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Conserved domains on  [gi|2484101044|gb|WFS16357|]
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SRPBCC family protein [Rhodococcus aetherivorans]

Protein Classification

SRPBCC family protein( domain architecture ID 51693)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SRPBCC super family cl14643
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
1-212 1.28e-65

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.


The actual alignment was detected with superfamily member cd08881:

Pssm-ID: 472699 [Multi-domain]  Cd Length: 206  Bit Score: 202.09  E-value: 1.28e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101044   1 MYHAAISHSSAMLALhedpAFHGLLNPPPDAPGRQFAGD--GHGSGSFWLPefgpdlhagpeysawqtahrdevfrriga 78
Cdd:cd08881    28 GYHTGTTHASALEAG----LPPDAADLPPIDLGLQFTAPwhGHGLGFFLDS----------------------------- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101044  79 dravkvSGHNLIFPNFSWL-GPVNTMRVWHPRGPGQIEVWAWTFVPKDASPEAKAGMRRGTQRSFSPAGVFETDDGENWT 157
Cdd:cd08881    75 ------PQHGTIFPNLSFLpGYFNTLRVWHPRGPDETEVWTWTLVDKDAPEEVKDRVRRQYTRTFGPAGTFEQDDGENWE 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2484101044 158 EVQQVLRGWKSRSTEFNVQMGMGFEERDSHGLPGLSND-VYSETAARGFYQRWLDL 212
Cdd:cd08881   149 EITRVARGYVARQVPLNYQMGLGVEPEPDPGGPGIVGPgFYSEANQRGFYRRWLEL 204
 
Name Accession Description Interval E-value
RHO_alpha_C_NDO-like cd08881
C-terminal catalytic domain of the oxygenase alpha subunit of naphthalene 1,2-dioxygenase (NDO) ...
1-212 1.28e-65

C-terminal catalytic domain of the oxygenase alpha subunit of naphthalene 1,2-dioxygenase (NDO) and related aromatic ring hydroxylating dioxygenases; C-terminal catalytic domain of the oxygenase alpha subunit of naphthalene 1,2-dioxygenase (NDO) and related Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs, also known as aromatic ring hydroxylating dioxygenases). This domain binds non-heme Fe(II). RHOs utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC) and an oxygenase. The ETC transfers reducing equivalents form the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and a C-terminal domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. Proteins belonging to this subgroup include the terminal oxygenase alpha subunits of biphenyl dioxygenase, cumene dioxygenase from Pseudomonas fluorescens IP01, ethylbenzene dioxygenase, naphthalene 1,2-dioxygenase, nitrobenzene dioxygenase from Comamonas sp. strain JS765, toluene 2,3-dioxygenase from Pseudomonas putida F1, dioxin dioxygenase of Sphingomonas sp. Strain RW1, and the polycyclic aromatic hydrocarbons (PAHs)degrading ring-hydroxylating dioxygenase from Sphingomonas CHY-1. This subfamily 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.


Pssm-ID: 176890 [Multi-domain]  Cd Length: 206  Bit Score: 202.09  E-value: 1.28e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101044   1 MYHAAISHSSAMLALhedpAFHGLLNPPPDAPGRQFAGD--GHGSGSFWLPefgpdlhagpeysawqtahrdevfrriga 78
Cdd:cd08881    28 GYHTGTTHASALEAG----LPPDAADLPPIDLGLQFTAPwhGHGLGFFLDS----------------------------- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101044  79 dravkvSGHNLIFPNFSWL-GPVNTMRVWHPRGPGQIEVWAWTFVPKDASPEAKAGMRRGTQRSFSPAGVFETDDGENWT 157
Cdd:cd08881    75 ------PQHGTIFPNLSFLpGYFNTLRVWHPRGPDETEVWTWTLVDKDAPEEVKDRVRRQYTRTFGPAGTFEQDDGENWE 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2484101044 158 EVQQVLRGWKSRSTEFNVQMGMGFEERDSHGLPGLSND-VYSETAARGFYQRWLDL 212
Cdd:cd08881   149 EITRVARGYVARQVPLNYQMGLGVEPEPDPGGPGIVGPgFYSEANQRGFYRRWLEL 204
Ring_hydroxyl_A pfam00848
Ring hydroxylating alpha subunit (catalytic domain); This family is the catalytic domain of ...
1-215 1.12e-13

Ring hydroxylating alpha subunit (catalytic domain); This family is the catalytic domain of aromatic-ring- hydroxylating dioxygenase systems. The active site contains a non-heme ferrous ion coordinated by three ligands.


