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Conserved domains on  [gi|493986387|ref|WP_006929196|]
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MULTISPECIES: SRPBCC family protein [Bacillus]

Protein Classification

SRPBCC family protein( domain architecture ID 10167503)

SRPBCC (START/RHOalphaC/PITP/Bet v1/CoxG/CalC) family protein may have a deep hydrophobic ligand-binding pocket

CATH:  3.30.530.20
PubMed:  18922149
SCOP:  3000738

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PYR_PYL_RCAR_like cd07821
Pyrabactin resistance 1 (PYR1), PYR1-like (PYL), regulatory component of abscisic acid ...
 7-135 2.80e-44

Pyrabactin resistance 1 (PYR1), PYR1-like (PYL), regulatory component of abscisic acid receptors (RCARs), and related proteins; The PYR/PYL/RCAR-like family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. PYR/PYL/RCAR plant proteins are receptors involved in signal transduction. They bind abscisic acid (ABA) and mediate its signaling. ABA is a vital plant hormone, which regulates plant growth, development, and response to environmental stresses. Upon binding ABA, these plant proteins interact with a type 2C protein phosphatase (PP2C), such as ABI1 and ABI2, and inhibit their activity. When ABA is bound, a loop (designated the gate/CL2 loop) closes over the ligand binding pocket, resulting in the weakening of the inactive PYL dimer and facilitating type 2C protein phosphatase binding. In the ABA:PYL1:ABI1 complex, the gate blocks substrate access to the phosphatase active site. A conserved Trp from PP2C inserts into PYL to lock the receptor in a closed formation. This group also contains Methylobacterium extorquens AM1 MxaD. The mxaD gene is located within the mxaFJGIR(S)ACKLDEHB cluster which encodes proteins involved in methanol oxidation. MxaD may participate in the periplasmic electron transport chain for oxidation of methanol. Mutants lacking MxaD exhibit a reduced growth on methanol, and a lower rate of respiration with methanol.


:

Pssm-ID: 176863 [Multi-domain]  Cd Length: 140  Bit Score: 141.69  E-value: 2.80e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493986387   7 SIQIPASPEQVWKLIGGFDALPDWLPYIPSSKVTEG----GRVRHLANPDGDAIVERLEAFNEKERYYTYSIMQAPFPVT 82
Cdd:cd07821    6 SVTIDAPADKVWALLSDFGGLHKWHPAVASCELEGGgpgvGAVRTVTLKDGGTVRERLLALDDAERRYSYRIVEGPLPVK 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493986387  83 NYLSTIRVKEGkDANTSLVEWSGSFTPVE-VTDEEAINLFYGIYKDGLEALQQA 135
Cdd:cd07821   86 NYVATIRVTPE-GDGGTRVTWTAEFDPPEgLTDELARAFLTGVYRAGLAALKAA 138
 
Name Accession Description Interval E-value
PYR_PYL_RCAR_like cd07821
Pyrabactin resistance 1 (PYR1), PYR1-like (PYL), regulatory component of abscisic acid ...
 7-135 2.80e-44

Pyrabactin resistance 1 (PYR1), PYR1-like (PYL), regulatory component of abscisic acid receptors (RCARs), and related proteins; The PYR/PYL/RCAR-like family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. PYR/PYL/RCAR plant proteins are receptors involved in signal transduction. They bind abscisic acid (ABA) and mediate its signaling. ABA is a vital plant hormone, which regulates plant growth, development, and response to environmental stresses. Upon binding ABA, these plant proteins interact with a type 2C protein phosphatase (PP2C), such as ABI1 and ABI2, and inhibit their activity. When ABA is bound, a loop (designated the gate/CL2 loop) closes over the ligand binding pocket, resulting in the weakening of the inactive PYL dimer and facilitating type 2C protein phosphatase binding. In the ABA:PYL1:ABI1 complex, the gate blocks substrate access to the phosphatase active site. A conserved Trp from PP2C inserts into PYL to lock the receptor in a closed formation. This group also contains Methylobacterium extorquens AM1 MxaD. The mxaD gene is located within the mxaFJGIR(S)ACKLDEHB cluster which encodes proteins involved in methanol oxidation. MxaD may participate in the periplasmic electron transport chain for oxidation of methanol. Mutants lacking MxaD exhibit a reduced growth on methanol, and a lower rate of respiration with methanol.


