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Conserved domains on  [gi|2100537199|ref|WP_223579700|]
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SRPBCC family protein [Kangiella taiwanensis]

Protein Classification

SRPBCC family protein( domain architecture ID 10167397)

SRPBCC (START/RHOalphaC/PITP/Bet v1/CoxG/CalC) family protein may have a deep hydrophobic ligand-binding pocket; similar to Penicillium simplicissimum penitrem biosynthesis cluster 1 protein I

CATH:  3.30.530.20
Gene Ontology:  GO:0005488
PubMed:  18922149
SCOP:  3000738

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 3-142 7.70e-23

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: 87.38  E-value: 7.70e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100537199   3 YQLDIIINKPVDEVIQLFDNPDNLKKWQPELVSFEHISGEEGQPGAKSKLVYLMGKR---ECEMIETIETRqlPQEFTGT 79
Cdd:cd07812     1 VEASIEIPAPPEAVWDLLSDPERWPEWSPGLERVEVLGGGEGGVGARFVGGRKGGRRltlTSEVTEVDPPR--PGRFRVT 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2100537199  80 YETKGVFNRIENRFKPVGADQTHWTTHNEFKFTSLGMKLMGFFMKKAFPKQTMQFMQQFKDFA 142
Cdd:cd07812    79 GGGGGVDGTGEWRLEPEGDGGTRVTYTVEYDPPGPLLKVFALLLAGALKRELAALLRALKARL 141
 
Name Accession Description Interval E-value
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 3-142 7.70e-23

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: 87.38  E-value: 7.70e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100537199   3 YQLDIIINKPVDEVIQLFDNPDNLKKWQPELVSFEHISGEEGQPGAKSKLVYLMGKR---ECEMIETIETRqlPQEFTGT 79
Cdd:cd07812     1 VEASIEIPAPPEAVWDLLSDPERWPEWSPGLERVEVLGGGEGGVGARFVGGRKGGRRltlTSEVTEVDPPR--PGRFRVT 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2100537199  80 YETKGVFNRIENRFKPVGADQTHWTTHNEFKFTSLGMKLMGFFMKKAFPKQTMQFMQQFKDFA 142
Cdd:cd07812    79 GGGGGVDGTGEWRLEPEGDGGTRVTYTVEYDPPGPLLKVFALLLAGALKRELAALLRALKARL 141
COG5637 COG5637
Uncharacterized protein, contains SRPBCC domain [Function unknown];
7-143 1.09e-05

Uncharacterized protein, contains SRPBCC domain [Function unknown];


Pssm-ID: 444363  Cd Length: 154  Bit Score: 42.59  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100537199   7 IIINKPVDEVIQLFDNPDNLKKWQPELVSFEHISGEEgqpgakSKLVYLMGK-RECEMIETIeTRQLPQEFTGTYETKG- 84
Cdd:COG5637     8 ITINAPVEEVYAYWRDFENLPRFMKGVESVTVLDDTR------SHWVAKGPLgVTVEWDAEI-TEQVPGERIAWRSVEGd 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2100537199  85 VFNRIENRFKPVGADQTHWTTHNEF--KFTSLGmKLMGFFMKKAFPKQTMQFMQQFKDFAE 143
Cdd:COG5637    81 IPNAGVVRFEPAGGRGTRVTVTIEYdpPGGLLG-KALAKLFGGVPERQLREDLERFKQLIE 140
Polyketide_cyc pfam03364
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 9-135 1.17e-03

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: 36.71  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100537199   9 INKPVDEVIQLFDNPDNLKKWQPELVSFEHISGEEGQpgAKSKLVYLMGKRECemieTIETRQLPQEFTGTYETKGVFNR 88
Cdd:pfam03364   1 VPAPAEQVWALVTDVERYPEFLPWCKSVEVLERDGSL--ADWRVAFGGLRRSF----TARVTLQPPERIEMVLVDGDFKR 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2100537199  89 IEN--RFKPVG-ADQTHWTTHNEFKFTSLGMK-LMGFFMKKAFPKQTMQFM 135
Cdd:pfam03364  75 LEGswRFEPGGpGTRVKVTLELDFEFASPLPGaLLGFVFRRVLRTLLEAFR 125
 
Name Accession Description Interval E-value
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 3-142 7.70e-23

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: 87.38  E-value: 7.70e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100537199   3 YQLDIIINKPVDEVIQLFDNPDNLKKWQPELVSFEHISGEEGQPGAKSKLVYLMGKR---ECEMIETIETRqlPQEFTGT 79
Cdd:cd07812     1 VEASIEIPAPPEAVWDLLSDPERWPEWSPGLERVEVLGGGEGGVGARFVGGRKGGRRltlTSEVTEVDPPR--PGRFRVT 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2100537199  80 YETKGVFNRIENRFKPVGADQTHWTTHNEFKFTSLGMKLMGFFMKKAFPKQTMQFMQQFKDFA 142
Cdd:cd07812    79 GGGGGVDGTGEWRLEPEGDGGTRVTYTVEYDPPGPLLKVFALLLAGALKRELAALLRALKARL 141
SRPBCC_10 cd08865
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 7-140 1.07e-12