Pssm-ID: 425905  Cd Length: 210  Bit Score: 67.48  E-value: 1.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101044   1 MYHAAISHSSamLALHEDPAFHgllnPPPDAPGRQFAGdGHGSGSFWLPEFGPDLHAGPEYSAWQTAhrdeVFRRIGADR 80
Cdd:pfam00848  28 CYHVPVLHPE--LLRASPPEDL----PPSEAAHFDGFG-PHGRLGQGGDLRLTPAAASMTLDAEAGR----PELPGLPEE 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101044  81 AVKVSGHNLIFPNFSW-LGPVN-TMRVWHPRGPGQIEVWAWTFVPKDASPEAKAGMRRgtQRSFSPAGVFETDDGENWTE 158
Cdd:pfam00848  97 QDRGALFYTLFPNLSIlLAPDHvVVYQLIPTGPDTTRVEVYWYVPPDALAEPEFAEEL--EAVWDRTFGVNQEDAELCER 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2484101044 159 VQQvlrGWKSRSTEFNVQMGmgfeerdshglpglsndvYSETAARGFYQRWLDLVDG 215
Cdd:pfam00848 175 VQR---GLRSRGYEPGPVFG------------------RQEGGVRHFHEWVRDRLAE 210
 
Name Accession Description Interval E-value
RHO_alpha_C_NDO-like cd08881
C-terminal catalytic domain of the oxygenase alpha subunit of naphthalene 1,2-dioxygenase (NDO) ...
1-212 1.28e-65

C-terminal catalytic domain of the oxygenase alpha subunit of naphthalene 1,2-dioxygenase (NDO) and related aromatic ring hydroxylating dioxygenases; C-terminal catalytic domain of the oxygenase alpha subunit of naphthalene 1,2-dioxygenase (NDO) and related Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs, also known as aromatic ring hydroxylating dioxygenases). This domain binds non-heme Fe(II). RHOs utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC) and an oxygenase. The ETC transfers reducing equivalents form the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and a C-terminal domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. Proteins belonging to this subgroup include the terminal oxygenase alpha subunits of biphenyl dioxygenase, cumene dioxygenase from Pseudomonas fluorescens IP01, ethylbenzene dioxygenase, naphthalene 1,2-dioxygenase, nitrobenzene dioxygenase from Comamonas sp. strain JS765, toluene 2,3-dioxygenase from Pseudomonas putida F1, dioxin dioxygenase of Sphingomonas sp. Strain RW1, and the polycyclic aromatic hydrocarbons (PAHs)degrading ring-hydroxylating dioxygenase from Sphingomonas CHY-1. This subfamily 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.


Pssm-ID: 176890 [Multi-domain]  Cd Length: 206  Bit Score: 202.09  E-value: 1.28e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101044   1 MYHAAISHSSAMLALhedpAFHGLLNPPPDAPGRQFAGD--GHGSGSFWLPefgpdlhagpeysawqtahrdevfrriga 78
Cdd:cd08881    28 GYHTGTTHASALEAG----LPPDAADLPPIDLGLQFTAPwhGHGLGFFLDS----------------------------- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101044  79 dravkvSGHNLIFPNFSWL-GPVNTMRVWHPRGPGQIEVWAWTFVPKDASPEAKAGMRRGTQRSFSPAGVFETDDGENWT 157
Cdd:cd08881    75 ------PQHGTIFPNLSFLpGYFNTLRVWHPRGPDETEVWTWTLVDKDAPEEVKDRVRRQYTRTFGPAGTFEQDDGENWE 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2484101044 158 EVQQVLRGWKSRSTEFNVQMGMGFEERDSHGLPGLSND-VYSETAARGFYQRWLDL 212
Cdd:cd08881   149 EITRVARGYVARQVPLNYQMGLGVEPEPDPGGPGIVGPgFYSEANQRGFYRRWLEL 204
RHO_alpha_C_AntDO-like cd08879
C-terminal catalytic domain of the oxygenase alpha subunit of Pseudomonas resinovorans strain ...
1-209 1.12e-19

