NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|490008517|ref|WP_003911328|]
View 

MULTISPECIES: SRPBCC family protein [Mycobacterium]

Protein Classification

SRPBCC family protein( domain architecture ID 10167496)

uncharacterized SRPBCC family protein; similar to Streptomyces canus cyclase which catalyzes a chemical reaction to form a cyclic compound

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SRPBCC_2 cd07819
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 2-141 1.28e-56

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: 176861  Cd Length: 140  Bit Score: 173.19  E-value: 1.28e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490008517   2 AIRASREVVIEAPPEVIVEALADMDAVPSWSSVHKRVEVVDTYSDGRPHHVKVTIKVAGIVDTELLEYHWGP-DWVVWDA 80
Cdd:cd07819    1 AIKVSREFEIEAPPAAVMDVLADVEAYPEWSPKVKSVEVLLRDNDGRPEMVRIGVGAYGIKDTYALEYTWDGaGSVSWTL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490008517  81 AKTAQQHGQHGEYNLRREDnDKTRVRFTLTVEPSAPLPAFWVNIARKKILHAATEGLRKQV 141
Cdd:cd07819   81 VEGEGNRSQEGSYTLTPKG-DGTRVTFDLTVELTVPLPGFLKRKAEPLVLDEALKGLKKRV 140
 
Name Accession Description Interval E-value
SRPBCC_2 cd07819
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 2-141 1.28e-56

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: 176861  Cd Length: 140  Bit Score: 173.19  E-value: 1.28e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490008517   2 AIRASREVVIEAPPEVIVEALADMDAVPSWSSVHKRVEVVDTYSDGRPHHVKVTIKVAGIVDTELLEYHWGP-DWVVWDA 80
Cdd:cd07819    1 AIKVSREFEIEAPPAAVMDVLADVEAYPEWSPKVKSVEVLLRDNDGRPEMVRIGVGAYGIKDTYALEYTWDGaGSVSWTL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490008517  81 AKTAQQHGQHGEYNLRREDnDKTRVRFTLTVEPSAPLPAFWVNIARKKILHAATEGLRKQV 141
Cdd:cd07819   81 VEGEGNRSQEGSYTLTPKG-DGTRVTFDLTVELTVPLPGFLKRKAEPLVLDEALKGLKKRV 140
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 1-140 7.44e-10

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


Pssm-ID: 442114  Cd Length: 137  Bit Score: 53.71  E-value: 7.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490008517   1 MAiRASREVVIEAPPEVIVEALADMDAVPSWSSVHKRVEVVDTysDGRPHHVKVTIKVAGIVDTELLEY-HWGPDWVVWD 79
Cdd:COG2867    1 MP-TISRSVLVPYSAEQMFDLVADVERYPEFLPWCKAARVLER--DGDEVVAELTVSFKGLRESFTTRNtLDPPERIDFE 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490008517  80 AAKTAQQHgQHGEYNLRREDNDKTRVRFTLTVEPSAPLPAFWVNIARKKILHAATEGLRKQ 140
Cdd:COG2867   78 LVDGPFKH-LEGRWRFEPLGEGGTKVTFDLDFEFKSPLLGALLGPVFNEAARRMVDAFKKR 137
Polyketide_cyc2 pfam10604
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 7-141 2.30e-06

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: 44.40  E-value: 2.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490008517    7 REVVIEAPPEVIVEALADMDAVPSWSSVHKRVEVVDTysDGRPHHVKVTIKVAGIVDT---ELLEYHWGPDWVVWDAAKT 83
Cdd:pfam10604   1 VSIEIAAPPEQVWALLSDFENWPRWHPGVLRVELEGG--GGPLRGVVGTLRVGGRRGTvreELVEYDPAPRLLAYRIVEP 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490008517   84 aqQHGQHGEYNLR-REDNDKTRVRFTLTVEPSAPLPAFWVNIAR---KKILHAATEGLRKQV 141
Cdd:pfam10604  79 --LGVANYVGTWTvTPAGGGTRVTWTGEFDGPPLGGPFRDPAAAravKGDYRAGLDRLKAVL 138
 
