|
Name |
Accession |
Description |
Interval |
E-value |
| Sec_lyase_SclA |
NF040779 |
selenocysteine lyase SclA; In bacteria, selenocysteine lyase activity (EC 4.4.1.16) usually is ... |
5-382 |
0e+00 |
|
selenocysteine lyase SclA; In bacteria, selenocysteine lyase activity (EC 4.4.1.16) usually is seen as a secondary activity of a cysteine desulfurase (EC 2.8.1.7). However, SclA, as studied in Enterococcus faecalis, acts primary on selenocysteine, binding cysteine just as well but acting on cysteine with much lower catalytic efficiency.
Pssm-ID: 468734 [Multi-domain] Cd Length: 378 Bit Score: 680.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 5 VYLNYAATSYKKFPATIEALTAYLAENQFMNYGRNAPLLREGLPLLETRQLLADFFQAPSAAQITFTNNATTSLNLALAG 84
Cdd:NF040779 1 VYLNHAATSNHKFEATIQALCAYLQENNNLNTNRGLQGLDELGLAFETRQALADFFHAPDPAHVIFTANATTSLNMVLNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 85 ILQPGDHVITTMLEHHAVARPLHLLEKERGISVTYVACQKTGLLDVEDIQRALRTNTKALVMTHASNVLGTILPIEECFQ 164
Cdd:NF040779 81 LLKPGDHVLTTSVEHNAVARPLHLLETEQNVSVTYLPCEKDGQLDPEQIEAAIRPETKVLVMTHASNVLGTILPVKECFK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 165 WAQQKGLLTVLDAAQTAGFLPIKMTQMAIDVLAFTGHKSLYGLAGIGGLAFSEQGAEAVKPLITGGTGSHSNSFDQPSFL 244
Cdd:NF040779 161 IAKKHGIITVLDSAQTAGFLPIDMEEMSIDVLAFTGHKSLMGLAGIGGFALAKNIEKKIDPWLTGGTGSASLSLEQPDFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 245 PDKFEAGTLNSLGILSLNSSVKELNKIGLAAIQKHERTLMQNFFNGLSGLPVTILGTKDVAQTVPVVSITLWNQEETVVA 324
Cdd:NF040779 241 PDKFEPGTPNTLGILSLKSSVKAIQELGLEKIQAHERALTARFLTGLKELPVTILGTKDAAQSVPVVSITAPGIDSGELA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 514883239 325 QQLAEQYGIMTRAGLHCAPLAHETAGTLATGTLRFSFGCQTTPEEITWTIHALQELLI 382
Cdd:NF040779 321 QQLFDRYGIITRSGLHCAPLAHQTAGTLKTGAVRFSFGWNTTAEEIDYTLSALKEILS 378
|
|
| am_tr_V_EF2568 |
TIGR01977 |
cysteine desulfurase family protein; This model describes a subfamily of probable pyridoxal ... |
5-380 |
0e+00 |
|
cysteine desulfurase family protein; This model describes a subfamily of probable pyridoxal phosphate-dependent enzymes in the aminotransferase class V family. Related families contain members active as cysteine desulfurases, selenocysteine lyases, or both. The members of this family form a distinct clade and all are shorter at the N-terminus. The function of this subfamily is unknown. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 131032 [Multi-domain] Cd Length: 376 Bit Score: 583.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 5 VYLNYAATSYKKFPATIEALTAYLAENQ-FMNYGRNAPLLREGLPLLETRQLLADFFQAPSAAQITFTNNATTSLNLALA 83
Cdd:TIGR01977 1 IYFDNAATTYPKPDEVYEAMADFYKNYGgSPGRGRYRLALRASREVEETRQLLAKLFNAPSSAHVVFTNNATTALNIALK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 84 GILQPGDHVITTMLEHHAVARPLHLLEKERGISVTYVACQKTGLLDVEDIQRALRTNTKALVMTHASNVLGTILPIEECF 163
Cdd:TIGR01977 81 GLLKEGDHVITTPMEHNSVARPLECLKEQIGVEITIVKCDNEGLISPERIKRAIKTNTKLIVVSHASNVTGTILPIEEIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 164 QWAQQKGLLTVLDAAQTAGFLPIKMTQMAIDVLAFTGHKSLYGLAGIGGLAFSEQGaeAVKPLITGGTGSHSNSFDQPSF 243
Cdd:TIGR01977 161 ELAQENGIFFILDAAQTAGVIPIDMTELAIDMLAFTGHKGLLGPQGTGGLYIREGI--KLKPLKSGGTGSHSALIDQPSE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 244 LPDKFEAGTLNSLGILSLNSSVKELNKIGLAAIQKHERTLMQNFFNGLS-GLPVTILGTKDVAQTVPVVSITLWNQEETV 322
Cdd:TIGR01977 239 LPDRFESGTLNTPGIAGLNAGIKFIEKIGIANIAKKECMLTEKLLNGLReINKVKIYGPADPANRVGVVSFTVEGIDSEE 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 514883239 323 VAQQLAEQYGIMTRAGLHCAPLAHETAGTLATGTLRFSFGCQTTPEEITWTIHALQEL 380
Cdd:TIGR01977 319 VADILDEKFDIATRTGLHCAPLAHKTIGTFATGTIRLSLGYFNTEEEIEKLLEALSEI 376
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
5-370 |
6.14e-111 |
|
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: 329.04 E-value: 6.14e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 5 VYLNYAATSYKKfPATIEALTAYlAENQFMNYGRNAPLL--REGLPLLETRQLLADFFQAPSAAQITFTNNATTSLNLAL 82
Cdd:cd06453 1 VYLDNAATSQKP-QPVIDAIVDY-YRHYNANVHRGVHELsaRATDAYEAAREKVARFINAPSPDEIIFTRNTTEAINLVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 83 AGIL---QPGDHVITTMLEHHAVARPLHLLEKERGISVTYVACQKTGLLDVEDIQRALRTNTKALVMTHASNVLGTILPI 159
Cdd:cd06453 79 YGLGranKPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 160 EECFQWAQQKGLLTVLDAAQTAGFLPIKMTQMAIDVLAFTGHKsLYGLAGIGGLAFSEQGAEAVKPLITGGTGSHSNSFD 239
Cdd:cd06453 159 KEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHK-MLGPTGIGVLYGKEELLEEMPPYGGGGEMIEEVSFE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 240 --QPSFLPDKFEAGTLNSLGILSLNSSVKELNKIGLAAIQKHERTLMQNFFNGLSGLP-VTILGTKDVAqtVPVVSITLW 316
Cdd:cd06453 238 etTYADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEIPgVRVYGDAEDR--AGVVSFNLE 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 514883239 317 NQEETVVAQQLaEQYGIMTRAGLHCAPLAHEtaGTLATGTLRFSFGCQTTPEEI 370
Cdd:cd06453 316 GIHPHDVATIL-DQYGIAVRAGHHCAQPLMR--RLGVPGTVRASFGLYNTEEEI 366
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
2-381 |
3.99e-107 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 320.16 E-value: 3.99e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 2 KDLVYLNYAATSyKKFPATIEALTAYL----AENQFMNY--GRNAPLLREglpllETRQLLADFFQAPSAAQITFTNNAT 75
Cdd:COG0520 14 KPLVYLDNAATG-QKPRPVIDAIRDYYepynANVHRGAHelSAEATDAYE-----AAREKVARFIGAASPDEIIFTRGTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 76 TSLNLALAGI--LQPGDHVITTMLEHHAVARPLHLLEKERGISVTYVACQKTGLLDVEDIQRALRTNTKALVMTHASNVL 153
Cdd:COG0520 88 EAINLVAYGLgrLKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDGELDLEALEALLTPRTKLVAVTHVSNVT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 154 GTILPIEECFQWAQQKGLLTVLDAAQTAGFLPIKMTQMAIDVLAFTGHKsLYGLAGIGGLAFSEQGAEAVKPLITGGTGS 233
Cdd:COG0520 168 GTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHK-LYGPTGIGVLYGKRELLEALPPFLGGGGMI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 234 HSNSFDQPSF--LPDKFEAGTLNSLGILSLNSSVKELNKIGLAAIQKHERTLMQNFFNGLSGLP-VTILGTKDVAQTVPV 310
Cdd:COG0520 247 EWVSFDGTTYadLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAIPgVRILGPADPEDRSGI 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514883239 311 VSITLWNQEETVVAQQLAEQyGIMTRAGLHCAPLAHETAGTlaTGTLRFSFGCQTTPEEITWTIHALQELL 381
Cdd:COG0520 327 VSFNVDGVHPHDVAALLDDE-GIAVRAGHHCAQPLMRRLGV--PGTVRASFHLYNTEEEIDRLVEALKKLA 394
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
5-370 |
6.91e-84 |
|
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: 259.87 E-value: 6.91e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 5 VYLNYAATSyKKFPATIEALTAYLaENQFMNYGRNAPLL--REGLPLLETRQLLADFFQAPSAAQITFTNNATTSLNLA- 81
Cdd:pfam00266 1 IYLDSAATT-QKPQEVLDAIQEYY-TDYNGNVHRGVHTLgkEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAINLVa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 82 --LAGILQPGDHVITTMLEHHAVARPLHLLEKERGISVTYVACQKTGLLDVEDIQRALRTNTKALVMTHASNVLGTILPI 159
Cdd:pfam00266 79 lsLGRSLKPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 160 EECFQWAQQKGLLTVLDAAQTAGFLPIKMTQMAIDVLAFTGHKsLYGLAGIGGLAFSEQGAEAVKPLITGGTGSHSNSFD 239
Cdd:pfam00266 159 PEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHK-LYGPTGIGVLYGRRDLLEKMPPLLGGGGMIETVSLQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 240 QPSF--LPDKFEAGTLNSLGILSLNSSVKELNKIGLAAIQKHERTLMQNFFNGLSGLP-VTILGTKdvaQTVPVVSITLW 316
Cdd:pfam00266 238 ESTFadAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPgIRLYGPE---RRASIISFNFK 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 514883239 317 NQEETVVAQQLAEqYGIMTRAGLHCAPLAHETAGTlaTGTLRFSFGCQTTPEEI 370
Cdd:pfam00266 315 GVHPHDVATLLDE-SGIAVRSGHHCAQPLMVRLGL--GGTVRASFYIYNTQEDV 365
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
2-379 |
6.07e-53 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 181.10 E-value: 6.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 2 KDLVYLNYAATSYKkfP-ATIEALTAYlaenqFMNYGRNaplLREGLPLL---------ETRQLLADFFQAPSAAQITFT 71
Cdd:PLN02855 31 SKLVYLDNAATSQK--PaAVLDALQDY-----YEEYNSN---VHRGIHALsakatdayeLARKKVAAFINASTSREIVFT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 72 NNATTSLNL-----ALAGiLQPGDHVITTMLEHHAVARPLHLLEKERGISVTYVACQKTGLLDVEDIQRALRTNTKALVM 146
Cdd:PLN02855 101 RNATEAINLvaytwGLAN-LKPGDEVILSVAEHHSNIVPWQLVAQKTGAVLKFVGLTPDEVLDVEQLKELLSEKTKLVAT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 147 THASNVLGTILPIEECFQWAQQKGLLTVLDAAQTAGFLPIKMTQMAIDVLAFTGHKsLYGLAGIGGLAFSEQGAEAVKPL 226
Cdd:PLN02855 180 HHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHK-MCGPTGIGFLWGKSDLLESMPPF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 227 ITGG------TGSHSNSFDQPSflpdKFEAGTLNSLGILSLNSSVKELNKIGLAAIQKHERTLMQNFFNGLSGLP-VTIL 299
Cdd:PLN02855 259 LGGGemisdvFLDHSTYAPPPS----RFEAGTPAIGEAIGLGAAIDYLSEIGMDRIHEYEVELGTYLYEKLSSVPgVRIY 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 300 GTKdVAQTVPVVSITLWNQE---ETVVAQQLAEQYGIMTRAGLHCAPLAHETAGTLATGtlRFSFGCQTTPEEITWTIHA 376
Cdd:PLN02855 335 GPK-PSEGVGRAALCAFNVEgihPTDLSTFLDQQHGVAIRSGHHCAQPLHRYLGVNASA--RASLYFYNTKEEVDAFIHA 411
|
...
gi 514883239 377 LQE 379
Cdd:PLN02855 412 LKD 414
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
2-342 |
2.61e-24 |
|
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: 104.55 E-value: 2.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 2 KDLVYLNYAATSYKkfP-ATIEALTAYLA-ENQfmNYGRNAPLL--R-----EGlplleTRQLLADFFQAPSAAQITFTN 72
Cdd:NF041166 244 KPLVWFDNAATTQK--PqAVIDRLSYFYEhENS--NIHRAAHELaaRatdayEG-----AREKVRRFIGAPSVDEIIFVR 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 73 NATTSLNLalagI--------LQPGDHVITTMLEHHAVARPLHLLekergisvtyvaCQKTGL-LDV-----------ED 132
Cdd:NF041166 315 GTTEAINL----VakswgrqnIGAGDEIIVSHLEHHANIVPWQQL------------AQETGAkLRVipvddsgqillDE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 133 IQRALRTNTKALVMTHASNVLGTILPIEECFQWAQQKGLLTVLDAAQTAGFLPIKMTQMAIDVLAFTGHKsLYGLAGIGG 212
Cdd:NF041166 379 YAKLLNPRTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHK-VFGPTGIGV 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 213 LAFSEQGAEAVKPLITGGtgshsN-----SFD----QPSflPDKFEAGTLNSLGILSLNSSVKELNKIGLAAIQKHERTL 283
Cdd:NF041166 458 VYGKRDLLEAMPPWQGGG-----NmiadvTFEktvyQPA--PNRFEAGTGNIADAVGLGAALDYVERIGIENIARYEHDL 530
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514883239 284 MQNFFNGLSGLP-VTILGT-KDVAQtvpVVSITL--WNQEEtvVAQQLAEQyGIMTRAGLHCA 342
Cdd:NF041166 531 LEYATAGLAEVPgLRLIGTaADKAS---VLSFVLdgYSTEE--VGKALNQE-GIAVRSGHHCA 587
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Sec_lyase_SclA |
NF040779 |
selenocysteine lyase SclA; In bacteria, selenocysteine lyase activity (EC 4.4.1.16) usually is ... |
5-382 |
0e+00 |
|
selenocysteine lyase SclA; In bacteria, selenocysteine lyase activity (EC 4.4.1.16) usually is seen as a secondary activity of a cysteine desulfurase (EC 2.8.1.7). However, SclA, as studied in Enterococcus faecalis, acts primary on selenocysteine, binding cysteine just as well but acting on cysteine with much lower catalytic efficiency.
Pssm-ID: 468734 [Multi-domain] Cd Length: 378 Bit Score: 680.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 5 VYLNYAATSYKKFPATIEALTAYLAENQFMNYGRNAPLLREGLPLLETRQLLADFFQAPSAAQITFTNNATTSLNLALAG 84
Cdd:NF040779 1 VYLNHAATSNHKFEATIQALCAYLQENNNLNTNRGLQGLDELGLAFETRQALADFFHAPDPAHVIFTANATTSLNMVLNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 85 ILQPGDHVITTMLEHHAVARPLHLLEKERGISVTYVACQKTGLLDVEDIQRALRTNTKALVMTHASNVLGTILPIEECFQ 164
Cdd:NF040779 81 LLKPGDHVLTTSVEHNAVARPLHLLETEQNVSVTYLPCEKDGQLDPEQIEAAIRPETKVLVMTHASNVLGTILPVKECFK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 165 WAQQKGLLTVLDAAQTAGFLPIKMTQMAIDVLAFTGHKSLYGLAGIGGLAFSEQGAEAVKPLITGGTGSHSNSFDQPSFL 244
Cdd:NF040779 161 IAKKHGIITVLDSAQTAGFLPIDMEEMSIDVLAFTGHKSLMGLAGIGGFALAKNIEKKIDPWLTGGTGSASLSLEQPDFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 245 PDKFEAGTLNSLGILSLNSSVKELNKIGLAAIQKHERTLMQNFFNGLSGLPVTILGTKDVAQTVPVVSITLWNQEETVVA 324
Cdd:NF040779 241 PDKFEPGTPNTLGILSLKSSVKAIQELGLEKIQAHERALTARFLTGLKELPVTILGTKDAAQSVPVVSITAPGIDSGELA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 514883239 325 QQLAEQYGIMTRAGLHCAPLAHETAGTLATGTLRFSFGCQTTPEEITWTIHALQELLI 382
Cdd:NF040779 321 QQLFDRYGIITRSGLHCAPLAHQTAGTLKTGAVRFSFGWNTTAEEIDYTLSALKEILS 378
|
|
| am_tr_V_EF2568 |
TIGR01977 |
cysteine desulfurase family protein; This model describes a subfamily of probable pyridoxal ... |
5-380 |
0e+00 |
|
cysteine desulfurase family protein; This model describes a subfamily of probable pyridoxal phosphate-dependent enzymes in the aminotransferase class V family. Related families contain members active as cysteine desulfurases, selenocysteine lyases, or both. The members of this family form a distinct clade and all are shorter at the N-terminus. The function of this subfamily is unknown. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 131032 [Multi-domain] Cd Length: 376 Bit Score: 583.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 5 VYLNYAATSYKKFPATIEALTAYLAENQ-FMNYGRNAPLLREGLPLLETRQLLADFFQAPSAAQITFTNNATTSLNLALA 83
Cdd:TIGR01977 1 IYFDNAATTYPKPDEVYEAMADFYKNYGgSPGRGRYRLALRASREVEETRQLLAKLFNAPSSAHVVFTNNATTALNIALK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 84 GILQPGDHVITTMLEHHAVARPLHLLEKERGISVTYVACQKTGLLDVEDIQRALRTNTKALVMTHASNVLGTILPIEECF 163
Cdd:TIGR01977 81 GLLKEGDHVITTPMEHNSVARPLECLKEQIGVEITIVKCDNEGLISPERIKRAIKTNTKLIVVSHASNVTGTILPIEEIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 164 QWAQQKGLLTVLDAAQTAGFLPIKMTQMAIDVLAFTGHKSLYGLAGIGGLAFSEQGaeAVKPLITGGTGSHSNSFDQPSF 243
Cdd:TIGR01977 161 ELAQENGIFFILDAAQTAGVIPIDMTELAIDMLAFTGHKGLLGPQGTGGLYIREGI--KLKPLKSGGTGSHSALIDQPSE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 244 LPDKFEAGTLNSLGILSLNSSVKELNKIGLAAIQKHERTLMQNFFNGLS-GLPVTILGTKDVAQTVPVVSITLWNQEETV 322
Cdd:TIGR01977 239 LPDRFESGTLNTPGIAGLNAGIKFIEKIGIANIAKKECMLTEKLLNGLReINKVKIYGPADPANRVGVVSFTVEGIDSEE 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 514883239 323 VAQQLAEQYGIMTRAGLHCAPLAHETAGTLATGTLRFSFGCQTTPEEITWTIHALQEL 380
Cdd:TIGR01977 319 VADILDEKFDIATRTGLHCAPLAHKTIGTFATGTIRLSLGYFNTEEEIEKLLEALSEI 376
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
5-370 |
6.14e-111 |
|
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: 329.04 E-value: 6.14e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 5 VYLNYAATSYKKfPATIEALTAYlAENQFMNYGRNAPLL--REGLPLLETRQLLADFFQAPSAAQITFTNNATTSLNLAL 82
Cdd:cd06453 1 VYLDNAATSQKP-QPVIDAIVDY-YRHYNANVHRGVHELsaRATDAYEAAREKVARFINAPSPDEIIFTRNTTEAINLVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 83 AGIL---QPGDHVITTMLEHHAVARPLHLLEKERGISVTYVACQKTGLLDVEDIQRALRTNTKALVMTHASNVLGTILPI 159
Cdd:cd06453 79 YGLGranKPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 160 EECFQWAQQKGLLTVLDAAQTAGFLPIKMTQMAIDVLAFTGHKsLYGLAGIGGLAFSEQGAEAVKPLITGGTGSHSNSFD 239
Cdd:cd06453 159 KEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHK-MLGPTGIGVLYGKEELLEEMPPYGGGGEMIEEVSFE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 240 --QPSFLPDKFEAGTLNSLGILSLNSSVKELNKIGLAAIQKHERTLMQNFFNGLSGLP-VTILGTKDVAqtVPVVSITLW 316
Cdd:cd06453 238 etTYADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEIPgVRVYGDAEDR--AGVVSFNLE 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 514883239 317 NQEETVVAQQLaEQYGIMTRAGLHCAPLAHEtaGTLATGTLRFSFGCQTTPEEI 370
Cdd:cd06453 316 GIHPHDVATIL-DQYGIAVRAGHHCAQPLMR--RLGVPGTVRASFGLYNTEEEI 366
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
2-381 |
3.99e-107 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 320.16 E-value: 3.99e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 2 KDLVYLNYAATSyKKFPATIEALTAYL----AENQFMNY--GRNAPLLREglpllETRQLLADFFQAPSAAQITFTNNAT 75
Cdd:COG0520 14 KPLVYLDNAATG-QKPRPVIDAIRDYYepynANVHRGAHelSAEATDAYE-----AAREKVARFIGAASPDEIIFTRGTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 76 TSLNLALAGI--LQPGDHVITTMLEHHAVARPLHLLEKERGISVTYVACQKTGLLDVEDIQRALRTNTKALVMTHASNVL 153
Cdd:COG0520 88 EAINLVAYGLgrLKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDGELDLEALEALLTPRTKLVAVTHVSNVT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 154 GTILPIEECFQWAQQKGLLTVLDAAQTAGFLPIKMTQMAIDVLAFTGHKsLYGLAGIGGLAFSEQGAEAVKPLITGGTGS 233
Cdd:COG0520 168 GTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHK-LYGPTGIGVLYGKRELLEALPPFLGGGGMI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 234 HSNSFDQPSF--LPDKFEAGTLNSLGILSLNSSVKELNKIGLAAIQKHERTLMQNFFNGLSGLP-VTILGTKDVAQTVPV 310
Cdd:COG0520 247 EWVSFDGTTYadLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAIPgVRILGPADPEDRSGI 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514883239 311 VSITLWNQEETVVAQQLAEQyGIMTRAGLHCAPLAHETAGTlaTGTLRFSFGCQTTPEEITWTIHALQELL 381
Cdd:COG0520 327 VSFNVDGVHPHDVAALLDDE-GIAVRAGHHCAQPLMRRLGV--PGTVRASFHLYNTEEEIDRLVEALKKLA 394
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
5-370 |
6.91e-84 |
|
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: 259.87 E-value: 6.91e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 5 VYLNYAATSyKKFPATIEALTAYLaENQFMNYGRNAPLL--REGLPLLETRQLLADFFQAPSAAQITFTNNATTSLNLA- 81
Cdd:pfam00266 1 IYLDSAATT-QKPQEVLDAIQEYY-TDYNGNVHRGVHTLgkEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAINLVa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 82 --LAGILQPGDHVITTMLEHHAVARPLHLLEKERGISVTYVACQKTGLLDVEDIQRALRTNTKALVMTHASNVLGTILPI 159
Cdd:pfam00266 79 lsLGRSLKPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 160 EECFQWAQQKGLLTVLDAAQTAGFLPIKMTQMAIDVLAFTGHKsLYGLAGIGGLAFSEQGAEAVKPLITGGTGSHSNSFD 239
Cdd:pfam00266 159 PEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHK-LYGPTGIGVLYGRRDLLEKMPPLLGGGGMIETVSLQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 240 QPSF--LPDKFEAGTLNSLGILSLNSSVKELNKIGLAAIQKHERTLMQNFFNGLSGLP-VTILGTKdvaQTVPVVSITLW 316
Cdd:pfam00266 238 ESTFadAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPgIRLYGPE---RRASIISFNFK 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 514883239 317 NQEETVVAQQLAEqYGIMTRAGLHCAPLAHETAGTlaTGTLRFSFGCQTTPEEI 370
Cdd:pfam00266 315 GVHPHDVATLLDE-SGIAVRSGHHCAQPLMVRLGL--GGTVRASFYIYNTQEDV 365
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
5-381 |
2.88e-58 |
|
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: 193.73 E-value: 2.88e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 5 VYLNYAATSyKKFPATIEALTAYLAEnQFMN------YGRNApllREglpLLET-RQLLADFFQApSAAQITFTNNATTS 77
Cdd:COG1104 4 IYLDNAATT-PVDPEVLEAMLPYLTE-YFGNpsslhsFGREA---RA---ALEEaREQVAALLGA-DPEEIIFTSGGTEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 78 LNLALAGIL----QPGDHVITTMLEHHAVARPLHLLEKErGISVTYVACQKTGLLDVEDIQRALRTNTkALV-MTHASNV 152
Cdd:COG1104 75 NNLAIKGAArayrKKGKHIITSAIEHPAVLETARFLEKE-GFEVTYLPVDEDGRVDLEALEAALRPDT-ALVsVMHANNE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 153 LGTILPIEECFQWAQQKGLLTVLDAAQTAGFLPIKMTQMAIDVLAFTGHKsLYGLAGIGGLAFSEqGAEaVKPLITGGTg 232
Cdd:COG1104 153 TGTIQPIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHK-IYGPKGVGALYVRK-GVR-LEPLIHGGG- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 233 shsnsfdQpsflpdkfE----AGTLNSLGILSLNSSVKELNKiGLAAIQKHERTLMQNFFNGL-SGLP-VTILGtkDVAQ 306
Cdd:COG1104 229 -------Q--------ErglrSGTENVPGIVGLGKAAELAAE-ELEEEAARLRALRDRLEEGLlAAIPgVVING--DPEN 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 307 TVP-VVSITLWNQE-ETVVAqqLAEQYGIMTRAGLHCaplaheTAGTL---------------ATGTLRFSFGCQTTPEE 369
Cdd:COG1104 291 RLPnTLNFSFPGVEgEALLL--ALDLAGIAVSSGSAC------SSGSLepshvllamgldeelAHGSIRFSLGRFTTEEE 362
|
410
....*....|..
