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Conserved domains on  [gi|255947362|ref|XP_002564448|]
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Pc22g04090 [Penicillium rubens Wisconsin 54-1255]

Protein Classification

PLP-dependent aminotransferase family protein( domain architecture ID 139552)

PLP-dependent aminotransferase family protein may combine pyridoxal phosphate with an alpha-amino acid to form a Schiff base or aldimine intermediate, which then acts as the substrate in a reaction such as a transamination, racemization, or decarboxylation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AAT_I super family cl18945
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 51-502 6.14e-142

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).


The actual alignment was detected with superfamily member PLN02822:

Pssm-ID: 450240 [Multi-domain]  Cd Length: 481  Bit Score: 416.83  E-value: 6.14e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362  51 LFLFAVRYLLAPKySTKPGVVPLTEDEIDDLVDEWTPEPLVgsPTTLEEMEVDKrTVIVGPVGPKSKLaNGRTVTNLGSF 130
Cdd:PLN02822  43 LLIVVIVFLLSQK-SYKPPKRPLTEKEIDELCDEWTPEPLI--PPITEEMRPEP-PVLESAAGPHTII-NGKDVVNFASA 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 131 NFYNFNTNESLKEQAIQTLRAYGVGPCGPRGFYGTQDVHMKTEDDVAAFIGTAACIMYSQAFSTISSVIPAFSKRGDIIV 210
Cdd:PLN02822 118 NYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSVIPAFCKKGDIIV 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 211 ADKGVSFAIRKGIQISRSIVRWYEHNDMEDLERVLAKVTKEQARKPLTRRFIITEGLFESYGDMADLPKIIELRLKYKFR 290
Cdd:PLN02822 198 ADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKLTAENKRKKKLRRYIVVEAIYQNSGQIAPLDEIVRLKEKYRFR 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 291 LILDETWSFGVLGRTGRGITEHQNVDAAEVDMIVGSLAGPLVAGGGFCAGSEEIVHHQRISAAAYTFSAALPALLSTTAS 370
Cdd:PLN02822 278 VLLDESNSFGVLGKSGRGLSEHFGVPIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSGYVFSASLPPYLASAAI 357

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 371 ATINILQNNPETVSQLRELTKAMRAQLDPRSDwVYCTSAPENPILILVIKPEVVAAKrltpDDQQfLLQDAVDESLAN-G 449
Cdd:PLN02822 358 TAIDVLEDNPSVLAKLKENIALLHKGLSDIPG-LSIGSNTLSPIVFLHLEKSTGSAK----EDLS-LLEHIADRMLKEdS 431

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 255947362 450 VLITRLK-TLEDNFEPkqvvPAALKVCVTTGLTKKEIEKAGTIIRHAITKVMSK 502
Cdd:PLN02822 432 VLVVVSKrSTLDKCRL----PVGIRLFVSAGHTESDILKASESLKRVAASVLKK 481
 
Name Accession Description Interval E-value
PLN02822 PLN02822
serine palmitoyltransferase
 51-502 6.14e-142

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 416.83  E-value: 6.14e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362  51 LFLFAVRYLLAPKySTKPGVVPLTEDEIDDLVDEWTPEPLVgsPTTLEEMEVDKrTVIVGPVGPKSKLaNGRTVTNLGSF 130
Cdd:PLN02822  43 LLIVVIVFLLSQK-SYKPPKRPLTEKEIDELCDEWTPEPLI--PPITEEMRPEP-PVLESAAGPHTII-NGKDVVNFASA 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 131 NFYNFNTNESLKEQAIQTLRAYGVGPCGPRGFYGTQDVHMKTEDDVAAFIGTAACIMYSQAFSTISSVIPAFSKRGDIIV 210
Cdd:PLN02822 118 NYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSVIPAFCKKGDIIV 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 211 ADKGVSFAIRKGIQISRSIVRWYEHNDMEDLERVLAKVTKEQARKPLTRRFIITEGLFESYGDMADLPKIIELRLKYKFR 290
Cdd:PLN02822 198 ADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKLTAENKRKKKLRRYIVVEAIYQNSGQIAPLDEIVRLKEKYRFR 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 291 LILDETWSFGVLGRTGRGITEHQNVDAAEVDMIVGSLAGPLVAGGGFCAGSEEIVHHQRISAAAYTFSAALPALLSTTAS 370
Cdd:PLN02822 278 VLLDESNSFGVLGKSGRGLSEHFGVPIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSGYVFSASLPPYLASAAI 357

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 371 ATINILQNNPETVSQLRELTKAMRAQLDPRSDwVYCTSAPENPILILVIKPEVVAAKrltpDDQQfLLQDAVDESLAN-G 449
Cdd:PLN02822 358 TAIDVLEDNPSVLAKLKENIALLHKGLSDIPG-LSIGSNTLSPIVFLHLEKSTGSAK----EDLS-LLEHIADRMLKEdS 431

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 255947362 450 VLITRLK-TLEDNFEPkqvvPAALKVCVTTGLTKKEIEKAGTIIRHAITKVMSK 502
Cdd:PLN02822 432 VLVVVSKrSTLDKCRL----PVGIRLFVSAGHTESDILKASESLKRVAASVLKK 481
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 104-498 3.65e-72

7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; 7-keto-8-aminopelargonate synthetase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 439926 [Multi-domain]  Cd Length: 385  Bit Score: 233.79  E-value: 3.65e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 104 KRTVIVGPVGPKSKLaNGRTVTNLGSFNFYNFNTNESLKEQAIQTLRAYGVGPCGPRGFYGTQDVHMKTEDDVAAFIGTA 183
Cdd:COG0156   20 YLRVLESPQGPRVTI-DGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTTPLHEELEEELAEFLGKE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 184 ACIMYSQAFSTISSVIPAFSKRGDIIVADKGVSFAIRKGIQISRSIVRWYEHNDMEDLERVLAKVTKEQarkpltRRFII 263
Cdd:COG0156   99 AALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKKARAAR------RKLIV 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 264 TEGLFESYGDMADLPKIIELRLKYKFRLILDETWSFGVLGRTGRGITEHQNVdAAEVDMIVGSLAGPLVAGGGFCAGSEE 343
Cdd:COG0156  173 TDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGL-EDRVDIIMGTLSKALGSSGGFVAGSKE 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 344 IVHHQRISAAAYTFSAALPALLSTTASATINILQNNPETVSQLRELTKAMRAQLDPRSdwvYCTSAPENPILILVIkPEV 423
Cdd:COG0156  252 LIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELG---FDLGPSESPIVPVIV-GDA 327

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255947362 424 VAAKRLTpddqQFLLQDAVdesLANGVlitrlktlednFEPkqVVP---AALKVCVTTGLTKKEIEKAGTIIRHAITK 498
Cdd:COG0156  328 ERALALA----DALLERGI---YVSAI-----------RPP--TVPkgtARLRITLSAAHTEEDIDRLLEALAEVGKE 385
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 122-397 4.15e-69

KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.


Pssm-ID: 99747 [Multi-domain]  Cd Length: 349  Bit Score: 224.75  E-value: 4.15e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 122 RTVTNLGSFNFYNFNTNESLKEQAIQTLRAYGVGPCGPRGFYGTQDVHMKTEDDVAAFIGTAACIMYSQAFSTISSVIPA 201
Cdd:cd06454    1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 202 FSKRGDIIVADKGVSFAIRKGIQISRSIVRWYEHNDMEDLERVLakvtkEQARKPLTRRFIITEGLFESYGDMADLPKII 281
Cdd:cd06454   81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLL-----REARRPYGKKLIVTEGVYSMDGDIAPLPELV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 282 ELRLKYKFRLILDETWSFGVLGRTGRGITEHQNvDAAEVDMIVGSLAGPLVAGGGFCAGSEEIVHHQRISAAAYTFSAAL 361
Cdd:cd06454  156 DLAKKYGAILFVDEAHSVGVYGPHGRGVEEFGG-LTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSL 234

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 255947362 362 PALLSTTASATINILQNNPETVSQLRELTKAMRAQL 397
Cdd:cd06454  235 PPAVAAAALAALEVLQGGPERRERLQENVRYLRRGL 270
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
122-488 1.01e-23