Name Accession Description Interval E-value
SRPBCC_2 cd07819
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 2-141 1.28e-56

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: 176861  Cd Length: 140  Bit Score: 173.19  E-value: 1.28e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490008517   2 AIRASREVVIEAPPEVIVEALADMDAVPSWSSVHKRVEVVDTYSDGRPHHVKVTIKVAGIVDTELLEYHWGP-DWVVWDA 80
Cdd:cd07819    1 AIKVSREFEIEAPPAAVMDVLADVEAYPEWSPKVKSVEVLLRDNDGRPEMVRIGVGAYGIKDTYALEYTWDGaGSVSWTL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490008517  81 AKTAQQHGQHGEYNLRREDnDKTRVRFTLTVEPSAPLPAFWVNIARKKILHAATEGLRKQV 141
Cdd:cd07819   81 VEGEGNRSQEGSYTLTPKG-DGTRVTFDLTVELTVPLPGFLKRKAEPLVLDEALKGLKKRV 140
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 1-140 7.44e-10

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


Pssm-ID: 442114  Cd Length: 137  Bit Score: 53.71  E-value: 7.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490008517   1 MAiRASREVVIEAPPEVIVEALADMDAVPSWSSVHKRVEVVDTysDGRPHHVKVTIKVAGIVDTELLEY-HWGPDWVVWD 79
Cdd:COG2867    1 MP-TISRSVLVPYSAEQMFDLVADVERYPEFLPWCKAARVLER--DGDEVVAELTVSFKGLRESFTTRNtLDPPERIDFE 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490008517  80 AAKTAQQHgQHGEYNLRREDNDKTRVRFTLTVEPSAPLPAFWVNIARKKILHAATEGLRKQ 140
Cdd:COG2867   78 LVDGPFKH-LEGRWRFEPLGEGGTKVTFDLDFEFKSPLLGALLGPVFNEAARRMVDAFKKR 137
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 6-139 3.39e-09

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: 51.94  E-value: 3.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490008517   6 SREVVIEAPPEVIVEALADMDAVPSWSSVHKRVEVVD--TYSDGRPHHVKVTIKVAGIVDTELLEYHWGPDwVVWDAAKT 83
Cdd:cd07812    2 EASIEIPAPPEAVWDLLSDPERWPEWSPGLERVEVLGggEGGVGARFVGGRKGGRRLTLTSEVTEVDPPRP-GRFRVTGG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490008517  84 AQQHGQHGEYNLRREDNDKTRVRFTLTVEPSAPLPAFWVNIARKKILHAATEGLRK 139
Cdd:cd07812   81 GGGVDGTGEWRLEPEGDGGTRVTYTVEYDPPGPLLKVFALLLAGALKRELAALLRA 136
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 2-141 2.89e-07

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: 47.65  E-value: 2.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490008517   2 AIRAsrEVVIEAPPEVIVEALADMDAVPSW-----------------SSVHKRVE------------VVDTYSDGRPHHV 52
Cdd:cd08876   42 EFKA--VAEVDASIEAFLALLRDTESYPQWmpnckesrvlkrtddneRSVYTVIDlpwpvkdrdmvlRSTTEQDADDGSV 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490008517  53 KVTIKVAgivdtelleyhwgPDWVvwdaaktAQQHGQH------GEYNLRREDNDKTRVRFTLTVEPSAPLPAFWVNIAR 126
Cdd:cd08876  120 TITLEAA-------------PEAL-------PEQKGYVriktveGQWTFTPLGNGKTRVTYQAYADPGGSIPGWLANAFA 179

                        170
                 ....*....|....*
gi 490008517 127 KKILHAATEGLRKQV 141
Cdd:cd08876  180 KDAPYNTLENLRKQL 194
Polyketide_cyc2 pfam10604
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 7-141 2.30e-06

