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Conserved domains on  [gi|446678152|ref|WP_000755498|]
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MULTISPECIES: enterotoxin EntFM [Bacillus]

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

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List of domain hits

 Name Accession Description Interval E-value
NlpC COG0791
Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];
278-426 6.92e-30

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


:

Pssm-ID: 440554 [Multi-domain]  Cd Length: 218  Bit Score: 115.57  E-value: 6.92e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152 278 VKGGVNNVTNNNNVTNNVQQPGKDVQKPTTGGDTSSIAGFARSLNGSPYRTAGTTPAGFDCSGFIHYVLNQTGHKGARqT 357
Cdd:COG0791   67 VGSAGAAAAAAAAKAGSSAAKSAAGASAPPSSTAEAIVAAALSYLGTPYVWGGTSPSGFDCSGLVQYVYRQAGISLPR-T 145

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446678152 358 VAGYWSSKTK--TSNPQPGDLVYFqNTYKSGPSHMGVYLGNGQFISAETDATGVRISSVSNSYWSKHLLGY 426
Cdd:COG0791  146 SADQAAAGTPvsRSELQPGDLVFF-RTGGGGISHVGIYLGNGKFIHASSSGKGVRISSLDSPYWKSRYVGA 215
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
 60-186 2.94e-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: 110.60  E-value: 2.94e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152  60 SELKYTVTADVLNVRSGAGTGHNVISKVKSGQVLQVVGQENGWFKVN-VNGQTGYVSGDFvttggktgttVQQGTGTYTV 138
Cdd:COG3103    3 AETRYVVDADALNVRSGPGTSYRIVGTLPKGEKVTVLGRSGGWYKVRySNGKTGWVSSRY----------LTVTPSARER 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446678152 139 NVSSLNVRTGPSTSHTVLGSVNKGKTVQVVGEVQDWFKINFNgGTGYV 186
Cdd:COG3103   73 LPDELNLRAGPSTSSEVLGLLPKGETVTVLKKSGGWFKVGYR-GTGWV 119
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
 131-270 5.82e-23

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: 93.26  E-value: 5.82e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152 131 QGTGTYTVNVSSLNVRTGPSTSHTVLGSVNKGKTVQVVGEVQDWFKINF-NGGTGYVSKDFVTKGGSAVsnetqqpttnn 209
Cdd:COG3103    2 AAETRYVVDADALNVRSGPGTSYRIVGTLPKGEKVTVLGRSGGWYKVRYsNGKTGWVSSRYLTVTPSAR----------- 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446678152 210 ntttvqtggsyVVNTGALKVRTGPATYNAVIGGVTNGKVLNVTGAENGWYKINHNGrTGYV 270
Cdd:COG3103   71 -----------ERLPDELNLRAGPSTSSEVLGLLPKGETVTVLKKSGGWFKVGYRG-TGWV 119
 
Name Accession Description Interval E-value
NlpC COG0791
Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];
278-426 6.92e-30

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


Pssm-ID: 440554 [Multi-domain]  Cd Length: 218  Bit Score: 115.57  E-value: 6.92e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152 278 VKGGVNNVTNNNNVTNNVQQPGKDVQKPTTGGDTSSIAGFARSLNGSPYRTAGTTPAGFDCSGFIHYVLNQTGHKGARqT 357
Cdd:COG0791   67 VGSAGAAAAAAAAKAGSSAAKSAAGASAPPSSTAEAIVAAALSYLGTPYVWGGTSPSGFDCSGLVQYVYRQAGISLPR-T 145

