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Conserved domains on  [gi|768013993|ref|XP_011527582|]
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serine palmitoyltransferase 3 isoform X2 [Homo sapiens]

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) ...
 11-358 0e+00

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 PLN02483:

Pssm-ID: 450240 [Multi-domain]  Cd Length: 489  Bit Score: 527.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  11 GGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLE 90
Cdd:PLN02483 142 GGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLE 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  91 KLLRDAVIYGQPRTRRAWKKILILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDPHE 170
Cdd:PLN02483 222 EVLREQIAEGQPRTHRPWKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPAD 301

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 171 VDVLMGTFTKSFGASGGYIAGRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSLKLIMGLDGTTQGLQRVQQLAKNTRYF 250
Cdd:PLN02483 302 VDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILGEDGTNRGAQKLAQIRENSNFF 381

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 251 RQRLQEMGFIIYGNENASVVPLLLYMPGKVAAFARHMLEKKIGVVVVGFPATPLAEARARFCVSAAHTREMLDTVLEALD 330
Cdd:PLN02483 382 RSELQKMGFEVLGDNDSPVMPIMLYNPAKIPAFSRECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVIS 461

                        330       340
                 ....*....|....*....|....*...
gi 768013993 331 EMGDLLQLKYSRHKKSARPELYDETSFE 358
Cdd:PLN02483 462 EVGDLVGIKYFPAEPKKQEQVKKFIKLE 489
 
Name Accession Description Interval E-value
PLN02483 PLN02483
serine palmitoyltransferase
 11-358 0e+00

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 527.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  11 GGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLE 90
Cdd:PLN02483 142 GGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLE 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  91 KLLRDAVIYGQPRTRRAWKKILILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDPHE 170
Cdd:PLN02483 222 EVLREQIAEGQPRTHRPWKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPAD 301

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 171 VDVLMGTFTKSFGASGGYIAGRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSLKLIMGLDGTTQGLQRVQQLAKNTRYF 250
Cdd:PLN02483 302 VDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILGEDGTNRGAQKLAQIRENSNFF 381

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 251 RQRLQEMGFIIYGNENASVVPLLLYMPGKVAAFARHMLEKKIGVVVVGFPATPLAEARARFCVSAAHTREMLDTVLEALD 330
Cdd:PLN02483 382 RSELQKMGFEVLGDNDSPVMPIMLYNPAKIPAFSRECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVIS 461

                        330       340
                 ....*....|....*....|....*...
gi 768013993 331 EMGDLLQLKYSRHKKSARPELYDETSFE 358
Cdd:PLN02483 462 EVGDLVGIKYFPAEPKKQEQVKKFIKLE 489
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 12-333 3.32e-154

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: 437.38  E-value: 3.32e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  12 GTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEK 91
Cdd:cd06454   43 GTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLSTLAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEK 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  92 LLRDAviygqprtRRAWKKILILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGlDPHEV 171
Cdd:cd06454  123 LLREA--------RRPYGKKLIVTEGVYSMDGDIAPLPELVDLAKKYGAILFVDEAHSVGVYGPHGRGVEEFGG-LTDDV 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 172 DVLMGTFTKSFGASGGYIAGRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSLKLIMGldgttqGLQRVQQLAKNTRYFR 251
Cdd:cd06454  194 DIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAAAALAALEVLQG------GPERRERLQENVRYLR 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 252 QRLQEMGFIIYGNENASVVPLLLYMPGKVAAFARHMLEKKIGVVVVGFPATPLAEARARFCVSAAHTREMLDTVLEALDE 331
Cdd:cd06454  268 RGLKELGFPVGGSPSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVPRGTARLRISLSAAHTKEDIDRLLEALKE 347


                 ..
gi 768013993 332 MG 333
Cdd:cd06454  348 VG 349
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 10-334 7.04e-121

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: 353.97  E-value: 7.04e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  10 VGGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSL 89
Cdd:COG0156   77 VSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDL 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  90 EKLLRDAviygqprtrRAWKKILILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDpH 169
Cdd:COG0156  157 ERLLKKA---------RAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLE-D 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 170 EVDVLMGTFTKSFGASGGYIAGRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSLKLIMGLDgttqglQRVQQLAKNTRY 249
Cdd:COG0156  227 RVDIIMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEP------ELRERLWENIAY 300

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 250 FRQRLQEMGFIIYGNENAsVVPLLLYMPGKVAAFARHMLEKKIGVVVVGFPATPLAEARARFCVSAAHTREMLDTVLEAL 329
Cdd:COG0156  301 FREGLKELGFDLGPSESP-IVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEAL 379