C-terminal catalytic domain of the oxygenase alpha subunit of Pseudomonas resinovorans strain CA10 anthranilate 1,2-dioxygenase and related aromatic ring hydroxylating dioxygenases; C-terminal catalytic domain of the oxygenase alpha subunit of anthranilate 1,2-dioxygenase (AntDO) and related Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs, also known as aromatic ring hydroxylating dioxygenases). RHOs utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC) and an oxygenase. The ETC transfers reducing equivalents from the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and the C-terminal catalytic domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. Oxygenases belonging to this subgroup include the alpha subunits of AntDO, aniline dioxygenase, Acinetobacter calcoaceticus benzoate 1,2-dioxygenase, 2-halobenzoate 1,2-dioxygenase from Pseudomonas cepacia 2CBS, 2,4,5-trichlorophenoxyacetic acid oxygenase from Pseudomonas cepacia AC1100, 2,4-dichlorophenoxyacetic acid oxygenase from Bradyrhizobium sp. strain HW13, p-cumate 2,3-dioxygenase, 2-halobenzoate 1,2-dioxygenase form Pseudomonas cepacia 2CBS, and Pseudomonas putida IacC, which may be involved in the catabolism of the plant hormone indole 3-acetic acid. This subfamily 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.


Pssm-ID: 176888 [Multi-domain]  Cd Length: 237  Bit Score: 84.32  E-value: 1.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101044   1 MYHAAISHSSAMLALHEDPAFH---GLLNPPPDAPGRQFAGDGHGSGSFWLPefgPDLHagpEYSAWQT-----AHRDEV 72
Cdd:cd08879    22 GYHPPFVHASYVATTGAAAADAtrgGLSSFMTGPQGGGVRDLGNGHSVLDSR---PEIP---RLDADRPkppiaEYRAAL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101044  73 FRRIGADRA---VKVSGHNL-IFPNFSWLGPVNTMRVWHPRGPGQIEVWAWTFVPKDASPEAKAGMRRGTQRSFSPAGVF 148
Cdd:cd08879    96 VAAHGEERArriLRGRGRNLnIFPNLFIIDISQQIRVIRPIAVDETEVTSWALRPKGAPDEVNRRRLRYSEDFFGPSGFA 175
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2484101044 149 ETDDGENWTEVQqvlRGWKSRSTEFN-VQMGMGFEERDSHGL-PGLSNDvysETAARGFYQRW 209
Cdd:cd08879   176 TPDDLEAFERCQ---RGLAARGEEWVdLSRGLGREKADEDGVvTGAVTD---ELPMRNQWRAW 232
Ring_hydroxyl_A pfam00848
Ring hydroxylating alpha subunit (catalytic domain); This family is the catalytic domain of ...
1-215 1.12e-13

Ring hydroxylating alpha subunit (catalytic domain); This family is the catalytic domain of aromatic-ring- hydroxylating dioxygenase systems. The active site contains a non-heme ferrous ion coordinated by three ligands.


Pssm-ID: 425905  Cd Length: 210  Bit Score: 67.48  E-value: 1.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101044   1 MYHAAISHSSamLALHEDPAFHgllnPPPDAPGRQFAGdGHGSGSFWLPEFGPDLHAGPEYSAWQTAhrdeVFRRIGADR 80
Cdd:pfam00848  28 CYHVPVLHPE--LLRASPPEDL----PPSEAAHFDGFG-PHGRLGQGGDLRLTPAAASMTLDAEAGR----PELPGLPEE 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101044  81 AVKVSGHNLIFPNFSW-LGPVN-TMRVWHPRGPGQIEVWAWTFVPKDASPEAKAGMRRgtQRSFSPAGVFETDDGENWTE 158
Cdd:pfam00848  97 QDRGALFYTLFPNLSIlLAPDHvVVYQLIPTGPDTTRVEVYWYVPPDALAEPEFAEEL--EAVWDRTFGVNQEDAELCER 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2484101044 159 VQQvlrGWKSRSTEFNVQMGmgfeerdshglpglsndvYSETAARGFYQRWLDLVDG 215
Cdd:pfam00848 175 VQR---GLRSRGYEPGPVFG------------------RQEGGVRHFHEWVRDRLAE 210
RHO_alpha_C cd00680
C-terminal catalytic domain of the oxygenase alpha subunit of Rieske-type non-heme iron ...
87-164 3.90e-05