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446678152 358 VAGYWSSKTK--TSNPQPGDLVYFqNTYKSGPSHMGVYLGNGQFISAETDATGVRISSVSNSYWSKHLLGY 426
Cdd:COG0791  146 SADQAAAGTPvsRSELQPGDLVFF-RTGGGGISHVGIYLGNGKFIHASSSGKGVRISSLDSPYWKSRYVGA 215
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
 60-186 2.94e-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: 110.60  E-value: 2.94e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152  60 SELKYTVTADVLNVRSGAGTGHNVISKVKSGQVLQVVGQENGWFKVN-VNGQTGYVSGDFvttggktgttVQQGTGTYTV 138
Cdd:COG3103    3 AETRYVVDADALNVRSGPGTSYRIVGTLPKGEKVTVLGRSGGWYKVRySNGKTGWVSSRY----------LTVTPSARER 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446678152 139 NVSSLNVRTGPSTSHTVLGSVNKGKTVQVVGEVQDWFKINFNgGTGYV 186
Cdd:COG3103   73 LPDELNLRAGPSTSSEVLGLLPKGETVTVLKKSGGWFKVGYR-GTGWV 119
NLPC_P60 pfam00877
NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.
 323-425 1.59e-26

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: 102.36  E-value: 1.59e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152  323 GSPYRTAGTTPAGFDCSGFIHYVLNQTGHKGARqtVAGYWSSKTKT----SNPQPGDLVYFQNTYksGPSHMGVYLGNGQ 398
Cdd:pfam00877   1 GVPYRWGGGSPSGFDCSGLVRYAFAKVGIELPR--SSGQQYNAGKKtipkSEPQRGDLVFFGTGK--GISHVGIYLGNGQ 76

                          90       100
                  ....*....|....*....|....*..
gi 446678152  399 FISAETDaTGVRISSVSNSYWSKHLLG 425
Cdd:pfam00877  77 MLHASTG-GGVSISSLNGGYWQKRLVG 102
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
 131-270 5.82e-23

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: 93.26  E-value: 5.82e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152 131 QGTGTYTVNVSSLNVRTGPSTSHTVLGSVNKGKTVQVVGEVQDWFKINF-NGGTGYVSKDFVTKGGSAVsnetqqpttnn 209
Cdd:COG3103    2 AAETRYVVDADALNVRSGPGTSYRIVGTLPKGEKVTVLGRSGGWYKVRYsNGKTGWVSSRYLTVTPSAR----------- 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446678152 210 ntttvqtggsyVVNTGALKVRTGPATYNAVIGGVTNGKVLNVTGAENGWYKINHNGrTGYV 270
Cdd:COG3103   71 -----------ERLPDELNLRAGPSTSSEVLGLLPKGETVTVLKKSGGWFKVGYRG-TGWV 119
PRK13914 PRK13914
invasion associated endopeptidase;
65-428 4.85e-22

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 97.95  E-value: 4.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152  65 TVTADVLNVRSGAGTGHNVISKVKSGQVLQVVGQE-NGWFKVNVN-GQTGYVSGDFVTTGGKTG---------------- 126
Cdd:PRK13914  83 SVSATWLNVRSGAGVDNSIITSIKGGTKVTVETTEsNGWHKITYNdGKTGFVNGKYLTDKVTSTpvaptqevkketttqq 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152 127 --------TTVQQGTGTYTVNVSSLNVRTGP-----STSHTVLG-------SVNKGKTVQvvgEVQDWFkiNFNGGTGYV 186
Cdd:PRK13914 163 aapaaetkTEVKQTTQATTPAPKVAETKETPvvdqnATTHAVKSgdtiwalSVKYGVSVQ---DIMSWN--NLSSSSIYV 237

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152 187 SKDFVTKGGSAVSNETQQPTTNNNTTTVQTGGSYVVNTGALKVRTGPATYNAVIGGVTNGKVLNVTGAENGWYKINHNGR 266
Cdd:PRK13914 238 GQKLAIKQTANTATPKAEVKTEAPAAEKQAAPVVKENTNTNTATTEKKETTTQQQTAPKAPTEAAKPAPAPSTNTNANKT 317

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152 267 TGYVSADFVKFVKGGVNNVTNNNNVTNNVQQPGKDVQKPTTGGDTSSIAGF----ARSLNGSPYRTAGTTPAGFDCSGFI 342
Cdd:PRK13914 318 NTNTNTNTNNTNTSTPSKNTNTNTNSNTNTNSNTNANQGSSNNNSNSSASAiiaeAQKHLGKAYSWGGNGPTTFDCSGYT 397

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152 343 HYVLNQTGHKGARQTVAGYWS-SKTKTSNPQPGDLVYFQntYKSGPSHMGVYLGNGQFISAETDatGVRISSVSNSYWSK 421
Cdd:PRK13914 398 KYVFAKAGISLPRTSGAQYAStTRISESQAKPGDLVFFD--YGSGISHVGIYVGNGQMINAQDN--GVKYDNIHGSGWGK 473


                 ....*..
gi 446678152 422 HLLGYTK 428
Cdd:PRK13914 474 YLVGFGR 480
wall_bind_EntB NF040676
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
 66-192 3.09e-21

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: 95.62  E-value: 3.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152  66 VTADVLNVRSGAGTGHNVISKVKSGQVLQVVGQENGWFKVNVNGQTGYVSGDFVTTggktgttvqqgtgTYTVNVSSLNV 145
Cdd:NF040676  28 VTADVLNVREKPTTESKVVEKVKNGQELKVINTEDGWSKIELNGKEVFVSSEFTKD-------------VYHVTANLLNV 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446678152 146 RTGPSTSHTVLGSVNKGKTVQVVGEVQD-WFKINFNGGTGYVSKDFVT 192
Cdd:NF040676  95 RTEANTESEILGRLKKDDVIESTHQVKDgWLQFEYKGKTAYANVSFLS 142
SH3_3 pfam08239
Bacterial SH3 domain;
141-192 7.21e-12

Bacterial SH3 domain;


Pssm-ID: 462405 [Multi-domain]  Cd Length: 54  Bit Score: 59.95  E-value: 7.21e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446678152  141 SSLNVRTGPSTSHTVLGSVNKGKTVQVVGEV-QDWFKI-NFNGGTGYVSKDFVT 192
Cdd:pfam08239   1 SGLNVRSGPSTSSEVVGTLPKGEKVEVLEEQgGGWYKVrTYDGYEGWVSSSYLS 54
SH3_3 pfam08239
Bacterial SH3 domain;
225-276 4.89e-10

Bacterial SH3 domain;


Pssm-ID: 462405 [Multi-domain]  Cd Length: 54  Bit Score: 54.95  E-value: 4.89e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446678152  225 GALKVRTGPATYNAVIGGVTNGKVLNVTGAENG-WYKI-NHNGRTGYVSADFVK 276
Cdd:pfam08239   1 SGLNVRSGPSTSSEVVGTLPKGEKVEVLEEQGGgWYKVrTYDGYEGWVSSSYLS 54
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
 143-276 1.24e-09

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: 58.98  E-value: 1.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152 143 LNVRTGPSTSHTVLGSVNKGKTVQVV---------GEVQD---WFKInfnGGTGYVSKDFVTKGGSAVSNETQQPTTNNN 210
Cdd:NF038016   1 LNVRSGPATDSAVVGTLANGAKVTVVckvrgeqirGTVRTtsqWDRL---GSGRYVSHAYVRWSPSLPTCPWCAPKAATV 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446678152 211 TTTVQTGgsyvvntGALKVRTGPATYNAVIGGVTNGKVLNVTGAENG--------WYKInhnGRTGYVSADFVK 276
Cdd:NF038016  78 ATVTTGG-------GALNVRAAAGTGAARVGTVANGATVTVECQVWGqevdgtgvWYRL---GDGRYVSAAYVR 141
SH3b smart00287
Bacterial SH3 domain homologues;
135-193 3.13e-07

Bacterial SH3 domain homologues;


Pssm-ID: 214600 [Multi-domain]  Cd Length: 63  Bit Score: 47.33  E-value: 3.13e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446678152   135 TYTVNVSSLNVRTGPSTSHTVLGSVNKGKTVQVVGEV-QDWFKINFNGG-TGYVSKDFVTK 193
Cdd:smart00287   3 TAVVTGDGLNVRTGPGTSSPIIGTLKKGDKVKVLGVDgQDWAKITYGSGqRGYVPGYVVNT 63
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
 71-174 8.05e-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: 50.51  E-value: 8.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152  71 LNVRSGAGTGHNVISKVKSGQVLQVVGQENG------------WFKVnvnGQTGYVSGDFVTTGGKT-----GTTVQQGT 133
Cdd:NF038016   1 LNVRSGPATDSAVVGTLANGAKVTVVCKVRGeqirgtvrttsqWDRL---GSGRYVSHAYVRWSPSLptcpwCAPKAATV 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446678152 134 GTYTVNVSSLNVRTGPSTSHTVLGSVNKGKTVQVvgEVQDW 174
Cdd:NF038016  78 ATVTTGGGALNVRAAAGTGAARVGTVANGATVTV--ECQVW 116
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
 72-119 5.36e-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: 40.76  E-value: 5.36e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 446678152   72 NVRSGAGTGHNVISKVKSGQVLQVVGQ-ENGWFKV-NVNGQTGYVSGDFV 119
Cdd:TIGR04211   9 YMRSGPGNQYRILGSLKSGTPVTVLERsEDGYSRVrTPKGREGWVLSRYL 58
SH3b smart00287
Bacterial SH3 domain homologues;
219-276 1.00e-03

Bacterial SH3 domain homologues;


Pssm-ID: 214600 [Multi-domain]  Cd Length: 63  Bit Score: 37.31  E-value: 1.00e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152   219 SYVVNTGALKVRTGPATYNAVIGGVTNGKVLNVTGAEN-GWYKINH-NGRTGYVSADFVK 276
Cdd:smart00287   3 TAVVTGDGLNVRTGPGTSSPIIGTLKKGDKVKVLGVDGqDWAKITYgSGQRGYVPGYVVN 62
SH3_GRAP2_N cd11947
N-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS ...
 88-119 1.35e-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: 36.70  E-value: 1.35e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 446678152  88 KSGQVLQVVGQENGWFKVNVNGQTGYVSGDFV 119
Cdd:cd11947   19 KKGDVLKILSSDDIWFKAELNGEEGYVPKNFV 50
 
Name Accession Description Interval E-value
NlpC COG0791
Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];
278-426 6.92e-30

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


Pssm-ID: 440554 [Multi-domain]  Cd Length: 218  Bit Score: 115.57  E-value: 6.92e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152 278 VKGGVNNVTNNNNVTNNVQQPGKDVQKPTTGGDTSSIAGFARSLNGSPYRTAGTTPAGFDCSGFIHYVLNQTGHKGARqT 357
Cdd:COG0791   67 VGSAGAAAAAAAAKAGSSAAKSAAGASAPPSSTAEAIVAAALSYLGTPYVWGGTSPSGFDCSGLVQYVYRQAGISLPR-T 145

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446678152 358 VAGYWSSKTK--TSNPQPGDLVYFqNTYKSGPSHMGVYLGNGQFISAETDATGVRISSVSNSYWSKHLLGY 426
Cdd:COG0791  146 SADQAAAGTPvsRSELQPGDLVFF-RTGGGGISHVGIYLGNGKFIHASSSGKGVRISSLDSPYWKSRYVGA 215
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
 60-186 2.94e-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: 110.60  E-value: 2.94e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152  60 SELKYTVTADVLNVRSGAGTGHNVISKVKSGQVLQVVGQENGWFKVN-VNGQTGYVSGDFvttggktgttVQQGTGTYTV 138
Cdd:COG3103    3 AETRYVVDADALNVRSGPGTSYRIVGTLPKGEKVTVLGRSGGWYKVRySNGKTGWVSSRY----------LTVTPSARER 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446678152 139 NVSSLNVRTGPSTSHTVLGSVNKGKTVQVVGEVQDWFKINFNgGTGYV 186
Cdd:COG3103   73 LPDELNLRAGPSTSSEVLGLLPKGETVTVLKKSGGWFKVGYR-GTGWV 119
NLPC_P60 pfam00877
NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.
 323-425 1.59e-26

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: 102.36  E-value: 1.59e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152  323 GSPYRTAGTTPAGFDCSGFIHYVLNQTGHKGARqtVAGYWSSKTKT----SNPQPGDLVYFQNTYksGPSHMGVYLGNGQ 398
Cdd:pfam00877   1 GVPYRWGGGSPSGFDCSGLVRYAFAKVGIELPR--SSGQQYNAGKKtipkSEPQRGDLVFFGTGK--GISHVGIYLGNGQ 76