                 ....*
gi 768013993 330 DEMGD 334
Cdd:COG0156  380 AEVGK 384
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 10-338 3.18e-59

5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an enzyme for one of two routes to the heme precursor 5-aminolevulinate. The protein is a pyridoxal phosphate-dependent enzyme related to 2-amino-3-ketobutyrate CoA tranferase and 8-amino-7-oxononanoate synthase. This enzyme appears restricted to the alpha Proteobacteria and mitochondrial derivatives. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273820 [Multi-domain]  Cd Length: 402  Bit Score: 196.49  E-value: 3.18e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993   10 VGGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGK--GCLILSDELNHTSLVLGARLSGATIRIFKHNNTQ 87
Cdd:TIGR01821  85 ISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIipGCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVA 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993   88 SLEKLLRdAVIYGQPRtrrawkkiLILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLd 167
Cdd:TIGR01821 165 HLEKLLQ-SVDPNRPK--------IIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGL- 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  168 PHEVDVLMGTFTKSFGASGGYIAGRKDLVDYLRVHSHSAVYASSMSPPI---AEQIIRSLKlimgldgTTQGLQRVQQla 244
Cdd:TIGR01821 235 MHRIDIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIaagATASIRHLK-------ESQDLRRAHQ-- 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  245 KNTRYFRQRLQEMGFIIYGNEnASVVPLLLYMPGKvAAFARHMLEKKIGVVV--VGFPATPLAEARARFCVSAAHTREML 322
Cdd:TIGR01821 306 ENVKRLKNLLEALGIPVIPNP-SHIVPVIIGDAAL-CKKVSDLLLNKHGIYVqpINYPTVPRGTERLRITPTPAHTDKMI 383

                         330
                  ....*....|....*.
gi 768013993  323 DTVLEALDEMGDLLQL 338
Cdd:TIGR01821 384 DDLVEALLLVWDRLGL 399
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
12-329 1.23e-46

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 162.09  E-value: 1.23e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993   12 GTLDKHKELEDLVAKF--------LNVEAAMVFGMGFATNSMNIPALVG-KGCLILSDELNHTSLVLGARLSGATIRIFK 82
Cdd:pfam00155  36 GPTDGHPELREALAKFlgrspvlkLDREAAVVFGSGAGANIEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYP 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993   83 -------HNNTQSLEKLLRDAVIygqprtrrawkkiLILVEGVYSMEGSIVHLPQ---IIALKKKYKAYLYIDEAHSIGA 152
Cdd:pfam00155 116 lydsndfHLDFDALEAALKEKPK-------------VVLHTSPHNPTGTVATLEElekLLDLAKEHNILLLVDEAYAGFV 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  153 VGPTGRGVTEFFgLDPHEVDVLMGTFTKSFGASG---GYIAGRKDLVDYLRVHShSAVYASSMSPPIAEQIIRSLKLIMG 229
Cdd:pfam00155 183 FGSPDAVATRAL-LAEGPNLLVVGSFSKAFGLAGwrvGYILGNAAVISQLRKLA-RPFYSSTHLQAAAAAALSDPLLVAS 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  230 ldgttQGLQRVQQLAKNTRYFRQRLQEMGFIIYGNENAsVVPLLLYMPGKVAAFARHMLEKKiGVVVVGFpATPLAEARA 309
Cdd:pfam00155 261 -----ELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAG-FFLLTGLDPETAKELAQVLLEEV-GVYVTPG-SSPGVPGWL 332

                         330       340
                  ....*....|....*....|
gi 768013993  310 RFCVsAAHTREMLDTVLEAL 329
Cdd:pfam00155 333 RITV-AGGTEEELEELLEAI 351
 
Name Accession Description Interval E-value
PLN02483 PLN02483
serine palmitoyltransferase
 11-358 0e+00

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 527.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  11 GGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLE 90
Cdd:PLN02483 142 GGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLE 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  91 KLLRDAVIYGQPRTRRAWKKILILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDPHE 170
Cdd:PLN02483 222 EVLREQIAEGQPRTHRPWKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPAD 301

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 171 VDVLMGTFTKSFGASGGYIAGRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSLKLIMGLDGTTQGLQRVQQLAKNTRYF 250
Cdd:PLN02483 302 VDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILGEDGTNRGAQKLAQIRENSNFF 381