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: 44.40  E-value: 2.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490008517    7 REVVIEAPPEVIVEALADMDAVPSWSSVHKRVEVVDTysDGRPHHVKVTIKVAGIVDT---ELLEYHWGPDWVVWDAAKT 83
Cdd:pfam10604   1 VSIEIAAPPEQVWALLSDFENWPRWHPGVLRVELEGG--GGPLRGVVGTLRVGGRRGTvreELVEYDPAPRLLAYRIVEP 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490008517   84 aqQHGQHGEYNLR-REDNDKTRVRFTLTVEPSAPLPAFWVNIAR---KKILHAATEGLRKQV 141
Cdd:pfam10604  79 --LGVANYVGTWTvTPAGGGTRVTWTGEFDGPPLGGPFRDPAAAravKGDYRAGLDRLKAVL 138
SRPBCC_4 cd07822
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 6-42 1.98e-03

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: 36.15  E-value: 1.98e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 490008517   6 SREVVIEAPPEVIVEALADMDAVPSWSSVHKRVEVVD 42
Cdd:cd07822    3 STEIEINAPPEKVWEVLTDFPSYPEWNPFVRSATGLS 39
PYR_PYL_RCAR_like cd07821
Pyrabactin resistance 1 (PYR1), PYR1-like (PYL), regulatory component of abscisic acid ...
 3-141 2.54e-03

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: 36.15  E-value: 2.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490008517   3 IRASREVVIEAPPEVIVEALADMDAVPSWSSVHKRVEVVDtySDGRPHHV-KVTIKVAGIVDTELLEyhwgpdwvvWDAA 81
Cdd:cd07821    1 AKVTVSVTIDAPADKVWALLSDFGGLHKWHPAVASCELEG--GGPGVGAVrTVTLKDGGTVRERLLA---------LDDA 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490008517  82 KT------------AQQHgqHGEYNLRREDNDKTRVRFTLTVEPSAPLPAFWVNIARKKILHAATEGLRKQV 141
Cdd:cd07821   70 ERrysyrivegplpVKNY--VATIRVTPEGDGGTRVTWTAEFDPPEGLTDELARAFLTGVYRAGLAALKAAL 139
SRPBCC_CalC_Aha1-like_5 cd08898
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 4-74 4.65e-03

Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and Aha1-like proteins; SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of a functionally uncharacterized subgroup of CalC- and Aha1-like proteins. This group shows similarity to the SRPBCC domains of Micromonospora echinospora CalC (a protein which confers resistance to enediynes) and human Aha1 (one of several co-chaperones which regulate the dimeric chaperone Hsp90), and belongs to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands.


Pssm-ID: 176907 [Multi-domain]  Cd Length: 145  Bit Score: 35.36  E-value: 4.65e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490008517   4 RASREVVIEAPPEVIVEALADMDAVPSWSSVHKRVEVVDTYSDGR---PH--HVKVTIKVAGIVDTELLEYHWGPD 74
Cdd:cd08898    2 RIERTILIDAPRERVWRALTDPEHFGQWFGVKLGPFVVGEGATGEityPGyeHGVFPVTVVEVDPPRRFSFRWHPP 77
SRPBCC_10 cd08865
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 5-117 7.68e-03

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: 176874  Cd Length: 140  Bit Score: 34.57  E-value: 7.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490008517   5 ASREVVIEAPPEVIVEALADMDAVPSWSSvhkRVEVVDTYSDGRP---HHVKVTIKVAGIVdtelLEYHWG-----PDWV 76
Cdd:cd08865    1 VEESIVIERPVEEVFAYLADFENAPEWDP---GVVEVEKITDGPVgvgTRYHQVRKFLGRR----IELTYEiteyePGRR 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 490008517  77 VWdAAKTAQQHGQHGEYNLrREDNDKTRVRFTLTVEPSAPL 117
Cdd:cd08865   74 VV-FRGSSGPFPYEDTYTF-EPVGGGTRVRYTAELEPGGFA 112
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH