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Conserved domains on  [gi|119629966|gb|EAX09561|]
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ubiquitin associated and SH3 domain containing, A, isoform CRA_b [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SH3_UBASH3A cd11937
Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing protein A; UBASH3A is ...
 279-338 6.79e-41

Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing protein A; UBASH3A is also called Cbl-Interacting Protein 4 (CLIP4), T cell Ubiquitin LigAnd (TULA), or T cell receptor Signaling (STS)-2. It is only found in lymphoid cells and exhibits weak phosphatase activity. UBASH3A facilitates T cell-induced apoptosis through interaction with the apoptosis-inducing factor AIF. It is involved in regulating the level of phosphorylation of the zeta-associated protein (ZAP)-70 tyrosine kinase. TULA proteins contain an N-terminal UBA domain, a central SH3 domain, and a C-terminal histidine phosphatase domain. They bind c-Cbl through the SH3 domain and to ubiquitin via UBA. 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: 212870 [Multi-domain]  Cd Length: 60  Bit Score: 142.85  E-value: 6.79e-41
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966 279 QTLRALFQYKPQNVDELTLSPGDYIFVDPTQQDEASEGWVIGISQRTGCRGFLPENYTDR 338
Cdd:cd11937    1 QTLRALFQYKPQNIDELMLSPGDYIFVDPTQQSEASEGWVIGISHRTGCRGFLPENYTER 60
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 450-612 4.25e-20

Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so named because catalysis centres on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches. The larger branch 1 contains a wide variety of catalytic functions, the best known being fructose 2,6-bisphosphatase (found in a bifunctional protein with 2-phosphofructokinase) and cofactor-dependent phosphoglycerate mutase. The latter is an unusual example of a mutase activity in the superfamily: the vast majority of members appear to be phosphatases. The bacterial regulatory protein phosphatase SixA is also in branch 1 and has a minimal, and possible ancestral-like structure, lacking the large domain insertions that contribute to binding of small molecules in branch 1 members.


:

Pssm-ID: 459751 [Multi-domain]  Cd Length: 194  Bit Score: 88.42  E-value: 4.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966  450 DPPLSSCGIFQSRIAGDALldSGIRISSVFASPALRCVQTAKLILEELKLEkkikIRVEPGIFEWT--KWEaGKTTPTLM 527
Cdd:pfam00300  22 DSPLTELGREQAEALAERL--AGEPFDAIYSSPLKRARQTAEIIAEALGLP----VEIDPRLREIDfgDWE-GLTFEEIA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966  528 S-LEELKEANFNIDTDYRPAfplsalmPAESYQEYMDRCTASMVQIVNTCPQDTgvILIVSHGSTLDSCTRPLLGLPPRE 606
Cdd:pfam00300  95 ErYPEEYDAWLADPADYRPP-------GGESLADVRARVRAALEELAARHPGKT--VLVVSHGGVIRALLAHLLGLPLEA 165


                  ....*.
gi 119629966  607 CGDFAQ 612
Cdd:pfam00300 166 LRRFPL 171
UBA_UBS3A_like cd14300
UBA domain found in ubiquitin-associated and SH3 domain-containing protein A (UBS3A) and ...
 25-61 8.41e-17

UBA domain found in ubiquitin-associated and SH3 domain-containing protein A (UBS3A) and similar proteins; UBS3A, also called Cbl-interacting protein 4 (CLIP4), suppressor of T-cell receptor signaling 2 (Sts-2), or T-cell ubiquitin ligand 1 (TULA-1), is a lymphoid protein only detected in thymus, spleen, and bone marrow. UBS3A exhibits extremely low phosphatase activity, but is capable of promoting T-cell apoptosis independent of either T cell receptor (TCR)/CD3-mediated signaling or caspase activity. It functions as a negative regulator of TCR signaling. UBS3A can also inhibit HIV-1 biogenesis through the binding of ATP-binding cassette protein family E member 1 (ABCE-1), a host factor of HIV-1 assembly. Moreover, UBS3A acts as the Cbl- and ubiquitin-interacting protein that can inhibit endocytosis and downregulation of ligand-activated epidermal growth factor receptor (EGFR) by impairing Cbl-induced ubiquitination, as well as inhibit clathrin-dependent endocytosis in general. This family also includes Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) and some uncharacterized AAA-type ATPase-like proteins found in plants.


:

Pssm-ID: 270485  Cd Length: 37  Bit Score: 74.11  E-value: 8.41e-17
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 119629966  25 LEPLLAMGFPVHTALKALAATGRKTAEEALAWLHDHC 61
Cdd:cd14300    1 LETLLAMGFPEDVARKALKATGGKSIEKATDWLLSHC 37
HP super family cl11399
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 370-502 5.82e-04

Histidine phosphatase domain found in a functionally diverse set of proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This set of proteins includes cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, histidine acid phosphatases, phytases, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system; phytases scavenge phosphate from extracellular sources. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG. Clinical applications include the use of prostatic acid phosphatase (PAP) as a serum marker for prostate cancer. Agricultural applications include the addition of phytases to animal feed.


