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Conserved domains on  [gi|1907157393|ref|XP_036020354|]
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hydroxysteroid dehydrogenase-like protein 2 isoform X3 [Mus musculus]

Protein Classification

hydroxysteroid dehydrogenase-like protein 2( domain architecture ID 10395550)

hydroxysteroid dehydrogenase-like protein 2 (HSDL2) may be involved in in fatty acid metabolism, as well as in cholesterol metabolism and homeostasis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCP2 pfam02036
SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the ...
 185-278 7.79e-25

SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the SCP2 protein as well as the C terminus of the enzyme estradiol 17 beta-dehydrogenase EC:1.1.1.62. The UNC-24 protein contains an SPFH domain pfam01145.


:

Pssm-ID: 460423 [Multi-domain]  Cd Length: 100  Bit Score: 95.40  E-value: 7.79e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157393 185 KDSLSDEVVRATQA-VYQFELSGEdGGTWFLDLKSKGGKVGHGEPSDrADVVMSMATDDFVKMFSGKLKPTMAFMSGKLK 263
Cdd:pfam02036   7 RDPAARELLKKLNGkVIRFDLTDL-GLSLTLDLKDGGGRVLAGDEGK-ADVTLSASDSDLLALATGKLNPQKAFMQGKLK 84

                          90
                  ....*....|....*
gi 1907157393 264 IKGNIALAIKLEKLM 278
Cdd:pfam02036  85 IEGDMELAQKLEGLL 99
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 3-69 1.76e-21

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.


The actual alignment was detected with superfamily member PRK08278:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 273  Bit Score: 91.12  E-value: 1.76e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907157393   3 MLGGSGVENQCRKVDIIADAAYSIFKRP-KSFTGNFIIDENILKEEGIKNFDVYAIAPGHPLLPDFFL 69
Cdd:PRK08278  206 LLGGDEAMRRSRTPEIMADAAYEILSRPaREFTGNFLIDEEVLREAGVTDFSRYAVDPGAPLMPDLFV 273
 
Name Accession Description Interval E-value
SCP2 pfam02036
SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the ...
 185-278 7.79e-25

SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the SCP2 protein as well as the C terminus of the enzyme estradiol 17 beta-dehydrogenase EC:1.1.1.62. The UNC-24 protein contains an SPFH domain pfam01145.


Pssm-ID: 460423 [Multi-domain]  Cd Length: 100  Bit Score: 95.40  E-value: 7.79e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157393 185 KDSLSDEVVRATQA-VYQFELSGEdGGTWFLDLKSKGGKVGHGEPSDrADVVMSMATDDFVKMFSGKLKPTMAFMSGKLK 263
Cdd:pfam02036   7 RDPAARELLKKLNGkVIRFDLTDL-GLSLTLDLKDGGGRVLAGDEGK-ADVTLSASDSDLLALATGKLNPQKAFMQGKLK 84

                          90
                  ....*....|....*
gi 1907157393 264 IKGNIALAIKLEKLM 278
Cdd:pfam02036  85 IEGDMELAQKLEGLL 99
SCP2 COG3255
Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];
198-281 9.64e-24

Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];


Pssm-ID: 442486 [Multi-domain]  Cd Length: 104  Bit Score: 92.66  E-value: 9.64e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157393 198 AVYQFELSGEDGGTWFLDLKSKGGKVGHGEPSDrADVVMSMATDDFVKMFSGKLKPTMAFMSGKLKIKGNIALAIKLEKL 277
Cdd:COG3255    22 GVVQFVITGEGGGAYYLVIDDGKCTVSEGDDDD-ADVTLTASYEDWKKLLTGELDPMTAFMTGKLKVEGDMGLAMKLMSL 100


                  ....
gi 1907157393 278 MTQM 281
Cdd:COG3255   101 FKAL 104
PRK08278 PRK08278
SDR family oxidoreductase;
3-69 1.76e-21

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 91.12  E-value: 1.76e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907157393   3 MLGGSGVENQCRKVDIIADAAYSIFKRP-KSFTGNFIIDENILKEEGIKNFDVYAIAPGHPLLPDFFL 69
Cdd:PRK08278  206 LLGGDEAMRRSRTPEIMADAAYEILSRPaREFTGNFLIDEEVLREAGVTDFSRYAVDPGAPLMPDLFV 273
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 1-43 1.89e-15

human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human HSDL2 and related protens. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 74.02  E-value: 1.89e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1907157393   1 MDMLGGSGVENQCRKVDIIADAAYSIFKRPKS-FTGNFIIDENI 43
Cdd:cd09762   200 MNMLGGVDVAACCRKPEIMADAAYAILTKPSSeFTGNFLIDEEV 243
 
Name Accession Description Interval E-value
SCP2 pfam02036
SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the ...
 185-278 7.79e-25

SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the SCP2 protein as well as the C terminus of the enzyme estradiol 17 beta-dehydrogenase EC:1.1.1.62. The UNC-24 protein contains an SPFH domain pfam01145.


Pssm-ID: 460423 [Multi-domain]  Cd Length: 100  Bit Score: 95.40  E-value: 7.79e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157393 185 KDSLSDEVVRATQA-VYQFELSGEdGGTWFLDLKSKGGKVGHGEPSDrADVVMSMATDDFVKMFSGKLKPTMAFMSGKLK 263
Cdd:pfam02036   7 RDPAARELLKKLNGkVIRFDLTDL-GLSLTLDLKDGGGRVLAGDEGK-ADVTLSASDSDLLALATGKLNPQKAFMQGKLK 84

                          90
                  ....*....|....*
gi 1907157393 264 IKGNIALAIKLEKLM 278
Cdd:pfam02036  85 IEGDMELAQKLEGLL 99
SCP2 COG3255
Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];
198-281 9.64e-24

Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];


Pssm-ID: 442486 [Multi-domain]  Cd Length: 104  Bit Score: 92.66  E-value: 9.64e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157393 198 AVYQFELSGEDGGTWFLDLKSKGGKVGHGEPSDrADVVMSMATDDFVKMFSGKLKPTMAFMSGKLKIKGNIALAIKLEKL 277
Cdd:COG3255    22 GVVQFVITGEGGGAYYLVIDDGKCTVSEGDDDD-ADVTLTASYEDWKKLLTGELDPMTAFMTGKLKVEGDMGLAMKLMSL 100


                  ....
gi 1907157393 278 MTQM 281
Cdd:COG3255   101 FKAL 104
PRK08278 PRK08278
SDR family oxidoreductase;
3-69 1.76e-21

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 91.12  E-value: 1.76e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907157393   3 MLGGSGVENQCRKVDIIADAAYSIFKRP-KSFTGNFIIDENILKEEGIKNFDVYAIAPGHPLLPDFFL 69
Cdd:PRK08278  206 LLGGDEAMRRSRTPEIMADAAYEILSRPaREFTGNFLIDEEVLREAGVTDFSRYAVDPGAPLMPDLFV 273
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 1-43 1.89e-15

human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human HSDL2 and related protens. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 74.02  E-value: 1.89e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1907157393   1 MDMLGGSGVENQCRKVDIIADAAYSIFKRPKS-FTGNFIIDENI 43
Cdd:cd09762   200 MNMLGGVDVAACCRKPEIMADAAYAILTKPSSeFTGNFLIDEEV 243
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 1-43 7.69e-08

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human DHRS1 and human HSDL2 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 52.01  E-value: 7.69e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1907157393   1 MDMLGGSGVENQCRKVDIIADAAYSIFKRPK-SFTGNFIIDENI 43
Cdd:cd05338   203 ATELSGGSDPARARSPEILSDAVLAILSRPAaERTGLVVIDEEL 246
BDS1 COG2015
Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary ...
 226-278 2.58e-04

Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441618 [Multi-domain]  Cd Length: 629  Bit Score: 42.13  E-value: 2.58e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907157393 226 GEPSDRADVVMSMATDDFVKMFSGKLKPTMAFMSGKLKIKGNialAIKLEKLM 278
Cdd:COG2015   567 GPQADDADATLTLTRADLLALLLGKTTLDDLVASGGAKVEGD---AAALARLL 616
Alkyl_sulf_C pfam14864
Alkyl sulfatase C-terminal; This domain is found at the C-terminus of alkyl sulfatases. ...
 226-278 2.13e-03

Alkyl sulfatase C-terminal; This domain is found at the C-terminus of alkyl sulfatases. Together with the N-terminal catalytic domain, this domain forms a hydrophobic chute and may recruit hydrophobic substrates.


Pssm-ID: 405542 [Multi-domain]  Cd Length: 124  Bit Score: 37.17  E-value: 2.13e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907157393 226 GEPSDRADVVMSMATDDFVKMFSGKLKPTMAFMSGKLKIKGNIAlaiKLEKLM 278
Cdd:pfam14864  60 GRQADDADATLTLTRADLLALLLGKATLGKLIAAGKIKVEGDPS---ALAELL 109
 
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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