NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|547470631|ref|WP_022089408|]
View 

SH3 domain-containing protein [Eubacterium sp. CAG:156]

Protein Classification

SH3 domain-containing protein( domain architecture ID 11471995)

Src Homology 3 (SH3) domain-containing protein plays versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others

CATH:  2.30.30.40
Gene Ontology:  GO:0005515|GO:0070064
SCOP:  4000369

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
YraI COG4991
Uncharacterized conserved protein YraI [Function unknown];
86-151 8.74e-14

Uncharacterized conserved protein YraI [Function unknown];


:

Pssm-ID: 444015 [Multi-domain]  Cd Length: 92  Bit Score: 63.54  E-value: 8.74e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 547470631  86 TTQAVLTMYTTDTLNLRQSASTEAEIITQVPSGKAVTVLN--NEGEWYQVQYGDKQGYLKAEYLKADE 151
Cdd:COG4991   18 AAAAAATAVATDDLNLRSGPGTGYPVVGTLPAGATVTVLGctSGGGWCKVSYGGQRGWVSARYLQVSY 85
 
Name Accession Description Interval E-value
YraI COG4991
Uncharacterized conserved protein YraI [Function unknown];
86-151 8.74e-14

Uncharacterized conserved protein YraI [Function unknown];


Pssm-ID: 444015 [Multi-domain]  Cd Length: 92  Bit Score: 63.54  E-value: 8.74e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 547470631  86 TTQAVLTMYTTDTLNLRQSASTEAEIITQVPSGKAVTVLN--NEGEWYQVQYGDKQGYLKAEYLKADE 151
Cdd:COG4991   18 AAAAAATAVATDDLNLRSGPGTGYPVVGTLPAGATVTVLGctSGGGWCKVSYGGQRGWVSARYLQVSY 85
SH3_3 pfam08239
Bacterial SH3 domain;
97-148 5.48e-11

Bacterial SH3 domain;


Pssm-ID: 462405 [Multi-domain]  Cd Length: 54  Bit Score: 55.33  E-value: 5.48e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 547470631   97 DTLNLRQSASTEAEIITQVPSGKAVTVLN-NEGEWYQVQ-YGDKQGYLKAEYLK 148
Cdd:pfam08239   1 SGLNVRSGPSTSSEVVGTLPKGEKVEVLEeQGGGWYKVRtYDGYEGWVSSSYLS 54
SH3b smart00287
Bacterial SH3 domain homologues;
94-149 8.14e-06

Bacterial SH3 domain homologues;


Pssm-ID: 214600 [Multi-domain]  Cd Length: 63  Bit Score: 41.55  E-value: 8.14e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 547470631    94 YTTDTLNLRQSASTEAEIITQVPSGKAVTVLNNEGE-WYQVQYG-DKQGYLKAEYLKA 149
Cdd:smart00287   6 VTGDGLNVRTGPGTSSPIIGTLKKGDKVKVLGVDGQdWAKITYGsGQRGYVPGYVVNT 63
PRK13914 PRK13914
invasion associated endopeptidase;
79-175 6.18e-04

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 39.40  E-value: 6.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547470631  79 EPTTVEETTQAVLTMYttdtLNLRQSASTEAEIITQVPSGKAVTVLNNEGE-WYQVQYGD-KQGYLKAEYL----KADES 152
Cdd:PRK13914  73 EVAAAEKTEKSVSATW----LNVRSGAGVDNSIITSIKGGTKVTVETTESNgWHKITYNDgKTGFVNGKYLtdkvTSTPV 148
                         90       100
                 ....*....|....*....|...
gi 547470631 153 QTTQQAGESGTVAETTSAVETTS 175
Cdd:PRK13914 149 APTQEVKKETTTQQAAPAAETKT 171
SH3_p47phox_like cd11856
Src homology 3 domains of the p47phox subunit of NADPH oxidase and similar domains; This ...
105-148 8.98e-04

