NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1267331323|ref|WP_098174180|]
View 

enterotoxin EntFM, partial [Bacillus toyonensis]

Protein Classification

C40 family peptidase( domain architecture ID 13493742)

C40 family peptidase is a cell-wall hydrolase that cleaves peptide cross-bridges between glycan chains and is essential for bacterial growth and viability; typically cleaves the linkage between D-Glu and diaminopimelic acid (or Lys) within peptidoglycan stem peptides; contains a Cys-His-His catalytic triad

Gene Ontology:  GO:0008233|GO:0016787|GO:0006508
MEROPS:  C40
PubMed:  12620121|11517925

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
NlpC COG0791
Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];
197-363 3.28e-31

Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440554 [Multi-domain]  Cd Length: 218  Bit Score: 117.88  E-value: 3.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323 197 TGAENGWYKINHNGRTGYVSADYVKFVKGGVTGGNQGSNQVQKPTAPTGGDTSSIAGFARSLNGSPYRTAGTTPAGFDCS 276
Cdd:COG0791    49 AALLAGPAAAVAGAAAPAVGSAGAAAAAAAAKAGSSAAKSAAGASAPPSSTAEAIVAAALSYLGTPYVWGGTSPSGFDCS 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323 277 GFIHYVLNQTGHKGARqTVAGYWSSKTK--TSNPQPGDLVYFqNTYKSGPSHMGVYLGNGQFISAETDATGVRISSVSNS 354
Cdd:COG0791   129 GLVQYVYRQAGISLPR-TSADQAAAGTPvsRSELQPGDLVFF-RTGGGGISHVGIYLGNGKFIHASSSGKGVRISSLDSP 206


                  ....*....
gi 1267331323 355 YWSKHILGY 363
Cdd:COG0791   207 YWKSRYVGA 215
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
 2-130 1.74e-29

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: 109.83  E-value: 1.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323   2 TTSELKYTVTADVLNVRSGAGTGHNVISKVKQGQVLQVIGQENGWFKV-SVNGQTGYVSGDFVTTGGNKGTTVQQGtgty 80
Cdd:COG3103     1 AAAETRYVVDADALNVRSGPGTSYRIVGTLPKGEKVTVLGRSGGWYKVrYSNGKTGWVSSRYLTVTPSARERLPDE---- 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1267331323  81 tvnvssLNVRTGPSTSHTVLGSVNKGKTVQVVGEVQDWFKINFNgGTGYV 130
Cdd:COG3103    77 ------LNLRAGPSTSSEVLGLLPKGETVTVLKKSGGWFKVGYR-GTGWV 119
YraI COG4991
Uncharacterized conserved protein YraI [Function unknown];
163-228 4.02e-12

Uncharacterized conserved protein YraI [Function unknown];


:

Pssm-ID: 444015 [Multi-domain]  Cd Length: 92  Bit Score: 61.62  E-value: 4.02e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267331323 163 GSYVVNTGALKVRTGPATYNAVIGGVTNGKVLNVTG--AENGWYKINHNGRTGYVSADYVKFVKGGVT 228
Cdd:COG4991    22 AATAVATDDLNLRSGPGTGYPVVGTLPAGATVTVLGctSGGGWCKVSYGGQRGWVSARYLQVSYDGQP 89
 
Name Accession Description Interval E-value
NlpC COG0791
Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];
197-363 3.28e-31

Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440554 [Multi-domain]  Cd Length: 218  Bit Score: 117.88  E-value: 3.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323 197 TGAENGWYKINHNGRTGYVSADYVKFVKGGVTGGNQGSNQVQKPTAPTGGDTSSIAGFARSLNGSPYRTAGTTPAGFDCS 276
Cdd:COG0791    49 AALLAGPAAAVAGAAAPAVGSAGAAAAAAAAKAGSSAAKSAAGASAPPSSTAEAIVAAALSYLGTPYVWGGTSPSGFDCS 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323 277 GFIHYVLNQTGHKGARqTVAGYWSSKTK--TSNPQPGDLVYFqNTYKSGPSHMGVYLGNGQFISAETDATGVRISSVSNS 354
Cdd:COG0791   129 GLVQYVYRQAGISLPR-TSADQAAAGTPvsRSELQPGDLVFF-RTGGGGISHVGIYLGNGKFIHASSSGKGVRISSLDSP 206


                  ....*....
gi 1267331323 355 YWSKHILGY 363
Cdd:COG0791   207 YWKSRYVGA 215
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
 2-130 1.74e-29

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: 109.83  E-value: 1.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323   2 TTSELKYTVTADVLNVRSGAGTGHNVISKVKQGQVLQVIGQENGWFKV-SVNGQTGYVSGDFVTTGGNKGTTVQQGtgty 80
Cdd:COG3103     1 AAAETRYVVDADALNVRSGPGTSYRIVGTLPKGEKVTVLGRSGGWYKVrYSNGKTGWVSSRYLTVTPSARERLPDE---- 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1267331323  81 tvnvssLNVRTGPSTSHTVLGSVNKGKTVQVVGEVQDWFKINFNgGTGYV 130
Cdd:COG3103    77 ------LNLRAGPSTSSEVLGLLPKGETVTVLKKSGGWFKVGYR-GTGWV 119
NLPC_P60 pfam00877
NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.
 260-362 1.01e-25

NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.