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 102.00  E-value: 1.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362  122 RTVTNLGSfNFYNFNTNESLKEQAIQTLRaygvgpCGPRGFYGTQDVHMKTEDDVAAFIGT--------AACIMYSQAFS 193
Cdd:pfam00155   1 TDKINLGS-NEYLGDTLPAVAKAEKDALA------GGTRNLYGPTDGHPELREALAKFLGRspvlkldrEAAVVFGSGAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362  194 TISSVIPAFSK-RGDIIVADKGVSFAIRKGIQISRSIVRWYE-------HNDMEDLERVLAKVTKeqarkpltrrFIITE 265
Cdd:pfam00155  74 ANIEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK----------VVLHT 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362  266 GLFESYGDMADLP---KIIELRLKYKFRLILDETWSFGVLGrTGRGITEHQNVDAAEVDMIVGSLAGPLVAGG---GFCA 339
Cdd:pfam00155 144 SPHNPTGTVATLEeleKLLDLAKEHNILLLVDEAYAGFVFG-SPDAVATRALLAEGPNLLVVGSFSKAFGLAGwrvGYIL 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362  340 GSEEIVHHQRISAAAYTFSAALPALLSTTASATINILQNNPETVSQLRELTKAMRAQLDpRSDWvYCTSAPENPILILVI 419
Cdd:pfam00155 223 GNAAVISQLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQ-AAGL-SVLPSQAGFFLLTGL 300

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255947362  420 KPEVVAAKrltpddQQFLLQDAvdeslanGVLITRLKTLEdnfepkqvVPAALKVCVtTGLTKKEIEKA 488
Cdd:pfam00155 301 DPETAKEL------AQVLLEEV-------GVYVTPGSSPG--------VPGWLRITV-AGGTEEELEEL 347
 
Name Accession Description Interval E-value
PLN02822 PLN02822
serine palmitoyltransferase
 51-502 6.14e-142

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 416.83  E-value: 6.14e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362  51 LFLFAVRYLLAPKySTKPGVVPLTEDEIDDLVDEWTPEPLVgsPTTLEEMEVDKrTVIVGPVGPKSKLaNGRTVTNLGSF 130
Cdd:PLN02822  43 LLIVVIVFLLSQK-SYKPPKRPLTEKEIDELCDEWTPEPLI--PPITEEMRPEP-PVLESAAGPHTII-NGKDVVNFASA 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 131 NFYNFNTNESLKEQAIQTLRAYGVGPCGPRGFYGTQDVHMKTEDDVAAFIGTAACIMYSQAFSTISSVIPAFSKRGDIIV 210
Cdd:PLN02822 118 NYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSVIPAFCKKGDIIV 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 211 ADKGVSFAIRKGIQISRSIVRWYEHNDMEDLERVLAKVTKEQARKPLTRRFIITEGLFESYGDMADLPKIIELRLKYKFR 290
Cdd:PLN02822 198 ADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKLTAENKRKKKLRRYIVVEAIYQNSGQIAPLDEIVRLKEKYRFR 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 291 LILDETWSFGVLGRTGRGITEHQNVDAAEVDMIVGSLAGPLVAGGGFCAGSEEIVHHQRISAAAYTFSAALPALLSTTAS 370
Cdd:PLN02822 278 VLLDESNSFGVLGKSGRGLSEHFGVPIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSGYVFSASLPPYLASAAI 357

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 371 ATINILQNNPETVSQLRELTKAMRAQLDPRSDwVYCTSAPENPILILVIKPEVVAAKrltpDDQQfLLQDAVDESLAN-G 449
Cdd:PLN02822 358 TAIDVLEDNPSVLAKLKENIALLHKGLSDIPG-LSIGSNTLSPIVFLHLEKSTGSAK----EDLS-LLEHIADRMLKEdS 431

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 255947362 450 VLITRLK-TLEDNFEPkqvvPAALKVCVTTGLTKKEIEKAGTIIRHAITKVMSK 502
Cdd:PLN02822 432 VLVVVSKrSTLDKCRL----PVGIRLFVSAGHTESDILKASESLKRVAASVLKK 481
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 126-502 2.76e-91

