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Conserved domains on  [gi|422398866|ref|NP_001258713|]
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fatty acyl-CoA reductase 2 isoform 2 [Homo sapiens]

Protein Classification

fatty acyl-CoA reductase( domain architecture ID 10859931)

fatty acyl-CoA reductase is an extended SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase that catalyzes the reduction of saturated and unsaturated C16 or C18 fatty acyl-CoA to fatty alcohols; in addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids

CATH:  3.40.50.720
EC:  1.2.1.84
Gene Ontology:  GO:0016620|GO:0070403|GO:0102965|GO:0080019|GO:0035337
PubMed:  19027726|12604210|19011750|19011748|20423462
SCOP:  4000029

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FAR-N_SDR_e cd05236
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding ...
 2-218 1.46e-106

fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding proteins, many of which may function as fatty acyl CoA reductases (FAR), acting on medium and long chain fatty acids, and have been reported to be involved in diverse processes such as biosynthesis of insect pheromones, plant cuticular wax production, and mammalian wax biosynthesis. In Arabidopsis thaliana, proteins with this particular architecture have also been identified as the MALE STERILITY 2 (MS2) gene product, which is implicated in male gametogenesis. Mutations in MS2 inhibit the synthesis of exine (sporopollenin), rendering plants unable to reduce pollen wall fatty acids to corresponding alcohols. This N-terminal domain shares the catalytic triad (but not the upstream Asn) and characteristic NADP-binding motif of the extended SDR family. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


:

Pssm-ID: 187547 [Multi-domain]  Cd Length: 320  Bit Score: 317.32  E-value: 1.46e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866   2 QELLSCTNIIFHCAATVRFDDTLRHAVQLNVTATRQLLLMASQMPKLEAFIHISTAYSNCNLKHIDEVIYPCPVEPKKII 81
Cdd:cd05236   89 QTLIEEVNIIIHCAATVTFDERLDEALSINVLGTLRLLELAKRCKKLKAFVHVSTAYVNGDRQLIEEKVYPPPADPEKLI 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866  82 DSLEWLDDAIIDEITPKLIRDWPNIYTYTKALGEMVVQQESRNLNIAIIRPSIVGATWQEPFPGWVDNINGPNGIIIATG 161
Cdd:cd05236  169 DILELMDDLELERATPKLLGGHPNTYTFTKALAERLVLKERGNLPLVIVRPSIVGATLKEPFPGWIDNFNGPDGLFLAYG 248

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 422398866 162 KGFLRAIKATPMAVADVIPVDTVVNLMLAVGWYTAVHRPKSTLVYHITSGNMNPCNW 218
Cdd:cd05236  249 KGILRTMNADPNAVADIIPVDVVANALLAAAAYSGVRKPRELEVYHCGSSDVNPFTW 305
Sterile pfam03015
Male sterility protein; This family represents the C-terminal region of the male sterility ...
 260-350 3.19e-37

Male sterility protein; This family represents the C-terminal region of the male sterility protein in a number of arabidopsis and drosophila. A sequence-related jojoba acyl CoA reductase is also included.


:

Pssm-ID: 460779 [Multi-domain]  Cd Length: 92  Bit Score: 130.67  E-value: 3.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866  260 HRAPAIIYDCYLRLTGRKPRMTKLMNRLLRTVSMLEYFINRSWEWSTYNTEMLMSELSPEDQRVFNFDVRQLNWLEYIEN 339
Cdd:pfam03015   2 HLLPAYLLDLLLRLLGKKPRLVRLYKKIHKALDVLEYFTTREWKFDNDNTEKLWDSLSPEDRKLFNFDIRSIDWDDYFEN 81

                          90
                  ....*....|.
gi 422398866  340 YVLGVKKYLLK 350
Cdd:pfam03015  82 YILGIRKYLLK 92
 