The actual alignment was detected with superfamily member PRK06193:

Pssm-ID: 472174  Cd Length: 206  Bit Score: 41.60  E-value: 5.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966 370 RCSGEFLPQTARSLSSLQALQATvarKSVLVVRHGERVDqifgkawlqqcSTPDgkYYRPDLNfPCSLPRRsrgikdfen 449
Cdd:PRK06193  20 GSGEEAASDEADDKTLLESLQKG---GYVIYFRHAATDR-----------SQAD--QDTSDMD-DCSTQRN--------- 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119629966 450 dppLSSCGIFQSRIAGDALLDSGIRISSVFASPALRCVQTAKLILEELKLEKK 502
Cdd:PRK06193  74 ---LSEEGREQARAIGEAFRALAIPVGKVISSPYCRAWETAQLAFGRHEKEIR 123
ThpR super family cl43441
RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA ligase) [Translation, ribosomal structure and ...
 76-166 2.80e-03

RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA ligase) [Translation, ribosomal structure and biogenesis];


The actual alignment was detected with superfamily member COG1514:

Pssm-ID: 441123 [Multi-domain]  Cd Length: 181  Bit Score: 39.24  E-value: 2.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966  76 LFLC--PTGPLLEKLQEFWRESKRQCAKNRAHEVFPHVTLCDFFTCEDQKVECLYEALKRAGDRL---------LGSFPT 144
Cdd:COG1514    3 LFIAlpPPEELREALAALRARLKAAPGGRWVRPENLHLTLAFLGEVDEERLEALAEALARAAAGAppfelrldgLGAFPR 82

                         90       100
                 ....*....|....*....|..
gi 119629966 145 AVPLALhssisYLGffVSGSPA 166
Cdd:COG1514   83 PRPRVL-----WLG--VEPSPE 97
 
Name Accession Description Interval E-value
SH3_UBASH3A cd11937
Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing protein A; UBASH3A is ...
 279-338 6.79e-41

Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing protein A; UBASH3A is also called Cbl-Interacting Protein 4 (CLIP4), T cell Ubiquitin LigAnd (TULA), or T cell receptor Signaling (STS)-2. It is only found in lymphoid cells and exhibits weak phosphatase activity. UBASH3A facilitates T cell-induced apoptosis through interaction with the apoptosis-inducing factor AIF. It is involved in regulating the level of phosphorylation of the zeta-associated protein (ZAP)-70 tyrosine kinase. TULA proteins contain an N-terminal UBA domain, a central SH3 domain, and a C-terminal histidine phosphatase domain. They bind c-Cbl through the SH3 domain and to ubiquitin via UBA. 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: 212870 [Multi-domain]  Cd Length: 60  Bit Score: 142.85  E-value: 6.79e-41
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966 279 QTLRALFQYKPQNVDELTLSPGDYIFVDPTQQDEASEGWVIGISQRTGCRGFLPENYTDR 338
Cdd:cd11937    1 QTLRALFQYKPQNIDELMLSPGDYIFVDPTQQSEASEGWVIGISHRTGCRGFLPENYTER 60
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 450-612 4.25e-20

Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so named because catalysis centres on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches. The larger branch 1 contains a wide variety of catalytic functions, the best known being fructose 2,6-bisphosphatase (found in a bifunctional protein with 2-phosphofructokinase) and cofactor-dependent phosphoglycerate mutase. The latter is an unusual example of a mutase activity in the superfamily: the vast majority of members appear to be phosphatases. The bacterial regulatory protein phosphatase SixA is also in branch 1 and has a minimal, and possible ancestral-like structure, lacking the large domain insertions that contribute to binding of small molecules in branch 1 members.


Pssm-ID: 459751 [Multi-domain]  Cd Length: 194  Bit Score: 88.42  E-value: 4.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966  450 DPPLSSCGIFQSRIAGDALldSGIRISSVFASPALRCVQTAKLILEELKLEkkikIRVEPGIFEWT--KWEaGKTTPTLM 527
Cdd:pfam00300  22 DSPLTELGREQAEALAERL--AGEPFDAIYSSPLKRARQTAEIIAEALGLP----VEIDPRLREIDfgDWE-GLTFEEIA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966  528 S-LEELKEANFNIDTDYRPAfplsalmPAESYQEYMDRCTASMVQIVNTCPQDTgvILIVSHGSTLDSCTRPLLGLPPRE 606
Cdd:pfam00300  95 ErYPEEYDAWLADPADYRPP-------GGESLADVRARVRAALEELAARHPGKT--VLVVSHGGVIRALLAHLLGLPLEA 165


                  ....*.
gi 119629966  607 CGDFAQ 612
Cdd:pfam00300 166 LRRFPL 171
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
450-612 2.83e-19

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 86.15  E-value: 2.83e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966 450 DPPLSSCGIFQSRIAGDALldSGIRISSVFASPALRCVQTAKLILEELKLEkkikIRVEPGIFEW--TKWEaGKTtptlm 527
Cdd:COG0406   25 DVPLTELGRAQARALAERL--ADIPFDAVYSSPLQRARQTAEALAEALGLP----VEVDPRLREIdfGDWE-GLT----- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966 528 sLEELKEANFNIDTDYRpAFPLSALMP-AESYQEYMDRCTASMVQIVNTCPQDTgvILIVSHGSTLDSCTRPLLGLPPRE 606
Cdd:COG0406   93 -FAELEARYPEALAAWL-ADPAEFRPPgGESLADVQARVRAALEELLARHPGGT--VLVVTHGGVIRALLAHLLGLPLEA 168


                 ....*.
gi 119629966 607 CGDFAQ 612
Cdd:COG0406  169 FWRLRI 174
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 398-610 2.37e-17

Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Subgroup of the catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This subgroup contains cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example, F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG.


Pssm-ID: 132718 [Multi-domain]  Cd Length: 153  Bit Score: 79.29  E-value: 2.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966 398 VLVVRHGERVDQIFGkawlqqcstpdgkyyrpdlnfpcslprRSRGIKDfendPPLSSCGIFQSRIAGDALLDSGIRISS 477
Cdd:cd07067    2 LYLVRHGESEWNAEG---------------------------RFQGWTD----VPLTEKGREQARALGKRLKELGIKFDR 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966 478 VFASPALRCVQTAKLILEELkleKKIKIRVEPGIFEwtkweagkttptlmsleelkeanfnidtdyrpafplsalmpaes 557
Cdd:cd07067   51 IYSSPLKRAIQTAEIILEEL---PGLPVEVDPRLRE-------------------------------------------- 83

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119629966 558 yqeymDRCTASMVQIVNTCPQDTgvILIVSHGSTLDSCTRPLLGLPPRECGDF 610
Cdd:cd07067   84 -----ARVLPALEELIAPHDGKN--VLIVSHGGVLRALLAYLLGLSDEDILRL 129
UBA_UBS3A_like cd14300
UBA domain found in ubiquitin-associated and SH3 domain-containing protein A (UBS3A) and ...
 25-61 8.41e-17

UBA domain found in ubiquitin-associated and SH3 domain-containing protein A (UBS3A) and similar proteins; UBS3A, also called Cbl-interacting protein 4 (CLIP4), suppressor of T-cell receptor signaling 2 (Sts-2), or T-cell ubiquitin ligand 1 (TULA-1), is a lymphoid protein only detected in thymus, spleen, and bone marrow. UBS3A exhibits extremely low phosphatase activity, but is capable of promoting T-cell apoptosis independent of either T cell receptor (TCR)/CD3-mediated signaling or caspase activity. It functions as a negative regulator of TCR signaling. UBS3A can also inhibit HIV-1 biogenesis through the binding of ATP-binding cassette protein family E member 1 (ABCE-1), a host factor of HIV-1 assembly. Moreover, UBS3A acts as the Cbl- and ubiquitin-interacting protein that can inhibit endocytosis and downregulation of ligand-activated epidermal growth factor receptor (EGFR) by impairing Cbl-induced ubiquitination, as well as inhibit clathrin-dependent endocytosis in general. This family also includes Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) and some uncharacterized AAA-type ATPase-like proteins found in plants.


Pssm-ID: 270485  Cd Length: 37  Bit Score: 74.11  E-value: 8.41e-17
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 119629966  25 LEPLLAMGFPVHTALKALAATGRKTAEEALAWLHDHC 61
Cdd:cd14300    1 LETLLAMGFPEDVARKALKATGGKSIEKATDWLLSHC 37
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 449-592 9.10e-16

Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase (BPGM) are structurally related enzymes that catalyse reactions involving the transfer of phospho groups between the three carbon atoms of phosphoglycerate... Both enzymes can catalyse three different reactions with different specificities, the isomerization of 2-phosphoglycerate (2-PGA) to 3-phosphoglycerate (3-PGA) with 2,3-diphosphoglycerate (2,3-DPG) as the primer of the reaction, the synthesis of 2,3-DPG from 1,3-DPG with 3-PGA as a primer and the degradation of 2,3-DPG to 3-PGA (phosphatase activity). In mammals, PGAM is a dimeric protein with two isoforms, the M (muscle) and B (brain) forms. In yeast, PGAM is a tetrameric protein.