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 251 RQRLQEMGFIIYGNENASVVPLLLYMPGKVAAFARHMLEKKIGVVVVGFPATPLAEARARFCVSAAHTREMLDTVLEALD 330
Cdd:PLN02483 382 RSELQKMGFEVLGDNDSPVMPIMLYNPAKIPAFSRECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVIS 461

                        330       340
                 ....*....|....*....|....*...
gi 768013993 331 EMGDLLQLKYSRHKKSARPELYDETSFE 358
Cdd:PLN02483 462 EVGDLVGIKYFPAEPKKQEQVKKFIKLE 489
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 12-333 3.32e-154

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: 437.38  E-value: 3.32e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  12 GTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEK 91
Cdd:cd06454   43 GTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLSTLAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEK 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  92 LLRDAviygqprtRRAWKKILILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGlDPHEV 171
Cdd:cd06454  123 LLREA--------RRPYGKKLIVTEGVYSMDGDIAPLPELVDLAKKYGAILFVDEAHSVGVYGPHGRGVEEFGG-LTDDV 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 172 DVLMGTFTKSFGASGGYIAGRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSLKLIMGldgttqGLQRVQQLAKNTRYFR 251
Cdd:cd06454  194 DIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAAAALAALEVLQG------GPERRERLQENVRYLR 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 252 QRLQEMGFIIYGNENASVVPLLLYMPGKVAAFARHMLEKKIGVVVVGFPATPLAEARARFCVSAAHTREMLDTVLEALDE 331
Cdd:cd06454  268 RGLKELGFPVGGSPSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVPRGTARLRISLSAAHTKEDIDRLLEALKE 347


                 ..
gi 768013993 332 MG 333
Cdd:cd06454  348 VG 349
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 10-334 7.04e-121

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: 353.97  E-value: 7.04e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  10 VGGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSL 89
Cdd:COG0156   77 VSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDL 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  90 EKLLRDAviygqprtrRAWKKILILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDpH 169
Cdd:COG0156  157 ERLLKKA---------RAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLE-D 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 170 EVDVLMGTFTKSFGASGGYIAGRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSLKLIMGLDgttqglQRVQQLAKNTRY 249
Cdd:COG0156  227 RVDIIMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEP------ELRERLWENIAY 300

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 250 FRQRLQEMGFIIYGNENAsVVPLLLYMPGKVAAFARHMLEKKIGVVVVGFPATPLAEARARFCVSAAHTREMLDTVLEAL 329
Cdd:COG0156  301 FREGLKELGFDLGPSESP-IVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEAL 379


                 ....*
gi 768013993 330 DEMGD 334
Cdd:COG0156  380 AEVGK 384
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 12-338 2.79e-88

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 271.30  E-value: 2.79e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  12 GTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEK 91
Cdd:PRK06939  84 GTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEA 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  92 LLRDAVIYGQprtrrawKKILILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDpHEV 171
Cdd:PRK06939 164 QLKEAKEAGA-------RHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVM-DRV 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 172 DVLMGTFTKSF-GASGGYIAGRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSLKLIMgldgttQGLQRVQQLAKNTRYF 250
Cdd:PRK06939 236 DIITGTLGKALgGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLE------ESDELRDRLWENARYF 309

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 251 RQRLQEMGFIIYGNENAsVVPLLLYMPGKVAAFARHMLEKkiGVVVVGF--PATPLAEARARFCVSAAHTREMLDTVLEA 328
Cdd:PRK06939 310 REGMTAAGFTLGPGEHP-IIPVMLGDAKLAQEFADRLLEE--GVYVIGFsfPVVPKGQARIRTQMSAAHTKEQLDRAIDA 386

                        330
                 ....*....|
gi 768013993 329 LDEMGDLLQL 338
Cdd:PRK06939 387 FEKVGKELGV 396
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 10-333 7.48e-87

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 267.02  E-value: 7.48e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  10 VGGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSL 89
Cdd:PRK05958  79 VTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDAL 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  90 EKLLRdaviygQPRTRRAWkkilILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDPH 169
Cdd:PRK05958 159 EALLA------KWRAGRAL----IVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGE 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 170 EVDVLMGTFTKSFGASGGYIAGRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSLKLIMGLDgttqglQRVQQLAKNTRY 249
Cdd:PRK05958 229 PDVILVGTLGKALGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREP------ERRERLAALIAR 302

