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Conserved domains on  [gi|1196905187|ref|WP_086343878|]
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MULTISPECIES: SRPBCC domain-containing protein [Bacillus]

Protein Classification

SRPBCC domain-containing protein( domain architecture ID 10167422)

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

CATH:  3.30.530.20
SCOP:  3000738

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SRPBCC_CalC_Aha1-like cd07814
Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human ...
 11-144 8.87e-25

Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human Aha1, and related proteins; This family includes the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of Micromonospora echinospora CalC, human Aha1, and related proteins. Proteins in this group belong to the SRPBCC domain superfamily of proteins, which bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. MeCalC confers resistance to the enediyne, calicheamicin gamma 1 (CLM), by a self sacrificing mechanism which results in inactivation of both CalC and the highly reactive diradical enediyne species. MeCalC can also inactivate two other enediynes, shishijimicin and namenamicin. A crucial Gly of the MeCalC CLM resistance mechanism is not conserved in this subgroup. This family also includes the C-terminal, Bet v1-like domain of Aha1, one of several co-chaperones, which regulate the dimeric chaperone Hsp90. Aha1 promotes dimerization of the N-terminal domains of Hsp90, and stimulates its low intrinsic ATPase activity, and may regulate the dwell time of Hsp90 with client proteins. Aha1 can act as either a positive or negative regulator of chaperone-dependent activation, depending on the client protein, but the mechanisms by which these opposing functions are achieved are unclear. Aha1 is upregulated in a number of tumor lines co-incident with the activation of several signaling kinases.


:

Pssm-ID: 176856 [Multi-domain]  Cd Length: 139  Bit Score: 92.04  E-value: 8.87e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905187  11 DITKSITLEAPIQKVWETVSTSEGIAKWFMPND---FQLKEGQEFHL-----QSPFGPSPCKVLAVQAPTELSFEW---- 78
Cdd:cd07814     1 TITIEREFDAPPELVWRALTDPELLAQWFGPTTtaeMDLRVGGRWFFfmtgpDGEEGWVSGEVLEVEPPRRLVFTWafsd 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1196905187  79 --DTEGWVVTFQLEDLGEKTGFTLIHSGWKEPnevigkanEKSSVVRGKMDGGWTGIVnERLRKAVEA 144
Cdd:cd07814    81 etPGPETTVTVTLEETGGGTRLTLTHSGFPEE--------DAEQEAREGMEEGWTGTL-DRLKALLEK 139
 
Name Accession Description Interval E-value
SRPBCC_CalC_Aha1-like cd07814
Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human ...
 11-144 8.87e-25

Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human Aha1, and related proteins; This family includes the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of Micromonospora echinospora CalC, human Aha1, and related proteins. Proteins in this group belong to the SRPBCC domain superfamily of proteins, which bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. MeCalC confers resistance to the enediyne, calicheamicin gamma 1 (CLM), by a self sacrificing mechanism which results in inactivation of both CalC and the highly reactive diradical enediyne species. MeCalC can also inactivate two other enediynes, shishijimicin and namenamicin. A crucial Gly of the MeCalC CLM resistance mechanism is not conserved in this subgroup. This family also includes the C-terminal, Bet v1-like domain of Aha1, one of several co-chaperones, which regulate the dimeric chaperone Hsp90. Aha1 promotes dimerization of the N-terminal domains of Hsp90, and stimulates its low intrinsic ATPase activity, and may regulate the dwell time of Hsp90 with client proteins. Aha1 can act as either a positive or negative regulator of chaperone-dependent activation, depending on the client protein, but the mechanisms by which these opposing functions are achieved are unclear. Aha1 is upregulated in a number of tumor lines co-incident with the activation of several signaling kinases.


Pssm-ID: 176856 [Multi-domain]  Cd Length: 139  Bit Score: 92.04  E-value: 8.87e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905187  11 DITKSITLEAPIQKVWETVSTSEGIAKWFMPND---FQLKEGQEFHL-----QSPFGPSPCKVLAVQAPTELSFEW---- 78
Cdd:cd07814     1 TITIEREFDAPPELVWRALTDPELLAQWFGPTTtaeMDLRVGGRWFFfmtgpDGEEGWVSGEVLEVEPPRRLVFTWafsd 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1196905187  79 --DTEGWVVTFQLEDLGEKTGFTLIHSGWKEPnevigkanEKSSVVRGKMDGGWTGIVnERLRKAVEA 144
Cdd:cd07814    81 etPGPETTVTVTLEETGGGTRLTLTHSGFPEE--------DAEQEAREGMEEGWTGTL-DRLKALLEK 139
YndB COG3832
Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and ...
 10-135 8.04e-20

Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and metabolism];


Pssm-ID: 443044 [Multi-domain]  Cd Length: 142  Bit Score: 79.70  E-value: 8.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905187  10 PDITKSITLEAPIQKVWETVSTSEGIAKWFMPN------DFQLKEGQEFHLQ--SPFG---PSPCKVLAVQAPTELSFEW 78
Cdd:COG3832     6 RTITIEREIDAPPERVWRAWTDPELLARWFGPKgwatvaEFDLRVGGRFRFRmrGPDGeefGFEGEVLEVEPPERLVFTW 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1196905187  79 DTEG-----WVVTFQLEDLGEKTGFTLIHSGWKEpnevigkaNEKSSVVRGKMDGGWTGIVN 135
Cdd:COG3832    86 GFEDdpegeSTVTVTLEPEGGGTRLTLTHTGFSA--------EDRDAVLAEGMEEGWTESLD 139
AHSA1 pfam08327
Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic ...
 20-105 9.62e-10

Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic and archaeal proteins that bear similarity to a C-terminal region of human activator of 90 kDa heat shock protein ATPase homolog 1 (AHSA1/p38). This protein is known to interact with the middle domain of Hsp90, and stimulate its ATPase activity. It is probably a general upregulator of Hsp90 function, particularly contributing to its efficiency in conditions of increased stress. p38 is also known to interact with the cytoplasmic domain of the VSV G protein, and may thus be involved in protein transport. It has also been reported as being underexpressed in Down's syndrome. This region is found repeated in two members of this family (Swiss:Q8XY04 and Swiss:Q6MH87). The structure of YndB from Bacillus subtilis showed the helix-grip fold consisting of a beta-sheet with two small and one long alpha-helix which form a hydrophobic cavity that preferentially binds lipid-like molecules. This structure confirms its similarity with the eukaryote protein Aha1 and its classification as a member of the AHSA1 family).


Pssm-ID: 429921 [Multi-domain]  Cd Length: 125  Bit Score: 53.09  E-value: 9.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905187  20 APIQKVWETVSTSEGIAKWFMPN--DFQLKEGQEFHLQSPFG----PSPCKVLAVQAPTELSFEWDTEGW------VVTF 87
Cdd:pfam08327   2 APPERVFRALTDPELLARWFTRTvaEMDLRPGGKFRFMRGPDgeefGGNGTYLELVPPKRIVYTWRLDDWpeggysTVTV 81

                          90
                  ....*....|....*...
gi 1196905187  88 QLEDLGEKTGFTLIHSGW 105
Cdd:pfam08327  82 ELEEVGGGTRLTLTHTGE 99
 
Name Accession Description Interval E-value
SRPBCC_CalC_Aha1-like cd07814
Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human ...
 11-144 8.87e-25

Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human Aha1, and related proteins; This family includes the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of Micromonospora echinospora CalC, human Aha1, and related proteins. Proteins in this group belong to the SRPBCC domain superfamily of proteins, which bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. MeCalC confers resistance to the enediyne, calicheamicin gamma 1 (CLM), by a self sacrificing mechanism which results in inactivation of both CalC and the highly reactive diradical enediyne species. MeCalC can also inactivate two other enediynes, shishijimicin and namenamicin. A crucial Gly of the MeCalC CLM resistance mechanism is not conserved in this subgroup. This family also includes the C-terminal, Bet v1-like domain of Aha1, one of several co-chaperones, which regulate the dimeric chaperone Hsp90. Aha1 promotes dimerization of the N-terminal domains of Hsp90, and stimulates its low intrinsic ATPase activity, and may regulate the dwell time of Hsp90 with client proteins. Aha1 can act as either a positive or negative regulator of chaperone-dependent activation, depending on the client protein, but the mechanisms by which these opposing functions are achieved are unclear. Aha1 is upregulated in a number of tumor lines co-incident with the activation of several signaling kinases.


