKLYGPEGVGVLYGRPQALEQL 243
Cdd:COG0520 157 LVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELLEAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 244 RHWQFGGEMVQLADYQSASFRPAPLGFEAGTPPIAGVIGLGAILDYLASLDATAVAHHETSLHHSLLRGLGDREGIRILG 323
Cdd:COG0520 237 PPFLGGGGMIEWVSFDGTTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAIPGVRILG 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1321283129 324 TP----QAALVSFVVEGVHNADIAHLLTEQGIAVRAGHHCAMPLLKGLGLEGAIRVSLALYNDSDDLQRFFDALDQ 395
Cdd:COG0520 317 PAdpedRSGIVSFNVDGVHPHDVAALLDDEGIAVRAGHHCAQPLMRRLGVPGTVRASFHLYNTEEEIDRLVEALKK 392
|
|
| sufS |
TIGR01979 |
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine ... |
8-401 |
7.48e-174 |
|
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: 491.02 E-value: 7.48e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 8 RADFPAIAALQRQHQ-TYLDSAATTQKPQVLLDALSHYYGHGAANVHRAQHLPGALATQAFEASRDKVAAWLNAADSRQI 86
Cdd:TIGR01979 4 RADFPILKRKINGKPlVYLDSAATSQKPQQVIDAVAEYYRNSNANVHRGIHTLSVRATEAYEAVREKVAKFINAASDEEI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 87 VFTHGATSALNLLAYGL-EYRFEAGDEIAISALEHHANLLPWQQLARRRGVRLVVLPLDEHGRIDLDQALQLIGPRTRLL 165
Cdd:TIGR01979 84 VFTRGTTESINLVAYSWgDSNLKAGDEIVISEMEHHANIVPWQLLAERTGATLKFIPLDDDGTLDLDDLEKLLTEKTKLV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 166 AVSQLSNVLGTWQPLPALLSHARAQGALTVVDGAQGVVHGRHDVQQLGCDFYVFSSHKLYGPEGVGVLYGRPQALEQLRH 245
Cdd:TIGR01979 164 AITHVSNVLGTVNPVEEIAKLAHQVGAKVLVDGAQAVPHMPVDVQALDCDFYVFSGHKMYGPTGIGVLYGKEELLEQMPP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 246 WQFGGEMVQLADYQSASFRPAPLGFEAGTPPIAGVIGLGAILDYLASLDATAVAHHETSLHHSLLRGLGDREGIRILGT- 324
Cdd:TIGR01979 244 FLGGGEMIAEVSFEETTYNEAPHKFEAGTPNIAGVIGLGAAIDYLEAIGLENIEAHEHELTAYALERLGEIPGLRIYGPr 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 325 ---PQAALVSFVVEGVHNADIAHLLTEQGIAVRAGHHCAMPLLKGLGLEGAIRVSLALYNDSDDLQRFFDALDQGLELLR 401
Cdd:TIGR01979 324 daeDRGGIISFNVEGVHPHDVGTILDEEGIAVRSGHHCAQPLMRRFGVPATCRASFYIYNTEEDIDALVEALKKVRKFFG 403
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
23-393 |
1.53e-171 |
|
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: 483.89 E-value: 1.53e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 23 TYLDSAATTQKPQVLLDALSHYYGHGAANVHRAQHLPGALATQAFEASRDKVAAWLNAADSRQIVFTHGATSALNLLAYG 102
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINAPSPDEIIFTRNTTEAINLVAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 103 LEYRFEAGDEIAISALEHHANLLPWQQLARRRGVRLVVLPLDEHGRIDLDQALQLIGPRTRLLAVSQLSNVLGTWQPLPA 182
Cdd:cd06453 81 LGRANKPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPVKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 183 LLSHARAQGALTVVDGAQGVVHGRHDVQQLGCDFYVFSSHKLYGPEGVGVLYGRPQALEQLRHWQFGGEMVQLADYQSAS 262
Cdd:cd06453 161 IGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMIEEVSFEETT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 263 FRPAPLGFEAGTPPIAGVIGLGAILDYLASLDATAVAHHETSLHHSLLRGLGDREGIRILGTPQ--AALVSFVVEGVHNA 340
Cdd:cd06453 241 YADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEIPGVRVYGDAEdrAGVVSFNLEGIHPH 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1321283129 341 DIAHLLTEQGIAVRAGHHCAMPLLKGLGLEGAIRVSLALYNDSDDLQRFFDAL 393
Cdd:cd06453 321 DVATILDQYGIAVRAGHHCAQPLMRRLGVPGTVRASFGLYNTEEEIDALVEAL 373
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
2-400 |
1.97e-142 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 410.97 E-value: 1.97e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 2 FQPSPWRADFPAIaalqRQHQTYLDSAATTQKPQVLLDALSHYYGHGAANVHRAQHLPGALATQAFEASRDKVAAWLNAA 81