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 250 FRQRLQEMGFIIYGNENAsVVPLLLYMPGKVAAFARHMLEKkiGVVVVGF--PATPLAEARARFCVSAAHTREMLDTVLE 327
Cdd:PRK05958 303 LRAGLRALGFQLMDSQSA-IQPLIVGDNERALALAAALQEQ--GFWVGAIrpPTVPAGTSRLRITLTAAHTEADIDRLLE 379


                 ....*.
gi 768013993 328 ALDEMG 333
Cdd:PRK05958 380 ALAEAL 385
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 10-338 3.18e-59

5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an enzyme for one of two routes to the heme precursor 5-aminolevulinate. The protein is a pyridoxal phosphate-dependent enzyme related to 2-amino-3-ketobutyrate CoA tranferase and 8-amino-7-oxononanoate synthase. This enzyme appears restricted to the alpha Proteobacteria and mitochondrial derivatives. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273820 [Multi-domain]  Cd Length: 402  Bit Score: 196.49  E-value: 3.18e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993   10 VGGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGK--GCLILSDELNHTSLVLGARLSGATIRIFKHNNTQ 87
Cdd:TIGR01821  85 ISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIipGCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVA 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993   88 SLEKLLRdAVIYGQPRtrrawkkiLILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLd 167
Cdd:TIGR01821 165 HLEKLLQ-SVDPNRPK--------IIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGL- 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  168 PHEVDVLMGTFTKSFGASGGYIAGRKDLVDYLRVHSHSAVYASSMSPPI---AEQIIRSLKlimgldgTTQGLQRVQQla 244
Cdd:TIGR01821 235 MHRIDIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIaagATASIRHLK-------ESQDLRRAHQ-- 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  245 KNTRYFRQRLQEMGFIIYGNEnASVVPLLLYMPGKvAAFARHMLEKKIGVVV--VGFPATPLAEARARFCVSAAHTREML 322
Cdd:TIGR01821 306 ENVKRLKNLLEALGIPVIPNP-SHIVPVIIGDAAL-CKKVSDLLLNKHGIYVqpINYPTVPRGTERLRITPTPAHTDKMI 383

                         330
                  ....*....|....*.
gi 768013993  323 DTVLEALDEMGDLLQL 338
Cdd:TIGR01821 384 DDLVEALLLVWDRLGL 399
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 10-338 1.96e-54

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 184.29  E-value: 1.96e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  10 VGGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGK--GCLILSDELNHTSLVLGARLSGATIRIFKHNNTQ 87
Cdd:PRK13392  86 ISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLlpGCVILSDALNHASMIEGIRRSGAEKQVFRHNDLA 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  88 SLEKLLRdAVIYGQPRtrrawkkiLILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLd 167
Cdd:PRK13392 166 DLEEQLA-SVDPDRPK--------LIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGL- 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 168 PHEVDVLMGTFTKSFGASGGYIAGRKDLVDYLRVHSHSAVYASSMSPPIAEQI---IRSLKlimgldgtTQGLQRvQQLA 244
Cdd:PRK13392 236 MDRIDMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGAtaaIRHLK--------TSQTER-DAHQ 306

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 245 KNTRYFRQRLQEMGFIIYGNEnASVVPLLLYMPGKVAAFA-RHMLEKKIGVVVVGFPATPLAEARARFCVSAAHTREMLD 323
Cdd:PRK13392 307 DRVAALKAKLNANGIPVMPSP-SHIVPVMVGDPTLCKAISdRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDID 385

                        330
                 ....*....|....*
gi 768013993 324 TVLEALDEMGDLLQL 338
Cdd:PRK13392 386 ALVAALVAIWDRLEL 400
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 12-345 1.33e-47

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 165.85  E-value: 1.33e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  12 GTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEK 91
Cdd:PLN03227  40 GTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAKRGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRR 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  92 LL-----RDAVIYGQPRTRRAWkkilILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGL 166
Cdd:PLN03227 120 VLeqvraQDVALKRKPTDQRRF----LVVEGLYKNTGTLAPLKELVALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGL 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 167 DP-HEVDVLMGTFTKSFGASGGYIAGRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSlklimgLDGTTQGLQRVQQLAK 245
Cdd:PLN03227 196 KPmVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCFSASAPPFLAKADATA------TAGELAGPQLLNRLHD 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 246 NTRYFRQRLQ----------EMGFIIYGNENASVVPLLLY-MPGK--------VAAFARHMLEKKIGVVVVGFPATPLAE 306
Cdd:PLN03227 270 SIANLYSTLTnsshpyalklRNRLVITSDPISPIIYLRLSdQEATrrtdetliLDQIAHHSLSEGVAVVSTGGHVKKFLQ 349