Pssm-ID: 176856 [Multi-domain]  Cd Length: 139  Bit Score: 92.04  E-value: 8.87e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905187  11 DITKSITLEAPIQKVWETVSTSEGIAKWFMPND---FQLKEGQEFHL-----QSPFGPSPCKVLAVQAPTELSFEW---- 78
Cdd:cd07814     1 TITIEREFDAPPELVWRALTDPELLAQWFGPTTtaeMDLRVGGRWFFfmtgpDGEEGWVSGEVLEVEPPRRLVFTWafsd 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1196905187  79 --DTEGWVVTFQLEDLGEKTGFTLIHSGWKEPnevigkanEKSSVVRGKMDGGWTGIVnERLRKAVEA 144
Cdd:cd07814    81 etPGPETTVTVTLEETGGGTRLTLTHSGFPEE--------DAEQEAREGMEEGWTGTL-DRLKALLEK 139
YndB COG3832
Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and ...
 10-135 8.04e-20

Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and metabolism];


Pssm-ID: 443044 [Multi-domain]  Cd Length: 142  Bit Score: 79.70  E-value: 8.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905187  10 PDITKSITLEAPIQKVWETVSTSEGIAKWFMPN------DFQLKEGQEFHLQ--SPFG---PSPCKVLAVQAPTELSFEW 78
Cdd:COG3832     6 RTITIEREIDAPPERVWRAWTDPELLARWFGPKgwatvaEFDLRVGGRFRFRmrGPDGeefGFEGEVLEVEPPERLVFTW 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1196905187  79 DTEG-----WVVTFQLEDLGEKTGFTLIHSGWKEpnevigkaNEKSSVVRGKMDGGWTGIVN 135
Cdd:COG3832    86 GFEDdpegeSTVTVTLEPEGGGTRLTLTHTGFSA--------EDRDAVLAEGMEEGWTESLD 139
SRPBCC_CalC_Aha1-like_6 cd08899
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 17-103 9.41e-17

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: 176908 [Multi-domain]  Cd Length: 157  Bit Score: 71.94  E-value: 9.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905187  17 TLEAPIQKVWETVSTSEGIAKWFMPNDFQLKEGQEFHLQSPFGPSP---CKVLAVQAPTELSFEWDTEG--WVVTFQLED 91
Cdd:cd08899    18 LLPAPIEDVWAALTDPERLARWFAPGTGDLRVGGRVEFVMDDEEGPnatGTILACEPPRLLAFTWGEGGgeSEVRFELAP 97

                          90
                  ....*....|..
gi 1196905187  92 LGEKTGFTLIHS 103
Cdd:cd08899    98 EGDGTRLTLTHR 109
AHSA1 pfam08327
Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic ...
 20-105 9.62e-10

Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic and archaeal proteins that bear similarity to a C-terminal region of human activator of 90 kDa heat shock protein ATPase homolog 1 (AHSA1/p38). This protein is known to interact with the middle domain of Hsp90, and stimulate its ATPase activity. It is probably a general upregulator of Hsp90 function, particularly contributing to its efficiency in conditions of increased stress. p38 is also known to interact with the cytoplasmic domain of the VSV G protein, and may thus be involved in protein transport. It has also been reported as being underexpressed in Down's syndrome. This region is found repeated in two members of this family (Swiss:Q8XY04 and Swiss:Q6MH87). The structure of YndB from Bacillus subtilis showed the helix-grip fold consisting of a beta-sheet with two small and one long alpha-helix which form a hydrophobic cavity that preferentially binds lipid-like molecules. This structure confirms its similarity with the eukaryote protein Aha1 and its classification as a member of the AHSA1 family).


Pssm-ID: 429921 [Multi-domain]  Cd Length: 125  Bit Score: 53.09  E-value: 9.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905187  20 APIQKVWETVSTSEGIAKWFMPN--DFQLKEGQEFHLQSPFG----PSPCKVLAVQAPTELSFEWDTEGW------VVTF 87
Cdd:pfam08327   2 APPERVFRALTDPELLARWFTRTvaEMDLRPGGKFRFMRGPDgeefGGNGTYLELVPPKRIVYTWRLDDWpeggysTVTV 81

                          90
                  ....*....|....*...
gi 1196905187  88 QLEDLGEKTGFTLIHSGW 105
Cdd:pfam08327  82 ELEEVGGGTRLTLTHTGE 99
SRPBCC_CalC_Aha1-like_5 cd08898
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 12-144 2.04e-09

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: 52.31  E-value: 2.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905187  12 ITKSITLEAPIQKVWETVSTSEGIAKWF--MPNDFQLKEGQEFHLQSP---FGPSPCKVLAVQAPTELSFEWDTEGW--- 83
Cdd:cd08898     3 IERTILIDAPRERVWRALTDPEHFGQWFgvKLGPFVVGEGATGEITYPgyeHGVFPVTVVEVDPPRRFSFRWHPPAIdpg 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905187  84 ---------VVTFQLEDLGEKTGFTLIHSGWKEPNEvigkanEKSSVVRGKMDGGWTGIVnERLRKAVEA 144
Cdd:cd08898    83 edysaepstLVEFTLEPIAGGTLLTVTESGFDALPA------ERRAEAYRMNEGGWDEQL-ENLVAYVEA 145
SRPBCC_CalC_Aha1-like_GntR-HTH cd08893
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 19-133 5.86e-07

Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and Aha1-like proteins; some contain an N-terminal GntR family winged HTH DNA-binding domain; 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. Some proteins in this subgroup contain an N-terminal winged helix-turn-helix DNA-binding domain found in the GntR family of proteins which include bacterial transcriptional regulators and their putative homologs from eukaryota and archaea.