Name Accession Description Interval E-value
FAR-N_SDR_e cd05236
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding ...
 2-218 1.46e-106

fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding proteins, many of which may function as fatty acyl CoA reductases (FAR), acting on medium and long chain fatty acids, and have been reported to be involved in diverse processes such as biosynthesis of insect pheromones, plant cuticular wax production, and mammalian wax biosynthesis. In Arabidopsis thaliana, proteins with this particular architecture have also been identified as the MALE STERILITY 2 (MS2) gene product, which is implicated in male gametogenesis. Mutations in MS2 inhibit the synthesis of exine (sporopollenin), rendering plants unable to reduce pollen wall fatty acids to corresponding alcohols. This N-terminal domain shares the catalytic triad (but not the upstream Asn) and characteristic NADP-binding motif of the extended SDR family. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187547 [Multi-domain]  Cd Length: 320  Bit Score: 317.32  E-value: 1.46e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866   2 QELLSCTNIIFHCAATVRFDDTLRHAVQLNVTATRQLLLMASQMPKLEAFIHISTAYSNCNLKHIDEVIYPCPVEPKKII 81
Cdd:cd05236   89 QTLIEEVNIIIHCAATVTFDERLDEALSINVLGTLRLLELAKRCKKLKAFVHVSTAYVNGDRQLIEEKVYPPPADPEKLI 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866  82 DSLEWLDDAIIDEITPKLIRDWPNIYTYTKALGEMVVQQESRNLNIAIIRPSIVGATWQEPFPGWVDNINGPNGIIIATG 161
Cdd:cd05236  169 DILELMDDLELERATPKLLGGHPNTYTFTKALAERLVLKERGNLPLVIVRPSIVGATLKEPFPGWIDNFNGPDGLFLAYG 248

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 422398866 162 KGFLRAIKATPMAVADVIPVDTVVNLMLAVGWYTAVHRPKSTLVYHITSGNMNPCNW 218
Cdd:cd05236  249 KGILRTMNADPNAVADIIPVDVVANALLAAAAYSGVRKPRELEVYHCGSSDVNPFTW 305
NAD_binding_4 pfam07993
Male sterility protein; This family represents the C-terminal region of the male sterility ...
 1-188 3.94e-63

Male sterility protein; This family represents the C-terminal region of the male sterility protein in a number of arabidopsis and drosophila. A sequence-related jojoba acyl CoA reductase is also included.


Pssm-ID: 462334 [Multi-domain]  Cd Length: 257  Bit Score: 203.61  E-value: 3.94e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866    1 MQELLSCTNIIFHCAATVRFDDTLRHAVQLNVTATRQLLLMASQMPKLEAFIHISTAYSNCNLK-HIDEVIYPCPvepkk 79
Cdd:pfam07993  82 FQELAEEVDVIIHSAATVNFVEPYDDARAVNVLGTREVLRLAKQGKQLKPFHHVSTAYVNGERGgLVEEKPYPEG----- 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866   80 iidslewLDDAIIDEITPKLIRDWPNIYTYTKALGEMVVQQES-RNLNIAIIRPSIVGAtwqEPFPGWVDNIN-GPNGII 157
Cdd:pfam07993 157 -------EDDMLLDEDEPALLGGLPNGYTQTKWLAEQLVREAArRGLPVVIYRPSIITG---EPKTGWINNFDfGPRGLL 226

                         170       180       190
                  ....*....|....*....|....*....|.
gi 422398866  158 IATGKGFLRAIKATPMAVADVIPVDTVVNLM 188
Cdd:pfam07993 227 GGIGKGVLPSILGDPDAVLDLVPVDYVANAI 257
PLN02503 PLN02503
fatty acyl-CoA reductase 2
 9-350 1.51e-39

fatty acyl-CoA reductase 2


Pssm-ID: 215279 [Multi-domain]  Cd Length: 605  Bit Score: 149.24  E-value: 1.51e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866   9 NIIFHCAATVRFDDTLRHAVQLNVTATRQLLLMASQMPKLEAFIHISTAYSNCNLK-HIDE---VIYPCPVEPKKIIDSL 84
Cdd:PLN02503 221 DVIINSAANTTFDERYDVAIDINTRGPCHLMSFAKKCKKLKLFLQVSTAYVNGQRQgRIMEkpfRMGDCIARELGISNSL 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866  85 EWLDDAIIDEITPKLIRD---------------------------WPNIYTYTKALGEMVVQQESRNLNIAIIRPSIVGA 137
Cdd:PLN02503 301 PHNRPALDIEAEIKLALDskrhgfqsnsfaqkmkdlgleraklygWQDTYVFTKAMGEMVINSMRGDIPVVIIRPSVIES 380