Pssm-ID: 395705 [Multi-domain]  Cd Length: 105  Bit Score: 99.28  E-value: 1.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323 260 GSPYRTAGTTPAGFDCSGFIHYVLNQTGHKGARqtVAGYWSSKTKT----SNPQPGDLVYFQNTYksGPSHMGVYLGNGQ 335
Cdd:pfam00877   1 GVPYRWGGGSPSGFDCSGLVRYAFAKVGIELPR--SSGQQYNAGKKtipkSEPQRGDLVFFGTGK--GISHVGIYLGNGQ 76

                          90       100
                  ....*....|....*....|....*..
gi 1267331323 336 FISAETDaTGVRISSVSNSYWSKHILG 362
Cdd:pfam00877  77 MLHASTG-GGVSISSLNGGYWQKRLVG 102
PRK13914 PRK13914
invasion associated endopeptidase;
2-365 1.74e-24

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 104.11  E-value: 1.74e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323   2 TTSELKYTVTADVLNVRSGAGTGHNVISKVKQGQVLQVIGQE-NGWFKVSVN-GQTGYVSGDFVTT-------------- 65
Cdd:PRK13914   76 AAEKTEKSVSATWLNVRSGAGVDNSIITSIKGGTKVTVETTEsNGWHKITYNdGKTGFVNGKYLTDkvtstpvaptqevk 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323  66 ----------GGNKGTTVQQGTGTYTVNVSSLNVRTGP-----STSHTVLG-------SVNKGKTVQvvgEVQDWFkiNF 123
Cdd:PRK13914  156 ketttqqaapAAETKTEVKQTTQATTPAPKVAETKETPvvdqnATTHAVKSgdtiwalSVKYGVSVQ---DIMSWN--NL 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323 124 NGGTGYVSKDFVTKGGSAVSN-----ETQKPTTNNNNTTTV------------------QTGGSYVVNTGALKVRTGPAT 180
Cdd:PRK13914  231 SSSSIYVGQKLAIKQTANTATpkaevKTEAPAAEKQAAPVVkentntntattekketttQQQTAPKAPTEAAKPAPAPST 310

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323 181 -YNAVIGGVTNGKVLNVTGAENGWYKINHNGRTGYVSADYvkfvkggvTGGNQGSNQVQKPTAptggdTSSIAGFARSLN 259
Cdd:PRK13914  311 nTNANKTNTNTNTNTNNTNTSTPSKNTNTNTNSNTNTNSN--------TNANQGSSNNNSNSS-----ASAIIAEAQKHL 377

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323 260 GSPYRTAGTTPAGFDCSGFIHYVLNQTGHKGARQTVAGYWS-SKTKTSNPQPGDLVYFQntYKSGPSHMGVYLGNGQFIS 338
Cdd:PRK13914  378 GKAYSWGGNGPTTFDCSGYTKYVFAKAGISLPRTSGAQYAStTRISESQAKPGDLVFFD--YGSGISHVGIYVGNGQMIN 455

                         410       420
                  ....*....|....*....|....*..
gi 1267331323 339 AETDatGVRISSVSNSYWSKHILGYTK 365
Cdd:PRK13914  456 AQDN--GVKYDNIHGSGWGKYLVGFGR 480
wall_bind_EntB NF040676
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
 2-136 9.64e-23

cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.


Pssm-ID: 468642 [Multi-domain]  Cd Length: 476  Bit Score: 99.09  E-value: 9.64e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323   2 TTSELKYTVTADVLNVRSGAGTGHNVISKVKQGQVLQVIGQENGWFKVSVNGQTGYVSGDFVTTggnkgttvqqgtgTYT 81
Cdd:NF040676   20 TTATAETIVTADVLNVREKPTTESKVVEKVKNGQELKVINTEDGWSKIELNGKEVFVSSEFTKD-------------VYH 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1267331323  82 VNVSSLNVRTGPSTSHTVLGSVNKGKTVQVVGEVQD-WFKINFNGGTGYVSKDFVT 136
Cdd:NF040676   87 VTANLLNVRTEANTESEILGRLKKDDVIESTHQVKDgWLQFEYKGKTAYANVSFLS 142
YraI COG4991
Uncharacterized conserved protein YraI [Function unknown];
163-228 4.02e-12

Uncharacterized conserved protein YraI [Function unknown];


Pssm-ID: 444015 [Multi-domain]  Cd Length: 92  Bit Score: 61.62  E-value: 4.02e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267331323 163 GSYVVNTGALKVRTGPATYNAVIGGVTNGKVLNVTG--AENGWYKINHNGRTGYVSADYVKFVKGGVT 228
Cdd:COG4991    22 AATAVATDDLNLRSGPGTGYPVVGTLPAGATVTVLGctSGGGWCKVSYGGQRGWVSARYLQVSYDGQP 89
SH3_3 pfam08239
Bacterial SH3 domain;
85-136 1.44e-11

Bacterial SH3 domain;


Pssm-ID: 462405 [Multi-domain]  Cd Length: 54  Bit Score: 58.80  E-value: 1.44e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1267331323  85 SSLNVRTGPSTSHTVLGSVNKGKTVQVVGEV-QDWFKI-NFNGGTGYVSKDFVT 136
Cdd:pfam08239   1 SGLNVRSGPSTSSEVVGTLPKGEKVEVLEEQgGGWYKVrTYDGYEGWVSSSYLS 54
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
 87-221 3.38e-11

sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain.


Pssm-ID: 411609 [Multi-domain]  Cd Length: 312  Bit Score: 63.61  E-value: 3.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323  87 LNVRTGPSTSHTVLGSVNKGKTVQVV---------GEVQD---WFKInfnGGTGYVSKDFVTKGGSAVSNETqkPTTNNN 154
Cdd:NF038016    1 LNVRSGPATDSAVVGTLANGAKVTVVckvrgeqirGTVRTtsqWDRL---GSGRYVSHAYVRWSPSLPTCPW--CAPKAA 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267331323 155 NTTTVQTGGsyvvntGALKVRTGPATYNAVIGGVTNGKVLNVTGAENG--------WYKInhnGRTGYVSADYVK 221
Cdd:NF038016   76 TVATVTTGG------GALNVRAAAGTGAARVGTVANGATVTVECQVWGqevdgtgvWYRL---GDGRYVSAAYVR 141
SH3_3 pfam08239
Bacterial SH3 domain;
170-221 3.35e-10

Bacterial SH3 domain;


Pssm-ID: 462405 [Multi-domain]  Cd Length: 54  Bit Score: 54.95  E-value: 3.35e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1267331323 170 GALKVRTGPATYNAVIGGVTNGKVLNVTGAENG-WYKI-NHNGRTGYVSADYVK 221
Cdd:pfam08239   1 SGLNVRSGPSTSSEVVGTLPKGEKVEVLEEQGGgWYKVrTYDGYEGWVSSSYLS 54
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
 15-118 2.19e-07

sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain.


Pssm-ID: 411609 [Multi-domain]  Cd Length: 312  Bit Score: 52.05  E-value: 2.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323  15 LNVRSGAGTGHNVISKVKQGQ----VLQVIGQE--------NGWFKVsvnGQTGYVSGDFVTTGGNK-----GTTVQQGT 77
Cdd:NF038016    1 LNVRSGPATDSAVVGTLANGAkvtvVCKVRGEQirgtvrttSQWDRL---GSGRYVSHAYVRWSPSLptcpwCAPKAATV 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1267331323  78 GTYTVNVSSLNVRTGPSTSHTVLGSVNKGKTVQVvgEVQDW 118
Cdd:NF038016   78 ATVTTGGGALNVRAAAGTGAARVGTVANGATVTV--ECQVW 116
SH3b smart00287
Bacterial SH3 domain homologues;
79-137 1.58e-06

Bacterial SH3 domain homologues;


Pssm-ID: 214600 [Multi-domain]  Cd Length: 63  Bit Score: 45.02  E-value: 1.58e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267331323   79 TYTVNVSSLNVRTGPSTSHTVLGSVNKGKTVQVVGEV-QDWFKINFNGG-TGYVSKDFVTK 137
Cdd:smart00287   3 TAVVTGDGLNVRTGPGTSSPIIGTLKKGDKVKVLGVDgQDWAKITYGSGqRGYVPGYVVNT 63
SH3_GRAP2_N cd11947
N-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS ...
 32-63 1.30e-04

N-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS (GRB2-related adapter downstream of Shc), GrpL, GRB2L, Mona, or GRID (Grb2-related protein with insert domain). It is expressed specifically in the hematopoietic system. It plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. It also have roles in antigen-receptor and tyrosine kinase mediated signaling. GRAP2 is unique from other GRB2-like adaptor proteins in that it can be regulated by caspase cleavage. It contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The N-terminal SH3 domain of the related protein GRB2 binds to Sos and Sos-derived proline-rich peptides. 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: 212880 [Multi-domain]  Cd Length: 52  Bit Score: 39.39  E-value: 1.30e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1267331323  32 KQGQVLQVIGQENGWFKVSVNGQTGYVSGDFV 63
Cdd:cd11947    19 KKGDVLKILSSDDIWFKAELNGEEGYVPKNFV 50
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
 16-65 6.32e-04

SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.


Pssm-ID: 275056 [Multi-domain]  Cd Length: 198  Bit Score: 40.38  E-value: 6.32e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1267331323  16 NVRSGAGTGHNVISKVKQGQVLQVIGQ-ENGWFKV-SVNGQTGYVSGDFVTT 65
Cdd:TIGR04211   9 YMRSGPGNQYRILGSLKSGTPVTVLERsEDGYSRVrTPKGREGWVLSRYLSD 60
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
 174-220 7.17e-03

SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.