C-terminal catalytic domain of the oxygenase alpha subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases; C-terminal catalytic domain of the oxygenase alpha subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenase (RHO) family. RHOs, also known as aromatic ring hydroxylating dioxygenases, utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC), and an oxygenase. The ETC transfers reducing equivalents from the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and a C-terminal domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. Oxygenases belonging to this family include the alpha subunits of Pseudomonas resinovorans strain CA10 anthranilate 1,2-dioxygenase, Stenotrophomonas maltophilia dicamba O-demethylase, Ralstonia sp. U2 salicylate-5-hydroxylase, Cycloclasticus sp. strain A5 polycyclic aromatic hydrocarbon dioxygenase, toluene 2,3-dioxygenase from Pseudomonas putida F1, dioxin dioxygenase of Sphingomonas sp. Strain RW1, plant choline monooxygenase, and the polycyclic aromatic hydrocarbon (PAH)-degrading ring-hydroxylating dioxygenase from Sphingomonas CHY-1. This group also includes the C-terminal catalytic domains of MupW, part of the mupirocin biosynthetic gene cluster in Pseudomonas fluorescens, and Pseudomonas aeruginosa GbcA (glycine betaine catabolism A). This 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.


Pssm-ID: 176852 [Multi-domain]  Cd Length: 188  Bit Score: 42.94  E-value: 3.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101044  87 HNLIFPN--FSWLGPVNTMRVWHPRGPGQIEVWAWTFVPKDASpeAKAGMRRGTQRSFSPAGVFETDDGENWTEVQQVLR 164
Cdd:cd00680    83 YLYLFPNlmIGLYPDSLQVQQFVPIGPNKTRLEVRLYRPKDED--AREEFDAELESLAGILRQVLDEDIELCERIQRGLR 160
RHO_alpha_C_ahdA1c-like cd08880
C-terminal catalytic domain of the large/alpha subunit (ahdA1c) of a ring-hydroxylating ...
90-214 1.74e-04

C-terminal catalytic domain of the large/alpha subunit (ahdA1c) of a ring-hydroxylating dioxygenase from Sphingomonas sp. strain P2 and related proteins; C-terminal catalytic domain of the large subunit (ahdA1c) of the AhdA3A4A2cA1c salicylate 1-hydroxylase complex from Sphingomonas sp. strain P2, and related Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs, also known as aromatic ring hydroxylating dioxygenases). AhdA3A4A2cA1c is one of three known isofunctional salicylate 1-hydroxylase complexes in strain P2, involved in phenanthrene degradation, which catalyze the monooxygenation of salicylate, the metabolite of phenanthene degradation, to produce catechol. This complex prefers salicylate over other substituted salicylates; the other two salicylate 1-hydroxylases have different substrate preferences. RHOs utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC) and an oxygenase. The ETC transfers reducing equivalents from the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and a C-terminal domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. Other oxygenases belonging to this subgroup include the alpha subunits of anthranilate 1,2-dioxygenase from Burkholderia cepacia DBO1, a polycyclic aromatic hydrocarbon dioxygenase from Cycloclasticus sp. strain A5 (PhnA dioxygenase), salicylate-5-hydroxylase from Ralstonia sp. U2, ortho-halobenzoate 1,2-dioxygenase from Pseudomonas aeruginosa strain JB2, and the terephthalate 1,2-dioxygenase system from Delftia tsuruhatensis strain T7. This subfamily 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.


Pssm-ID: 176889  Cd Length: 222  Bit Score: 41.48  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101044  90 IFPNFSWLGPVNTMRVWH--PRGPGQIEVwAWTFVP-KDASPEakagMRRGTQRS---FSPAGVFETDDGENWTEVQQVL 163
Cdd:cd08880   107 IFPSLVVQQIQNTLAVRHiiPKGPDSFEL-VWTYFGyEDDDEE----MTRLRLRQanlVGPAGFVSMEDGEAIEFVQRGV 181
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2484101044 164 RGwKSRSTEFnVQMGmGFEERDSHGLpglsndvYSETAARGFYQRWLDLVD 214
Cdd:cd08880   182 EG-DGGDRSV-IEMG-GGDVESSDHM-------VTEAAIRGFWKYYRKVMG 222
 
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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