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866 138 TWQEPFPGWVDNINGPNGIIIATGKGFLRAIKATPMAVADVIPVDTVVNLMLA-VGWYTAVHRPkSTLVYHITSGNMNPC 216
Cdd:PLN02503 381 TWKDPFPGWMEGNRMMDPIVLYYGKGQLTGFLADPNGVLDVVPADMVVNATLAaMAKHGGAAKP-EINVYQIASSVVNPL 459

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866 217 NWHKMGVQVLATFEKIPFE----RPFRRPNANF--TSNSFTSQYWNAVSHRApaiiydcylRLTGRKPRMTKLMNRL--- 287
Cdd:PLN02503 460 VFQDLARLLYEHYKSSPYMdskgRPIHVPPMKLfsSMEDFSSHLWRDALLRS---------GLAGMSSSDRKLSQKLeni 530

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 422398866 288 -LRTVSMLEYFINRSWEWSTY-------NTEMLMSELSPEDQRVFNFDVRQLNWLEYIEN-YVLGVKKYLLK 350
Cdd:PLN02503 531 cAKSVEQAKYLASIYEPYTFYggrfdnsNTQRLMERMSEEEKAEFGFDVGSIDWRDYITNvHIPGLRRHVMK 602
Sterile pfam03015
Male sterility protein; This family represents the C-terminal region of the male sterility ...
 260-350 3.19e-37

Male sterility protein; This family represents the C-terminal region of the male sterility protein in a number of arabidopsis and drosophila. A sequence-related jojoba acyl CoA reductase is also included.


Pssm-ID: 460779 [Multi-domain]  Cd Length: 92  Bit Score: 130.67  E-value: 3.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866  260 HRAPAIIYDCYLRLTGRKPRMTKLMNRLLRTVSMLEYFINRSWEWSTYNTEMLMSELSPEDQRVFNFDVRQLNWLEYIEN 339
Cdd:pfam03015   2 HLLPAYLLDLLLRLLGKKPRLVRLYKKIHKALDVLEYFTTREWKFDNDNTEKLWDSLSPEDRKLFNFDIRSIDWDDYFEN 81

                          90
                  ....*....|.
gi 422398866  340 YVLGVKKYLLK 350
Cdd:pfam03015  82 YILGIRKYLLK 92
FAR_C cd09071
C-terminal domain of fatty acyl CoA reductases; C-terminal domain of fatty acyl CoA reductases, ...
 258-349 3.83e-34

C-terminal domain of fatty acyl CoA reductases; C-terminal domain of fatty acyl CoA reductases, a family of SDR-like proteins. SDRs or short-chain dehydrogenases/reductases are Rossmann-fold NAD(P)H-binding proteins. Many proteins in this FAR_C family may function as fatty acyl-CoA reductases (FARs), acting on medium and long chain fatty acids, and have been reported to be involved in diverse processes such as the biosynthesis of insect pheromones, plant cuticular wax production, and mammalian wax biosynthesis. In Arabidopsis thaliana, proteins with this particular architecture have also been identified as the MALE STERILITY 2 (MS2) gene product, which is implicated in male gametogenesis. Mutations in MS2 inhibit the synthesis of exine (sporopollenin), rendering plants unable to reduce pollen wall fatty acids to corresponding alcohols. The function of this C-terminal domain is unclear.


Pssm-ID: 176924 [Multi-domain]  Cd Length: 92  Bit Score: 122.28  E-value: 3.83e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866 258 VSHRAPAIIYDCYLRLTGRKPRMTKLMNRLLRTVSMLEYFINRSWEWSTYNTEMLMSELSPEDQRVFNFDVRQLNWLEYI 337
Cdd:cd09071    1 FLHLLPAYLLDLLLRLLGRKPRLLKLYRKIHKLLDLLEYFTTNEWRFDNDNTRALWERLSEEDRELFNFDIRSIDWDDYF 80