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: 61.15  E-value: 1.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100537199   7 IIINKPVDEVIQLFDNPDNLKKWQPELVSFEHISGEEGQPGAKSKLVYLMGKRECEMIETIeTRQLPQEFTGTYETKGVF 86
Cdd:cd08865     5 IVIERPVEEVFAYLADFENAPEWDPGVVEVEKITDGPVGVGTRYHQVRKFLGRRIELTYEI-TEYEPGRRVVFRGSSGPF 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2100537199  87 N-RIENRFKPVGaDQTHWTTHNEFKFtSLGMKLMGFFMKKAFPKQTMQFMQQFKD 140
Cdd:cd08865    84 PyEDTYTFEPVG-GGTRVRYTAELEP-GGFARLLDPLMAPAFRRRARAALENLKA 136
COG5637 COG5637
Uncharacterized protein, contains SRPBCC domain [Function unknown];
7-143 1.09e-05

Uncharacterized protein, contains SRPBCC domain [Function unknown];


Pssm-ID: 444363  Cd Length: 154  Bit Score: 42.59  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100537199   7 IIINKPVDEVIQLFDNPDNLKKWQPELVSFEHISGEEgqpgakSKLVYLMGK-RECEMIETIeTRQLPQEFTGTYETKG- 84
Cdd:COG5637     8 ITINAPVEEVYAYWRDFENLPRFMKGVESVTVLDDTR------SHWVAKGPLgVTVEWDAEI-TEQVPGERIAWRSVEGd 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2100537199  85 VFNRIENRFKPVGADQTHWTTHNEF--KFTSLGmKLMGFFMKKAFPKQTMQFMQQFKDFAE 143
Cdd:COG5637    81 IPNAGVVRFEPAGGRGTRVTVTIEYdpPGGLLG-KALAKLFGGVPERQLREDLERFKQLIE 140
SRPBCC_Smu440-like cd08862
Ligand-binding SRPBCC domain of Streptococcus mutans Smu.440 and related proteins; This family ...
 1-144 9.53e-05

Ligand-binding SRPBCC domain of Streptococcus mutans Smu.440 and related proteins; This family includes the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of Streptococcus mutans Smu.440 and related proteins. This domain belongs to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Streptococcus mutans is a dental pathogen, and the leading cause of dental caries. In this pathogen, the gene encoding Smu.440 is in the same operon as the gene encoding SMU.441, a member of the MarR protein family of transcriptional regulators involved in multiple antibiotic resistance. It has been suggested that SMU.440 is involved in polyketide-like antibiotic resistance.


Pssm-ID: 176871  Cd Length: 138  Bit Score: 39.65  E-value: 9.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100537199   1 MKYQLDIIINKPVDEVIQLFDNPDNLKKWQPELvsfEHISGEEGQPGAKSKLVYLMGKREcEMIETIETRQLPQEFTGTY 80
Cdd:cd08862     1 MKFEATIVIDAPPERVWAVLTDVENWPAWTPSV---ETVRLEGPPPAVGSSFKMKPPGLV-RSTFTVTELRPGHSFTWTG 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2100537199  81 ETKGVFNRIENRFKPVGADQTHWTTHNEFKFTSLGMklMGFFMKKAFPKQTMQFMQQFKDFAEK 144
Cdd:cd08862    77 PAPGISAVHRHEFEAKPDGGVRVTTSESLSGPLAFL--FGLFVGKKLRALLPEWLEGLKAAAEQ 138
PYR_PYL_RCAR_like cd07821
Pyrabactin resistance 1 (PYR1), PYR1-like (PYL), regulatory component of abscisic acid ...
 7-127 1.38e-04

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: 39.23  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100537199   7 IIINKPVDEVIQLFDNPDNLKKWQPELVSFEHISGEEGqPGAksklvylmgKRECEM------IETIETRQlPQEFTGTY 80
Cdd:cd07821     7 VTIDAPADKVWALLSDFGGLHKWHPAVASCELEGGGPG-VGA---------VRTVTLkdggtvRERLLALD-DAERRYSY 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2100537199  81 E-TKGVFnRIEN-----RFKPVGADQT--HWTthneFKFTSLGM-------KLMGFFMKKAF 127
Cdd:cd07821    76 RiVEGPL-PVKNyvatiRVTPEGDGGTrvTWT----AEFDPPEGltdelarAFLTGVYRAGL 132
Polyketide_cyc pfam03364
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 9-135 1.17e-03

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: 36.71  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100537199   9 INKPVDEVIQLFDNPDNLKKWQPELVSFEHISGEEGQpgAKSKLVYLMGKRECemieTIETRQLPQEFTGTYETKGVFNR 88
Cdd:pfam03364   1 VPAPAEQVWALVTDVERYPEFLPWCKSVEVLERDGSL--ADWRVAFGGLRRSF----TARVTLQPPERIEMVLVDGDFKR 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2100537199  89 IEN--RFKPVG-ADQTHWTTHNEFKFTSLGMK-LMGFFMKKAFPKQTMQFM 135
Cdd:pfam03364  75 LEGswRFEPGGpGTRVKVTLELDFEFASPLPGaLLGFVFRRVLRTLLEAFR 125
Polyketide_cyc2 pfam10604
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 7-127 1.31e-03

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: 36.69  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100537199   7 IIINKPVDEVIQLFDNPDNLKKWQPELVSFEHISGeeGQPGAKSKLVYLMGKRECEMIETIETRQlPQEFTGTYE---TK 83
Cdd:pfam10604   3 IEIAAPPEQVWALLSDFENWPRWHPGVLRVELEGG--GGPLRGVVGTLRVGGRRGTVREELVEYD-PAPRLLAYRivePL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2100537199  84 GVFNRIEN-RFKPVGA-DQTHWTThnEFKFTSLGMKLMGFFMKKAF 127
Cdd:pfam10604  80 GVANYVGTwTVTPAGGgTRVTWTG--EFDGPPLGGPFRDPAAARAV 123
 
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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