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 768013993 307 ARA----RFCVSAAHTREMLDTVLEALDEMGDLLQLKYSRHKK 345
Cdd:PLN03227 350 LVPppclRVVANASHTREDIDKLLTVLGEAVEAILCKIIDENK 392
PLN02822 PLN02822
serine palmitoyltransferase
 12-329 2.39e-47

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 167.23  E-value: 2.39e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  12 GTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEK 91
Cdd:PLN02822 151 GTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRN 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  92 LLrDAVIYGQPRTRRAWKkiLILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDPHEV 171
Cdd:PLN02822 231 TL-EKLTAENKRKKKLRR--YIVVEAIYQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEKI 307

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 172 DVLMGTFTKSFGASGGYIAGRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSLKLimgLDGTTQGLQRvqqLAKNTRYFR 251
Cdd:PLN02822 308 DIITAAMGHALATEGGFCTGSARVVDHQRLSSSGYVFSASLPPYLASAAITAIDV---LEDNPSVLAK---LKENIALLH 381

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 252 QRLQEM-GFIIYGNENASVVPLLLYMPGKVA--------AFARHMLeKKIGVVVVGFPATPLAEARA----RFCVSAAHT 318
Cdd:PLN02822 382 KGLSDIpGLSIGSNTLSPIVFLHLEKSTGSAkedlslleHIADRML-KEDSVLVVVSKRSTLDKCRLpvgiRLFVSAGHT 460

                        330
                 ....*....|.
gi 768013993 319 REMLDTVLEAL 329
Cdd:PLN02822 461 ESDILKASESL 471
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
12-329 1.23e-46

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 162.09  E-value: 1.23e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993   12 GTLDKHKELEDLVAKF--------LNVEAAMVFGMGFATNSMNIPALVG-KGCLILSDELNHTSLVLGARLSGATIRIFK 82
Cdd:pfam00155  36 GPTDGHPELREALAKFlgrspvlkLDREAAVVFGSGAGANIEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYP 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993   83 -------HNNTQSLEKLLRDAVIygqprtrrawkkiLILVEGVYSMEGSIVHLPQ---IIALKKKYKAYLYIDEAHSIGA 152
Cdd:pfam00155 116 lydsndfHLDFDALEAALKEKPK-------------VVLHTSPHNPTGTVATLEElekLLDLAKEHNILLLVDEAYAGFV 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  153 VGPTGRGVTEFFgLDPHEVDVLMGTFTKSFGASG---GYIAGRKDLVDYLRVHShSAVYASSMSPPIAEQIIRSLKLIMG 229
Cdd:pfam00155 183 FGSPDAVATRAL-LAEGPNLLVVGSFSKAFGLAGwrvGYILGNAAVISQLRKLA-RPFYSSTHLQAAAAAALSDPLLVAS 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  230 ldgttQGLQRVQQLAKNTRYFRQRLQEMGFIIYGNENAsVVPLLLYMPGKVAAFARHMLEKKiGVVVVGFpATPLAEARA 309
Cdd:pfam00155 261 -----ELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAG-FFLLTGLDPETAKELAQVLLEEV-GVYVTPG-SSPGVPGWL 332

                         330       340
                  ....*....|....*....|
gi 768013993  310 RFCVsAAHTREMLDTVLEAL 329
Cdd:pfam00155 333 RITV-AGGTEEELEELLEAI 351
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
20-338 3.00e-37

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 138.60  E-value: 3.00e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  20 LEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLRDaviY 99
Cdd:PRK07179 104 FEKKLAAFTGFESCLLCQSGWAANVGLLQTIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIER---H 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 100 GQPrtrrawkkiLILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDpHEVDVLMGTFT 179
Cdd:PRK07179 181 GPG---------IIVVDSVYSTTGTIAPLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLT-SRVHFITASLA 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 180 KSFGASGGYIAGRKDLVDYLRVHSHSAVYASSMSPpiaeqiirslKLIMGLDGTT----QGLQRVQQLAKNTRYFRQRLQ 255
Cdd:PRK07179 251 KAFAGRAGIITCPRELAEYVPFVSYPAIFSSTLLP----------HEIAGLEATLevieSADDRRARLHANARFLREGLS 320