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 283.72  E-value: 2.76e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 126 NLGSFNFYNFNTNESLKEQAIQTLRAYGVGPCGPRGFYGTQDVHMKTEDDVAAFIGTAACIMYSQAFSTISSVIPAFSKR 205
Cdd:PLN03227   2 NFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAKR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 206 GDIIVADKGVSFAIRKGIQISRSIVRWYEHNDMEDLERVLAKVTKE--QARKPLT--RRFIITEGLFESYGDMADLPKII 281
Cdd:PLN03227  82 GDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLEQVRAQdvALKRKPTdqRRFLVVEGLYKNTGTLAPLKELV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 282 ELRLKYKFRLILDETWSFGVLGRTGRGITEHQNVD-AAEVDMIVGSLAGPLVAGGGFCAGSEEIVHHQRISAAAYTFSAA 360
Cdd:PLN03227 162 ALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLKpMVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCFSAS 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 361 LPALLSTTASATINILQNNPETVSQLRELTKAMRAQLDPRS--------DWVYCTSAPENPILILVIKpEVVAAKRLtpd 432
Cdd:PLN03227 242 APPFLAKADATATAGELAGPQLLNRLHDSIANLYSTLTNSShpyalklrNRLVITSDPISPIIYLRLS-DQEATRRT--- 317

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 433 DQQFLLQDAVDESLANGVLITRLKTLEDNFePKQVVPAALKVCVTTGLTKKEIEKAGTIIRHAITKVMSK 502
Cdd:PLN03227 318 DETLILDQIAHHSLSEGVAVVSTGGHVKKF-LQLVPPPCLRVVANASHTREDIDKLLTVLGEAVEAILCK 386
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 104-498 3.65e-72

7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; 7-keto-8-aminopelargonate synthetase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 439926 [Multi-domain]  Cd Length: 385  Bit Score: 233.79  E-value: 3.65e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 104 KRTVIVGPVGPKSKLaNGRTVTNLGSFNFYNFNTNESLKEQAIQTLRAYGVGPCGPRGFYGTQDVHMKTEDDVAAFIGTA 183
Cdd:COG0156   20 YLRVLESPQGPRVTI-DGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTTPLHEELEEELAEFLGKE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 184 ACIMYSQAFSTISSVIPAFSKRGDIIVADKGVSFAIRKGIQISRSIVRWYEHNDMEDLERVLAKVTKEQarkpltRRFII 263
Cdd:COG0156   99 AALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKKARAAR------RKLIV 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 264 TEGLFESYGDMADLPKIIELRLKYKFRLILDETWSFGVLGRTGRGITEHQNVdAAEVDMIVGSLAGPLVAGGGFCAGSEE 343
Cdd:COG0156  173 TDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGL-EDRVDIIMGTLSKALGSSGGFVAGSKE 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 344 IVHHQRISAAAYTFSAALPALLSTTASATINILQNNPETVSQLRELTKAMRAQLDPRSdwvYCTSAPENPILILVIkPEV 423
Cdd:COG0156  252 LIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELG---FDLGPSESPIVPVIV-GDA 327

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255947362 424 VAAKRLTpddqQFLLQDAVdesLANGVlitrlktlednFEPkqVVP---AALKVCVTTGLTKKEIEKAGTIIRHAITK 498
Cdd:COG0156  328 ERALALA----DALLERGI---YVSAI-----------RPP--TVPkgtARLRITLSAAHTEEDIDRLLEALAEVGKE 385
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 122-397 4.15e-69

KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.