Pssm-ID: 275056 [Multi-domain]  Cd Length: 198  Bit Score: 37.29  E-value: 7.17e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1267331323 174 VRTGPATYNAVIGGVTNG---KVLNVTgaENGWYKI-NHNGRTGYVSADYV 220
Cdd:TIGR04211  10 MRSGPGNQYRILGSLKSGtpvTVLERS--EDGYSRVrTPKGREGWVLSRYL 58
 
Name Accession Description Interval E-value
NlpC COG0791
Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];
197-363 3.28e-31

Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440554 [Multi-domain]  Cd Length: 218  Bit Score: 117.88  E-value: 3.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323 197 TGAENGWYKINHNGRTGYVSADYVKFVKGGVTGGNQGSNQVQKPTAPTGGDTSSIAGFARSLNGSPYRTAGTTPAGFDCS 276
Cdd:COG0791    49 AALLAGPAAAVAGAAAPAVGSAGAAAAAAAAKAGSSAAKSAAGASAPPSSTAEAIVAAALSYLGTPYVWGGTSPSGFDCS 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323 277 GFIHYVLNQTGHKGARqTVAGYWSSKTK--TSNPQPGDLVYFqNTYKSGPSHMGVYLGNGQFISAETDATGVRISSVSNS 354
Cdd:COG0791   129 GLVQYVYRQAGISLPR-TSADQAAAGTPvsRSELQPGDLVFF-RTGGGGISHVGIYLGNGKFIHASSSGKGVRISSLDSP 206


                  ....*....
gi 1267331323 355 YWSKHILGY 363
Cdd:COG0791   207 YWKSRYVGA 215
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
 2-130 1.74e-29

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: 109.83  E-value: 1.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323   2 TTSELKYTVTADVLNVRSGAGTGHNVISKVKQGQVLQVIGQENGWFKV-SVNGQTGYVSGDFVTTGGNKGTTVQQGtgty 80
Cdd:COG3103     1 AAAETRYVVDADALNVRSGPGTSYRIVGTLPKGEKVTVLGRSGGWYKVrYSNGKTGWVSSRYLTVTPSARERLPDE---- 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1267331323  81 tvnvssLNVRTGPSTSHTVLGSVNKGKTVQVVGEVQDWFKINFNgGTGYV 130
Cdd:COG3103    77 ------LNLRAGPSTSSEVLGLLPKGETVTVLKKSGGWFKVGYR-GTGWV 119
NLPC_P60 pfam00877
NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.
 260-362 1.01e-25

NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.


Pssm-ID: 395705 [Multi-domain]  Cd Length: 105  Bit Score: 99.28  E-value: 1.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323 260 GSPYRTAGTTPAGFDCSGFIHYVLNQTGHKGARqtVAGYWSSKTKT----SNPQPGDLVYFQNTYksGPSHMGVYLGNGQ 335
Cdd:pfam00877   1 GVPYRWGGGSPSGFDCSGLVRYAFAKVGIELPR--SSGQQYNAGKKtipkSEPQRGDLVFFGTGK--GISHVGIYLGNGQ 76

                          90       100
                  ....*....|....*....|....*..
gi 1267331323 336 FISAETDaTGVRISSVSNSYWSKHILG 362
Cdd:pfam00877  77 MLHASTG-GGVSISSLNGGYWQKRLVG 102
PRK13914 PRK13914
invasion associated endopeptidase;
2-365 1.74e-24

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 104.11  E-value: 1.74e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323   2 TTSELKYTVTADVLNVRSGAGTGHNVISKVKQGQVLQVIGQE-NGWFKVSVN-GQTGYVSGDFVTT-------------- 65
Cdd:PRK13914   76 AAEKTEKSVSATWLNVRSGAGVDNSIITSIKGGTKVTVETTEsNGWHKITYNdGKTGFVNGKYLTDkvtstpvaptqevk 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323  66 ----------GGNKGTTVQQGTGTYTVNVSSLNVRTGP-----STSHTVLG-------SVNKGKTVQvvgEVQDWFkiNF 123
Cdd:PRK13914  156 ketttqqaapAAETKTEVKQTTQATTPAPKVAETKETPvvdqnATTHAVKSgdtiwalSVKYGVSVQ---DIMSWN--NL 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323 124 NGGTGYVSKDFVTKGGSAVSN-----ETQKPTTNNNNTTTV------------------QTGGSYVVNTGALKVRTGPAT 180
Cdd:PRK13914  231 SSSSIYVGQKLAIKQTANTATpkaevKTEAPAAEKQAAPVVkentntntattekketttQQQTAPKAPTEAAKPAPAPST 310

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323 181 -YNAVIGGVTNGKVLNVTGAENGWYKINHNGRTGYVSADYvkfvkggvTGGNQGSNQVQKPTAptggdTSSIAGFARSLN 259
Cdd:PRK13914  311 nTNANKTNTNTNTNTNNTNTSTPSKNTNTNTNSNTNTNSN--------TNANQGSSNNNSNSS-----ASAIIAEAQKHL 377

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323 260 GSPYRTAGTTPAGFDCSGFIHYVLNQTGHKGARQTVAGYWS-SKTKTSNPQPGDLVYFQntYKSGPSHMGVYLGNGQFIS 338
Cdd:PRK13914  378 GKAYSWGGNGPTTFDCSGYTKYVFAKAGISLPRTSGAQYAStTRISESQAKPGDLVFFD--YGSGISHVGIYVGNGQMIN 455

                         410       420
                  ....*....|....*....|....*..
gi 1267331323 339 AETDatGVRISSVSNSYWSKHILGYTK 365
Cdd:PRK13914  456 AQDN--GVKYDNIHGSGWGKYLVGFGR 480
wall_bind_EntB NF040676
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
 2-136 9.64e-23

cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.


Pssm-ID: 468642 [Multi-domain]  Cd Length: 476  Bit Score: 99.09  E-value: 9.64e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323   2 TTSELKYTVTADVLNVRSGAGTGHNVISKVKQGQVLQVIGQENGWFKVSVNGQTGYVSGDFVTTggnkgttvqqgtgTYT 81
Cdd:NF040676   20 TTATAETIVTADVLNVREKPTTESKVVEKVKNGQELKVINTEDGWSKIELNGKEVFVSSEFTKD-------------VYH 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1267331323  82 VNVSSLNVRTGPSTSHTVLGSVNKGKTVQVVGEVQD-WFKINFNGGTGYVSKDFVT 136
Cdd:NF040676   87 VTANLLNVRTEANTESEILGRLKKDDVIESTHQVKDgWLQFEYKGKTAYANVSFLS 142
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
 75-215 6.26e-22

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: 89.80  E-value: 6.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323  75 QGTGTYTVNVSSLNVRTGPSTSHTVLGSVNKGKTVQVVGEVQDWFKINF-NGGTGYVSKDFVTKGGSAVsnetqkpttnn 153
Cdd:COG3103     2 AAETRYVVDADALNVRSGPGTSYRIVGTLPKGEKVTVLGRSGGWYKVRYsNGKTGWVSSRYLTVTPSAR----------- 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1267331323 154 nntttvqtggsyVVNTGALKVRTGPATYNAVIGGVTNGKVLNVTGAENGWYKINHNGrTGYV 215
Cdd:COG3103    71 ------------ERLPDELNLRAGPSTSSEVLGLLPKGETVTVLKKSGGWFKVGYRG-TGWV 119
spr PRK10838
bifunctional murein DD-endopeptidase/murein LD-carboxypeptidase;
260-358 6.26e-14

bifunctional murein DD-endopeptidase/murein LD-carboxypeptidase;


Pssm-ID: 236773 [Multi-domain]  Cd Length: 190  Bit Score: 69.41  E-value: 6.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323 260 GSPYRTAGTTPAGFDCSGFIHYVL-NQTGHKGARQTV----AGywsSKTKTSNPQPGDLVYFqntyKSGPS--HMGVYLG 332
Cdd:PRK10838   79 GVRYRLGGSTKKGIDCSAFVQRTFrEQFGLELPRSTYeqqeMG---KSVSRSKLRTGDLVLF----RAGSTgrHVGIYIG 151

                          90       100
                  ....*....|....*....|....*.
gi 1267331323 333 NGQFISAETdATGVRISSVSNSYWSK 358
Cdd:PRK10838  152 NNQFVHAST-SSGVIISSMNEPYWKK 176
YraI COG4991
Uncharacterized conserved protein YraI [Function unknown];
9-74 1.19e-12

Uncharacterized conserved protein YraI [Function unknown];


Pssm-ID: 444015 [Multi-domain]  Cd Length: 92  Bit Score: 63.16  E-value: 1.19e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267331323   9 TVTADVLNVRSGAGTGHNVISKVKQGQVLQVIG--QENGWFKVSVNGQTGYVSGDFVTTGGNKGTTVQ 74
Cdd:COG4991    25 AVATDDLNLRSGPGTGYPVVGTLPAGATVTVLGctSGGGWCKVSYGGQRGWVSARYLQVSYDGQPVPL 92
YraI COG4991
Uncharacterized conserved protein YraI [Function unknown];
78-139 1.78e-12

Uncharacterized conserved protein YraI [Function unknown];


Pssm-ID: 444015 [Multi-domain]  Cd Length: 92  Bit Score: 62.77  E-value: 1.78e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267331323  78 GTYTVNVSSLNVRTGPSTSHTVLGSVNKGKTVQVVGEVQD--WFKINFNGGTGYVSKDFVTKGG 139
Cdd:COG4991    22 AATAVATDDLNLRSGPGTGYPVVGTLPAGATVTVLGCTSGggWCKVSYGGQRGWVSARYLQVSY 85
YraI COG4991
Uncharacterized conserved protein YraI [Function unknown];
163-228 4.02e-12

Uncharacterized conserved protein YraI [Function unknown];