Cdd:PRK10874 4 FNPAQFRAQFPAL----QDAGVYLDSAATALKPQAVIEATQQFYSLSAGNVHRSQFAAAQRLTARYEAAREQVAQLLNAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 82 DSRQIVFTHGATSALNLLAYG-LEYRFEAGDEIAISALEHHANLLPWQQLARRRGVRLVVLPLDEHGRIDLDQALQLIGP 160
Cdd:PRK10874 80 DAKNIVWTRGTTESINLVAQSyARPRLQPGDEIIVSEAEHHANLVPWLMVAQQTGAKVVKLPLGADRLPDVDLLPELITP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 161 RTRLLAVSQLSNVLGTWQPLPALLSHARAQGALTVVDGAQGVVHGRHDVQQLGCDFYVFSSHKLYGPEGVGVLYGRPQAL 240
Cdd:PRK10874 160 RTRILALGQMSNVTGGCPDLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKSELL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 241 EQLRHWQFGGEMVQLADYQSASFRPAPLGFEAGTPPIAGVIGLGAILDYLASLDATAVAHHETSLHHSLLRGLGDREGIR 320
Cdd:PRK10874 240 EAMSPWQGGGKMLTEVSFDGFTPQSAPWRFEAGTPNVAGVIGLSAALEWLADIDINQAESWSRSLATLAEDALAKLPGFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 321 ILGTPQAALVSFVVEGVHNADIAHLLTEQGIAVRAGHHCAMPLLKGLGLEGAIRVSLALYNDSDDLQRFFDALDQGLELL 400
Cdd:PRK10874 320 SFRCQDSSLLAFDFAGVHHSDLVTLLAEYGIALRAGQHCAQPLLAALGVTGTLRASFAPYNTQSDVDALVNAVDRALELL 399
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
8-393 |
1.41e-132 |
|
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: 393.84 E-value: 1.41e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 8 RADFPAIAALQRQHQ-TYLDSAATTQKPQVLLDALSHYYGHGAANVHRAQHLPGALATQAFEASRDKVAAWLNAADSRQI 86
Cdd:NF041166 231 RRDFPILQERVNGKPlVWFDNAATTQKPQAVIDRLSYFYEHENSNIHRAAHELAARATDAYEGAREKVRRFIGAPSVDEI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 87 VFTHGATSALNLLA--YGlEYRFEAGDEIAISALEHHANLLPWQQLARRRGVRLVVLPLDEHGRIDLDQALQLIGPRTRL 164
Cdd:NF041166 311 IFVRGTTEAINLVAksWG-RQNIGAGDEIIVSHLEHHANIVPWQQLAQETGAKLRVIPVDDSGQILLDEYAKLLNPRTKL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 165 LAVSQLSNVLGTWQPLPALLSHARAQGALTVVDGAQGVVHGRHDVQQLGCDFYVFSSHKLYGPEGVGVLYGRPQALEQLR 244
Cdd:NF041166 390 VSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGIGVVYGKRDLLEAMP 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 245 HWQFGGEMVQLADYQSASFRPAPLGFEAGTPPIAGVIGLGAILDYLASLDATAVAHHEtslhHSLL----RGLGDREGIR 320
Cdd:NF041166 470 PWQGGGNMIADVTFEKTVYQPAPNRFEAGTGNIADAVGLGAALDYVERIGIENIARYE----HDLLeyatAGLAEVPGLR 545
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1321283129 321 ILGTPQ--AALVSFVVEGVHNADIAHLLTEQGIAVRAGHHCAMPLLKGLGLEGAIRVSLALYNDSDDLQRFFDAL 393
Cdd:NF041166 546 LIGTAAdkASVLSFVLDGYSTEEVGKALNQEGIAVRSGHHCAQPILRRFGVEATVRPSLAFYNTCEEVDALVAVL 620
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
8-393 |
2.84e-126 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 371.00 E-value: 2.84e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 8 RADFPAIaalqrqHQT-------YLDSAATTQKPQVLLDALSHYYGHGAANVHRAQHLPGALATQAFEASRDKVAAWLNA 80
Cdd:PLN02855 18 RPDFPIL------DQTvngsklvYLDNAATSQKPAAVLDALQDYYEEYNSNVHRGIHALSAKATDAYELARKKVAAFINA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 81 ADSRQIVFTHGATSALNLLAY--GLEYrFEAGDEIAISALEHHANLLPWQQLARRRGVRLVVLPLDEHGRIDLDQALQLI 158
Cdd:PLN02855 92 STSREIVFTRNATEAINLVAYtwGLAN-LKPGDEVILSVAEHHSNIVPWQLVAQKTGAVLKFVGLTPDEVLDVEQLKELL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 159 GPRTRLLAVSQLSNVLGTWQPLPALLSHARAQGALTVVDGAQGVVHGRHDVQQLGCDFYVFSSHKLYGPEGVGVLYGRPQ 238
Cdd:PLN02855 171 SEKTKLVATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLWGKSD 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 239 ALEQLRHWQFGGEMVQLADYQSASFRPAPLGFEAGTPPIAGVIGLGAILDYLASLDATAVAHHETSLHHSLLRGLGDREG 318
Cdd:PLN02855 251 LLESMPPFLGGGEMISDVFLDHSTYAPPPSRFEAGTPAIGEAIGLGAAIDYLSEIGMDRIHEYEVELGTYLYEKLSSVPG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 319 IRILGTP------QAALVSFVVEGVHNADIAHLLTEQ-GIAVRAGHHCAMPLLKGLGLEGAIRVSLALYNDSDDLQRFFD 391
Cdd:PLN02855 331 VRIYGPKpsegvgRAALCAFNVEGIHPTDLSTFLDQQhGVAIRSGHHCAQPLHRYLGVNASARASLYFYNTKEEVDAFIH 410
|
..