Pssm-ID: 99747 [Multi-domain]  Cd Length: 349  Bit Score: 224.75  E-value: 4.15e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 122 RTVTNLGSFNFYNFNTNESLKEQAIQTLRAYGVGPCGPRGFYGTQDVHMKTEDDVAAFIGTAACIMYSQAFSTISSVIPA 201
Cdd:cd06454    1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 202 FSKRGDIIVADKGVSFAIRKGIQISRSIVRWYEHNDMEDLERVLakvtkEQARKPLTRRFIITEGLFESYGDMADLPKII 281
Cdd:cd06454   81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLL-----REARRPYGKKLIVTEGVYSMDGDIAPLPELV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 282 ELRLKYKFRLILDETWSFGVLGRTGRGITEHQNvDAAEVDMIVGSLAGPLVAGGGFCAGSEEIVHHQRISAAAYTFSAAL 361
Cdd:cd06454  156 DLAKKYGAILFVDEAHSVGVYGPHGRGVEEFGG-LTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSL 234

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 255947362 362 PALLSTTASATINILQNNPETVSQLRELTKAMRAQL 397
Cdd:cd06454  235 PPAVAAAALAALEVLQGGPERRERLQENVRYLRRGL 270
PLN02483 PLN02483
serine palmitoyltransferase
 116-397 1.68e-46

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 168.79  E-value: 1.68e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 116 SKLANGRTVTNLGSFNFYNF-NTNESLKEQAIQTLRAYGVGPCGPRGFYGTQDVHMKTEDDVAAFIGTAACIMYSQAFST 194
Cdd:PLN02483  94 KRTTKTRRCLNLGSYNYLGFaAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYAT 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 195 ISSVIPAFSKRGDIIVADKGVSFAIRKGIQISRSIVRWYEHNDMEDLERVLAK-VTKEQAR--KPLTRRFIITEGLFESY 271
Cdd:PLN02483 174 NSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREqIAEGQPRthRPWKKIIVIVEGIYSME 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 272 GDMADLPKIIELRLKYKFRLILDETWSFGVLGRTGRGITEHQNVDAAEVDMIVGSLAGPLVAGGGFCAGSEEIVHHQRIS 351
Cdd:PLN02483 254 GELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRT 333

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 255947362 352 AAAYTFSAAL-PALLSTTASATINILQNN-----PETVSQLRELTKAMRAQL 397
Cdd:PLN02483 334 CPAHLYATSMsPPAVQQVISAIKVILGEDgtnrgAQKLAQIRENSNFFRSEL 385
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 107-397 4.49e-46

2-amino-3-ketobutyrate coenzyme A ligase; Provisional


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 165.37  E-value: 4.49e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 107 VIVGPVGPKSKLANGRTVTNLGSFNFYNFNTNESLKEQAIQTLRAYGVGPCGPRGFYGTQDVHMKTEDDVAAFIGTAACI 186
Cdd:PRK06939  27 VITSPQGADITVADGKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVRFICGTQDLHKELEEKLAKFLGTEDAI 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 187 MYSQAFSTISSVIPAFSKRGDIIVADKGVSFAIRKGIQISRS-IVRwYEHNDMEDLERVLAKVTKEQARKpltrRFIITE 265
Cdd:PRK06939 107 LYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAkRYR-YANNDMADLEAQLKEAKEAGARH----KLIATD 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 266 GLFESYGDMADLPKIIELRLKYKFRLILDETWSFGVLGRTGRGITEHQNVDaAEVDMIVGSLAGPLV-AGGGFCAGSEEI 344
Cdd:PRK06939 182 GVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVM-DRVDIITGTLGKALGgASGGYTAGRKEV 260

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 255947362 345 VHHQRISAAAYTFSAALPALLSTTASATINILQNNPETVSQLRELTKAMRAQL 397
Cdd:PRK06939 261 IDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGM 313
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 105-496 1.38e-40

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 150.31  E-value: 1.38e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 105 RTVIVGPVGPKSKLaNGRTVTNLGSFNFYNFNTNESLKEQAIQTLRAYGVGPCGPRGFYGTQDVHMKTEDDVAAFIGTAA 184
Cdd:PRK05958  23 LRPREGGAGRWLVV-DGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTGNSPAHEALEEELAEWFGAER 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 185 CIMYSQAFSTISSVIPAFSKRGDIIVADKGVSFAIRKGIQISRSIVRWYEHNDMEDLERVLAKVTKEQArkpltrrFIIT 264
Cdd:PRK05958 102 ALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLAKWRAGRA-------LIVT 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 265 EGLFESYGDMADLPKIIELRLKYKFRLILDETWSFGVLGRTGRGITEHQNVDAAEVDMIVGSLAGPLVAGGGFCAGSEEI 344
Cdd:PRK05958 175 ESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDVILVGTLGKALGSSGAAVLGSETL 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 345 VHHQRISAAAYTFSAALPALLSTTASATINILQNNPETVSQLRELTKAMRAQLDPRSdwvYCTSAPENPILILVIkpevv 424
Cdd:PRK05958 255 IDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALG---FQLMDSQSAIQPLIV----- 326