Pssm-ID: 176863 [Multi-domain]  Cd Length: 140  Bit Score: 141.69  E-value: 2.80e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493986387   7 SIQIPASPEQVWKLIGGFDALPDWLPYIPSSKVTEG----GRVRHLANPDGDAIVERLEAFNEKERYYTYSIMQAPFPVT 82
Cdd:cd07821    6 SVTIDAPADKVWALLSDFGGLHKWHPAVASCELEGGgpgvGAVRTVTLKDGGTVRERLLALDDAERRYSYRIVEGPLPVK 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493986387  83 NYLSTIRVKEGkDANTSLVEWSGSFTPVE-VTDEEAINLFYGIYKDGLEALQQA 135
Cdd:cd07821   86 NYVATIRVTPE-GDGGTRVTWTAEFDPPEgLTDELARAFLTGVYRAGLAALKAA 138
Polyketide_cyc2 pfam10604
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 6-135 3.12e-25

Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases/dehydrases which are enzymes involved in polyketide synthesis. It also includes other proteins of the START superfamily.


Pssm-ID: 431388  Cd Length: 139  Bit Score: 93.32  E-value: 3.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493986387    6 TSIQIPASPEQVWKLIGGFDALPDWLPYIPSSKVTEGG-----RVRHLANPDGDA-IVERLEAFNEKERYYTYSIMqAPF 79
Cdd:pfam10604   1 VSIEIAAPPEQVWALLSDFENWPRWHPGVLRVELEGGGgplrgVVGTLRVGGRRGtVREELVEYDPAPRLLAYRIV-EPL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493986387   80 PVTNYLSTIRVKEgkDANTSLVEWSGSFTPVE----VTDEEAINLFYGIYKDGLEALQQA 135
Cdd:pfam10604  80 GVANYVGTWTVTP--AGGGTRVTWTGEFDGPPlggpFRDPAAARAVKGDYRAGLDRLKAV 137
COG4891 COG4891
Uncharacterized conserved protein [Function unknown];
6-57 7.47e-08

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443919  Cd Length: 138  Bit Score: 47.99  E-value: 7.47e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 493986387   6 TSIQIPASPEQVWKLIGGFDALPDWLPYIPS--SKVTEGGRVR-HLANPDGDAIV 57
Cdd:COG4891    1 TEIEIDAPPERVWQVLTDFPSYPEWNPFIRSieGELRVGARLTlRLRPPGGRPMT 55
 
Name Accession Description Interval E-value
PYR_PYL_RCAR_like cd07821
Pyrabactin resistance 1 (PYR1), PYR1-like (PYL), regulatory component of abscisic acid ...
 7-135 2.80e-44

Pyrabactin resistance 1 (PYR1), PYR1-like (PYL), regulatory component of abscisic acid receptors (RCARs), and related proteins; The PYR/PYL/RCAR-like family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. PYR/PYL/RCAR plant proteins are receptors involved in signal transduction. They bind abscisic acid (ABA) and mediate its signaling. ABA is a vital plant hormone, which regulates plant growth, development, and response to environmental stresses. Upon binding ABA, these plant proteins interact with a type 2C protein phosphatase (PP2C), such as ABI1 and ABI2, and inhibit their activity. When ABA is bound, a loop (designated the gate/CL2 loop) closes over the ligand binding pocket, resulting in the weakening of the inactive PYL dimer and facilitating type 2C protein phosphatase binding. In the ABA:PYL1:ABI1 complex, the gate blocks substrate access to the phosphatase active site. A conserved Trp from PP2C inserts into PYL to lock the receptor in a closed formation. This group also contains Methylobacterium extorquens AM1 MxaD. The mxaD gene is located within the mxaFJGIR(S)ACKLDEHB cluster which encodes proteins involved in methanol oxidation. MxaD may participate in the periplasmic electron transport chain for oxidation of methanol. Mutants lacking MxaD exhibit a reduced growth on methanol, and a lower rate of respiration with methanol.


Pssm-ID: 176863 [Multi-domain]  Cd Length: 140  Bit Score: 141.69  E-value: 2.80e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493986387   7 SIQIPASPEQVWKLIGGFDALPDWLPYIPSSKVTEG----GRVRHLANPDGDAIVERLEAFNEKERYYTYSIMQAPFPVT 82
Cdd:cd07821    6 SVTIDAPADKVWALLSDFGGLHKWHPAVASCELEGGgpgvGAVRTVTLKDGGTVRERLLALDDAERRYSYRIVEGPLPVK 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493986387  83 NYLSTIRVKEGkDANTSLVEWSGSFTPVE-VTDEEAINLFYGIYKDGLEALQQA 135
Cdd:cd07821   86 NYVATIRVTPE-GDGGTRVTWTAEFDPPEgLTDELARAFLTGVYRAGLAALKAA 138
Polyketide_cyc2 pfam10604
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 6-135 3.12e-25

Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases/dehydrases which are enzymes involved in polyketide synthesis. It also includes other proteins of the START superfamily.