                         90
                 ....*....|..
gi 422398866 338 ENYVLGVKKYLL 349
Cdd:cd09071   81 ENYIPGLRKYLL 92
Lys2b COG3320
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ...
 2-212 9.25e-18

Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary metabolites biosynthesis, transport and catabolism]; Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 442549 [Multi-domain]  Cd Length: 265  Bit Score: 82.56  E-value: 9.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866   2 QELLSCTNIIFHCAATVRFDDTLRHAVQLNVTATRQLLLMASQMpKLEAFIHISTAYsncnlkhideVIYPCPVEPKkii 81
Cdd:COG3320   82 QELAEEVDAIVHLAALVNLVAPYSELRAVNVLGTREVLRLAATG-RLKPFHYVSTIA----------VAGPADRSGV--- 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866  82 dsleWLDDAIIDEitpkliRDWPNIYTYTKALGEMVVQQES-RNLNIAIIRPSIVGA---TwqepfpGWVDNINGPNGII 157
Cdd:COG3320  148 ----FEEDDLDEG------QGFANGYEQSKWVAEKLVREAReRGLPVTIYRPGIVVGdsrT------GETNKDDGFYRLL 211

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 422398866 158 iatgKGF--LRAIKATPMAVADVIPVDTVVNLMLAVGwytavHRPKSTL-VYHITSGN 212
Cdd:COG3320  212 ----KGLlrLGAAPGLGDARLNLVPVDYVARAIVHLS-----RQPEAAGrTFHLTNPQ 260
 
Name Accession Description Interval E-value
FAR-N_SDR_e cd05236
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding ...
 2-218 1.46e-106

fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding proteins, many of which may function as fatty acyl CoA reductases (FAR), acting on medium and long chain fatty acids, and have been reported to be involved in diverse processes such as biosynthesis of insect pheromones, plant cuticular wax production, and mammalian wax biosynthesis. In Arabidopsis thaliana, proteins with this particular architecture have also been identified as the MALE STERILITY 2 (MS2) gene product, which is implicated in male gametogenesis. Mutations in MS2 inhibit the synthesis of exine (sporopollenin), rendering plants unable to reduce pollen wall fatty acids to corresponding alcohols. This N-terminal domain shares the catalytic triad (but not the upstream Asn) and characteristic NADP-binding motif of the extended SDR family. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187547 [Multi-domain]  Cd Length: 320  Bit Score: 317.32  E-value: 1.46e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866   2 QELLSCTNIIFHCAATVRFDDTLRHAVQLNVTATRQLLLMASQMPKLEAFIHISTAYSNCNLKHIDEVIYPCPVEPKKII 81
Cdd:cd05236   89 QTLIEEVNIIIHCAATVTFDERLDEALSINVLGTLRLLELAKRCKKLKAFVHVSTAYVNGDRQLIEEKVYPPPADPEKLI 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866  82 DSLEWLDDAIIDEITPKLIRDWPNIYTYTKALGEMVVQQESRNLNIAIIRPSIVGATWQEPFPGWVDNINGPNGIIIATG 161
Cdd:cd05236  169 DILELMDDLELERATPKLLGGHPNTYTFTKALAERLVLKERGNLPLVIVRPSIVGATLKEPFPGWIDNFNGPDGLFLAYG 248

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 422398866 162 KGFLRAIKATPMAVADVIPVDTVVNLMLAVGWYTAVHRPKSTLVYHITSGNMNPCNW 218
Cdd:cd05236  249 KGILRTMNADPNAVADIIPVDVVANALLAAAAYSGVRKPRELEVYHCGSSDVNPFTW 305
NAD_binding_4 pfam07993
Male sterility protein; This family represents the C-terminal region of the male sterility ...
 1-188 3.94e-63

Male sterility protein; This family represents the C-terminal region of the male sterility protein in a number of arabidopsis and drosophila. A sequence-related jojoba acyl CoA reductase is also included.