                          90       100
                  ....*....|....*....|....*..
gi 446678152  399 FISAETDaTGVRISSVSNSYWSKHLLG 425
Cdd:pfam00877  77 MLHASTG-GGVSISSLNGGYWQKRLVG 102
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
 131-270 5.82e-23

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: 93.26  E-value: 5.82e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152 131 QGTGTYTVNVSSLNVRTGPSTSHTVLGSVNKGKTVQVVGEVQDWFKINF-NGGTGYVSKDFVTKGGSAVsnetqqpttnn 209
Cdd:COG3103    2 AAETRYVVDADALNVRSGPGTSYRIVGTLPKGEKVTVLGRSGGWYKVRYsNGKTGWVSSRYLTVTPSAR----------- 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446678152 210 ntttvqtggsyVVNTGALKVRTGPATYNAVIGGVTNGKVLNVTGAENGWYKINHNGrTGYV 270
Cdd:COG3103   71 -----------ERLPDELNLRAGPSTSSEVLGLLPKGETVTVLKKSGGWFKVGYRG-TGWV 119
PRK13914 PRK13914
invasion associated endopeptidase;
65-428 4.85e-22

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 97.95  E-value: 4.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152  65 TVTADVLNVRSGAGTGHNVISKVKSGQVLQVVGQE-NGWFKVNVN-GQTGYVSGDFVTTGGKTG---------------- 126
Cdd:PRK13914  83 SVSATWLNVRSGAGVDNSIITSIKGGTKVTVETTEsNGWHKITYNdGKTGFVNGKYLTDKVTSTpvaptqevkketttqq 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152 127 --------TTVQQGTGTYTVNVSSLNVRTGP-----STSHTVLG-------SVNKGKTVQvvgEVQDWFkiNFNGGTGYV 186
Cdd:PRK13914 163 aapaaetkTEVKQTTQATTPAPKVAETKETPvvdqnATTHAVKSgdtiwalSVKYGVSVQ---DIMSWN--NLSSSSIYV 237

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152 187 SKDFVTKGGSAVSNETQQPTTNNNTTTVQTGGSYVVNTGALKVRTGPATYNAVIGGVTNGKVLNVTGAENGWYKINHNGR 266
Cdd:PRK13914 238 GQKLAIKQTANTATPKAEVKTEAPAAEKQAAPVVKENTNTNTATTEKKETTTQQQTAPKAPTEAAKPAPAPSTNTNANKT 317

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152 267 TGYVSADFVKFVKGGVNNVTNNNNVTNNVQQPGKDVQKPTTGGDTSSIAGF----ARSLNGSPYRTAGTTPAGFDCSGFI 342
Cdd:PRK13914 318 NTNTNTNTNNTNTSTPSKNTNTNTNSNTNTNSNTNANQGSSNNNSNSSASAiiaeAQKHLGKAYSWGGNGPTTFDCSGYT 397

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152 343 HYVLNQTGHKGARQTVAGYWS-SKTKTSNPQPGDLVYFQntYKSGPSHMGVYLGNGQFISAETDatGVRISSVSNSYWSK 421
Cdd:PRK13914 398 KYVFAKAGISLPRTSGAQYAStTRISESQAKPGDLVFFD--YGSGISHVGIYVGNGQMINAQDN--GVKYDNIHGSGWGK 473


                 ....*..
gi 446678152 422 HLLGYTK 428
Cdd:PRK13914 474 YLVGFGR 480
wall_bind_EntB NF040676
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
 66-192 3.09e-21

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: 95.62  E-value: 3.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152  66 VTADVLNVRSGAGTGHNVISKVKSGQVLQVVGQENGWFKVNVNGQTGYVSGDFVTTggktgttvqqgtgTYTVNVSSLNV 145
Cdd:NF040676  28 VTADVLNVREKPTTESKVVEKVKNGQELKVINTEDGWSKIELNGKEVFVSSEFTKD-------------VYHVTANLLNV 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446678152 146 RTGPSTSHTVLGSVNKGKTVQVVGEVQD-WFKINFNGGTGYVSKDFVT 192
Cdd:NF040676  95 RTEANTESEILGRLKKDDVIESTHQVKDgWLQFEYKGKTAYANVSFLS 142
spr PRK10838
bifunctional murein DD-endopeptidase/murein LD-carboxypeptidase;
323-421 5.10e-14

bifunctional murein DD-endopeptidase/murein LD-carboxypeptidase;