Pssm-ID: 214859 [Multi-domain]  Cd Length: 158  Bit Score: 75.19  E-value: 9.10e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966   449 NDPPLSSCGIFQSRIAGDALLD-SGIRISSVFASPALRCVQTAKLILEELKLEKKIKIrvEPGIFEwtkweaGKTTPTLM 527
Cdd:smart00855  22 TDVPLTELGRAQAEALGRLLASlLLPRFDVVYSSPLKRARQTAEALAIALGLPGLRER--DFGAWE------GLTWDEIA 93

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119629966   528 slEELKEANFNIDTDYRPAFPlSALMPAESYQEYMDRCTASMVQIVNTCPQDTGVILIVSHGSTL 592
Cdd:smart00855  94 --AKYPEEYLAAWRDPYDPAP-PAPPGGESLADLVERVEPALDELIATADASGQNVLIVSHGGVI 155
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 450-612 2.50e-11

alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of Salmonella and Eschichia coli species, and homologous proteins found in cobalamin biosynthesis regions in other bacteria. This protein is alpha-ribazole phosphatase (EC 3.1.3.73) and, like many phosphatases, can be closely related in sequence to other phosphatases with different functions. Close homologs excluded from this model include proteins with duplications, so this model is built in -g mode to suppress hits to those proteins. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274461 [Multi-domain]  Cd Length: 177  Bit Score: 62.64  E-value: 2.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966  450 DPPLSSCGIFQSRIAGDALldSGIRISSVFASPALRCVQTAKLILEELKLekkiKIRVEPGIFE--WTKWEagkttptLM 527
Cdd:TIGR03162  21 DVPLAESGEEQAAALREKL--ADVPFDAVYSSPLSRCRELAEILAERRGL----PIIKDDRLREmdFGDWE-------GR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966  528 SLEELKEANFNIDtdYRPAFPLSALMP-AESYQEYMDRCTASMVQIVNTCPQDTgvILIVSHGSTLDSCTRPLLGLPPRE 606
Cdd:TIGR03162  88 SWDEIPEAYPELD--AWAADWQHARPPgGESFADFYQRVSEFLEELLKAHEGDN--VLIVTHGGVIRALLAHLLGLPLEQ 163


                  ....*.
gi 119629966  607 CGDFAQ 612
Cdd:TIGR03162 164 WWSFAV 169
SH3_9 pfam14604
Variant SH3 domain;
283-337 7.50e-11

Variant SH3 domain;


Pssm-ID: 434066 [Multi-domain]  Cd Length: 49  Bit Score: 57.63  E-value: 7.50e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 119629966  283 ALFQYKPQNVDELTLSPGDYIFVDPtqqdEASEGWVIGisQRTGCRGFLPENYTD 337
Cdd:pfam14604   1 ALYPYEPKDDDELSLQRGDVITVIE----ESEDGWWEG--INTGRTGLVPANYVE 49
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 279-335 1.05e-08

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 51.77  E-value: 1.05e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 119629966   279 QTLRALFQYKPQNVDELTLSPGDYIFVDptqqDEASEGWVIGISQRtGCRGFLPENY 335
Cdd:smart00326   3 PQVRALYDYTAQDPDELSFKKGDIITVL----EKSDDGWWKGRLGR-GKEGLFPSNY 54
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 434-604 5.77e-05

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 45.74  E-value: 5.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966 434 PCSLPRRSRGIkdfeNDPPLSSCGIFQSRIAGDALLDSGiRISSVFASPALRCVQTAKLILEELKLEkkikIRVEPGIFE 513
Cdd:PRK07238 183 ELSVQRRYSGR----GNPELTEVGRRQAAAAARYLAARG-GIDAVVSSPLQRARDTAAAAAKALGLD----VTVDDDLIE 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966 514 -----W---TKWEAGKTTPtlmsleELKEANFNiDTDYRPafplsalmPA-ESYQEYMDRCTASMVQIVNTCPQDTgvIL 584
Cdd:PRK07238 254 tdfgaWeglTFAEAAERDP------ELHRAWLA-DTSVAP--------PGgESFDAVARRVRRARDRLIAEYPGAT--VL 316

                        170       180
                 ....*....|....*....|
gi 119629966 585 IVSHGSTLDSCTRPLLGLPP 604
Cdd:PRK07238 317 VVSHVTPIKTLLRLALDAGP 336
PRK06193 PRK06193
hypothetical protein; Provisional
 370-502 5.82e-04

hypothetical protein; Provisional


Pssm-ID: 235734  Cd Length: 206  Bit Score: 41.60  E-value: 5.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966 370 RCSGEFLPQTARSLSSLQALQATvarKSVLVVRHGERVDqifgkawlqqcSTPDgkYYRPDLNfPCSLPRRsrgikdfen 449
Cdd:PRK06193  20 GSGEEAASDEADDKTLLESLQKG---GYVIYFRHAATDR-----------SQAD--QDTSDMD-DCSTQRN--------- 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119629966 450 dppLSSCGIFQSRIAGDALLDSGIRISSVFASPALRCVQTAKLILEELKLEKK 502
Cdd:PRK06193  74 ---LSEEGREQARAIGEAFRALAIPVGKVISSPYCRAWETAQLAFGRHEKEIR 123
ThpR COG1514
RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA ligase) [Translation, ribosomal structure and ...
 76-166 2.80e-03

RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA ligase) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441123 [Multi-domain]  Cd Length: 181  Bit Score: 39.24  E-value: 2.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966  76 LFLC--PTGPLLEKLQEFWRESKRQCAKNRAHEVFPHVTLCDFFTCEDQKVECLYEALKRAGDRL---------LGSFPT 144
Cdd:COG1514    3 LFIAlpPPEELREALAALRARLKAAPGGRWVRPENLHLTLAFLGEVDEERLEALAEALARAAAGAppfelrldgLGAFPR 82

                         90       100
                 ....*....|....*....|..
gi 119629966 145 AVPLALhssisYLGffVSGSPA 166
Cdd:COG1514   83 PRPRVL-----WLG--VEPSPE 97
 
Name Accession Description Interval E-value
SH3_UBASH3A cd11937
Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing protein A; UBASH3A is ...
 279-338 6.79e-41

Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing protein A; UBASH3A is also called Cbl-Interacting Protein 4 (CLIP4), T cell Ubiquitin LigAnd (TULA), or T cell receptor Signaling (STS)-2. It is only found in lymphoid cells and exhibits weak phosphatase activity. UBASH3A facilitates T cell-induced apoptosis through interaction with the apoptosis-inducing factor AIF. It is involved in regulating the level of phosphorylation of the zeta-associated protein (ZAP)-70 tyrosine kinase. TULA proteins contain an N-terminal UBA domain, a central SH3 domain, and a C-terminal histidine phosphatase domain. They bind c-Cbl through the SH3 domain and to ubiquitin via UBA. 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: 212870 [Multi-domain]  Cd Length: 60  Bit Score: 142.85  E-value: 6.79e-41
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966 279 QTLRALFQYKPQNVDELTLSPGDYIFVDPTQQDEASEGWVIGISQRTGCRGFLPENYTDR 338
Cdd:cd11937    1 QTLRALFQYKPQNIDELMLSPGDYIFVDPTQQSEASEGWVIGISHRTGCRGFLPENYTER 60
SH3_UBASH3 cd11791
Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing proteins, also called ...
 280-338 4.08e-30

Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing proteins, also called TULA (T cell Ubiquitin LigAnd) family of proteins; UBASH3 or TULA proteins are also referred to as Suppressor of T cell receptor Signaling (STS) proteins. They contain an N-terminal UBA domain, a central SH3 domain, and a C-terminal histidine phosphatase domain. They bind c-Cbl through the SH3 domain and to ubiquitin via UBA. In some vertebrates, there are two TULA family proteins, called UBASH3A (also called TULA or STS-2) and UBASH3B (also called TULA-2 or STS-1), which show partly overlapping as well as distinct functions. UBASH3B is widely expressed while UBASH3A is only found in lymphoid cells. UBASH3A facilitates apoptosis induced in T cells through its interaction with the apoptosis-inducing factor AIF. UBASH3B is an active phosphatase while UBASH3A is not. 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: 212725 [Multi-domain]  Cd Length: 59  Bit Score: 112.78  E-value: 4.08e-30
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 119629966 280 TLRALFQYKPQNVDELTLSPGDYIFVDPTQQDEASEGWVIGISQRTGCRGFLPENYTDR 338
Cdd:cd11791    1 VLRVLYPYTPQEEDELELVPGDYIYVSPEELDSSSDGWVEGTSWLTGCSGLLPENYTEK 59
SH3_UBASH3B cd11936
Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing protein B; UBASH3B, ...
 278-339 1.90e-22

Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing protein B; UBASH3B, also called Suppressor of T cell receptor Signaling (STS)-1 or T cell Ubiquitin LigAnd (TULA)-2 is an active phosphatase that is expressed ubiquitously. The phosphatase activity of UBASH3B is essential for its roles in the suppression of TCR signaling and the regulation of EGFR. It also interacts with Syk and functions as a negative regulator of platelet glycoprotein VI signaling. TULA proteins contain an N-terminal UBA domain, a central SH3 domain, and a C-terminal histidine phosphatase domain. They bind c-Cbl through the SH3 domain and to ubiquitin via UBA. 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: 212869  Cd Length: 62  Bit Score: 90.87  E-value: 1.90e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119629966 278 YQTLRALFQYKPQNVDELTLSPGDYIFVDPTQQDEASEGWVIGISQRTGCRGFLPENYTDRA 339
Cdd:cd11936    1 HETLQVIYPYTPQNDDELELVPGDYIFMSPMEQTSTSEGWIYGTSLTTGCSGLLPENYITKA 62
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 450-612 4.25e-20

Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so named because catalysis centres on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches. The larger branch 1 contains a wide variety of catalytic functions, the best known being fructose 2,6-bisphosphatase (found in a bifunctional protein with 2-phosphofructokinase) and cofactor-dependent phosphoglycerate mutase. The latter is an unusual example of a mutase activity in the superfamily: the vast majority of members appear to be phosphatases. The bacterial regulatory protein phosphatase SixA is also in branch 1 and has a minimal, and possible ancestral-like structure, lacking the large domain insertions that contribute to binding of small molecules in branch 1 members.