Pssm-ID: 462334 [Multi-domain]  Cd Length: 257  Bit Score: 203.61  E-value: 3.94e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866    1 MQELLSCTNIIFHCAATVRFDDTLRHAVQLNVTATRQLLLMASQMPKLEAFIHISTAYSNCNLK-HIDEVIYPCPvepkk 79
Cdd:pfam07993  82 FQELAEEVDVIIHSAATVNFVEPYDDARAVNVLGTREVLRLAKQGKQLKPFHHVSTAYVNGERGgLVEEKPYPEG----- 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866   80 iidslewLDDAIIDEITPKLIRDWPNIYTYTKALGEMVVQQES-RNLNIAIIRPSIVGAtwqEPFPGWVDNIN-GPNGII 157
Cdd:pfam07993 157 -------EDDMLLDEDEPALLGGLPNGYTQTKWLAEQLVREAArRGLPVVIYRPSIITG---EPKTGWINNFDfGPRGLL 226

                         170       180       190
                  ....*....|....*....|....*....|.
gi 422398866  158 IATGKGFLRAIKATPMAVADVIPVDTVVNLM 188
Cdd:pfam07993 227 GGIGKGVLPSILGDPDAVLDLVPVDYVANAI 257
PLN02503 PLN02503
fatty acyl-CoA reductase 2
 9-350 1.51e-39

fatty acyl-CoA reductase 2


Pssm-ID: 215279 [Multi-domain]  Cd Length: 605  Bit Score: 149.24  E-value: 1.51e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866   9 NIIFHCAATVRFDDTLRHAVQLNVTATRQLLLMASQMPKLEAFIHISTAYSNCNLK-HIDE---VIYPCPVEPKKIIDSL 84
Cdd:PLN02503 221 DVIINSAANTTFDERYDVAIDINTRGPCHLMSFAKKCKKLKLFLQVSTAYVNGQRQgRIMEkpfRMGDCIARELGISNSL 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866  85 EWLDDAIIDEITPKLIRD---------------------------WPNIYTYTKALGEMVVQQESRNLNIAIIRPSIVGA 137
Cdd:PLN02503 301 PHNRPALDIEAEIKLALDskrhgfqsnsfaqkmkdlgleraklygWQDTYVFTKAMGEMVINSMRGDIPVVIIRPSVIES 380

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866 138 TWQEPFPGWVDNINGPNGIIIATGKGFLRAIKATPMAVADVIPVDTVVNLMLA-VGWYTAVHRPkSTLVYHITSGNMNPC 216
Cdd:PLN02503 381 TWKDPFPGWMEGNRMMDPIVLYYGKGQLTGFLADPNGVLDVVPADMVVNATLAaMAKHGGAAKP-EINVYQIASSVVNPL 459

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866 217 NWHKMGVQVLATFEKIPFE----RPFRRPNANF--TSNSFTSQYWNAVSHRApaiiydcylRLTGRKPRMTKLMNRL--- 287
Cdd:PLN02503 460 VFQDLARLLYEHYKSSPYMdskgRPIHVPPMKLfsSMEDFSSHLWRDALLRS---------GLAGMSSSDRKLSQKLeni 530

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 422398866 288 -LRTVSMLEYFINRSWEWSTY-------NTEMLMSELSPEDQRVFNFDVRQLNWLEYIEN-YVLGVKKYLLK 350
Cdd:PLN02503 531 cAKSVEQAKYLASIYEPYTFYggrfdnsNTQRLMERMSEEEKAEFGFDVGSIDWRDYITNvHIPGLRRHVMK 602
Sterile pfam03015
Male sterility protein; This family represents the C-terminal region of the male sterility ...
 260-350 3.19e-37

Male sterility protein; This family represents the C-terminal region of the male sterility protein in a number of arabidopsis and drosophila. A sequence-related jojoba acyl CoA reductase is also included.


Pssm-ID: 460779 [Multi-domain]  Cd Length: 92  Bit Score: 130.67  E-value: 3.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866  260 HRAPAIIYDCYLRLTGRKPRMTKLMNRLLRTVSMLEYFINRSWEWSTYNTEMLMSELSPEDQRVFNFDVRQLNWLEYIEN 339
Cdd:pfam03015   2 HLLPAYLLDLLLRLLGKKPRLVRLYKKIHKALDVLEYFTTREWKFDNDNTEKLWDSLSPEDRKLFNFDIRSIDWDDYFEN 81