Src homology 3 domains of the p47phox subunit of NADPH oxidase and similar domains; This family is composed of the tandem SH3 domains of p47phox subunit of NADPH oxidase and Nox Organizing protein 1 (NoxO1), the four SH3 domains of Tks4 (Tyr kinase substrate with four SH3 domains), the five SH3 domains of Tks5, the SH3 domain of obscurin, Myosin-I, and similar domains. Most members of this group also contain Phox homology (PX) domains, except for obscurin and Myosin-I. p47phox and NoxO1 are regulators of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) and nonphagocytic NADPH oxidase Nox1, respectively. They play roles in the activation of their respective NADPH oxidase, which catalyzes the transfer of electrons from NADPH to molecular oxygen to form superoxide. Tks proteins are Src substrates and scaffolding proteins that play important roles in the formation of podosomes and invadopodia, the dynamic actin-rich structures that are related to cell migration and cancer cell invasion. Obscurin is a giant muscle protein that plays important roles in the organization and assembly of the myofibril and the sarcoplasmic reticulum. Type I myosins (Myosin-I) are actin-dependent motors in endocytic actin structures and actin patches. They play roles in membrane traffic in endocytic and secretory pathways, cell motility, and mechanosensing. Myosin-I contains an N-terminal actin-activated ATPase, a phospholipid-binding TH1 (tail homology 1) domain, and a C-terminal extension which includes an F-actin-binding TH2 domain, an SH3 domain, and an acidic peptide that participates in activating the Arp2/3complex. The SH3 domain of myosin-I is required for myosin-I-induced actin polymerization. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212790 [Multi-domain]  Cd Length: 53  Bit Score: 35.69  E-value: 8.98e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 547470631 105 ASTEAEIitQVPSGKAVTVL--NNEGEWYqVQYGDKQGYLKAEYLK 148
Cdd:cd11856   10 AQGDDEI--SLQEGEVVEVLekNDSGWWY-VRKGDKEGWVPASYLE 52
 
Name Accession Description Interval E-value
YraI COG4991
Uncharacterized conserved protein YraI [Function unknown];
86-151 8.74e-14

Uncharacterized conserved protein YraI [Function unknown];


Pssm-ID: 444015 [Multi-domain]  Cd Length: 92  Bit Score: 63.54  E-value: 8.74e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 547470631  86 TTQAVLTMYTTDTLNLRQSASTEAEIITQVPSGKAVTVLN--NEGEWYQVQYGDKQGYLKAEYLKADE 151
Cdd:COG4991   18 AAAAAATAVATDDLNLRSGPGTGYPVVGTLPAGATVTVLGctSGGGWCKVSYGGQRGWVSARYLQVSY 85
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
95-160 4.79e-13

Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family [General function prediction only];


Pssm-ID: 442337 [Multi-domain]  Cd Length: 119  Bit Score: 62.45  E-value: 4.79e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 547470631  95 TTDTLNLRQSASTEAEIITQVPSGKAVTVLNNEGEWYQVQYGD-KQGYLKAEYLKADESQTTQQAGE 160
Cdd:COG3103   10 DADALNVRSGPGTSYRIVGTLPKGEKVTVLGRSGGWYKVRYSNgKTGWVSSRYLTVTPSARERLPDE 76
SH3_3 pfam08239
Bacterial SH3 domain;
97-148 5.48e-11

Bacterial SH3 domain;


Pssm-ID: 462405 [Multi-domain]  Cd Length: 54  Bit Score: 55.33  E-value: 5.48e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 547470631   97 DTLNLRQSASTEAEIITQVPSGKAVTVLN-NEGEWYQVQ-YGDKQGYLKAEYLK 148
Cdd:pfam08239   1 SGLNVRSGPSTSSEVVGTLPKGEKVEVLEeQGGGWYKVRtYDGYEGWVSSSYLS 54
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
86-142 8.27e-08

Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family [General function prediction only];


Pssm-ID: 442337 [Multi-domain]  Cd Length: 119  Bit Score: 48.58  E-value: 8.27e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 547470631  86 TTQAVLTMYTTDTLNLRQSASTEAEIITQVPSGKAVTVLNNEGEWYQVQYgDKQGYL 142
Cdd:COG3103   64 TVTPSARERLPDELNLRAGPSTSSEVLGLLPKGETVTVLKKSGGWFKVGY-RGTGWV 119
SH3b smart00287
Bacterial SH3 domain homologues;
94-149 8.14e-06

Bacterial SH3 domain homologues;


Pssm-ID: 214600 [Multi-domain]  Cd Length: 63  Bit Score: 41.55  E-value: 8.14e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 547470631    94 YTTDTLNLRQSASTEAEIITQVPSGKAVTVLNNEGE-WYQVQYG-DKQGYLKAEYLKA 149
Cdd:smart00287   6 VTGDGLNVRTGPGTSSPIIGTLKKGDKVKVLGVDGQdWAKITYGsGQRGYVPGYVVNT 63
SH3 COG3807
SH3-like domain [Function unknown];
95-147 1.67e-04