Pssm-ID: 236773 [Multi-domain]  Cd Length: 190  Bit Score: 70.18  E-value: 5.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152 323 GSPYRTAGTTPAGFDCSGFIHYVL-NQTGHKGARQTV----AGywsSKTKTSNPQPGDLVYFqntyKSGPS--HMGVYLG 395
Cdd:PRK10838  79 GVRYRLGGSTKKGIDCSAFVQRTFrEQFGLELPRSTYeqqeMG---KSVSRSKLRTGDLVLF----RAGSTgrHVGIYIG 151

                         90       100
                 ....*....|....*....|....*.
gi 446678152 396 NGQFISAETdATGVRISSVSNSYWSK 421
Cdd:PRK10838 152 NNQFVHAST-SSGVIISSMNEPYWKK 176
YraI COG4991
Uncharacterized conserved protein YraI [Function unknown];
134-195 6.85e-13

Uncharacterized conserved protein YraI [Function unknown];


Pssm-ID: 444015 [Multi-domain]  Cd Length: 92  Bit Score: 64.32  E-value: 6.85e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446678152 134 GTYTVNVSSLNVRTGPSTSHTVLGSVNKGKTVQVVGEVQD--WFKINFNGGTGYVSKDFVTKGG 195
Cdd:COG4991   22 AATAVATDDLNLRSGPGTGYPVVGTLPAGATVTVLGCTSGggWCKVSYGGQRGWVSARYLQVSY 85
YraI COG4991
Uncharacterized conserved protein YraI [Function unknown];
65-119 5.71e-12

Uncharacterized conserved protein YraI [Function unknown];


Pssm-ID: 444015 [Multi-domain]  Cd Length: 92  Bit Score: 61.62  E-value: 5.71e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446678152  65 TVTADVLNVRSGAGTGHNVISKVKSGQVLQVVG--QENGWFKVNVNGQTGYVSGDFV 119
Cdd:COG4991   25 AVATDDLNLRSGPGTGYPVVGTLPAGATVTVLGctSGGGWCKVSYGGQRGWVSARYL 81
SH3_3 pfam08239
Bacterial SH3 domain;
141-192 7.21e-12

Bacterial SH3 domain;


Pssm-ID: 462405 [Multi-domain]  Cd Length: 54  Bit Score: 59.95  E-value: 7.21e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446678152  141 SSLNVRTGPSTSHTVLGSVNKGKTVQVVGEV-QDWFKI-NFNGGTGYVSKDFVT 192
Cdd:pfam08239   1 SGLNVRSGPSTSSEVVGTLPKGEKVEVLEEQgGGWYKVrTYDGYEGWVSSSYLS 54
YraI COG4991
Uncharacterized conserved protein YraI [Function unknown];
218-281 1.16e-11

Uncharacterized conserved protein YraI [Function unknown];


Pssm-ID: 444015 [Multi-domain]  Cd Length: 92  Bit Score: 60.85  E-value: 1.16e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446678152 218 GSYVVNTGALKVRTGPATYNAVIGGVTNGKVLNVTG--AENGWYKINHNGRTGYVSADFVKFVKGG 281
Cdd:COG4991   22 AATAVATDDLNLRSGPGTGYPVVGTLPAGATVTVLGctSGGGWCKVSYGGQRGWVSARYLQVSYDG 87
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
 220-276 7.46e-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: 59.37  E-value: 7.46e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446678152 220 YVVNTGALKVRTGPATYNAVIGGVTNGKVLNVTGAENGWYKINH-NGRTGYVSADFVK 276
Cdd:COG3103    7 YVVDADALNVRSGPGTSYRIVGTLPKGEKVTVLGRSGGWYKVRYsNGKTGWVSSRYLT 64
SH3_3 pfam08239
Bacterial SH3 domain;
69-119 2.42e-10