                          90
                  ....*....|.
gi 422398866  340 YVLGVKKYLLK 350
Cdd:pfam03015  82 YILGIRKYLLK 92
PLN02996 PLN02996
fatty acyl-CoA reductase
 2-350 5.93e-35

fatty acyl-CoA reductase


Pssm-ID: 215538 [Multi-domain]  Cd Length: 491  Bit Score: 135.22  E-value: 5.93e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866   2 QELLSCTNIIFHCAATVRFDDTLRHAVQLNVTATRQLLLMASQMPKLEAFIHISTAYSnCNLKH--IDEVIYP------- 72
Cdd:PLN02996 107 EEMWKEIDIVVNLAATTNFDERYDVALGINTLGALNVLNFAKKCVKVKMLLHVSTAYV-CGEKSglILEKPFHmgetlng 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866  73 -----CPVEPKKIIDSLEWLD--DAIIDEITpKLIRD----------WPNIYTYTKALGEMVVQQESRNLNIAIIRPSIV 135
Cdd:PLN02996 186 nrkldINEEKKLVKEKLKELNeqDASEEEIT-QAMKDlgmeraklhgWPNTYVFTKAMGEMLLGNFKENLPLVIIRPTMI 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866 136 GATWQEPFPGWVDNINGPNGIIIATGKGFLRAIKATPMAVADVIPVDTVVNLMLAVgwyTAVHRPK--STLVYHITSGNM 213
Cdd:PLN02996 265 TSTYKEPFPGWIEGLRTIDSVIVGYGKGKLTCFLADPNSVLDVIPADMVVNAMIVA---MAAHAGGqgSEIIYHVGSSLK 341

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866 214 NPcnwhkmgvqvlATFEKIPfERPFRRpnanFTSNSFTSQYWNAVS-------------HRAPAIIYDCYLR-------- 272
Cdd:PLN02996 342 NP-----------VKFSNLH-DFAYRY----FSKNPWINKEGSPVKvgkgtilstmasfSLYMTIRYLLPLKalqlvnii 405

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866 273 LTGRKPRMTKLMNR----LLRTVSMLEYFINRSWEWSTYNTE---MLMSELSPEDQRVFNFDVRQLNWLEYIEN-YVLGV 344
Cdd:PLN02996 406 LPKRYGDKYTDLNRkiklVMRLVDLYKPYVFFKGIFDDTNTEklrIKRKETGKEEADMFDFDPKSIDWEDYMTNvHIPGL 485


                 ....*.
gi 422398866 345 KKYLLK 350
Cdd:PLN02996 486 VKYVLK 491
FAR_C cd09071
C-terminal domain of fatty acyl CoA reductases; C-terminal domain of fatty acyl CoA reductases, ...
 258-349 3.83e-34

C-terminal domain of fatty acyl CoA reductases; C-terminal domain of fatty acyl CoA reductases, a family of SDR-like proteins. SDRs or short-chain dehydrogenases/reductases are Rossmann-fold NAD(P)H-binding proteins. Many proteins in this FAR_C family may function as fatty acyl-CoA reductases (FARs), acting on medium and long chain fatty acids, and have been reported to be involved in diverse processes such as the biosynthesis of insect pheromones, plant cuticular wax production, and mammalian wax biosynthesis. In Arabidopsis thaliana, proteins with this particular architecture have also been identified as the MALE STERILITY 2 (MS2) gene product, which is implicated in male gametogenesis. Mutations in MS2 inhibit the synthesis of exine (sporopollenin), rendering plants unable to reduce pollen wall fatty acids to corresponding alcohols. The function of this C-terminal domain is unclear.