gi 1321283129 392 AL 393
Cdd:PLN02855 411 AL 412
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
8-400 |
1.55e-120 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 355.60 E-value: 1.55e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 8 RADFPAIA-ALQRQHQTYLDSAATTQKPQVLLDALSHYYGHGAANVHRAQHLPGALATQAFEASRDKVAAWLNAADSRQI 86
Cdd:PRK09295 9 RADFPVLSrEVNGLPLAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKQAALFINARSAEEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 87 VFTHGATSALNLLAYGLEYRF-EAGDEIAISALEHHANLLPWQQLARRRGVRLVVLPLDEHGRIDLDQALQLIGPRTRLL 165
Cdd:PRK09295 89 VFVRGTTEGINLVANSWGNSNvRAGDNIIISEMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPALFDERTRLL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 166 AVSQLSNVLGTWQPLPALLSHARAQGALTVVDGAQGVVHGRHDVQQLGCDFYVFSSHKLYGPEGVGVLYGRPQALEQLRH 245
Cdd:PRK09295 169 AITHVSNVLGTENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKEALLQEMPP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 246 WQFGGEMV-QLADYQSASFRPAPLGFEAGTPPIAGVIGLGAILDYLASLDATAVAHHETSLHHSLLRGLGDREGIRILGT 324
Cdd:PRK09295 249 WEGGGSMIaTVSLTEGTTWAKAPWRFEAGTPNTGGIIGLGAALDYVSALGLNNIAEYEQNLMHYALSQLESVPDLTLYGP 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1321283129 325 PQAALVSFVVEGVHNA-DIAHLLTEQGIAVRAGHHCAMPLLKGLGLEGAIRVSLALYNDSDDLQRFFDALDQGLELL 400
Cdd:PRK09295 329 QNRLGVIAFNLGKHHAyDVGSFLDNYGIAVRTGHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVAGLQRIHRLL 405
|
|
| am_tr_V_VC1184 |
TIGR01976 |
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of ... |
2-393 |
1.24e-74 |
|
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: 237.73 E-value: 1.24e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 2 FQPSPWRADFPAiaaLQRQHQTYLDSAATTQKPQVLLDALSHYYGhgAANVHRAQHLPGALATQAF-EASRDKVAAWLNA 80
Cdd:TIGR01976 1 FDVEAVRGQFPA---LADGDRVFFDNPAGTQIPQSVADAVSAALT--RSNANRGGAYESSRRADQVvDDAREAVADLLNA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 81 aDSRQIVFTHGATSALNLLAYGLEYRFEAGDEIAISALEHHANLLPWQQLARRRGVRLVVLPLDEH-GRIDLDQALQLIG 159
Cdd:TIGR01976 76 -DPPEVVFGANATSLTFLLSRAISRRWGPGDEVIVTRLDHEANISPWLQAAERAGAKVKWARVDEAtGELHPDDLASLLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 160 PRTRLLAVSQLSNVLGTWQPLPALLSHARAQGALTVVDGAQGVVHGRHDVQQLGCDFYVFSSHKLYGPEgVGVLYGRPQA 239
Cdd:TIGR01976 155 PRTRLVAVTAASNTLGSIVDLAAITELVHAAGALVVVDAVHYAPHGLIDVQATGADFLTCSAYKFFGPH-MGILWGRPEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 240 LEQLRhwqfggemvqlADYQSASFRPAPLGFEAGTPPIAGVIGLGAILDYLASLDAT--------------AVAHHETSL 305
Cdd:TIGR01976 234 LMNLP-----------PYKLTFSYDTGPERFELGTPQYELLAGVVAAVDYLAGLGESangsrrerlvasfqAIDAYENRL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 306 HHSLLRGLGDREGIRILGTPQAA----LVSFVVEGVHNADIAHLLTEQGIAVRAGHHCAMPLLKGLGLE---GAIRVSLA 378
Cdd:TIGR01976 303 AEYLLVGLSDLPGVTLYGVARLAarvpTVSFTVHGLPPQRVVRRLADQGIDAWAGHFYAVRLLRRLGLNdegGVVRVGLA 382
|
410
....*....|....*
gi 1321283129 379 LYNDSDDLQRFFDAL 393
Cdd:TIGR01976 383 HYNTAEEVDRLLEAL 397
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
24-401 |
1.65e-64 |
|
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: 210.68 E-value: 1.65e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 24 YLDSAATTQ-KPQVL---LDALSHYYGHgAANVHRAqhlpGALATQAFEASRDKVAAWLNAaDSRQIVFTHGATSALNLL 99