Pssm-ID: 444015 [Multi-domain]  Cd Length: 92  Bit Score: 61.62  E-value: 4.02e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267331323 163 GSYVVNTGALKVRTGPATYNAVIGGVTNGKVLNVTG--AENGWYKINHNGRTGYVSADYVKFVKGGVT 228
Cdd:COG4991    22 AATAVATDDLNLRSGPGTGYPVVGTLPAGATVTVLGctSGGGWCKVSYGGQRGWVSARYLQVSYDGQP 89
SH3_3 pfam08239
Bacterial SH3 domain;
85-136 1.44e-11

Bacterial SH3 domain;


Pssm-ID: 462405 [Multi-domain]  Cd Length: 54  Bit Score: 58.80  E-value: 1.44e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1267331323  85 SSLNVRTGPSTSHTVLGSVNKGKTVQVVGEV-QDWFKI-NFNGGTGYVSKDFVT 136
Cdd:pfam08239   1 SGLNVRSGPSTSSEVVGTLPKGEKVEVLEEQgGGWYKVrTYDGYEGWVSSSYLS 54
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
 165-235 3.14e-11

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: 60.14  E-value: 3.14e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1267331323 165 YVVNTGALKVRTGPATYNAVIGGVTNGKVLNVTGAENGWYKINH-NGRTGYVSADYVKFVKGGVTGGNQGSN 235
Cdd:COG3103     7 YVVDADALNVRSGPGTSYRIVGTLPKGEKVTVLGRSGGWYKVRYsNGKTGWVSSRYLTVTPSARERLPDELN 78
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
 87-221 3.38e-11

sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain.


Pssm-ID: 411609 [Multi-domain]  Cd Length: 312  Bit Score: 63.61  E-value: 3.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323  87 LNVRTGPSTSHTVLGSVNKGKTVQVV---------GEVQD---WFKInfnGGTGYVSKDFVTKGGSAVSNETqkPTTNNN 154
Cdd:NF038016    1 LNVRSGPATDSAVVGTLANGAKVTVVckvrgeqirGTVRTtsqWDRL---GSGRYVSHAYVRWSPSLPTCPW--CAPKAA 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267331323 155 NTTTVQTGGsyvvntGALKVRTGPATYNAVIGGVTNGKVLNVTGAENG--------WYKInhnGRTGYVSADYVK 221
Cdd:NF038016   76 TVATVTTGG------GALNVRAAAGTGAARVGTVANGATVTVECQVWGqevdgtgvWYRL---GDGRYVSAAYVR 141
SH3 COG3807
SH3-like domain [Function unknown];
49-220 1.70e-10

SH3-like domain [Function unknown];


Pssm-ID: 443020 [Multi-domain]  Cd Length: 150  Bit Score: 58.76  E-value: 1.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323  49 VSVNGQTGYVSG----DFVTTGGNKGttvqqgtgtytvnvsslNVRTGPSTSHTVLGSVN-KGKTVQVVGEVQDWFKI-N 122
Cdd:COG3807     4 AAAAAQLGPVSGlpapRFVSLKSDEV-----------------NLRDGPSTKYPILWVYKrRGLPVEVIAEFGNWRRVrD 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323 123 FNGGTGYVSKdfvtkggSAVSNETqkpttnnnntttvqtggSYVVNTGALKVRTGPATYNAVIGGVTNGKVLNVTGAENG 202
Cdd:COG3807    67 PEGDEGWVHQ-------SLLSGRR-----------------TVIVTGDLANLRASPDENAAVVARLEPGVVLRLLECDGG 122

                         170
                  ....*....|....*...
gi 1267331323 203 WYKINHNGRTGYVSADYV 220
Cdd:COG3807   123 WCKVRADGYKGWVRQSLL 140
SH3_3 pfam08239
Bacterial SH3 domain;
170-221 3.35e-10

Bacterial SH3 domain;


Pssm-ID: 462405 [Multi-domain]  Cd Length: 54  Bit Score: 54.95  E-value: 3.35e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1267331323 170 GALKVRTGPATYNAVIGGVTNGKVLNVTGAENG-WYKI-NHNGRTGYVSADYVK 221
Cdd:pfam08239   1 SGLNVRSGPSTSSEVVGTLPKGEKVEVLEEQGGgWYKVrTYDGYEGWVSSSYLS 54
SH3_3 pfam08239
Bacterial SH3 domain;
13-64 4.20e-10

Bacterial SH3 domain;


Pssm-ID: 462405 [Multi-domain]  Cd Length: 54  Bit Score: 54.95  E-value: 4.20e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1267331323  13 DVLNVRSGAGTGHNVISKVKQGQVLQVIG-QENGWFKV-SVNGQTGYVSGDFVT 64
Cdd:pfam08239   1 SGLNVRSGPSTSSEVVGTLPKGEKVEVLEeQGGGWYKVrTYDGYEGWVSSSYLS 54
SH3 COG3807
SH3-like domain [Function unknown];
10-63 1.16e-08

SH3-like domain [Function unknown];


Pssm-ID: 443020 [Multi-domain]  Cd Length: 150  Bit Score: 53.37  E-value: 1.16e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1267331323  10 VTADVLNVRSGAGTGHNVISKVKQGQVLQVIGQENGWFKVSVNGQTGYVSGDFV 63
Cdd:COG3807    87 VTGDLANLRASPDENAAVVARLEPGVVLRLLECDGGWCKVRADGYKGWVRQSLL 140
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
 15-118 2.19e-07

sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain.