gi 514883239 370 ITWTIHALQELL 381
Cdd:COG1104 363 IDRAIEALKEIV 374
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
2-379 |
6.07e-53 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 181.10 E-value: 6.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 2 KDLVYLNYAATSYKkfP-ATIEALTAYlaenqFMNYGRNaplLREGLPLL---------ETRQLLADFFQAPSAAQITFT 71
Cdd:PLN02855 31 SKLVYLDNAATSQK--PaAVLDALQDY-----YEEYNSN---VHRGIHALsakatdayeLARKKVAAFINASTSREIVFT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 72 NNATTSLNL-----ALAGiLQPGDHVITTMLEHHAVARPLHLLEKERGISVTYVACQKTGLLDVEDIQRALRTNTKALVM 146
Cdd:PLN02855 101 RNATEAINLvaytwGLAN-LKPGDEVILSVAEHHSNIVPWQLVAQKTGAVLKFVGLTPDEVLDVEQLKELLSEKTKLVAT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 147 THASNVLGTILPIEECFQWAQQKGLLTVLDAAQTAGFLPIKMTQMAIDVLAFTGHKsLYGLAGIGGLAFSEQGAEAVKPL 226
Cdd:PLN02855 180 HHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHK-MCGPTGIGFLWGKSDLLESMPPF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 227 ITGG------TGSHSNSFDQPSflpdKFEAGTLNSLGILSLNSSVKELNKIGLAAIQKHERTLMQNFFNGLSGLP-VTIL 299
Cdd:PLN02855 259 LGGGemisdvFLDHSTYAPPPS----RFEAGTPAIGEAIGLGAAIDYLSEIGMDRIHEYEVELGTYLYEKLSSVPgVRIY 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 300 GTKdVAQTVPVVSITLWNQE---ETVVAQQLAEQYGIMTRAGLHCAPLAHETAGTLATGtlRFSFGCQTTPEEITWTIHA 376
Cdd:PLN02855 335 GPK-PSEGVGRAALCAFNVEgihPTDLSTFLDQQHGVAIRSGHHCAQPLHRYLGVNASA--RASLYFYNTKEEVDAFIHA 411
|
...
gi 514883239 377 LQE 379
Cdd:PLN02855 412 LKD 414
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
5-370 |
2.88e-41 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 148.65 E-value: 2.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 5 VYLNYAATSyKKFPATIEALTAYLAEnQFMN-------YGRNAPLLREglpllETRQLLADFFQApSAAQITFTNNATTS 77
Cdd:PLN02651 1 LYLDMQATT-PIDPRVLDAMLPFLIE-HFGNphsrthlYGWESEDAVE-----KARAQVAALIGA-DPKEIIFTSGATES 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 78 LNLALAGILQ----PGDHVITTMLEHHAVARPLHLLEKErGISVTYVACQKTGLLDVEDIQRALRTNTKALVMTHASNVL 153
Cdd:PLN02651 73 NNLAIKGVMHfykdKKKHVITTQTEHKCVLDSCRHLQQE-GFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 154 GTILPIEECFQWAQQKGLLTVLDAAQTAGFLPIKMTQMAIDVLAFTGHKsLYGLAGIGGLAFSEQGAEAVKPLITGGtGS 233
Cdd:PLN02651 152 GVIQPVEEIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHK-IYGPKGVGALYVRRRPRVRLEPLMSGG-GQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 234 HSNsfdqpsflpdkFEAGTLNSLGILSLNSSVkELNKIGLAAIQKHERTLMQNFFNGL-SGL-PVTILGTKDVAQTVP-V 310
Cdd:PLN02651 230 ERG-----------RRSGTENTPLVVGLGAAC-ELAMKEMDYDEKHMKALRERLLNGLrAKLgGVRVNGPRDPEKRYPgT 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514883239 311 VSITLWNQEETVVAQQLAEqygIMTRAGLHCAPLAHETAGTL---------ATGTLRFSFGCQTTPEEI 370
Cdd:PLN02651 298 LNLSFAYVEGESLLMGLKE---VAVSSGSACTSASLEPSYVLralgvpeemAHGSLRLGVGRFTTEEEV 363
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
4-378 |
5.20e-40 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 146.43 E-value: 5.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 4 LVYLNYAAtSYKKFPATIEAltaylaENQFMNYGRNA------PLLREGLPLLET-RQLLADFFQAPSAAQITFTNNATT 76
Cdd:PRK09295 24 LAYLDSAA-SAQKPSQVIDA------EAEFYRHGYAAvhrgihTLSAQATEKMENvRKQAALFINARSAEELVFVRGTTE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 77 SLNLAL----AGILQPGDHVITTMLEHHAVARPLHLLEKERGISVTYVACQKTGLLDVEDIQRALRTNTKALVMTHASNV 152
Cdd:PRK09295 97 GINLVAnswgNSNVRAGDNIIISEMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPALFDERTRLLAITHVSNV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 153 LGTILPIEECFQWAQQKGLLTVLDAAQTAGFLPIKMTQMAIDVLAFTGHKsLYGLAGIGGLAFSEQGAEAVKPLITGGTG 232
Cdd:PRK09295 177 LGTENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHK-LYGPTGIGILYVKEALLQEMPPWEGGGSM 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 233 SHSNSFDQPSFL---PDKFEAGTLNSLGILSLNSSVKELNKIGLAAIQKHERTLMQNFFNGLSGLP-VTILGTkdvAQTV 308
Cdd:PRK09295 256 IATVSLTEGTTWakaPWRFEAGTPNTGGIIGLGAALDYVSALGLNNIAEYEQNLMHYALSQLESVPdLTLYGP---QNRL 332
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514883239 309 PVVSITLWNQEETVVAQQLaEQYGIMTRAGLHCA-PL-AHETAGTLAtgtlRFSFGCQTTPEEITWTIHALQ 378
Cdd:PRK09295 333 GVIAFNLGKHHAYDVGSFL-DNYGIAVRTGHHCAmPLmAYYNVPAMC----RASLAMYNTHEEVDRLVAGLQ 399
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
5-382 |
6.80e-38 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 140.56 E-value: 6.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 5 VYLNYAATSYKkfP-ATIEALTAYLAENQfMNYGRNAplLREGLPLLE----TRQLLADFFQAPSAAQITFTNNATTSLN 79
Cdd:PRK10874 21 VYLDSAATALK--PqAVIEATQQFYSLSA-GNVHRSQ--FAAAQRLTAryeaAREQVAQLLNAPDAKNIVWTRGTTESIN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 80 LALAGI----LQPGDHVITTMLEHHAVARPLHLLEKERGISVTYVACQKTGLLDVEDIQRALRTNTKALVMTHASNVLGT 155
Cdd:PRK10874 96 LVAQSYarprLQPGDEIIVSEAEHHANLVPWLMVAQQTGAKVVKLPLGADRLPDVDLLPELITPRTRILALGQMSNVTGG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 156 ILPIEECFQWAQQKGLLTVLDAAQTAGFLPIKMTQMAIDVLAFTGHKsLYGLAGIGGLAFSEQGAEAVKPLITGGTGSHS 235
Cdd:PRK10874 176 CPDLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHK-LYGPTGIGVLYGKSELLEAMSPWQGGGKMLTE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 236 NSFD--QPSFLPDKFEAGTLNSLGILSLNSSVKELNKIGLAAIQKHERTLMQNFFNGLSGLPvtilGTKDV-AQTVPVVS 312
Cdd:PRK10874 255 VSFDgfTPQSAPWRFEAGTPNVAGVIGLSAALEWLADIDINQAESWSRSLATLAEDALAKLP----GFRSFrCQDSSLLA 330
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514883239 313 ITLWNQEETVVAQQLAEQyGIMTRAGLHCA-PLaheTAGTLATGTLRFSFGCQTTPEEITWTIHALQ---ELLI 382
Cdd:PRK10874 331 FDFAGVHHSDLVTLLAEY-GIALRAGQHCAqPL---LAALGVTGTLRASFAPYNTQSDVDALVNAVDralELLV 400
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
1-374 |
9.74e-37 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 137.38 E-value: 9.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 1 MKDLVYLNYAATSyKKFPATIEALTAYLA-ENQFMN-------YGRNAPLLREglpllETRQLLADFFQApSAAQITFTN 72
Cdd:PRK14012 1 MKLPIYLDYSATT-PVDPRVAEKMMPYLTmDGTFGNpasrshrFGWQAEEAVD-----IARNQIADLIGA-DPREIVFTS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 73 NATTSLNLALAGILQ----PGDHVITTMLEHHAVARPLHLLEKErGISVTYVACQKTGLLDVEDIQRALRTNTKALVMTH 148
Cdd:PRK14012 74 GATESDNLAIKGAAHfyqkKGKHIITSKTEHKAVLDTCRQLERE-GFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 149 ASNVLGTILPIEECFQWAQQKGLLTVLDAAQTAGFLPIKMTQMAIDVLAFTGHKsLYGLAGIGGLAFSEQGAEAVKPLIT 228
Cdd:PRK14012 153 VNNEIGVIQDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHK-IYGPKGIGALYVRRKPRVRLEAQMH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 229 GgtGSHSNSfdqpsflpdkFEAGTLNSLGILSLNSSVkELNKIGLAAIQKHERTLMQNFFNGLSGLP-VTILGtkDVAQT 307
Cdd:PRK14012 232 G--GGHERG----------MRSGTLPTHQIVGMGEAA-RIAKEEMATENERIRALRDRLWNGIKDIEeVYLNG--DLEQR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 308 VPV---VSITLWNQEETVVA-QQLAEQYG-IMTRAGLHcaP--------LAHEtagtLATGTLRFSFGCQTTPEEITWTI 374
Cdd:PRK14012 297 VPGnlnVSFNYVEGESLIMAlKDLAVSSGsACTSASLE--PsyvlralgLNDE----LAHSSIRFSLGRFTTEEEIDYAI 370
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
4-380 |
2.21e-36 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 136.01 E-value: 2.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 4 LVYLNYAATSykkfPATIEALTAY--LAENQFMNY-------GRNAPLLREglplleTRQLLADFFQApSAAQITFTNNA 74
Cdd:PRK02948 1 MIYLDYAATT----PMSKEALQTYqkAASQYFGNEsslhdigGTASSLLQV------CRKTFAEMIGG-EEQGIYFTSGG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 75 TTSLNLA----LAGILQPGDHVITTMLEHHAVARPLHLLEKErGISVTYVACQKTGLLDVEDIQRALRTNTKALVMTHAS 150
Cdd:PRK02948 70 TESNYLAiqslLNALPQNKKHIITTPMEHASIHSYFQSLESQ-GYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHAN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 151 NVLGTILPIEECFQWAQQKGLLTVLDAAQTAGFLPIKMTQMAIDVLAFTGHKsLYGLAGIGGLAFSEQGA-EAVKPLITg 229
Cdd:PRK02948 149 SEIGTIQPIAEIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHK-IYGPKGVGAVYINPQVRwKPVFPGTT- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 230 gtgsHSNSfdqpsflpdkFEAGTLNSLGILSLNSSVKELNKiGLAAIQKHERTLMQNFFNGLS--GLPVTILGTKDvAQT 307
Cdd:PRK02948 227 ----HEKG----------FRPGTVNVPGIAAFLTAAENILK-NMQEESLRFKELRSYFLEQIQtlPLPIEVEGHST-SCL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 308 VPVVSITLWNQEETVVAQQlAEQYGIMTRAGLHCAPLAHETAGT-LATGT--------LRFSFGCQTTPEEITWTIHALQ 378
Cdd:PRK02948 291 PHIIGVTIKGIEGQYTMLE-CNRRGIAISTGSACQVGKQEPSKTmLAIGKtyeeakqfVRFSFGQQTTKDQIDTTIHALE 369
|
..
gi 514883239 379 EL 380
Cdd:PRK02948 370 TI 371
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
2-342 |
2.61e-24 |
|
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: 104.55 E-value: 2.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 2 KDLVYLNYAATSYKkfP-ATIEALTAYLA-ENQfmNYGRNAPLL--R-----EGlplleTRQLLADFFQAPSAAQITFTN 72
Cdd:NF041166 244 KPLVWFDNAATTQK--PqAVIDRLSYFYEhENS--NIHRAAHELaaRatdayEG-----AREKVRRFIGAPSVDEIIFVR 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 73 NATTSLNLalagI--------LQPGDHVITTMLEHHAVARPLHLLekergisvtyvaCQKTGL-LDV-----------ED 132
Cdd:NF041166 315 GTTEAINL----VakswgrqnIGAGDEIIVSHLEHHANIVPWQQL------------AQETGAkLRVipvddsgqillDE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 133 IQRALRTNTKALVMTHASNVLGTILPIEECFQWAQQKGLLTVLDAAQTAGFLPIKMTQMAIDVLAFTGHKsLYGLAGIGG 212
Cdd:NF041166 379 YAKLLNPRTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHK-VFGPTGIGV 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 213 LAFSEQGAEAVKPLITGGtgshsN-----SFD----QPSflPDKFEAGTLNSLGILSLNSSVKELNKIGLAAIQKHERTL 283
Cdd:NF041166 458 VYGKRDLLEAMPPWQGGG-----NmiadvTFEktvyQPA--PNRFEAGTGNIADAVGLGAALDYVERIGIENIARYEHDL 530
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514883239 284 MQNFFNGLSGLP-VTILGT-KDVAQtvpVVSITL--WNQEEtvVAQQLAEQyGIMTRAGLHCA 342
Cdd:NF041166 531 LEYATAGLAEVPgLRLIGTaADKAS---VLSFVLdgYSTEE--VGKALNQE-GIAVRSGHHCA 587
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
5-371 |
9.21e-15 |
|
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: 74.69 E-value: 9.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 5 VYLNYAATSYKKFPATIEALTAYLAENQFMNYGRNApllreGLPLLetRQLLADFFQ-----APSAAQITFTNNATTSLN 79
Cdd:cd00609 1 IDLSIGEPDFPPPPEVLEALAAAALRAGLLGYYPDP-----GLPEL--REAIAEWLGrrggvDVPPEEIVVTNGAQEALS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 80 LALAGILQPGDHVITTM---LEHHAVARPLhllekerGISVTYVAC--QKTGLLDVEDIQRALRTNTKALVMTHASNVLG 154
Cdd:cd00609 74 LLLRALLNPGDEVLVPDptyPGYEAAARLA-------GAEVVPVPLdeEGGFLLDLELLEAAKTPKTKLLYLNNPNNPTG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 155 TILP---IEECFQWAQQKGLLTVLDAA----QTAGFLPIKMTQMAIDVLAFTGH---KSlYGLAG--IGGLAFSEQGAEA 222
Cdd:cd00609 147 AVLSeeeLEELAELAKKHGILIISDEAyaelVYDGEPPPALALLDAYERVIVLRsfsKT-FGLPGlrIGYLIAPPEELLE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 223 VKPLITGGTGSHSNSFDQpsflpdkfeagtlnSLGILSLNSSVKELNKIgLAAIQKhERTLMQNFFNGLSGLPVTIlgtk 302
Cdd:cd00609 226 RLKKLLPYTTSGPSTLSQ--------------AAAAAALDDGEEHLEEL-RERYRR-RRDALLEALKELGPLVVVK---- 285
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514883239 303 dvaqtvPVVSITLW----NQEETVVAQQLAEQYGIMTRAGlhcaplahETAGTLATGTLRFSFGCqtTPEEIT 371
Cdd:cd00609 286 ------PSGGFFLWldlpEGDDEEFLERLLLEAGVVVRPG--------SAFGEGGEGFVRLSFAT--PEEELE 342
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
49-281 |
3.54e-13 |
|
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: 70.01 E-value: 3.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 49 LLETRQLLADFFQAPSAAQITFTNNATTSLNLALAGILQPGDHVITT-----------MLEHHAvaRPLHLLEKERGISV 117
Cdd:cd06451 34 MDEILEGLRYVFQTENGLTFLLSGSGTGAMEAALSNLLEPGDKVLVGvngvfgdrwadMAERYG--ADVDVVEKPWGEAV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 118 tyvacqktgllDVEDIQRALRTNT-KALVMTHASNVLGTILPIEECFQWAQQKGLLTVLDAAQTAGFLPIKMTQMAIDVl 196
Cdd:cd06451 112 -----------SPEEIAEALEQHDiKAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVDAVSSLGGEPFRMDEWGVDV- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 197 AFTG-HKSLYGLAGIGGLAFSEQGAEAvkplITGGTGSHSNSFDQPSFL--PDKFEA--GTLNSLGILSLNSSVKELNKI 271
Cdd:cd06451 180 AYTGsQKALGAPPGLGPIAFSERALER----IKKKTKPKGFYFDLLLLLkyWGEGYSypHTPPVNLLYALREALDLILEE 255
|
250
....*....|.
gi 514883239 272 GLAA-IQKHER 281
Cdd:cd06451 256 GLENrWARHRR 266
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
48-215 |
3.55e-13 |
|
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: 67.02 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 48 PLLETRQLLADFFQaPSAAQITFTNNATTSLNLALAGILQPGDHVITTMLEHHAvarplHLLEKERGISVTYVACQKT-- 125
Cdd:cd01494 1 KLEELEEKLARLLQ-PGNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGS-----RYWVAAELAGAKPVPVPVDda 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 126 --GLLDVEDIQRALRTNTKALVMTHASNVLGTILPIEECFQW-AQQKGLLTVLDAAQTAGFLPIKMTQM---AIDVLAFT 199
Cdd:cd01494 75 gyGGLDVAILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKiAKEYGILLLVDAASAGGASPAPGVLIpegGADVVTFS 154
|
170
....*....|....*.
gi 514883239 200 GHKSLyGLAGIGGLAF 215
Cdd:cd01494 155 LHKNL-GGEGGGVVIV 169
|
|
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
1-369 |
3.59e-10 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 61.81 E-value: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 1 MKDLVYLNYA-ATSYKKfpATIEALTAYLAENQFMNYGRNAPLLREGLPLLET-RQLLADFFQAPSAAQI-TFTNNATTS 77
Cdd:PLN02724 32 LKGVVYLDHAgATLYSE--SQLEAALADFSSNVYGNPHSQSDSSMRSSDTIESaRQQVLEYFNAPPSDYAcVFTSGATAA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 78 LNL-ALAGILQPGDHVITTMLEHHAV--ARPLHLlekERGISVTYVACQ------KTGLLDVEDIQRALRTNTKALVMTH 148
Cdd:PLN02724 110 LKLvGETFPWSSESHFCYTLENHNSVlgIREYAL---EKGAAAIAVDIEeaanqpTNSQGSVVVKSRGLQRRNTSKLQKR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 149 AS--------------NVLGTILPIE--------ECFQWAQQKGLLTVLDAAQTAGFLPIKMTQMAIDVLAFTGHKsLYG 206
Cdd:PLN02724 187 EDdgeaynlfafpsecNFSGAKFPLDlvklikdnQHSNFSKSGRWMVLLDAAKGCGTSPPDLSRYPADFVVVSFYK-IFG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 207 L-AGIGGLAFSEQGAEAVKPLITGGtGSHSNSFDQPSF------LPDKFEAGTLNSLGILSLNSSVKELNKIGLAAIQKH 279
Cdd:PLN02724 266 YpTGLGALLVRRDAAKLLKKKYFGG-GTVAASIADIDFvkrrerVEQRFEDGTISFLSIAALRHGFKLLNRLTISAIAMH 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 280 ERTLMQNFFNGLSGL------PVTILGTKDVAQ-----TVPVVSITLWNQEETVVA----QQLAEQYGIMTRAGLHCAP- 343
Cdd:PLN02724 345 TWALTHYVANSLRNLkhgngaPVCVLYGNHTFKlefhiQGPIVTFNLKRADGSWVGhrevEKLASLSGIQLRTGCFCNPg 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 514883239 344 -------LAHE------TAGTLA-----------TGTLRFSFGCQTTPEE 369
Cdd:PLN02724 425 acakylgLSHKdlqanfEAGHVCwddqdvihgrpTGAVRVSFGYMSTFED 474
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
17-377 |
2.36e-09 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 58.09 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 17 FPATIEALTAYLAENQFMNYGRnapllREGLPLLetRQLLADFFQAP------SAAQITFTNNATTSLNLALAGILQPGD 90
Cdd:pfam00155 16 LPAVAKAEKDALAGGTRNLYGP-----TDGHPEL--REALAKFLGRSpvlkldREAAVVFGSGAGANIEALIFLLANPGD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 91 HVIT---TMLEHHAVARplhllekERGISVTYVAC--QKTGLLDVEDIQRALRTNTKALVMTHASNVLGTILP---IEEC 162
Cdd:pfam00155 89 AILVpapTYASYIRIAR-------LAGGEVVRYPLydSNDFHLDFDALEAALKEKPKVVLHTSPHNPTGTVATleeLEKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 163 FQWAQQKGLLTVLD------AAQTAGFLPIKMTQMAIDVLAFTGhkSL---YGLAG--IGGLAFSEQGAEAVKPLITGGT 231
Cdd:pfam00155 162 LDLAKEHNILLLVDeayagfVFGSPDAVATRALLAEGPNLLVVG--SFskaFGLAGwrVGYILGNAAVISQLRKLARPFY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 232 GShsnsfdqpSFLPDKFEAGTLNSLGIlslNSSVKELNKIglaaIQKHERTlmqnFFNGLS--GLPVTIlgtkdvAQTvP 309
Cdd:pfam00155 240 SS--------THLQAAAAAALSDPLLV---ASELEEMRQR----IKERRDY----LRDGLQaaGLSVLP------SQA-G 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514883239 310 VVSITLWNQE-ETVVAQQLAEQYGIMTRAGLHCaplahetagtLATGTLRFSFGCqTTPEEITWTIHAL 377
Cdd:pfam00155 294 FFLLTGLDPEtAKELAQVLLEEVGVYVTPGSSP----------GVPGWLRITVAG-GTEEELEELLEAI 351
|
|
| MetC |
COG0626 |
Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; ... |
74-176 |
1.38e-08 |
|
Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; Cystathionine beta-lyase/cystathionine gamma-synthase is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 440391 [Multi-domain] Cd Length: 389 Bit Score: 56.21 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 74 ATTSLNLALagiLQPGDHVIttmlehhaVARPL-----HLLEKE---RGISVTYVAcqktgLLDVEDIQRALRTNTKALV 145
Cdd:COG0626 85 AISAVLLAL---LKAGDHVV--------ASDDLyggtrRLLDKVlarFGIEVTFVD-----PTDLAAVEAAIRPNTKLVF 148
|
90 100 110
....*....|....*....|....*....|.
gi 514883239 146 MTHASNVLGTILPIEECFQWAQQKGLLTVLD 176
Cdd:COG0626 149 LETPSNPTLEVVDIAAIAAIAHAAGALLVVD 179
|
|
| AHBA_syn |
cd00616 |
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ... |
21-182 |
1.39e-08 |
|
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The members of this CD are involved in various biosynthetic pathways for secondary metabolites. Some well studied proteins in this CD are AHBA_synthase, protein product of pleiotropic regulatory gene degT, Arnb aminotransferase and pilin glycosylation protein. The prototype of this family, the AHBA_synthase, is a dimeric PLP dependent enzyme. AHBA_syn is the terminal enzyme of 3-amino-5-hydroxybenzoic acid (AHBA) formation which is involved in the biosynthesis of ansamycin antibiotics, including rifamycin B. Some members of this CD are involved in 4-amino-6-deoxy-monosaccharide D-perosamine synthesis. Perosamine is an important element in the glycosylation of several cell products, such as antibiotics and lipopolysaccharides of gram-positive and gram-negative bacteria. The pilin glycosylation protein encoded by gene pglA, is a galactosyltransferase involved in pilin glycosylation. Additionally, this CD consists of ArnB (PmrH) aminotransferase, a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme. This CD also consists of several predicted pyridoxal phosphate-dependent enzymes apparently involved in regulation of cell wall biogenesis. The catalytic lysine which is present in all characterized PLP dependent enzymes is replaced by histidine in some members of this CD.
Pssm-ID: 99740 [Multi-domain] Cd Length: 352 Bit Score: 56.01 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 21 IEALTAYLAENQFMNYgrnaPLLREglplLEtrQLLADFFQAPSAAqitFTNNATTSLNLAL--AGIlQPGDHVITTMLE 98
Cdd:cd00616 2 LEAVEEVLDSGWLTLG----PKVRE----FE--KAFAEYLGVKYAV---AVSSGTAALHLALraLGI-GPGDEVIVPSFT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 99 HHAVARPLHLLekerGISVTYVACQ-KTGLLDVEDIQRALRTNTKALVMTHasnVLGTILPIEECFQWAQQKGLLTVLDA 177
Cdd:cd00616 68 FVATANAILLL----GATPVFVDIDpDTYNIDPELIEAAITPRTKAIIPVH---LYGNPADMDAIMAIAKRHGLPVIEDA 140
|
....*
gi 514883239 178 AQTAG 182
Cdd:cd00616 141 AQALG 145
|
|
| PRK06176 |
PRK06176 |
cystathionine gamma-synthase; |
81-381 |
1.69e-08 |
|
cystathionine gamma-synthase;
Pssm-ID: 180443 [Multi-domain] Cd Length: 380 Bit Score: 55.67 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 81 ALAGILQPGDHVITTMLEHHAVARPLHLLEKERGISVTYVacqktGLLDVEDIQRALRTNTKALVMTHASNVLGTILPIE 160
Cdd:PRK06176 80 AVFSLFQSGDHVLLGDDVYGGTFRLFDKVLVKNGLSCTII-----DTSDLSQIKKAIKPNTKALYLETPSNPLLKITDLA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 161 ECFQWAQQKGLLTVLDAAQTAGFL--PIkmtQMAIDVLAFTGHKSLYGLAG-IGGLAFSEQGAEA-----VKPLITGGTG 232
Cdd:PRK06176 155 QCASVAKDHGLLTIVDNTFATPYYqnPL---LLGADIVVHSGTKYLGGHSDvVAGLVTTNNEALAqeiafFQNAIGGVLG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 233 SHSNSFDQPSF--LPDKFEAGTLNSLGI---LSLNSSVKELNKIGLAAIQKHErtLMQNFFNGLSGLpVTILGTKDVAQT 307
Cdd:PRK06176 232 PQDSWLLQRGIktLGLRMEAHQKNALCVaefLEKHPKVEKVYYPGLPTHPNHE--LAKKQMRGFSGM-LSFTLKNDSEAV 308
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514883239 308 VPVVSITLWNQEETVVA-QQLAEQYGIMTRAglhCAPLAHETAGTLATGTLRFSFGcqttpeeitwtIHALQELL 381
Cdd:PRK06176 309 AFVESLKLFILGESLGGvESLVGIPAFMTHA---CIPKEQREAAGIRDGLVRLSVG-----------IEHEQDLL 369
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
9-176 |
5.22e-08 |
|
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.
Pssm-ID: 99738 [Multi-domain] Cd Length: 369 Bit Score: 54.13 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 9 YAATSYKkFPATIEALTAYLAENQFMNYGRnapllrEGLPlleTRQLLADFFQA--PSAAQITFTN--NATTSLNLALag 84
Cdd:cd00614 8 YQTSTFV-FPSPAEAADLFALREGGYIYSR------IGNP---TVDALEKKLAAleGGEAALAFSSgmAAISTVLLAL-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 85 iLQPGDHVITTMLEHHAVARPLHLLEKERGISVTYVacqktGLLDVEDIQRALRTNTKALVMTHASNVLGTILPIEECFQ 164
Cdd:cd00614 76 -LKAGDHVVASDDLYGGTYRLFERLLPKLGIEVTFV-----DPDDPEALEAAIKPETKLVYVESPTNPTLKVVDIEAIAE 149
|
170
....*....|..
gi 514883239 165 WAQQKGLLTVLD 176
Cdd:cd00614 150 LAHEHGALLVVD 161
|
|
| PRK07324 |
PRK07324 |
transaminase; Validated |
34-158 |
5.36e-07 |
|
transaminase; Validated
Pssm-ID: 235989 Cd Length: 373 Bit Score: 51.09 E-value: 5.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 34 MNYGrnaplLREGLPllETRQLLADFFQAPSAAQITFTNNATTSLNLALAGILQPGDHVIT---TMLEHHAVARPL---- 106
Cdd:PRK07324 56 LTYG-----WIEGSP--EFKEAVASLYQNVKPENILQTNGATGANFLVLYALVEPGDHVISvypTYQQLYDIPESLgaev 128
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 514883239 107 ---HLLEKERgisvtyvacqktGLLDVEDIQRALRTNTKALVMTHASNVLGTILP 158
Cdd:PRK07324 129 dywQLKEENG------------WLPDLDELRRLVRPNTKLICINNANNPTGALMD 171
|
|
| PRK07550 |
PRK07550 |
aminotransferase; |
4-176 |
6.29e-07 |
|
aminotransferase;
Pssm-ID: 181026 [Multi-domain] Cd Length: 386 Bit Score: 50.73 E-value: 6.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 4 LVYLNYAATSYKKFPATIEALTAYLAENQFMNYGR--NAPLLREGLplleTRQLLADFFQAPSAAQITFTNNATTSLNLA 81
Cdd:PRK07550 31 LIDLSQAVPGYPPPPELLRALAEAAADPAAHLYGPveGLPELREAY----AAHYSRLYGAAISPEQVHITSGCNQAFWAA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 82 LAGILQPGDHVITTMLEH--HAVArpLHLLekerGISVTYVACQKT--GLLDVEDIQRALRTNTKALVMTHASNVLGTIL 157
Cdd:PRK07550 107 MVTLAGAGDEVILPLPWYfnHKMW--LDML----GIRPVYLPCDEGpgLLPDPAAAEALITPRTRAIALVTPNNPTGVVY 180
|
170 180
....*....|....*....|..
gi 514883239 158 P---IEECFQWAQQKGLLTVLD 176
Cdd:PRK07550 181 PpelLHELYDLARRHGIALILD 202
|
|
| PRK05764 |
PRK05764 |
aspartate aminotransferase; Provisional |
46-176 |
1.60e-06 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 235596 Cd Length: 393 Bit Score: 49.74 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 46 GLPllETRQLLADFFQ-----APSAAQITFTNNATTSLNLALAGILQPGDHVIttMLEHHAVARP--LHLLEkerGISVT 118
Cdd:PRK05764 69 GIP--ELREAIAAKLKrdnglDYDPSQVIVTTGAKQALYNAFMALLDPGDEVI--IPAPYWVSYPemVKLAG---GVPVF 141
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514883239 119 YVACQKTGL-LDVEDIQRALRTNTKALVMTHASNVLGTILP---IEECFQWAQQKGLLTVLD 176
Cdd:PRK05764 142 VPTGEENGFkLTVEQLEAAITPKTKALILNSPSNPTGAVYSpeeLEAIADVAVEHDIWVLSD 203
|
|
| SepCysS |
cd06452 |
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ... |
56-223 |
5.64e-06 |
|
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: 47.77 E-value: 5.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 56 LADFFqapSAAQITFTNNATTSLNLALAGILQPGDHVITTMLEHHAvarplhllekergisvTYVACQKTGL-------- 127
Cdd:cd06452 53 LAEFL---GMDEARVTPGAREGKFAVMHSLCEKGDWVVVDGLAHYT----------------SYVAAERAGLnvrevpnt 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 128 ------LDVEDIQRALRTNTKA-------LVMTHASNVLGTILPIEECFQWAQQKGLLTVLDAAQTAGFLPIKMTQMAID 194
Cdd:cd06452 114 ghpeyhITPEGYAEVIEEVKDEfgkppalALLTHVDGNYGNLHDAKKIAKVCHEYGVPLLLNGAYTVGRMPVSGKELGAD 193
|
170 180
....*....|....*....|....*....
gi 514883239 195 VLAFTGHKSLYGLAGIGGLAFSEQGAEAV 223
Cdd:cd06452 194 FIVGSGHKSMAASAPIGVLATTEEWADIV 222
|
|
| PLN02409 |
PLN02409 |
serine--glyoxylate aminotransaminase |
52-224 |
8.18e-06 |
|
serine--glyoxylate aminotransaminase
Pssm-ID: 178031 [Multi-domain] Cd Length: 401 Bit Score: 47.44 E-value: 8.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 52 TRQLLAD---FFQAPSAAQITFTNNATTSLNLALAGILQPGDHVITTMLEHHAvarplHL---LEKERGISVTYVACQKT 125
Cdd:PLN02409 44 TKELLEDvkyIFKTKSGTPFIFPTTGTGAWESALTNTLSPGDKVVSFRIGQFS-----LLwidQMQRLNFDVDVVESPWG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 126 GLLDVEDIQRALRTNT----KALVMTHASNVLGT---ILPIEECFQWAQQKGLLTVlDAAQTAGFLPIKMTQMAIDVlAF 198
Cdd:PLN02409 119 QGADLDILKSKLRQDTnhkiKAVCVVHNETSTGVtndLAGVRKLLDCAQHPALLLV-DGVSSIGALDFRMDEWGVDV-AL 196
|
170 180
....*....|....*....|....*..
gi 514883239 199 TG-HKSLYGLAGIGGLAFSEQGAEAVK 224
Cdd:PLN02409 197 TGsQKALSLPTGLGIVCASPKALEASK 223
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
21-182 |
1.35e-05 |
|
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.
Pssm-ID: 395827 Cd Length: 360 Bit Score: 46.51 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 21 IEALTAYLAENQFmnygRNAPLLREglplLETRqlLADFFQAPSAaqITfTNNATTSLNLALAGI-LQPGDHVITTMLEH 99
Cdd:pfam01041 8 LAAVREVLKSGWL----TTGPYVRE----FERA--FAAYLGVKHA--IA-VSSGTAALHLALRALgVGPGDEVITPSFTF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 100 HAVARPLHLLekerGISVTYVACQ-KTGLLDVEDIQRALRTNTKALVMTHasnVLGTILPIEECFQWAQQKGLLTVLDAA 178
Cdd:pfam01041 75 VATANAALRL----GAKPVFVDIDpDTYNIDPEAIEAAITPRTKAIIPVH---LYGQPADMDAIRAIAARHGLPVIEDAA 147
|
....
gi 514883239 179 QTAG 182
Cdd:pfam01041 148 HALG 151
|
|
| Cys_Met_Meta_PP |
pfam01053 |
Cys/Met metabolism PLP-dependent enzyme; This family includes enzymes involved in cysteine and ... |
71-238 |
2.10e-05 |
|
Cys/Met metabolism PLP-dependent enzyme; This family includes enzymes involved in cysteine and methionine metabolism. The following are members: Cystathionine gamma-lyase, Cystathionine gamma-synthase, Cystathionine beta-lyase, Methionine gamma-lyase, OAH/OAS sulfhydrylase, O-succinylhomoserine sulfhydrylase All of these members participate is slightly different reactions. All these enzymes use PLP (pyridoxal-5'-phosphate) as a cofactor.
Pssm-ID: 395837 [Multi-domain] Cd Length: 376 Bit Score: 46.07 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 71 TNNATTSLNLALAGILQPGDHVITTmlehHAVARPLHLL----EKERGISVTYVACqktglLDVEDIQRALRTNTKALVM 146
Cdd:pfam01053 68 FSSGMAAITAAILALLKAGDHIVAT----DDLYGGTYRLfnkvLPRFGIEVTFVDT-----SDPEDLEAAIKPNTKAVYL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 147 THASNVLGTILPIEECFQWAQQKGLLTVLDAAQTAGFL--PIKmtqMAIDVLAFTGHKSLYGLA-GIGGL----AFSEQG 219
Cdd:pfam01053 139 ETPTNPLLKVVDIEAIAKLAKKHGILVVVDNTFASPYLqrPLD---LGADIVVHSATKYIGGHSdVVGGVivvnGEELGK 215
|
170
....*....|....*....
gi 514883239 220 AEAVKPLITGGTGSHSNSF 238
Cdd:pfam01053 216 ELYFLQNATGAVLSPFDAW 234
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
66-218 |
6.99e-05 |
|
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.
Pssm-ID: 99748 [Multi-domain] Cd Length: 338 Bit Score: 44.25 E-value: 6.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 66 AQITFTNNATTSLNLALAGILQPGDHVIttmLEHHAvarplHLLEKERGISVTYVACQ------KTGLLDVEDIQRALR- 138
Cdd:cd06502 48 EAALFVPSGTAANQLALAAHTQPGGSVI---CHETA-----HIYTDEAGAPEFLSGVKllpvpgENGKLTPEDLEAAIRp 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 139 ------TNTKALVMTHASNvLGTILPIEE---CFQWAQQKGLLTVLDAAQ-----TAGFLPIKMTQMAIDVLAFTGHKSL 204
Cdd:cd06502 120 rddihfPPPSLVSLENTTE-GGTVYPLDElkaISALAKENGLPLHLDGARlanaaAALGVALKTYKSGVDSVSFCLSKGG 198
|
170
....*....|....*..
gi 514883239 205 YGLAG---IGGLAFSEQ 218
Cdd:cd06502 199 GAPVGavvVGNRDFIAR 215
|
|
| PRK06836 |
PRK06836 |
pyridoxal phosphate-dependent aminotransferase; |
46-180 |
2.34e-04 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180720 Cd Length: 394 Bit Score: 42.87 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 46 GLPllETRQLLADF----FQAP-SAAQITFTNNATTSLNLALAGILQPGDHVIT---------TMLEHHavarplhllek 111
Cdd:PRK06836 74 GYP--EVREAIAESlnrrFGTPlTADHIVMTCGAAGALNVALKAILNPGDEVIVfapyfveyrFYVDNH----------- 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514883239 112 eRGISVTYVACQKTGLLDVEDIQRALRTNTKALVMTHASNVLGTILPIEECfqwaqqKGLLTVLDAAQT 180
Cdd:PRK06836 141 -GGKLVVVPTDTDTFQPDLDALEAAITPKTKAVIINSPNNPTGVVYSEETL------KALAALLEEKSK 202
|
|
| PRK09331 |
PRK09331 |
Sep-tRNA:Cys-tRNA synthetase; Provisional |
56-223 |
2.65e-04 |
|
Sep-tRNA:Cys-tRNA synthetase; Provisional
Pssm-ID: 236469 Cd Length: 387 Bit Score: 42.61 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 56 LADFFqapSAAQITFTNNATTSLNLALAGILQPGDHVITTMLEHHAvarplhllekergisvTYVACQKTGL-------- 127
Cdd:PRK09331 72 LAEFL---GMDEARVTHGAREGKFAVMHSLCKKGDYVVLDGLAHYT----------------SYVAAERAGLnvrevpkt 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 128 ------LDVED----IQRALRTNTKA---LVMTHASNVLGTILPIEECFQWAQQKGLLTVLDAAQTAGFLPIKMTQMAID 194
Cdd:PRK09331 133 gypeykITPEAyaekIEEVKEETGKPpalALLTHVDGNYGNLADAKKVAKVAHEYGIPFLLNGAYTVGRMPVDGKKLGAD 212
|
170 180
....*....|....*....|....*....
gi 514883239 195 VLAFTGHKSLYGLAGIGGLAFSEQGAEAV 223
Cdd:PRK09331 213 FIVGSGHKSMAASAPSGVLATTEEYADKV 241
|
|
| YnbB |
COG4100 |
Cystathionine beta-lyase family protein involved in aluminum resistance [Inorganic ion ... |
57-142 |
3.82e-04 |
|
Cystathionine beta-lyase family protein involved in aluminum resistance [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 443276 Cd Length: 409 Bit Score: 42.40 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 57 ADFFQAPSAA---QITftnNATTSLNLALAGILQPGDHVITtmlehhAVARPLHLLE-------------KERGISVTYV 120
Cdd:COG4100 67 ADVFGAEDALvrpQIV---SGTHAIALALFGVLRPGDELLS------ITGKPYDTLEevigirgegqgslKEFGISYRQV 137
|
90 100
....*....|....*....|..
gi 514883239 121 ACQKTGLLDVEDIQRALRTNTK 142
Cdd:COG4100 138 PLTEDGKIDLEAIKKAINEKTK 159
|
|
| PRK13479 |
PRK13479 |
2-aminoethylphosphonate--pyruvate transaminase; Provisional |
114-211 |
4.99e-03 |
|
2-aminoethylphosphonate--pyruvate transaminase; Provisional
Pssm-ID: 184076 [Multi-domain] Cd Length: 368 Bit Score: 38.74 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514883239 114 GISVTYVACQKTGLLDVEDIQRALRTNTKA--LVMTHASNVLGTILPIEECFQWAQQKGLLTVLDAAQTAGFLPIKMTQM 191
Cdd:PRK13479 103 GIAHVVLDTGEDEPPDAAEVEAALAADPRIthVALVHCETTTGILNPLDEIAAVAKRHGKRLIVDAMSSFGAIPIDIAEL 182
|
90 100
....*....|....*....|
gi 514883239 192 AIDVLAFTGHKSLYGLAGIG 211
Cdd:PRK13479 183 GIDALISSANKCIEGVPGFG 202
|
|
| |