Cdd:COG1104 5 YLDNAATTPvDPEVLeamLPYLTEYFGN-PSSLHSF----GREARAALEEAREQVAALLGA-DPEEIIFTSGGTEANNLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 100 AYG-LEYRFEAGDEIAISALEHHANLLPWQQLARRrGVRLVVLPLDEHGRIDLDQALQLIGPRTRLLAVSQLSNVLGTWQ 178
Cdd:COG1104 79 IKGaARAYRKKGKHIITSAIEHPAVLETARFLEKE-GFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 179 PLPALLSHARAQGALTVVDGAQGVVHGRHDVQQLGCDFYVFSSHKLYGPEGVGVLYGRPQAleQLRHWQFGGEmvqlady 258
Cdd:COG1104 158 PIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRKGV--RLEPLIHGGG------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 259 QSASFRpaplgfeAGTPPIAGVIGLGAILDyLASLDATAVAHHETSLHHSLLRGLGDR-EGIRILGTPQAAL---VSFVV 334
Cdd:COG1104 229 QERGLR-------SGTENVPGIVGLGKAAE-LAAEELEEEAARLRALRDRLEEGLLAAiPGVVINGDPENRLpntLNFSF 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1321283129 335 EGVHNADIAHLLTEQGIAVRAGHHCA------MPLLKGLGLE-----GAIRVSLALYNDSDDLQRFFDALDQGLELLR 401
Cdd:COG1104 301 PGVEGEALLLALDLAGIAVSSGSACSsgslepSHVLLAMGLDeelahGSIRFSLGRFTTEEEIDRAIEALKEIVARLR 378
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
24-377 |
1.12e-32 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 125.92 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 24 YLDSAATTQ-KPQVLlDALSHYYGHGAANVHRAQHLPGALATQAFEASRDKVAAwLNAADSRQIVFTHGATSALNLLAYG 102
Cdd:PLN02651 2 YLDMQATTPiDPRVL-DAMLPFLIEHFGNPHSRTHLYGWESEDAVEKARAQVAA-LIGADPKEIIFTSGATESNNLAIKG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 103 LEYRFEAGDEIAIS-ALEHHANLLPWQQLARRrGVRLVVLPLDEHGRIDLDQALQLIGPRTRLLAVSQLSNVLGTWQPLP 181
Cdd:PLN02651 80 VMHFYKDKKKHVITtQTEHKCVLDSCRHLQQE-GFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 182 ALLSHARAQGALTVVDGAQGVVHGRHDVQQLGCDFYVFSSHKLYGPEGVGVLYGRPQALEQLRHWQFGGEmvqladyQSA 261
Cdd:PLN02651 159 EIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRLEPLMSGGG-------QER 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 262 SFRpaplgfeAGTPPIAGVIGLGAILDyLASLDATAVAHHETSLHHSLLRGLGDR-EGIRILGTPQAA-----LVSFVVE 335
Cdd:PLN02651 232 GRR-------SGTENTPLVVGLGAACE-LAMKEMDYDEKHMKALRERLLNGLRAKlGGVRVNGPRDPEkrypgTLNLSFA 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1321283129 336 GVHNAdiAHLLTEQGIAVRAGHHCAMP------LLKGLGLE-----GAIRVSL 377
Cdd:PLN02651 304 YVEGE--SLLMGLKEVAVSSGSACTSAslepsyVLRALGVPeemahGSLRLGV 354
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
24-316 |
5.69e-30 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 119.28 E-value: 5.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 24 YLDSAATTQ-KPQVLLDALSHYYGHGA-ANVHRAQHLPGALATQAFEASRDKVAAWLNAaDSRQIVFTHGATSALNLLAY 101
Cdd:PRK14012 6 YLDYSATTPvDPRVAEKMMPYLTMDGTfGNPASRSHRFGWQAEEAVDIARNQIADLIGA-DPREIVFTSGATESDNLAIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 102 GLEYRFEA-GDEIAISALEHHANLLPWQQLaRRRGVRLVVLPLDEHGRIDLDQALQLIGPRTRLLAVSQLSNVLGTWQPL 180
Cdd:PRK14012 85 GAAHFYQKkGKHIITSKTEHKAVLDTCRQL-EREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVIQDI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 181 PALLSHARAQGALTVVDGAQGVVHGRHDVQQLGCDFYVFSSHKLYGPEGVGVLYGR--PQA-LEQLRHwqfGG--EMvql 255
Cdd:PRK14012 164 AAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRrkPRVrLEAQMH---GGghER--- 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1321283129 256 adyqsasfrpaplGFEAGTPPIAGVIGLGaildylaslDATAVAHHETSLHHSLLRGLGDR 316