Pssm-ID: 431388  Cd Length: 139  Bit Score: 93.32  E-value: 3.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493986387    6 TSIQIPASPEQVWKLIGGFDALPDWLPYIPSSKVTEGG-----RVRHLANPDGDA-IVERLEAFNEKERYYTYSIMqAPF 79
Cdd:pfam10604   1 VSIEIAAPPEQVWALLSDFENWPRWHPGVLRVELEGGGgplrgVVGTLRVGGRRGtVREELVEYDPAPRLLAYRIV-EPL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493986387   80 PVTNYLSTIRVKEgkDANTSLVEWSGSFTPVE----VTDEEAINLFYGIYKDGLEALQQA 135
Cdd:pfam10604  80 GVANYVGTWTVTP--AGGGTRVTWTGEFDGPPlggpFRDPAAARAVKGDYRAGLDRLKAV 137
COG4891 COG4891
Uncharacterized conserved protein [Function unknown];
6-57 7.47e-08

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443919  Cd Length: 138  Bit Score: 47.99  E-value: 7.47e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 493986387   6 TSIQIPASPEQVWKLIGGFDALPDWLPYIPS--SKVTEGGRVR-HLANPDGDAIV 57
Cdd:COG4891    1 TEIEIDAPPERVWQVLTDFPSYPEWNPFIRSieGELRVGARLTlRLRPPGGRPMT 55
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 1-41 9.81e-08

Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442114  Cd Length: 137  Bit Score: 47.55  E-value: 9.81e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 493986387   1 MAKTITSIQIPASPEQVWKLIGGFDALPDWLPYIPSSKVTE 41
Cdd:COG2867    1 MPTISRSVLVPYSAEQMFDLVADVERYPEFLPWCKAARVLE 41
Bet_v1-like cd07816
Ligand-binding bet_v_1 domain of major pollen allergen of white birch (Betula verrucosa), Bet ...
 5-122 2.18e-07

Ligand-binding bet_v_1 domain of major pollen allergen of white birch (Betula verrucosa), Bet v 1, and related proteins; This family includes the ligand binding domain of Bet v 1 (the major pollen allergen of white birch, Betula verrucosa) and related proteins. In addition to birch Bet v 1, this family includes other plant intracellular pathogenesis-related class 10 (PR-10) proteins, norcoclaurine synthases (NCSs), cytokinin binding proteins (CSBPs), major latex proteins (MLPs), and ripening-related proteins. It belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Members of this family binds a diverse range of ligands. Bet v 1 can bind brassinosteroids, cytokinins, flavonoids and fatty acids. Hyp-1, a PR-10 from Hypericum perforatum/St. John's wort, catalyzes the condensation of two molecules of emodin to the bioactive naphthodianthrone hypericin. NCSs catalyze the condensation of dopamine and 4-hydroxyphenylacetaldehyde to (S)-norcoclaurine, the first committed step in the biosynthesis of benzylisoquinoline alkaloids such as morphine. The role of MLPs is unclear; however, they are associated with fruit and flower development and in pathogen defense responses. A number of PR-10 proteins in this subgroup, including Bet v 1, have in vitro RNase activity, the biological significance of which is unclear. Bet v 1 family proteins have a conserved glycine-rich P (phosphate-binding)-loop proximal to the entrance of the ligand-binding pocket. However, its conformation differs from that of the canonical P-loop structure found in nucleotide-binding proteins. Several PR-10 members including Bet v1 are allergenic. Cross-reactivity of Bet v 1 with homologs from plant foods results in birch-fruit syndrome.


Pssm-ID: 176858  Cd Length: 148  Bit Score: 46.80  E-value: 2.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493986387   5 ITSIQIPASPEQVWKLIGGFDAL--PDWLPYIPSSKVTEG----GRVRHL-ANPDGDA--IVERLEAFNEKERYYTYSIM 75
Cdd:cd07816    4 EHEVELKVPAEKLWKAFVLDSHLlpPKLPPVIKSVELLEGdggpGSIKLItFGPGGKVkyVKERIDAVDEENKTYKYTVI 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 493986387  76 QAPfPVTNYLSTIRVK---EGKDANTSLVEWSGSFTPV--EVTDEEAINLFY 122
Cdd:cd07816   84 EGD-VLKDGYKSYKVEikfVPKGDGGCVVKWTIEYEKKgdAEPPEEEIKAGK 134
SRPBCC_4 cd07822
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 6-55 3.70e-06

Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.