Pssm-ID: 176924 [Multi-domain]  Cd Length: 92  Bit Score: 122.28  E-value: 3.83e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866 258 VSHRAPAIIYDCYLRLTGRKPRMTKLMNRLLRTVSMLEYFINRSWEWSTYNTEMLMSELSPEDQRVFNFDVRQLNWLEYI 337
Cdd:cd09071    1 FLHLLPAYLLDLLLRLLGRKPRLLKLYRKIHKLLDLLEYFTTNEWRFDNDNTRALWERLSEEDRELFNFDIRSIDWDDYF 80

                         90
                 ....*....|..
gi 422398866 338 ENYVLGVKKYLL 349
Cdd:cd09071   81 ENYIPGLRKYLL 92
Lys2b COG3320
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ...
 2-212 9.25e-18

Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary metabolites biosynthesis, transport and catabolism]; Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 442549 [Multi-domain]  Cd Length: 265  Bit Score: 82.56  E-value: 9.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866   2 QELLSCTNIIFHCAATVRFDDTLRHAVQLNVTATRQLLLMASQMpKLEAFIHISTAYsncnlkhideVIYPCPVEPKkii 81
Cdd:COG3320   82 QELAEEVDAIVHLAALVNLVAPYSELRAVNVLGTREVLRLAATG-RLKPFHYVSTIA----------VAGPADRSGV--- 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866  82 dsleWLDDAIIDEitpkliRDWPNIYTYTKALGEMVVQQES-RNLNIAIIRPSIVGA---TwqepfpGWVDNINGPNGII 157
Cdd:COG3320  148 ----FEEDDLDEG------QGFANGYEQSKWVAEKLVREAReRGLPVTIYRPGIVVGdsrT------GETNKDDGFYRLL 211

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 422398866 158 iatgKGF--LRAIKATPMAVADVIPVDTVVNLMLAVGwytavHRPKSTL-VYHITSGN 212
Cdd:COG3320  212 ----KGLlrLGAAPGLGDARLNLVPVDYVARAIVHLS-----RQPEAAGrTFHLTNPQ 260
MupV_like_SDR_e cd05263
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ...
 1-250 2.27e-13

Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family domains have the characteristic active site tetrad and a well-conserved NAD(P)-binding motif. This subgroup is not well characterized, its members are annotated as having a variety of putative functions. One characterized member is Pseudomonas fluorescens MupV a protein involved in the biosynthesis of Mupirocin, a polyketide-derived antibiotic. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187573 [Multi-domain]  Cd Length: 293  Bit Score: 70.09  E-value: 2.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866   1 MQELLSCTNIIFHCAATVRFDDTLRHAVQLNVTATRQLL-LMASQMPKleAFIHISTAYsncnlkhideviypCPVEPKK 79
Cdd:cd05263   70 SRELAGKVDHVIHCAASYDFQAPNEDAWRTNIDGTEHVLeLAARLDIQ--RFHYVSTAY--------------VAGNREG 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866  80 IIdSLEWLDDAiideitpkliRDWPNIYTYTKALGEMVVQQESRNLNIAIIRPSIVgatWQEPFPGWVDNINGPngiiia 159
Cdd:cd05263  134 NI-RETELNPG----------QNFKNPYEQSKAEAEQLVRAAATQIPLTVYRPSIV---VGDSKTGRIEKIDGL------ 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866 160 tgKGFLRAIKATPM---------AVADVIPVDTVVNLMLAVgwytaVHRPKST-LVYHITSGNmnpcnwhKMGVQVLATF 229
Cdd:cd05263  194 --YELLNLLAKLGRwlpmpgnkgARLNLVPVDYVADAIVYL-----SKKPEANgQIFHLTDPT-------PQTLREIADL 259

                        250       260
                 ....*....|....*....|.
gi 422398866 230 EKIPFERPFRRPNANFTSNSF 250
Cdd:cd05263  260 FKSAFLSPGLLVLLMNEPNAS 280
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
 10-289 5.00e-11

uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, extended (e) SDRs; This subgroup contains proteins of unknown function related to aldehyde reductase and flavonoid reductase of the extended SDR-type. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187539 [Multi-domain]  Cd Length: 318  Bit Score: 63.46  E-value: 5.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866  10 IIFHCAATVRFDDTLRHAV-QLNVTATRQLLlMASQMPKLEAFIHISTaysncnlkhideviypcpvepkkiIDSLEWLD 88
Cdd:cd05228   65 RVFHLAAFTSLWAKDRKELyRTNVEGTRNVL-DAALEAGVRRVVHTSS------------------------IAALGGPP 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866  89 DAIIDEITPKLIRDWPNIYTYTKALGEMVVQQESRN-LNIAIIRPS-IVGatwqepfPGwvDNINGPNGIIIATG-KGFL 165
Cdd:cd05228  120 DGRIDETTPWNERPFPNDYYRSKLLAELEVLEAAAEgLDVVIVNPSaVFG-------PG--DEGPTSTGLDVLDYlNGKL 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866 166 RAIkatPMAVADVIPVDTVVNLMLAvgwytAVHRPKSTLVYHITSGNMnpcnwhkMGVQVLATFEKIPFERPFRRpnanf 245
Cdd:cd05228  191 PAY---PPGGTSFVDVRDVAEGHIA-----AMEKGRRGERYILGGENL-------SFKQLFETLAEITGVKPPRR----- 250