Pssm-ID: 459751 [Multi-domain]  Cd Length: 194  Bit Score: 88.42  E-value: 4.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966  450 DPPLSSCGIFQSRIAGDALldSGIRISSVFASPALRCVQTAKLILEELKLEkkikIRVEPGIFEWT--KWEaGKTTPTLM 527
Cdd:pfam00300  22 DSPLTELGREQAEALAERL--AGEPFDAIYSSPLKRARQTAEIIAEALGLP----VEIDPRLREIDfgDWE-GLTFEEIA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966  528 S-LEELKEANFNIDTDYRPAfplsalmPAESYQEYMDRCTASMVQIVNTCPQDTgvILIVSHGSTLDSCTRPLLGLPPRE 606
Cdd:pfam00300  95 ErYPEEYDAWLADPADYRPP-------GGESLADVRARVRAALEELAARHPGKT--VLVVSHGGVIRALLAHLLGLPLEA 165


                  ....*.
gi 119629966  607 CGDFAQ 612
Cdd:pfam00300 166 LRRFPL 171
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
450-612 2.83e-19

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 86.15  E-value: 2.83e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966 450 DPPLSSCGIFQSRIAGDALldSGIRISSVFASPALRCVQTAKLILEELKLEkkikIRVEPGIFEW--TKWEaGKTtptlm 527
Cdd:COG0406   25 DVPLTELGRAQARALAERL--ADIPFDAVYSSPLQRARQTAEALAEALGLP----VEVDPRLREIdfGDWE-GLT----- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966 528 sLEELKEANFNIDTDYRpAFPLSALMP-AESYQEYMDRCTASMVQIVNTCPQDTgvILIVSHGSTLDSCTRPLLGLPPRE 606
Cdd:COG0406   93 -FAELEARYPEALAAWL-ADPAEFRPPgGESLADVQARVRAALEELLARHPGGT--VLVVTHGGVIRALLAHLLGLPLEA 168


                 ....*.
gi 119629966 607 CGDFAQ 612
Cdd:COG0406  169 FWRLRI 174
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 398-610 2.37e-17

Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Subgroup of the catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This subgroup contains cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example, F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG.


Pssm-ID: 132718 [Multi-domain]  Cd Length: 153  Bit Score: 79.29  E-value: 2.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966 398 VLVVRHGERVDQIFGkawlqqcstpdgkyyrpdlnfpcslprRSRGIKDfendPPLSSCGIFQSRIAGDALLDSGIRISS 477
Cdd:cd07067    2 LYLVRHGESEWNAEG---------------------------RFQGWTD----VPLTEKGREQARALGKRLKELGIKFDR 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966 478 VFASPALRCVQTAKLILEELkleKKIKIRVEPGIFEwtkweagkttptlmsleelkeanfnidtdyrpafplsalmpaes 557
Cdd:cd07067   51 IYSSPLKRAIQTAEIILEEL---PGLPVEVDPRLRE-------------------------------------------- 83

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119629966 558 yqeymDRCTASMVQIVNTCPQDTgvILIVSHGSTLDSCTRPLLGLPPRECGDF 610
Cdd:cd07067   84 -----ARVLPALEELIAPHDGKN--VLIVSHGGVLRALLAYLLGLSDEDILRL 129
UBA_UBS3A_like cd14300
UBA domain found in ubiquitin-associated and SH3 domain-containing protein A (UBS3A) and ...
 25-61 8.41e-17

UBA domain found in ubiquitin-associated and SH3 domain-containing protein A (UBS3A) and similar proteins; UBS3A, also called Cbl-interacting protein 4 (CLIP4), suppressor of T-cell receptor signaling 2 (Sts-2), or T-cell ubiquitin ligand 1 (TULA-1), is a lymphoid protein only detected in thymus, spleen, and bone marrow. UBS3A exhibits extremely low phosphatase activity, but is capable of promoting T-cell apoptosis independent of either T cell receptor (TCR)/CD3-mediated signaling or caspase activity. It functions as a negative regulator of TCR signaling. UBS3A can also inhibit HIV-1 biogenesis through the binding of ATP-binding cassette protein family E member 1 (ABCE-1), a host factor of HIV-1 assembly. Moreover, UBS3A acts as the Cbl- and ubiquitin-interacting protein that can inhibit endocytosis and downregulation of ligand-activated epidermal growth factor receptor (EGFR) by impairing Cbl-induced ubiquitination, as well as inhibit clathrin-dependent endocytosis in general. This family also includes Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) and some uncharacterized AAA-type ATPase-like proteins found in plants.