Bacterial SH3 domain;


Pssm-ID: 462405 [Multi-domain]  Cd Length: 54  Bit Score: 55.72  E-value: 2.42e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446678152   69 DVLNVRSGAGTGHNVISKVKSGQVLQVVG-QENGWFKV-NVNGQTGYVSGDFV 119
Cdd:pfam08239   1 SGLNVRSGPSTSSEVVGTLPKGEKVEVLEeQGGGWYKVrTYDGYEGWVSSSYL 53
SH3 COG3807
SH3-like domain [Function unknown];
137-275 3.31e-10

SH3-like domain [Function unknown];


Pssm-ID: 443020 [Multi-domain]  Cd Length: 150  Bit Score: 57.99  E-value: 3.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152 137 TVNVSSLNVRTGPSTSHTVLGSVN-KGKTVQVVGEVQDWFKI-NFNGGTGYVSKdfvtkggSAVSNETQQpttnnntttv 214
Cdd:COG3807   23 SLKSDEVNLRDGPSTKYPILWVYKrRGLPVEVIAEFGNWRRVrDPEGDEGWVHQ-------SLLSGRRTV---------- 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446678152 215 qtggsyVVNTGALKVRTGPATYNAVIGGVTNGKVLNVTGAENGWYKINHNGRTGYVSADFV 275
Cdd:COG3807   86 ------IVTGDLANLRASPDENAAVVARLEPGVVLRLLECDGGWCKVRADGYKGWVRQSLL 140
SH3_3 pfam08239
Bacterial SH3 domain;
225-276 4.89e-10

Bacterial SH3 domain;


Pssm-ID: 462405 [Multi-domain]  Cd Length: 54  Bit Score: 54.95  E-value: 4.89e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446678152  225 GALKVRTGPATYNAVIGGVTNGKVLNVTGAENG-WYKI-NHNGRTGYVSADFVK 276
Cdd:pfam08239   1 SGLNVRSGPSTSSEVVGTLPKGEKVEVLEEQGGgWYKVrTYDGYEGWVSSSYLS 54
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
 143-276 1.24e-09

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: 58.98  E-value: 1.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152 143 LNVRTGPSTSHTVLGSVNKGKTVQVV---------GEVQD---WFKInfnGGTGYVSKDFVTKGGSAVSNETQQPTTNNN 210
Cdd:NF038016   1 LNVRSGPATDSAVVGTLANGAKVTVVckvrgeqirGTVRTtsqWDRL---GSGRYVSHAYVRWSPSLPTCPWCAPKAATV 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446678152 211 TTTVQTGgsyvvntGALKVRTGPATYNAVIGGVTNGKVLNVTGAENG--------WYKInhnGRTGYVSADFVK 276
Cdd:NF038016  78 ATVTTGG-------GALNVRAAAGTGAARVGTVANGATVTVECQVWGqevdgtgvWYRL---GDGRYVSAAYVR 141
SH3 COG3807
SH3-like domain [Function unknown];
66-119 1.35e-07

SH3-like domain [Function unknown];


Pssm-ID: 443020 [Multi-domain]  Cd Length: 150  Bit Score: 50.67  E-value: 1.35e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446678152  66 VTADVLNVRSGAGTGHNVISKVKSGQVLQVVGQENGWFKVNVNGQTGYVSGDFV 119
Cdd:COG3807   87 VTGDLANLRASPDENAAVVARLEPGVVLRLLECDGGWCKVRADGYKGWVRQSLL 140
SH3b smart00287
Bacterial SH3 domain homologues;
135-193 3.13e-07

Bacterial SH3 domain homologues;