Cdd:PRK14012 238 -------------GMRSGTLPTHQIVGMG---------EAARIAKEEMATENERIRALRDR 276
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
24-395 |
3.71e-23 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 99.80 E-value: 3.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 24 YLDSAATTQKPQVLLDALSH----YYGHgAANVHRAqhlpGALATQAFEASRDKVAAWLNAADSrQIVFTHGATSAlNLL 99
Cdd:PRK02948 3 YLDYAATTPMSKEALQTYQKaasqYFGN-ESSLHDI----GGTASSLLQVCRKTFAEMIGGEEQ-GIYFTSGGTES-NYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 100 A-----YGLEYRfeaGDEIAISALEHHANLLPWQQLARRrGVRLVVLPLDEHGRIDLDQALQLIGPRTRLLAVSQLSNVL 174
Cdd:PRK02948 76 AiqsllNALPQN---KKHIITTPMEHASIHSYFQSLESQ-GYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 175 GTWQPLPALLSHARAQGALTVVDGAQGVVHGRHDVQQLGCDFYVFSSHKLYGPEGVGVLYGRPQaleqlRHWQfggEMVQ 254
Cdd:PRK02948 152 GTIQPIAEIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYINPQ-----VRWK---PVFP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 255 LADYQSasfrpaplGFEAGTPPIAGVIGLGAILDYLASLDATAVAHHETsLHHSLLRGLGDRE-GIRILGTPQAALVSFV 333
Cdd:PRK02948 224 GTTHEK--------GFRPGTVNVPGIAAFLTAAENILKNMQEESLRFKE-LRSYFLEQIQTLPlPIEVEGHSTSCLPHII 294
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1321283129 334 VEGVHNADIAHLLTE---QGIAVRAGHHCAMPL------LKGLGL--EGA---IRVSLALYNDSDDLQRFFDALDQ 395
Cdd:PRK02948 295 GVTIKGIEGQYTMLEcnrRGIAISTGSACQVGKqepsktMLAIGKtyEEAkqfVRFSFGQQTTKDQIDTTIHALET 370
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
67-236 |
2.57e-14 |
|
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: 70.49 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 67 FEASRDKVAAWLNAADSRqIVFTHGATSALNLLAYGLeyrFEAGDEIAISALEHHANLlpwQQLARRRGVRLVVLPLDE- 145
Cdd:cd01494 2 LEELEEKLARLLQPGNDK-AVFVPSGTGANEAALLAL---LGPGDEVIVDANGHGSRY---WVAAELAGAKPVPVPVDDa 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 146 -HGRIDLDQALQLIGPRTRLLAVSQLSNVLGTWQPLPALL-SHARAQGALTVVDGAQGVVH---GRHDVQQLGCDFYVFS 220
Cdd:cd01494 75 gYGGLDVAILEELKAKPNVALIVITPNTTSGGVLVPLKEIrKIAKEYGILLLVDAASAGGAspaPGVLIPEGGADVVTFS 154
|
170
....*....|....*.
gi 1321283129 221 SHKLYGPEGVGVLYGR 236
Cdd:cd01494 155 LHKNLGGEGGGVVIVK 170
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
71-395 |
2.73e-11 |
|
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: 64.28 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 71 RDKVAAWLN-----AADSRQIVFTHGATSALNLLAYGLeyrFEAGDEIAISALEHHanllPWQQLARRRGVRLVVLPLDE 145
Cdd:cd00609 42 REAIAEWLGrrggvDVPPEEIVVTNGAQEALSLLLRAL---LNPGDEVLVPDPTYP----GYEAAARLAGAEVVPVPLDE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 146 HGRIDLDQAL--QLIGPRTRLLAVSQLSNVLGTWQPLP---ALLSHARAQGALTVVDGA-QGVVHGRHDVQQLGCD---- 215
Cdd:cd00609 115 EGGFLLDLELleAAKTPKTKLLYLNNPNNPTGAVLSEEeleELAELAKKHGILIISDEAyAELVYDGEPPPALALLdaye 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 216 --FYVFS-ShKLYGPEG--VGVLYGRPQALEQlrhwqfggemvQLADYQSASFrpaplgfeaGTPPIAGVIGLGAILDYL 290
Cdd:cd00609 195 rvIVLRSfS-KTFGLPGlrIGYLIAPPEELLE-----------RLKKLLPYTT---------SGPSTLSQAAAAAALDDG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 291 ASlDATAVAHHETSLHHSLLRGLGDREGIRILgTPQAALVSFVV--EGVHNADIAHLLTEQGIAVRAGHHCampllkGLG 368
Cdd:cd00609 254 EE-HLEELRERYRRRRDALLEALKELGPLVVV-KPSGGFFLWLDlpEGDDEEFLERLLLEAGVVVRPGSAF------GEG 325
|
330 340
....*....|....*....|....*..
gi 1321283129 369 LEGAIRVSLAlyNDSDDLQRFFDALDQ 395
Cdd:cd00609 326 GEGFVRLSFA--TPEEELEEALERLAE 350
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
71-393 |
1.28e-10 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 62.32 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 71 RDKVAAWLNAAD------SRQIVFTHGATSALNLLAYGLeyrFEAGDEIAISALeHHANLlpwQQLARRRGVRLVVLPLD 144
Cdd:pfam00155 45 REALAKFLGRSPvlkldrEAAVVFGSGAGANIEALIFLL---ANPGDAILVPAP-TYASY---IRIARLAGGEVVRYPLY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 145 --EHGRIDLDQALQLIGPRTRLLAVSQLSNVLGTWQPLP---ALLSHARAQGALTVVDGA-QGVVHGRHDVQQLGCD--- 215
Cdd:pfam00155 118 dsNDFHLDFDALEAALKEKPKVVLHTSPHNPTGTVATLEeleKLLDLAKEHNILLLVDEAyAGFVFGSPDAVATRALlae 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 216 ------FYVFS-SHKLYGpEGVGVLYGRPQALEQLRHWQfggemvqladyqsasfrpAPLGFEAGTPPIAGVIgLGAILD 288
Cdd:pfam00155 198 gpnllvVGSFSkAFGLAG-WRVGYILGNAAVISQLRKLA------------------RPFYSSTHLQAAAAAA-LSDPLL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 289 YLASLDATAVAHHEtslHHSLLRGLGDREGIRILGtPQAALVSFVvegVHNADIAH-----LLTEQGIAVRAGhhcampl 363
Cdd:pfam00155 258 VASELEEMRQRIKE---RRDYLRDGLQAAGLSVLP-SQAGFFLLT---GLDPETAKelaqvLLEEVGVYVTPG------- 323
|
330 340 350
....*....|....*....|....*....|
gi 1321283129 364 lKGLGLEGAIRVSLALYNDsDDLQRFFDAL 393
Cdd:pfam00155 324 -SSPGVPGWLRITVAGGTE-EELEELLEAI 351
|
|
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
24-313 |
7.75e-08 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 54.49 E-value: 7.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 24 YLDSAATT-----QKPQVLLDALSHYYGhgaaNVHrAQHLPGALATQAFEASRDKVAAWLNAADSRQI-VFTHGATSALN 97
Cdd:PLN02724 37 YLDHAGATlysesQLEAALADFSSNVYG----NPH-SQSDSSMRSSDTIESARQQVLEYFNAPPSDYAcVFTSGATAALK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 98 LLayGLEYRFEAGDEIAISaLEHHANLLPWQQLARRRGVRLVVLPLDEHGRIDLDQALQL-IGPRT---RLLAVSQLSNV 173
Cdd:PLN02724 112 LV--GETFPWSSESHFCYT-LENHNSVLGIREYALEKGAAAIAVDIEEAANQPTNSQGSVvVKSRGlqrRNTSKLQKRED 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 174 LGTWQPLPALLSHARAQGA------------------------LTVVDGAQGVVHGRHDVQQLGCDFYVFSSHKLYG-PE 228
Cdd:PLN02724 189 DGEAYNLFAFPSECNFSGAkfpldlvklikdnqhsnfsksgrwMVLLDAAKGCGTSPPDLSRYPADFVVVSFYKIFGyPT 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 229 GVGVLYGRPQALEQLRHWQFGGEMVQL----ADYQSASFRPAPLgFEAGTPPIAGVIGLGAILDYLASLDATAVAHHETS 304
Cdd:PLN02724 269 GLGALLVRRDAAKLLKKKYFGGGTVAAsiadIDFVKRRERVEQR-FEDGTISFLSIAALRHGFKLLNRLTISAIAMHTWA 347
|
330
....*....|..
gi 1321283129 305 LHH---SLLRGL 313
Cdd:PLN02724 348 LTHyvaNSLRNL 359
|
|
| ARO8 |
COG1167 |
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ... |
71-197 |
1.18e-06 |
|
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain [Transcription, Amino acid transport and metabolism]; DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 440781 [Multi-domain] Cd Length: 471 Bit Score: 50.21 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 71 RDKVAAWLN----AADSRQIVFTHGATSALNLLAYGLeyrFEAGDEIAISALEHHANLlpwqQLARRRGVRLVVLPLDEH 146
Cdd:COG1167 154 REAIARYLArrgvPASPDQILITSGAQQALDLALRAL---LRPGDTVAVESPTYPGAL----AALRAAGLRLVPVPVDED 226
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1321283129 147 GrIDLDqALQLIGPRTR---LLAVSQLSNVLGTwqPLP-----ALLSHARAQGALTVVD 197
Cdd:COG1167 227 G-LDLD-ALEAALRRHRpraVYVTPSHQNPTGA--TMSlerrrALLELARRHGVPIIED 281
|
|
| PLN02409 |
PLN02409 |
serine--glyoxylate aminotransaminase |
43-313 |
2.02e-05 |
|
serine--glyoxylate aminotransaminase
Pssm-ID: 178031 [Multi-domain] Cd Length: 401 Bit Score: 46.29 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 43 HYYGHGAANVH----RAQHLPGA-LATQAFEASRDKVAAwlnaaDSRQIVFTHGAT-------------SAL-NLLaygl 103
Cdd:PLN02409 11 HLFVPGPVNIPervlRAMNRPNEdHRSPAFPALTKELLE-----DVKYIFKTKSGTpfifpttgtgaweSALtNTL---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 104 eyrfEAGDEIaISALEHHANLLpWQQLARRRGVRLVVLPLDEHGRIDLD---QAL-QLIGPRTRLLAVSQLSNVLGTWQP 179
Cdd:PLN02409 82 ----SPGDKV-VSFRIGQFSLL-WIDQMQRLNFDVDVVESPWGQGADLDilkSKLrQDTNHKIKAVCVVHNETSTGVTND 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 180 LPAL--LSHARAQGALTVVDGAQ--GVVHGRHDvqQLGCDFYVFSSHK-LYGPEGVGVLYGRPQALEQLRHWQFGGEMVQ 254
Cdd:PLN02409 156 LAGVrkLLDCAQHPALLLVDGVSsiGALDFRMD--EWGVDVALTGSQKaLSLPTGLGIVCASPKALEASKTAKSPRVFFD 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1321283129 255 LADYqsasFRPAPLG-FEAGTPPIAGVIGLGAILDYLAS--LDATAVAHHEtsLHHSLLRGL 313
Cdd:PLN02409 234 WADY----LKFYKLGtYWPYTPSIQLLYGLRAALDLIFEegLENVIARHAR--LGEATRLAV 289
|
|
| PRK07324 |
PRK07324 |
transaminase; Validated |
55-197 |
5.16e-05 |
|
transaminase; Validated
Pssm-ID: 235989 Cd Length: 373 Bit Score: 44.93 E-value: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 55 AQHLPGALATQAFEAS---RDKVAAWLNAADSRQIVFTHGATSALNLLAYGLeyrFEAGDEIaISalehhanLLP-WQQL 130
Cdd:PRK07324 49 QELGQKKLTYGWIEGSpefKEAVASLYQNVKPENILQTNGATGANFLVLYAL---VEPGDHV-IS-------VYPtYQQL 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1321283129 131 ---ARRRGVRLVVLPLDEHGRI--DLDQALQLIGPRTRLLAVSQLSNVLGTWQPlPALLSH----ARAQGALTVVD 197
Cdd:PRK07324 118 ydiPESLGAEVDYWQLKEENGWlpDLDELRRLVRPNTKLICINNANNPTGALMD-RAYLEEiveiARSVDAYVLSD 192
|
|
| tyr_amTase_E |
TIGR01264 |
tyrosine aminotransferase, eukaryotic; This model describes tyrosine aminotransferase as found ... |
60-176 |
1.56e-04 |
|
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: 43.62 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 60 GALATQAFEASRDKVAAWLNAAD----SRQIVFTHGATSALNllaYGLEYRFEAGDEIaisaLEHHANLLPWQQLARRRG 135
Cdd:TIGR01264 68 GYAPTVGALSAREAIASYYHNPDgpieADDVVLCSGCSHAIE---MCIAALANAGQNI----LVPRPGFPLYETLAESMG 140
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1321283129 136 --VRLVVLPLDEHGRIDLDQALQLIGPRTRLLAVSQLSNVLGT 176
Cdd:TIGR01264 141 ieVKLYNLLPDKSWEIDLKQLESLIDEKTAALIVNNPSNPCGS 183
|
|
| SepCysS |
cd06452 |
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ... |
72-230 |
5.40e-04 |
|
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: 41.61 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 72 DKVAAWLNAADSRqivFTHGATSALNLLAYGLeyrFEAGDEIAISALEHHANLLPwqqlARRRGVRLVVLPLDEH--GRI 149
Cdd:cd06452 51 HDLAEFLGMDEAR---VTPGAREGKFAVMHSL---CEKGDWVVVDGLAHYTSYVA----AERAGLNVREVPNTGHpeYHI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 150 DLDQALQLIGPRTR----LLAVSQLSNVLGTWQPLP---ALLSHARAQGALTVVDGAQGVvhGRHDV--QQLGCDFYVFS 220
Cdd:cd06452 121 TPEGYAEVIEEVKDefgkPPALALLTHVDGNYGNLHdakKIAKVCHEYGVPLLLNGAYTV--GRMPVsgKELGADFIVGS 198
|
170
....*....|...
gi 1321283129 221 SHKLY---GPEGV 230
Cdd:cd06452 199 GHKSMaasAPIGV 211
|
|
| PRK06108 |
PRK06108 |
pyridoxal phosphate-dependent aminotransferase; |
80-197 |
7.24e-04 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180404 Cd Length: 382 Bit Score: 41.47 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 80 AADSRQIVFTHGATSALNLlayGLEYRFEAGDE-IAISALehhanllpWQQLA---RRRGVRLVVLPLD--EHG-RIDLD 152
Cdd:PRK06108 81 ATPPERIAVTSSGVQALML---AAQALVGPGDEvVAVTPL--------WPNLVaapKILGARVVCVPLDfgGGGwTLDLD 149
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1321283129 153 QALQLIGPRTRLLAVSQLSNVLG---TWQPLPALLSHARAQGALTVVD 197
Cdd:PRK06108 150 RLLAAITPRTRALFINSPNNPTGwtaSRDDLRAILAHCRRHGLWIVAD 197
|
|
| PRK06836 |
PRK06836 |
pyridoxal phosphate-dependent aminotransferase; |
34-163 |
1.47e-03 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180720 Cd Length: 394 Bit Score: 40.56 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 34 PQVLLDALSHYYGHGAANVHraqhlpGALATQAFEASRDKVAAWLN-----AADSRQIVFTHGATSALNLLaygLEYRFE 108
Cdd:PRK06836 48 PAAVKEALRELAEEEDPGLH------GYMPNAGYPEVREAIAESLNrrfgtPLTADHIVMTCGAAGALNVA---LKAILN 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1321283129 109 AGDEIAISA---------LEHHanllpwqqlarrrGVRLVVLPLDEHG-RIDLDQALQLIGPRTR 163
Cdd:PRK06836 119 PGDEVIVFApyfveyrfyVDNH-------------GGKLVVVPTDTDTfQPDLDALEAAITPKTK 170
|
|
| PRK00451 |
PRK00451 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPA; |
134-196 |
4.02e-03 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
Pssm-ID: 234769 [Multi-domain] Cd Length: 447 Bit Score: 39.35 E-value: 4.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1321283129 134 RGVRLVVLPLDEhGRIDLDQALQLIGPRTRLLAVsQLSNVLGTWQPLPALLSHARAQGALTVV 196
Cdd:PRK00451 178 QGIEVVEVPYED-GVTDLEALEAAVDDDTAAVVV-QYPNFFGVIEDLEEIAEIAHAGGALFIV 238
|
|
| tyr_nico_aTase |
TIGR01265 |
tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal ... |
60-197 |
6.29e-03 |
|
tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal phosphate-dependent enzymes includes known examples of both tyrosine aminotransferase from animals and nicotianamine aminotransferase from barley.