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 256 EMGFIIYGNENasVVPLllyMPGKVAA--FARHMLEKK--IGVVVVGfPATPLAEARARFCVSAAHTREMLDTVLEALDE 331
Cdd:PRK07179 321 ELGYNIRSESQ--IIAL---ETGSERNteVLRDALEERnvFGAVFCA-PATPKNRNLIRLSLNADLTASDLDRVLEVCRE 394


                 ....*..
gi 768013993 332 MGDLLQL 338
Cdd:PRK07179 395 ARDEVDL 401
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 4-339 9.99e-26

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 107.45  E-value: 9.99e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993   4 GQALfpVGGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGKGCL--------------ILSDELNHTSLVL 69
Cdd:PLN02955 138 GSAL--ICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMVAIGSVASLlaasgkplknekvaIFSDALNHASIID 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  70 GARLS----GATIRIFKHNNTQSLEKLLRDAVIygqprtrrawKKILILVEGVYSMEGSIVHLPQIIALKKKYKAYLYID 145
Cdd:PLN02955 216 GVRLAerqgNVEVFVYRHCDMYHLNSLLSSCKM----------KRKVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVID 285

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 146 EAHSIGAVGPTGRGVTEFFGLDPhEVDVLMGTFTKSFGASGGYIAGRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSLK 225
Cdd:PLN02955 286 DAHGTFVCGENGGGVAEEFNCEA-DVDLCVGTLSKAAGCHGGFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVV 364

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 226 LimgldgTTQGLQRVQQLAKNTRYFRqrlqEMGFIIYGnenASVVPLLLYMPGKVAAFARHMLEKKIGVVVVGFPATPLA 305
Cdd:PLN02955 365 V------ARKEKWRRKAIWERVKEFK----ALSGVDIS---SPIISLVVGNQEKALKASRYLLKSGFHVMAIRPPTVPPN 431

                        330       340       350
                 ....*....|....*....|....*....|....
gi 768013993 306 EARARFCVSAAHTREMLDTVLEALDEMGDLLQLK 339
Cdd:PLN02955 432 SCRLRVTLSAAHTTEDVKKLITALSSCLDFDNTA 465
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 19-214 6.92e-22

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 95.23  E-value: 6.92e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  19 ELEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLrdavi 98
Cdd:PRK05937  60 DLEHKIAHFHGAPEAFIVPSGYMANLGLCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLL----- 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  99 ygQPRTRRAWKKILILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDphEVDVLMGTF 178
Cdd:PRK05937 135 --ESCRQRSFGRIFIFVCSVYSFKGTLAPLEQIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGYE--NFYAVLVTY 210

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 768013993 179 TKSFGASGGYIAGRKDLVDYLRVHSHSAVYASSMSP 214
Cdd:PRK05937 211 SKALGSMGAALLSSSEVKQDLMLNSPPLRYSTGLPP 246
PRK07505 PRK07505
hypothetical protein; Provisional
 109-334 9.28e-20

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 89.65  E-value: 9.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 109 KKILILVEGVYSMeGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRG-VTEFFGLDPHEVDVLMGTFTKSFGASGG 187
Cdd:PRK07505 180 KTVAYVADGVYSM-GGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGyVRSELDYRLNERTIIAASLGKAFGASGG 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 188 YIA-GRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSLKLimGLDGTTQGLQrvQQLAKNTRYFRQRLQemgfiiygNEN 266
Cdd:PRK07505 259 VIMlGDAEQIELILRYAGPLAFSQSLNVAALGAILASAEI--HLSEELDQLQ--QKLQNNIALFDSLIP--------TEQ 326

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768013993 267 A-SVVPLLLYMPGK---VAAFARHMLEKKIGVVVVGFPATPLAEARARFCVSAAHTREMLDTVLEALDEMGD 334
Cdd:PRK07505 327 SgSFLPIRLIYIGDedtAIKAAKQLLDRGFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLLKEILD 398
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 71-331 2.02e-12

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: 67.37  E-value: 2.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  71 ARLSGATIRIF--KHNNTQSLEKLLRDAVIygQPRTrrawkKILILV-----EG-VYSMEgsivHLPQIIALKKKYKAYL 142
Cdd:cd00609  100 ARLAGAEVVPVplDEEGGFLLDLELLEAAK--TPKT-----KLLYLNnpnnpTGaVLSEE----ELEELAELAKKHGILI 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 143 YIDEAHSigAVGPTGRGVTEFFGLDPHEVDVLMGTFTKSFGASG---GYIAGRKDLVDYLRVHSHSavYASSMSPPIAEQ 219
Cdd:cd00609  169 ISDEAYA--ELVYDGEPPPALALLDAYERVIVLRSFSKTFGLPGlriGYLIAPPEELLERLKKLLP--YTTSGPSTLSQA 244