Pssm-ID: 176902 [Multi-domain]  Cd Length: 136  Bit Score: 45.70  E-value: 5.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905187  19 EAPIQKVWETVSTSEGIAKWF--MPNDFQLKEGQEFHLQSPFGPSPC---KVLAVQAPTELSFEWDTeGW---------- 83
Cdd:cd08893     9 RATPEKVWQALTDPEFTRQYWggTTVESDWKVGSAFEYRRGDDGTVDvegEVLESDPPRRLVHTWRA-VWdpemaaepps 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1196905187  84 VVTFQLEDLGEKTGFTLIHSGWKEPnevigkaneksSVVRGKMDGGWTGI 133
Cdd:cd08893    88 RVTFEIEPVGDVVKLTVTHDGFPPG-----------SPTLEGVSGGWPAI 126
PYR_PYL_RCAR_like cd07821
Pyrabactin resistance 1 (PYR1), PYR1-like (PYL), regulatory component of abscisic acid ...
 12-39 2.55e-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: 35.76  E-value: 2.55e-03
                          10        20
                  ....*....|....*....|....*...
gi 1196905187  12 ITKSITLEAPIQKVWETVSTSEGIAKWF 39
Cdd:cd07821     3 VTVSVTIDAPADKVWALLSDFGGLHKWH 30
SRPBCC_CalC_Aha1-like_3 cd08896
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 11-99 3.76e-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: 176905 [Multi-domain]  Cd Length: 146  Bit Score: 35.29  E-value: 3.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905187  11 DITKSITLEAPIQKVWETVSTSEGIAKWFMPN-------DFQLKEGQEFH--LQSPFG---PSPCKVLAVQAPTELSFEw 78
Cdd:cd08896     1 DLVLSRTIDAPRELVWRAWTEPELLKQWFCPKpwttevaELDLRPGGAFRtvMRGPDGeefPNPGCFLEVVPGERLVFT- 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1196905187  79 D--TEGW----------VVTFqlEDLGEKTGFT 99
Cdd:cd08896    80 DalTPGWrpaekpfmtaIITF--EDEGGGTRYT 110
SRPBCC_4 cd07822
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 12-103 5.97e-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: 35.00  E-value: 5.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905187  12 ITKSITLEAPIQKVWETVSTSEGIAKW--FMPND--FQLKEGQEFHLQSPFGPSP-----CKVLAVQAPTELSFEWDTEG 82
Cdd:cd07822     2 ISTEIEINAPPEKVWEVLTDFPSYPEWnpFVRSAtgLSLALGARLRFVVKLPGGPprsfkPRVTEVEPPRRLAWRGGLPF 81

                          90       100
                  ....*....|....*....|....*.
gi 1196905187  83 WVV-----TFQLEDLGeKTGFTLIHS 103
Cdd:cd07822    82 PGLldgehSFELEPLG-DGGTRFVHR 106
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 12-94 8.72e-03

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: 34.61  E-value: 8.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905187  12 ITKSITLEAPIQKVWETVSTSEGIAKWFMPN-------DFQLKEGQEFHLQSPFGPSP---CKVLAVQAPTELSFEWDTE 81
Cdd:cd07812     1 VEASIEIPAPPEAVWDLLSDPERWPEWSPGLervevlgGGEGGVGARFVGGRKGGRRLtltSEVTEVDPPRPGRFRVTGG 80

                          90
                  ....*....|....*..
gi 1196905187  82 GW----VVTFQLEDLGE 94
Cdd:cd07812    81 GGgvdgTGEWRLEPEGD 97
SRPBCC_CalC_Aha1-like_4 cd08897
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 12-43 9.84e-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: 176906 [Multi-domain]  Cd Length: 133  Bit Score: 34.19  E-value: 9.84e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1196905187  12 ITKSITLEAPIQKVWETVSTSEGIAKWFMPND 43
Cdd:cd08897     2 ITVETTVDAPIEKVWEAWTTPEHITKWNFASD 33
 
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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