Pssm-ID: 176864  Cd Length: 141  Bit Score: 43.47  E-value: 3.70e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493986387   6 TSIQIPASPEQVWKLIGGFDALPDWLPYIPSS---KVTEGGRVRHLANPDGDA 55
Cdd:cd07822    4 TEIEINAPPEKVWEVLTDFPSYPEWNPFVRSAtglSLALGARLRFVVKLPGGP 56
Polyketide_cyc pfam03364
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 10-44 4.90e-06

Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases/dehydrases which are enzymes involved in polyketide synthesis. The family also includes proteins which are involved in the binding/transport of lipids.


Pssm-ID: 397441  Cd Length: 125  Bit Score: 42.87  E-value: 4.90e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 493986387   10 IPASPEQVWKLIGGFDALPDWLPYIPSSKVTEGGR 44
Cdd:pfam03364   1 VPAPAEQVWALVTDVERYPEFLPWCKSVEVLERDG 35
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 7-111 5.87e-06

START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC domains have a deep hydrophobic ligand-binding pocket; they bind diverse ligands. Included in this superfamily are the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), as well as the SRPBCC domains of phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of this superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.


Pssm-ID: 176854  Cd Length: 141  Bit Score: 43.08  E-value: 5.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493986387   7 SIQIPASPEQVWKLIGGFDALPDWLPYIPSSKVTEGGRVRhlanpDGDAIVERLEAFNEKERYYTYSIMQAPFPVtnyls 86
Cdd:cd07812    4 SIEIPAPPEAVWDLLSDPERWPEWSPGLERVEVLGGGEGG-----VGARFVGGRKGGRRLTLTSEVTEVDPPRPG----- 73

                         90       100
                 ....*....|....*....|....*
gi 493986387  87 TIRVKEGKDANTSLVEWsgSFTPVE 111
Cdd:cd07812   74 RFRVTGGGGGVDGTGEW--RLEPEG 96
SRPBCC_11 cd08866
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 7-46 1.08e-05

Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.


Pssm-ID: 176875  Cd Length: 144  Bit Score: 42.22  E-value: 1.08e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 493986387   7 SIQIPASPEQVWKLIGGFDALPDWLPYIPSSKV--TEGGRVR 46
Cdd:cd08866    4 RVRVPAPPETVWAVLTDYDNLAEFIPNLAESRLleRNGNRVV 45
M14-like cd06232
Peptidase M14-like domain; uncharacterized subfamily; Peptidase M14-like domain of a ...
 30-123 2.69e-03

Peptidase M14-like domain; uncharacterized subfamily; Peptidase M14-like domain of a functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.


Pssm-ID: 349451  Cd Length: 276  Bit Score: 36.21  E-value: 2.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493986387  30 WLPYIPSSKvTEGGRVRHLANPDGDAIVERLE------AFNEK--ERYYTYSIMQAP--FPVTNYLSTIRVKEGKDANTS 99
Cdd:cd06232  174 FYGYFPYLD-DEAYPGGELAEELAEAITKALNqdpalaAFNRRwyDRYRKYAVKWGPkvFPLEYYKPVLIYWSIFRQHRY 252

                         90       100
                 ....*....|....*....|....
gi 493986387 100 LVEWSGSFTPVEVTDEEAINLFYG 123
Cdd:cd06232  253 LSARYPQITPVELITEVADETAYG 276
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 10-83 8.51e-03

Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domain family; Functionally uncharacterized subgroup of the START domain family. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. For some mammalian members of the START family (STARDs), it is known which lipids bind in this pocket; these include cholesterol (STARD1, -3, -4, and -5), 25-hydroxycholesterol (STARD5), phosphatidylcholine (STARD2, -7, and -10), phosphatidylethanolamine (STARD10) and ceramides (STARD11). Mammalian STARDs participate in the control of various cellular processes, including lipid trafficking between intracellular compartments, lipid metabolism, and modulation of signaling events. Mutation or altered expression of STARDs is linked to diseases such as cancer, genetic disorders, and autoimmune disease.


Pssm-ID: 176885  Cd Length: 195  Bit Score: 34.55  E-value: 8.51e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493986387  10 IPASPEQVWKLIGGFDALPDWLPYipsskVTEggrvrhlanpdgdaiVERLEAFNEKERyYTYSIMQAPFPVTN 83
Cdd:cd08876   49 VDASIEAFLALLRDTESYPQWMPN-----CKE---------------SRVLKRTDDNER-SVYTVIDLPWPVKD 101
 
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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