Pssm-ID: 188123 Cd Length: 403 Bit Score: 38.48 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 60 GALATQAFEASRDKVAAWLNAA-----DSRQIVFTHGATSALnllaygleyrfeagdEIAISALehhAN-----LLP--- 126
Cdd:TIGR01265 68 GYAPSVGALAAREAVAEYLSSDlpgklTADDVVLTSGCSQAI---------------EICIEAL---ANpganiLVPrpg 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1321283129 127 ---WQQLARRRG--VRLVVLPLDEHGRIDLDQALQLIGPRTRLLAVSQLSNVLG---TWQPLPALLSHARAQGALTVVD 197
Cdd:TIGR01265 130 fplYDTRAAFSGleVRLYDLLPEKDWEIDLDGLESLADEKTVAIVVINPSNPCGsvfSRDHLQKIAEVAEKLGIPIIAD 208
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
34-401 |
7.20e-03 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 38.70 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 34 PQVLLDALSHYYGHGAA-------NVHRAQHLPgaLATQAFEasRDKVAAWLNAADSRQIVFTHGATSALNLLAYGLEYR 106
Cdd:COG3321 830 LAQLLTALAQLWVAGVPvdwsalyPGRGRRRVP--LPTYPFQ--REDAAAALLAAALAAALAAAAALGALLLAALAAALA 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 107 FEAGDEIAISALEHHANLLPWQQLARRRGVRLVVLPLDEHGRIDLDQALQLIGPRTRLLAVSQLSNVLGTWQPLPALLSH 186
Cdd:COG3321 906 AALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAA 985
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 187 ARAQGALTVVDGAQGVVHGRHDVQQLGCDFYVFSSHKLYGPEGVGVLYGRPQALEQLRHWQFGGEMVQLADYQSASFRPA 266
Cdd:COG3321 986 AAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALAL 1065
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 267 PLGFEAGTPPIAGVIGLGAILDYLASLDATAVAHHETSLHHSLLRGLGDREGIRILGTPQAALVSFVVEGVHNADIAHLL 346
Cdd:COG3321 1066 AALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAA 1145
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1321283129 347 TEQGIAVRAGHHCAMPLLKGLGLEGAIRVSLALYNDSDDLQRFFDALDQGLELLR 401
Cdd:COG3321 1146 AAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAAL 1200
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
87-395 |
8.16e-03 |
|
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism]; Glutamate or tyrosine decarboxylase or a related PLP-dependent protein is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 439846 [Multi-domain] Cd Length: 460 Bit Score: 38.27 E-value: 8.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 87 VFTHGATSAlNLLAyGLEYRFEAGD--------------EIAISALEHHAnllpWQQLAR-----RRGVRLVvlPLDEHG 147
Cdd:COG0076 129 VFTSGGTEA-NLLA-LLAARDRALArrvraeglpgaprpRIVVSEEAHSS----VDKAARllglgRDALRKV--PVDEDG 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 148 RIDLDQALQLI------GPRTRLLAVSQLSNVLGTWQPLPALLSHARAQGALTVVDGAQG-----VVHGRHDVQQL-GCD 215
Cdd:COG0076 201 RMDPDALEAAIdedraaGLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGgfalpSPELRHLLDGIeRAD 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 216 FYVFSSHK-LYGPEGVG-VLYGRPQALEQLRH------WQFGGEMVQLADYQ---SASFRPAP-------LGFEagtppi 277
Cdd:COG0076 281 SITVDPHKwLYVPYGCGaVLVRDPELLREAFSfhasylGPADDGVPNLGDYTlelSRRFRALKlwatlraLGRE------ 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321283129 278 agviGLGAILDylASLDATAVAHhetslhhsllRGLGDREGIRILGTPQAALVSF-------VVEGVHNADIAHLLTEQG 350
Cdd:COG0076 355 ----GYRELIE--RCIDLARYLA----------EGIAALPGFELLAPPELNIVCFrykpaglDEEDALNYALRDRLRARG 418
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1321283129 351 IAVRAGHHcamplLKGlglEGAIRVSLALYN-DSDDLQRFFDALDQ 395
Cdd:COG0076 419 RAFLSPTK-----LDG---RVVLRLVVLNPRtTEDDVDALLDDLRE 456
|
|
| |