Pssm-ID: 270485  Cd Length: 37  Bit Score: 74.11  E-value: 8.41e-17
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 119629966  25 LEPLLAMGFPVHTALKALAATGRKTAEEALAWLHDHC 61
Cdd:cd14300    1 LETLLAMGFPEDVARKALKATGGKSIEKATDWLLSHC 37
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 449-592 9.10e-16

Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase (BPGM) are structurally related enzymes that catalyse reactions involving the transfer of phospho groups between the three carbon atoms of phosphoglycerate... Both enzymes can catalyse three different reactions with different specificities, the isomerization of 2-phosphoglycerate (2-PGA) to 3-phosphoglycerate (3-PGA) with 2,3-diphosphoglycerate (2,3-DPG) as the primer of the reaction, the synthesis of 2,3-DPG from 1,3-DPG with 3-PGA as a primer and the degradation of 2,3-DPG to 3-PGA (phosphatase activity). In mammals, PGAM is a dimeric protein with two isoforms, the M (muscle) and B (brain) forms. In yeast, PGAM is a tetrameric protein.


Pssm-ID: 214859 [Multi-domain]  Cd Length: 158  Bit Score: 75.19  E-value: 9.10e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966   449 NDPPLSSCGIFQSRIAGDALLD-SGIRISSVFASPALRCVQTAKLILEELKLEKKIKIrvEPGIFEwtkweaGKTTPTLM 527
Cdd:smart00855  22 TDVPLTELGRAQAEALGRLLASlLLPRFDVVYSSPLKRARQTAEALAIALGLPGLRER--DFGAWE------GLTWDEIA 93

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119629966   528 slEELKEANFNIDTDYRPAFPlSALMPAESYQEYMDRCTASMVQIVNTCPQDTGVILIVSHGSTL 592
Cdd:smart00855  94 --AKYPEEYLAAWRDPYDPAP-PAPPGGESLADLVERVEPALDELIATADASGQNVLIVSHGGVI 155
SH3_Amphiphysin cd11790
Src Homology 3 domain of Amphiphysin and related domains; Amphiphysins function primarily in ...
 280-338 8.70e-14

Src Homology 3 domain of Amphiphysin and related domains; Amphiphysins function primarily in endocytosis and other membrane remodeling events. They exist in several isoforms and mammals possess two amphiphysin proteins from distinct genes. Amphiphysin I proteins, enriched in the brain and nervous system, contain domains that bind clathrin, Adaptor Protein complex 2 (AP2), dynamin, and synaptojanin. They function in synaptic vesicle endocytosis. Human autoantibodies to amphiphysin I hinder GABAergic signaling and contribute to the pathogenesis of paraneoplastic stiff-person syndrome. Some amphiphysin II isoforms, also called Bridging integrator 1 (Bin1), are localized in many different tissues and may function in intracellular vesicle trafficking. In skeletal muscle, Bin1 plays a role in the organization and maintenance of the T-tubule network. Mutations in Bin1 are associated with autosomal recessive centronuclear myopathy. Amphiphysins contain an N-terminal BAR domain with an additional N-terminal amphipathic helix (an N-BAR), a variable central domain, and a C-terminal SH3 domain. The SH3 domain of amphiphysins bind proline-rich motifs present in binding partners such as dynamin, synaptojanin, and nsP3. It also belongs to a subset of SH3 domains that bind ubiquitin in a site that overlaps with the peptide binding site. 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: 212724 [Multi-domain]  Cd Length: 64  Bit Score: 66.20  E-value: 8.70e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966 280 TLRALFQYKPQNVDELTLSPGDYIFVDPTQ-QDEASEGWVIGISQRTGCRGFLPENYTDR 338
Cdd:cd11790    4 KVRATHDYTAEDTDELTFEKGDVILVIPFDdPEEQDEGWLMGVKESTGCRGVFPENFTER 63
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 398-637 9.32e-14

Histidine phosphatase domain found in a functionally diverse set of proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This set of proteins includes cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, histidine acid phosphatases, phytases, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system; phytases scavenge phosphate from extracellular sources. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG. Clinical applications include the use of prostatic acid phosphatase (PAP) as a serum marker for prostate cancer. Agricultural applications include the addition of phytases to animal feed.