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255947362 425 aakrltPDDQQFLlqdAVDESL-ANGVLIT--RLKTlednfepkqvVP---AALKVCVTTGLTKKEIEKAGTIIRHAI 496
Cdd:PRK05958 327 ------GDNERAL---ALAAALqEQGFWVGaiRPPT----------VPagtSRLRITLTAAHTEADIDRLLEALAEAL 385
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
122-488 1.01e-23

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 102.00  E-value: 1.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362  122 RTVTNLGSfNFYNFNTNESLKEQAIQTLRaygvgpCGPRGFYGTQDVHMKTEDDVAAFIGT--------AACIMYSQAFS 193
Cdd:pfam00155   1 TDKINLGS-NEYLGDTLPAVAKAEKDALA------GGTRNLYGPTDGHPELREALAKFLGRspvlkldrEAAVVFGSGAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362  194 TISSVIPAFSK-RGDIIVADKGVSFAIRKGIQISRSIVRWYE-------HNDMEDLERVLAKVTKeqarkpltrrFIITE 265
Cdd:pfam00155  74 ANIEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK----------VVLHT 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362  266 GLFESYGDMADLP---KIIELRLKYKFRLILDETWSFGVLGrTGRGITEHQNVDAAEVDMIVGSLAGPLVAGG---GFCA 339
Cdd:pfam00155 144 SPHNPTGTVATLEeleKLLDLAKEHNILLLVDEAYAGFVFG-SPDAVATRALLAEGPNLLVVGSFSKAFGLAGwrvGYIL 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362  340 GSEEIVHHQRISAAAYTFSAALPALLSTTASATINILQNNPETVSQLRELTKAMRAQLDpRSDWvYCTSAPENPILILVI 419
Cdd:pfam00155 223 GNAAVISQLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQ-AAGL-SVLPSQAGFFLLTGL 300

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255947362  420 KPEVVAAKrltpddQQFLLQDAvdeslanGVLITRLKTLEdnfepkqvVPAALKVCVtTGLTKKEIEKA 488
Cdd:pfam00155 301 DPETAKEL------AQVLLEEV-------GVYVTPGSSPG--------VPGWLRITV-AGGTEEELEEL 347
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 143-398 5.40e-23

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 101.08  E-value: 5.40e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 143 EQAIQTLRAYGVGPCGPRGFYGTQDVHMKTEDDVAAFIGTAACIMYSQAF-------STISSVIPafskrGDIIVADKGV 215
Cdd:PRK13392  67 GAMVDALDRYGAGAGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYvsndaalSTLGKLLP-----GCVILSDALN 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 216 SFAIRKGIQISRSIVRWYEHNDMEDLERVLAKVtkeqarkPLTR-RFIITEGLFESYGDMADLPKIIELRLKYKFRLILD 294
Cdd:PRK13392 142 HASMIEGIRRSGAEKQVFRHNDLADLEEQLASV-------DPDRpKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVD 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 295 ETWSFGVLGRTGRGITEHQNVdAAEVDMIVGSLAGPLVAGGGFCAGSEEIVHHQRISAAAYTFSAALPALLSTTASATIN 374
Cdd:PRK13392 215 EVHAVGLYGARGGGIAERDGL-MDRIDMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIR 293

                        250       260
                 ....*....|....*....|....
gi 255947362 375 ILQNNPETVSQLRELTKAMRAQLD 398
Cdd:PRK13392 294 HLKTSQTERDAHQDRVAALKAKLN 317
PRK07505 PRK07505
hypothetical protein; Provisional
 118-373 4.82e-10