SH3-like domain [Function unknown];


Pssm-ID: 443020 [Multi-domain]  Cd Length: 150  Bit Score: 39.89  E-value: 1.67e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 547470631  95 TTDTLNLRQSASTEAEIITQVPSGKAVTVLNNEGEWYQVQYGDKQGYLKAEYL 147
Cdd:COG3807   88 TGDLANLRASPDENAAVVARLEPGVVLRLLECDGGWCKVRADGYKGWVRQSLL 140
SH3_16 pfam18348
Bacterial dipeptidyl-peptidase Sh3 domain; This is the first of two N-terminal bacterial SH3 ...
101-145 1.87e-04

Bacterial dipeptidyl-peptidase Sh3 domain; This is the first of two N-terminal bacterial SH3 (SH3b) domains found in bacterial dipeptidyl-peptidases VI such as gamma-D-glutamyl-L-diamino acid endopeptidases. The first SH3b domain plays an important role in defining substrate specificity by contributing to the formation of the active site, such that only murein peptides with a free N-terminal alanine are allowed.


Pssm-ID: 436429  Cd Length: 49  Bit Score: 37.49  E-value: 1.87e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 547470631  101 LRQSASTEAEIITQVPSGKAVTVLNNEGEWYQVQ-----YgdkQGYLKAE 145
Cdd:pfam18348   1 LRDSPDPDAELATQALFGEHLRVLEERDGWAWVQlcedgY---VGWLPLS 47
PRK13914 PRK13914
invasion associated endopeptidase;
79-175 6.18e-04

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 39.40  E-value: 6.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547470631  79 EPTTVEETTQAVLTMYttdtLNLRQSASTEAEIITQVPSGKAVTVLNNEGE-WYQVQYGD-KQGYLKAEYL----KADES 152
Cdd:PRK13914  73 EVAAAEKTEKSVSATW----LNVRSGAGVDNSIITSIKGGTKVTVETTESNgWHKITYNDgKTGFVNGKYLtdkvTSTPV 148
                         90       100
                 ....*....|....*....|...
gi 547470631 153 QTTQQAGESGTVAETTSAVETTS 175
Cdd:PRK13914 149 APTQEVKKETTTQQAAPAAETKT 171
SH3_p47phox_like cd11856
Src homology 3 domains of the p47phox subunit of NADPH oxidase and similar domains; This ...
105-148 8.98e-04

Src homology 3 domains of the p47phox subunit of NADPH oxidase and similar domains; This family is composed of the tandem SH3 domains of p47phox subunit of NADPH oxidase and Nox Organizing protein 1 (NoxO1), the four SH3 domains of Tks4 (Tyr kinase substrate with four SH3 domains), the five SH3 domains of Tks5, the SH3 domain of obscurin, Myosin-I, and similar domains. Most members of this group also contain Phox homology (PX) domains, except for obscurin and Myosin-I. p47phox and NoxO1 are regulators of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) and nonphagocytic NADPH oxidase Nox1, respectively. They play roles in the activation of their respective NADPH oxidase, which catalyzes the transfer of electrons from NADPH to molecular oxygen to form superoxide. Tks proteins are Src substrates and scaffolding proteins that play important roles in the formation of podosomes and invadopodia, the dynamic actin-rich structures that are related to cell migration and cancer cell invasion. Obscurin is a giant muscle protein that plays important roles in the organization and assembly of the myofibril and the sarcoplasmic reticulum. Type I myosins (Myosin-I) are actin-dependent motors in endocytic actin structures and actin patches. They play roles in membrane traffic in endocytic and secretory pathways, cell motility, and mechanosensing. Myosin-I contains an N-terminal actin-activated ATPase, a phospholipid-binding TH1 (tail homology 1) domain, and a C-terminal extension which includes an F-actin-binding TH2 domain, an SH3 domain, and an acidic peptide that participates in activating the Arp2/3complex. The SH3 domain of myosin-I is required for myosin-I-induced actin polymerization. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212790 [Multi-domain]  Cd Length: 53  Bit Score: 35.69  E-value: 8.98e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 547470631 105 ASTEAEIitQVPSGKAVTVL--NNEGEWYqVQYGDKQGYLKAEYLK 148
Cdd:cd11856   10 AQGDDEI--SLQEGEVVEVLekNDSGWWY-VRKGDKEGWVPASYLE 52
 
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