Pssm-ID: 411609 [Multi-domain]  Cd Length: 312  Bit Score: 52.05  E-value: 2.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323  15 LNVRSGAGTGHNVISKVKQGQ----VLQVIGQE--------NGWFKVsvnGQTGYVSGDFVTTGGNK-----GTTVQQGT 77
Cdd:NF038016    1 LNVRSGPATDSAVVGTLANGAkvtvVCKVRGEQirgtvrttSQWDRL---GSGRYVSHAYVRWSPSLptcpwCAPKAATV 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1267331323  78 GTYTVNVSSLNVRTGPSTSHTVLGSVNKGKTVQVvgEVQDW 118
Cdd:NF038016   78 ATVTTGGGALNVRAAAGTGAARVGTVANGATVTV--ECQVW 116
SH3b smart00287
Bacterial SH3 domain homologues;
79-137 1.58e-06

Bacterial SH3 domain homologues;


Pssm-ID: 214600 [Multi-domain]  Cd Length: 63  Bit Score: 45.02  E-value: 1.58e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267331323   79 TYTVNVSSLNVRTGPSTSHTVLGSVNKGKTVQVVGEV-QDWFKINFNGG-TGYVSKDFVTK 137
Cdd:smart00287   3 TAVVTGDGLNVRTGPGTSSPIIGTLKKGDKVKVLGVDgQDWAKITYGSGqRGYVPGYVVNT 63
SH3b smart00287
Bacterial SH3 domain homologues;
8-65 4.53e-05

Bacterial SH3 domain homologues;


Pssm-ID: 214600 [Multi-domain]  Cd Length: 63  Bit Score: 40.78  E-value: 4.53e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267331323    8 YTVTADVLNVRSGAGTGHNVISKVKQGQVLQVIGQEN-GWFKVSV-NGQTGYVSGDFVTT 65
Cdd:smart00287   4 AVVTGDGLNVRTGPGTSSPIIGTLKKGDKVKVLGVDGqDWAKITYgSGQRGYVPGYVVNT 63
SH3_GRAP2_N cd11947
N-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS ...
 32-63 1.30e-04

N-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS (GRB2-related adapter downstream of Shc), GrpL, GRB2L, Mona, or GRID (Grb2-related protein with insert domain). It is expressed specifically in the hematopoietic system. It plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. It also have roles in antigen-receptor and tyrosine kinase mediated signaling. GRAP2 is unique from other GRB2-like adaptor proteins in that it can be regulated by caspase cleavage. It contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The N-terminal SH3 domain of the related protein GRB2 binds to Sos and Sos-derived proline-rich peptides. 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: 212880 [Multi-domain]  Cd Length: 52  Bit Score: 39.39  E-value: 1.30e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1267331323  32 KQGQVLQVIGQENGWFKVSVNGQTGYVSGDFV 63
Cdd:cd11947    19 KKGDVLKILSSDDIWFKAELNGEEGYVPKNFV 50
SH3_4 pfam06347
Bacterial SH3 domain; SH3 (src Homology-3) domains are small protein modules containing ...
 12-58 2.20e-04

Bacterial SH3 domain; SH3 (src Homology-3) domains are small protein modules containing approximately 50 amino acid residues. They are found in a great variety of intracellular or membrane-associated proteins, in a variety of proteins with enzymatic activity, in adaptor proteins, such as fodrin and yeast actin binding protein ABP-1. The SH3 domain has a characteriztic fold which consists of five or six beta-strands arranged as two tightly packed anti-parallel beta sheets. The linker regions may contain short helices. The surface of the SH3-domain bears a flat, hydrophobic ligand-binding pocket which consists of three shallow grooves defined by conservative aromatic residues in which the ligand adopts an extended left-handed helical arrangement. The ligand binds with low affinity but this may be enhanced by multiple interactions. The region bound by the SH3 domain is in all cases proline-rich and contains PXXP as a core-conserved binding motif. The function of the SH3 domain is not well understood but they may mediate many diverse processes such as increasing local concentration of proteins, altering their subcellular location and mediating the assembly of large multiprotein complexes. This family consists of several hypothetical bacterial proteins of unknown function, but that contain an SH-3 region. Family members include probable invasion-associated protein p60 that are conceptually translated from iap genes. The iap gene, which is regarded as a virulence-associated gene in L. monocytogenes, codes for a gene product that has murein-lytic activity and is involved in cell division.