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 61.53  E-value: 4.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 118 LANGRTVTNLGSFNFYNFNTNESLKEQAIQTLRAYGV-GPCGPRGFYGTQdVHMKTEDDVAAFIGtAACIMYSQAFSTIS 196
Cdd:PRK07505  42 LADGHTFVNFVSCSYLGLDTHPAIIEGAVDALKRTGSlHLSSSRTRVRSQ-ILKDLEEALSELFG-ASVLTFTSCSAAHL 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 197 SVIP-----AFSKRGDII-VADKG--VSFAIRKGIQISRSIVRWYEHNDMEDLERVlakvtKEQARKPltrrFIITEGLF 268
Cdd:PRK07505 120 GILPllasgHLTGGVPPHmVFDKNahASLNILKGICADETEVETIDHNDLDALEDI-----CKTNKTV----AYVADGVY 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 269 eSYGDMADLPKIIELRLKYKFRLILDETWSFGVLGRTGRG-ITEHQNVDAAEVDMIVGSLAGPLVAGGGFCA-GSEEIVH 346
Cdd:PRK07505 191 -SMGGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGyVRSELDYRLNERTIIAASLGKAFGASGGVIMlGDAEQIE 269

                        250       260
                 ....*....|....*....|....*....
gi 255947362 347 HQRISAAAYTFSAAL--PALLSTTASATI 373
Cdd:PRK07505 270 LILRYAGPLAFSQSLnvAALGAILASAEI 298
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 124-309 1.57e-09

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 59.79  E-value: 1.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 124 VTNlgsfNFYNFNTNESLKEQAIQTLRAY-------GVGPCGPRGFYGTQDVHMKTEDDVAAFIGTAACIMYSQAFSTIS 196
Cdd:PRK05937  10 VTN----DFLGFSRSDTLVHEVEKRYRLYcrqfphaQLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 197 SVIPAFSKRGDIIVADKGVSFAIRKGIQISRSIVRWYEHNDMEDLERVLAKVTKEQARkpltRRFIITEGLFESYGDMAD 276
Cdd:PRK05937  86 GLCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLESCRQRSFG----RIFIFVCSVYSFKGTLAP 161

                        170       180       190
                 ....*....|....*....|....*....|...
gi 255947362 277 LPKIIELRLKYKFRLILDETWSFGVLGRTGRGI 309
Cdd:PRK05937 162 LEQIIALSKKYHAHLIVDEAHAMGIFGDDGKGF 194
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
222-397 4.89e-08

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 55.02  E-value: 4.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 222 GIQISRSIVRWYEHNDMEDLERvlakvtkeqarkpLTRRF----IITEGLFESYGDMADLPKIIELRLKYKFRLILDETW 297
Cdd:PRK07179 154 GVRAAGAQAHPFRHNDVDHLRR-------------QIERHgpgiIVVDSVYSTTGTIAPLADIVDIAEEFGCVLVVDESH 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 298 SFGVLGRTGRGITEHQNVdAAEVDMIVGSLAGPLVAGGGFCAGSEEIvhhqrisaaAYTFS-AALPALLSTTA------- 369
Cdd:PRK07179 221 SLGTHGPQGAGLVAELGL-TSRVHFITASLAKAFAGRAGIITCPREL---------AEYVPfVSYPAIFSSTLlpheiag 290

                        170       180
                 ....*....|....*....|....*....
gi 255947362 370 -SATINILQNNPETVSQLRELTKAMRAQL 397
Cdd:PRK07179 291 lEATLEVIESADDRRARLHANARFLREGL 319
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 173-304 9.80e-03

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: 38.34  E-value: 9.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255947362 173 EDDVAAFIGTAACIMYSQAFSTISSVIPAFSKRGDIIVADK---GVSFAI------RKGIQisrsiVRWYEHNDMEDLER 243
Cdd:cd00614   46 EKKLAALEGGEAALAFSSGMAAISTVLLALLKAGDHVVASDdlyGGTYRLferllpKLGIE-----VTFVDPDDPEALEA 120

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255947362 244 VLAKVTKeqarkpltrrfIItegLFES----YGDMADLPKIIELRLKYKFRLILDETWSFGVLGR 304
Cdd:cd00614  121 AIKPETK-----------LV---YVESptnpTLKVVDIEAIAELAHEHGALLVVDNTFATPYLQR 171
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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