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 220 IIRSLklimgLDGTTQGLQRV-QQLAKNTRYFRQRLQEMGFIIYGNENASvvpllLYM-----PGKVAAFARHMLEKKIG 293
Cdd:cd00609  245 AAAAA-----LDDGEEHLEELrERYRRRRDALLEALKELGPLVVVKPSGG-----FFLwldlpEGDDEEFLERLLLEAGV 314

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 768013993 294 VVVVGFPATPLAEARARFCVsaAHTREMLDTVLEALDE 331
Cdd:cd00609  315 VVRPGSAFGEGGEGFVRLSF--ATPEEELEEALERLAE 350
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 16-192 3.46e-12

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: 63.94  E-value: 3.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  16 KHKELEDLVAKFLN--VEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTS-LVLGARLSGATIRIFKHNNTQslekl 92
Cdd:cd01494    1 KLEELEEKLARLLQpgNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSrYWVAAELAGAKPVPVPVDDAG----- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  93 lrDAVIYGQPRTRRAWKKI--LILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFgldphe 170
Cdd:cd01494   76 --YGGLDVAILEELKAKPNvaLIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGG------ 147

                        170       180
                 ....*....|....*....|...
gi 768013993 171 VDVLMGTFTKSFGASG-GYIAGR 192
Cdd:cd01494  148 ADVVTFSLHKNLGGEGgGVVIVK 170
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 19-329 3.91e-07

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: 51.18  E-value: 3.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  19 ELEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLV-LGA--RLSGATIRIFKHNN-TQSLEKLLR 94
Cdd:cd06502   36 KLEARAAELFGKEAALFVPSGTAANQLALAAHTQPGGSVICHETAHIYTDeAGApeFLSGVKLLPVPGENgKLTPEDLEA 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  95 DAVIYGQ---PRTRrawkkiLILVE------GVYSMEgsivHLPQIIALKKKYKAYLYIDEAHSIGAVgpTGRGVTEFFG 165
Cdd:cd06502  116 AIRPRDDihfPPPS------LVSLEntteggTVYPLD----ELKAISALAKENGLPLHLDGARLANAA--AALGVALKTY 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 166 LDPheVDVLMGTFTKSFGASGGYI-AGRKDLV---DYLRVHSHSAVYASSMsppIAEQIIRSLKlimgldgTTQGLQRVQ 241
Cdd:cd06502  184 KSG--VDSVSFCLSKGGGAPVGAVvVGNRDFIaraRRRRKQAGGGMRQSGF---LAAAGLAALE-------NDLWLRRLR 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 242 QLAKNTRYFRQRLQEMGfiiyGNENASVVPLLLYMPGKVAAFARHMLEKKIGVVVVGFPATPLAEARARFCVSAAHTREM 321
Cdd:cd06502  252 HDHEMARRLAEALEELG----GLESEVQTNIVLLDPVEANAVFVELSKEAIERRGEGVLFYAWGEGGVRFVTHWDTTEED 327


                 ....*...
gi 768013993 322 LDTVLEAL 329
Cdd:cd06502  328 VDELLSAL 335
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
19-266 5.81e-07

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 50.29  E-value: 5.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993   19 ELEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLVLG---ARLSGATIRIFKHNNT-----QSLE 90
Cdd:pfam01212  36 RLEDRVAELFGKEAALFVPSGTAANQLALMAHCQRGDEVICGEPAHIHFDETgghAELGGVQPRPLDGDEAgnmdlEDLE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993   91 KLLRDAVIYGQPRTRrawkkiLILVE--------GVYSMEgsivHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTE 162
Cdd:pfam01212 116 AAIREVGADIFPPTG------LISLEnthnsaggQVVSLE----NLREIAALAREHGIPVHLDGARFANAAVALGVIVKE 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  163 FFGLdpheVDVLMGTFTKSFGAS-GGYIAGRKDLVDYlRVHSHSAvYASSMSP---PIAeqiirslkliMGLDGTTQGLQ 238
Cdd:pfam01212 186 ITSY----ADSVTMCLSKGLGAPvGSVLAGSDDFIAK-AIRQRKY-LGGGLRQagvLAA----------AGLRALEEGVA 249