Pssm-ID: 214600 [Multi-domain]  Cd Length: 63  Bit Score: 47.33  E-value: 3.13e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446678152   135 TYTVNVSSLNVRTGPSTSHTVLGSVNKGKTVQVVGEV-QDWFKINFNGG-TGYVSKDFVTK 193
Cdd:smart00287   3 TAVVTGDGLNVRTGPGTSSPIIGTLKKGDKVKVLGVDgQDWAKITYGSGqRGYVPGYVVNT 63
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
 71-174 8.05e-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: 50.51  E-value: 8.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152  71 LNVRSGAGTGHNVISKVKSGQVLQVVGQENG------------WFKVnvnGQTGYVSGDFVTTGGKT-----GTTVQQGT 133
Cdd:NF038016   1 LNVRSGPATDSAVVGTLANGAKVTVVCKVRGeqirgtvrttsqWDRL---GSGRYVSHAYVRWSPSLptcpwCAPKAATV 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446678152 134 GTYTVNVSSLNVRTGPSTSHTVLGSVNKGKTVQVvgEVQDW 174
Cdd:NF038016  78 ATVTTGGGALNVRAAAGTGAARVGTVANGATVTV--ECQVW 116
SH3_4 pfam06347
Bacterial SH3 domain; SH3 (src Homology-3) domains are small protein modules containing ...
 68-114 5.99e-05

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: 40.41  E-value: 5.99e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 446678152   68 ADVLNVRSGAGTGHNVISKVKSGQVLQVVGQENGWFKVNV-NGQTGYV 114
Cdd:pfam06347   2 KDEVNLRRGPSDKAAVAAYLEAGVPVRVVACKDNWCRVRDaDGAEGWI 49
SH3b smart00287
Bacterial SH3 domain homologues;
64-119 6.70e-05

Bacterial SH3 domain homologues;


Pssm-ID: 214600 [Multi-domain]  Cd Length: 63  Bit Score: 40.78  E-value: 6.70e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 446678152    64 YTVTADVLNVRSGAGTGHNVISKVKSGQVLQVVGQEN-GWFKVNV-NGQTGYVSGDFV 119
Cdd:smart00287   4 AVVTGDGLNVRTGPGTSSPIIGTLKKGDKVKVLGVDGqDWAKITYgSGQRGYVPGYVV 61
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
 72-119 5.36e-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: 40.76  E-value: 5.36e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 446678152   72 NVRSGAGTGHNVISKVKSGQVLQVVGQ-ENGWFKV-NVNGQTGYVSGDFV 119
Cdd:TIGR04211   9 YMRSGPGNQYRILGSLKSGTPVTVLERsEDGYSRVrTPKGREGWVLSRYL 58
SH3b smart00287
Bacterial SH3 domain homologues;
219-276 1.00e-03

Bacterial SH3 domain homologues;


Pssm-ID: 214600 [Multi-domain]  Cd Length: 63  Bit Score: 37.31  E-value: 1.00e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678152   219 SYVVNTGALKVRTGPATYNAVIGGVTNGKVLNVTGAEN-GWYKINH-NGRTGYVSADFVK 276
Cdd:smart00287   3 TAVVTGDGLNVRTGPGTSSPIIGTLKKGDKVKVLGVDGqDWAKITYgSGQRGYVPGYVVN 62
SH3_GRAP2_N cd11947
N-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS ...
 88-119 1.35e-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: 36.70  E-value: 1.35e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 446678152  88 KSGQVLQVVGQENGWFKVNVNGQTGYVSGDFV 119
Cdd:cd11947   19 KKGDVLKILSSDDIWFKAELNGEEGYVPKNFV 50
SH3_GRAP2_N cd11947
N-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS ...
 158-191 3.87e-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: 35.16  E-value: 3.87e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 446678152 158 SVNKGKTVQVVGEVQDWFKINFNGGTGYVSKDFV 191
Cdd:cd11947   17 SFKKGDVLKILSSDDIWFKAELNGEEGYVPKNFV 50
SH3_4 pfam06347
Bacterial SH3 domain; SH3 (src Homology-3) domains are small protein modules containing ...
 144-188 7.11e-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: 7.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 446678152  144 NVRTGPSTSHTVLGSVNKGKTVQVVGEVQDWFKINF-NGGTGYVSK 188
Cdd:pfam06347   6 NLRRGPSDKAAVAAYLEAGVPVRVVACKDNWCRVRDaDGAEGWIYK 51
 
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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