Pssm-ID: 428898 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 2.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1267331323  12 ADVLNVRSGAGTGHNVISKVKQGQVLQVIGQENGWFKVSV-NGQTGYV 58
Cdd:pfam06347   2 KDEVNLRRGPSDKAAVAAYLEAGVPVRVVACKDNWCRVRDaDGAEGWI 49
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
 16-65 6.32e-04

SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.


Pssm-ID: 275056 [Multi-domain]  Cd Length: 198  Bit Score: 40.38  E-value: 6.32e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1267331323  16 NVRSGAGTGHNVISKVKQGQVLQVIGQ-ENGWFKV-SVNGQTGYVSGDFVTT 65
Cdd:TIGR04211   9 YMRSGPGNQYRILGSLKSGTPVTVLERsEDGYSRVrTPKGREGWVLSRYLSD 60
SH3_GRAP2_N cd11947
N-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS ...
 102-135 2.75e-03

N-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS (GRB2-related adapter downstream of Shc), GrpL, GRB2L, Mona, or GRID (Grb2-related protein with insert domain). It is expressed specifically in the hematopoietic system. It plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. It also have roles in antigen-receptor and tyrosine kinase mediated signaling. GRAP2 is unique from other GRB2-like adaptor proteins in that it can be regulated by caspase cleavage. It contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The N-terminal SH3 domain of the related protein GRB2 binds to Sos and Sos-derived proline-rich peptides. 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: 212880 [Multi-domain]  Cd Length: 52  Bit Score: 35.54  E-value: 2.75e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1267331323 102 SVNKGKTVQVVGEVQDWFKINFNGGTGYVSKDFV 135
Cdd:cd11947    17 SFKKGDVLKILSSDDIWFKAELNGEEGYVPKNFV 50
SH3_PSTPIP1 cd11824
Src homology 3 domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; PSTPIP1, ...
 31-64 4.18e-03

Src homology 3 domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; PSTPIP1, also called CD2 Binding Protein 1 (CD2BP1), is mainly expressed in hematopoietic cells. It is a binding partner of the cell surface receptor CD2 and PTP-PEST, a tyrosine phosphatase which functions in cell motility and Rac1 regulation. It also plays a role in the activation of the Wiskott-Aldrich syndrome protein (WASP), which couples actin rearrangement and T cell activation. Mutations in the gene encoding PSTPIP1 cause the autoinflammatory disorder known as PAPA (pyogenic sterile arthritis, pyoderma gangrenosum, and acne) syndrome. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain. 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: 212758 [Multi-domain]  Cd Length: 53  Bit Score: 35.04  E-value: 4.18e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1267331323  31 VKQGQVLQVIGQ-ENGWFKVSVNGQTGYVSGDFVT 64
Cdd:cd11824    18 ISKGDVVAVIEKgEDGWWTVERNGQKGLVPGTYLE 52
SH3_4 pfam06347
Bacterial SH3 domain; SH3 (src Homology-3) domains are small protein modules containing ...
 88-132 5.69e-03

Bacterial SH3 domain; SH3 (src Homology-3) domains are small protein modules containing approximately 50 amino acid residues. They are found in a great variety of intracellular or membrane-associated proteins, in a variety of proteins with enzymatic activity, in adaptor proteins, such as fodrin and yeast actin binding protein ABP-1. The SH3 domain has a characteriztic fold which consists of five or six beta-strands arranged as two tightly packed anti-parallel beta sheets. The linker regions may contain short helices. The surface of the SH3-domain bears a flat, hydrophobic ligand-binding pocket which consists of three shallow grooves defined by conservative aromatic residues in which the ligand adopts an extended left-handed helical arrangement. The ligand binds with low affinity but this may be enhanced by multiple interactions. The region bound by the SH3 domain is in all cases proline-rich and contains PXXP as a core-conserved binding motif. The function of the SH3 domain is not well understood but they may mediate many diverse processes such as increasing local concentration of proteins, altering their subcellular location and mediating the assembly of large multiprotein complexes. This family consists of several hypothetical bacterial proteins of unknown function, but that contain an SH-3 region. Family members include probable invasion-associated protein p60 that are conceptually translated from iap genes. The iap gene, which is regarded as a virulence-associated gene in L. monocytogenes, codes for a gene product that has murein-lytic activity and is involved in cell division.


Pssm-ID: 428898 [Multi-domain]  Cd Length: 56  Bit Score: 34.63  E-value: 5.69e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1267331323  88 NVRTGPSTSHTVLGSVNKGKTVQVVGEVQDWFKINF-NGGTGYVSK 132
Cdd:pfam06347   6 NLRRGPSDKAAVAAYLEAGVPVRVVACKDNWCRVRDaDGAEGWIYK 51
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
 174-220 7.17e-03

SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.


Pssm-ID: 275056 [Multi-domain]  Cd Length: 198  Bit Score: 37.29  E-value: 7.17e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1267331323 174 VRTGPATYNAVIGGVTNG---KVLNVTgaENGWYKI-NHNGRTGYVSADYV 220
Cdd:TIGR04211  10 MRSGPGNQYRILGSLKSGtpvTVLERS--EDGYSRVrTPKGREGWVLSRYL 58
 
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