                         250       260       270
                  ....*....|....*....|....*....|..
gi 768013993  239 RVQQLAKNTRYFRQRLQEMGFII----YGNEN 266
Cdd:pfam01212 250 RLARDHATARRLAEGLELLRLAIprrvYTNTH 281
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 15-270 4.23e-05

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: 44.93  E-value: 4.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993   15 DKHKELEDLVAKFLNVEAA--MVFGMGfATNSMNI------PALVGKGCLILSDELNHTSLVLGARLS---GATIRIFKH 83
Cdd:pfam00266  43 QAYEEAREKVAEFINAPSNdeIIFTSG-TTEAINLvalslgRSLKPGDEIVITEMEHHANLVPWQELAkrtGARVRVLPL 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993   84 N-----NTQSLEKLLRdaviygqPRTRrawkkiLILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAvGPtgr 158
Cdd:pfam00266 122 DedgllDLDELEKLIT-------PKTK------LVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIGH-RP--- 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993  159 gvteffgLDPHEVDVLMGTFT--KSFGASG-GYIAGRKDLVDYLR-----------VHSHSAVYASSMS------PPIAe 218
Cdd:pfam00266 185 -------IDVQKLGVDFLAFSghKLYGPTGiGVLYGRRDLLEKMPpllggggmietVSLQESTFADAPWkfeagtPNIA- 256

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 768013993  219 QII---RSLKLIMGLdGTTQGLQRVQQLAKntrYFRQRLQEMGFI-IYGN-ENASVV 270
Cdd:pfam00266 257 GIIglgAALEYLSEI-GLEAIEKHEHELAQ---YLYERLLSLPGIrLYGPeRRASII 309
GcvP1 COG0403
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport ...
 235-331 4.93e-05

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


Pssm-ID: 440172 [Multi-domain]  Cd Length: 442  Bit Score: 45.02  E-value: 4.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 235 QGLQRV-QQLAKNTRYFRQRLQEMGFIIYGNE---NASVVPLllymPGKVAAFARHMLEKKIgvvVVGFPATPLAEARAR 310
Cdd:COG0403  349 EGLKEIaERIHQKAHYLAERLAALGVEVPFNGpffDEFVVRL----PKPAAEINAALLEKGI---LGGLNLRRVDDDTLL 421

                         90       100
                 ....*....|....*....|.
gi 768013993 311 FCVSAAHTREMLDTVLEALDE 331
Cdd:COG0403  422 VAVTETTTKEDIDALVEALAE 442
PRK00451 PRK00451
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
235-332 1.26e-03

aminomethyl-transferring glycine dehydrogenase subunit GcvPA;


Pssm-ID: 234769 [Multi-domain]  Cd Length: 447  Bit Score: 40.51  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 235 QGLQRV-QQLAKNTRYFRQRLQEMGFII-----YGNENAsvvpllLYMPGKVAAFARHMLEKKIgvvVVGFPAT---PLA 305
Cdd:PRK00451 348 EGLRELaEQNHQKAHYLAERLAEIGGVElfdgpFFNEFV------VRLPKPAEEVNEALLEKGI---LGGYDLGryyPEL 418

                         90       100
                 ....*....|....*....|....*..
gi 768013993 306 EARARFCVSAAHTREMLDTVLEALDEM 332
Cdd:PRK00451 419 GNHLLVCVTEKRTKEDIDALVAALGEV 445
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
 165-332 3.02e-03

DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain [Transcription, Amino acid transport and metabolism]; DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 440781 [Multi-domain]  Cd Length: 471  Bit Score: 39.43  E-value: 3.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 165 GLDPHEVDVLMGTFTKSFgASG---GYIAGRKDLVDYLRvhshSAVYASSMSPPIAEQiirslkLIMGL---DGT-TQGL 237
Cdd:COG1167  299 ALDAPGRVIYIGSFSKTL-APGlrlGYLVAPGRLIERLA----RLKRATDLGTSPLTQ------LALAEfleSGHyDRHL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013993 238 QRV-QQLAKNTRYFRQRLQEmgfiiYGNENASVVP------LLLYMPGKV--AAFARHMLEKKIGVV-VVGFPATPLAEA 307
Cdd:COG1167  368 RRLrREYRARRDLLLAALAR-----HLPDGLRVTGppgglhLWLELPEGVdaEALAAAALARGILVApGSAFSADGPPRN 442

                        170       180
                 ....*....|....*....|....*...
gi 768013993 308 RARFCVSAAHTREM---LDTVLEALDEM 332
Cdd:COG1167  443 GLRLGFGAPSEEELeeaLRRLAELLREL 470
 
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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