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 422398866 246 tsnsfTSQYWNAVSHRAPAIIYDcylRLTGRKPRMTKLMNRLLR 289
Cdd:cd05228  251 -----TIPPWLLKAVAALSELKA---RLTGKPPLLTPRTARVLR 286
SDR_e1 cd05235
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins ...
 2-212 9.14e-08

extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins identified as putative polyketide sythases fatty acid synthases (FAS), and nonribosomal peptide synthases, among others. However, unlike the usual ketoreductase modules of FAS and polyketide synthase, these domains are related to the extended SDRs, and have canonical NAD(P)-binding motifs and an active site tetrad. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187546 [Multi-domain]  Cd Length: 290  Bit Score: 53.04  E-value: 9.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866   2 QELLSCTNIIFHCAATVRF---DDTLRHAvqlNVTATRQLLLMASQMpKLEAFIHISTAYSncnlkhideviypCPVEPK 78
Cdd:cd05235   84 QELAEEVDVIIHNGANVNWvypYEELKPA---NVLGTKELLKLAATG-KLKPLHFVSTLSV-------------FSAEEY 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866  79 KIIDslewlDDAIIDEITPKLirDWPNIYTYTKALGEMVVQQ-ESRNLNIAIIRP-SIVGATWQepfpgwvdningpnGI 156
Cdd:cd05235  147 NALD-----DEESDDMLESQN--GLPNGYIQSKWVAEKLLREaANRGLPVAIIRPgNIFGDSET--------------GI 205

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 422398866 157 IIaTGKGFLRAIKATPM--------AVADVIPVDTVVNLMLAvgwyTAVHRPKSTLVYHITSGN 212
Cdd:cd05235  206 GN-TDDFFWRLLKGCLQlgiypisgAPLDLSPVDWVARAIVK----LALNESNEFSIYHLLNPP 264
SDR_e cd08946
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ...
 9-208 1.30e-06

extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 212494 [Multi-domain]  Cd Length: 200  Bit Score: 48.84  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866   9 NIIFHCAATVRFDDTLRHAV---QLNVTATRQLLLMASQMpKLEAFIHISTAYsncnlkhidevIYPcpvepkkiidSLE 85
Cdd:cd08946   32 DVVVHLAALVGVPASWDNPDedfETNVVGTLNLLEAARKA-GVKRFVYASSAS-----------VYG----------SPE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422398866  86 WLDDAIIDEITPKlirdwpNIYTYTKALGEMVVQ--QESRNLNIAIIRPSIV-----GATWQEPFPGWVDNINGPNGIII 158
Cdd:cd08946   90 GLPEEEETPPRPL------SPYGVSKLAAEHLLRsyGESYGLPVVILRLANVygpgqRPRLDGVVNDFIRRALEGKPLTV 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 422398866 159 ATGKGFLRaikatpmavaDVIPVDTVVNLMLAVgwytAVHRPKSTLVYHI 208
Cdd:cd08946  164 FGGGNQTR----------DFIHVDDVVRAILHA----LENPLEGGGVYNI 199
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
 19-87 7.45e-04

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 41.53  E-value: 7.45e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 422398866  19 RFD--DTLRHAVQLNVTATRQLLLMASQMPKLEAfiHISTAYSNCNLKHIDEVIYPCPVEPKKIIdsLEWL 87
Cdd:PRK13390 228 RFDaqATLGHVERYRITVTQMVPTMFVRLLKLDA--DVRTRYDVSSLRAVIHAAAPCPVDVKHAM--IDWL 294
 
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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