Pssm-ID: 132716 [Multi-domain]  Cd Length: 153  Bit Score: 68.98  E-value: 9.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966 398 VLVVRHGERVDQIFGKAWLQqcstpdgkyyrpdlnfpcslprrsrgikdfeNDPPLSSCGIFQSRIAGDALLDSGIRISS 477
Cdd:cd07040    2 LYLVRHGEREPNAEGRFTGW-------------------------------GDGPLTEKGRQQARELGKALRERYIKFDR 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966 478 VFASPALRCVQTAKLILEELKLekKIKIRVEPGifewtkweagkttptlmsleelkeanfnidtdyrpafplsalmpaes 557
Cdd:cd07040   51 IYSSPLKRAIQTAEIILEGLFE--GLPVEVDPR----------------------------------------------- 81

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966 558 yqeymDRCTASMVQIVNTCPQDTGVILIVSHGSTLDSCTRPLLGLPPRECGDFaqlvrKIPSLGMCFCEENKEEGKWELV 637
Cdd:cd07040   82 -----ARVLNALLELLARHLLDGKNVLIVSHGGTIRALLAALLGLSDEEILSL-----NLPNGSILVLELDECGGKYVRL 151
SH3_Sorbs_3 cd11780
Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing (Sorbs) ...
 282-338 1.83e-13

Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing (Sorbs) proteins and similar domains; This family, also called the vinexin family, is composed predominantly of adaptor proteins containing one sorbin homology (SoHo) and three SH3 domains. Members include the third SH3 domains of Sorbs1 (or ponsin), Sorbs2 (or ArgBP2), Vinexin (or Sorbs3), and similar domains. They are involved in the regulation of cytoskeletal organization, cell adhesion, and growth factor signaling. Members of this family bind multiple partners including signaling molecules like c-Abl, c-Arg, Sos, and c-Cbl, as well as cytoskeletal molecules such as vinculin and afadin. They may have overlapping functions. 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: 212714 [Multi-domain]  Cd Length: 55  Bit Score: 65.02  E-value: 1.83e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119629966 282 RALFQYKPQNVDELTLSPGDYIFVdptqQDEASEGWVIGISQRTGCRGFLPENYTDR 338
Cdd:cd11780    3 RALYSYTPQNEDELELREGDIVYV----MEKCDDGWFVGTSERTGLFGTFPGNYVAR 55
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 450-612 2.50e-11

alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of Salmonella and Eschichia coli species, and homologous proteins found in cobalamin biosynthesis regions in other bacteria. This protein is alpha-ribazole phosphatase (EC 3.1.3.73) and, like many phosphatases, can be closely related in sequence to other phosphatases with different functions. Close homologs excluded from this model include proteins with duplications, so this model is built in -g mode to suppress hits to those proteins. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274461 [Multi-domain]  Cd Length: 177  Bit Score: 62.64  E-value: 2.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966  450 DPPLSSCGIFQSRIAGDALldSGIRISSVFASPALRCVQTAKLILEELKLekkiKIRVEPGIFE--WTKWEagkttptLM 527
Cdd:TIGR03162  21 DVPLAESGEEQAAALREKL--ADVPFDAVYSSPLSRCRELAEILAERRGL----PIIKDDRLREmdFGDWE-------GR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966  528 SLEELKEANFNIDtdYRPAFPLSALMP-AESYQEYMDRCTASMVQIVNTCPQDTgvILIVSHGSTLDSCTRPLLGLPPRE 606
Cdd:TIGR03162  88 SWDEIPEAYPELD--AWAADWQHARPPgGESFADFYQRVSEFLEELLKAHEGDN--VLIVTHGGVIRALLAHLLGLPLEQ 163


                  ....*.
gi 119629966  607 CGDFAQ 612
Cdd:TIGR03162 164 WWSFAV 169
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
440-513 7.01e-11

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 60.66  E-value: 7.01e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119629966 440 RSRGIKDFenDPPLSSCGIFQSRIAGDALLDSGIRISSVFASPALRCVQTAKLILEELKLEKkiKIRVEPGIFE 513
Cdd:COG2062   12 RAPGGDDF--DRPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEILAEALGLPP--KVEVEDELYD 81
SH3_9 pfam14604
Variant SH3 domain;
283-337 7.50e-11

Variant SH3 domain;


Pssm-ID: 434066 [Multi-domain]  Cd Length: 49  Bit Score: 57.63  E-value: 7.50e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 119629966  283 ALFQYKPQNVDELTLSPGDYIFVDPtqqdEASEGWVIGisQRTGCRGFLPENYTD 337
Cdd:pfam14604   1 ALYPYEPKDDDELSLQRGDVITVIE----ESEDGWWEG--INTGRTGLVPANYVE 49
SH3_Vinexin_3 cd11918
Third (or C-terminal) Src Homology 3 domain of Vinexin, also called Sorbin and SH3 domain ...
 279-335 1.73e-10

Third (or C-terminal) Src Homology 3 domain of Vinexin, also called Sorbin and SH3 domain containing 3 (Sorbs3); Vinexin is also called Sorbs3, SH3P3, and SH3-containing adapter molecule 1 (SCAM-1). It is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. Vinexin was first identified as a vinculin binding protein; it is co-localized with vinculin at cell-ECM and cell-cell adhesion sites. There are several splice variants of vinexin: alpha, which contains the SoHo and three SH3 domains and displays tissue-specific expression; and beta, which contains only the three SH3 domains and is widely expressed. Vinexin alpha stimulates the accumulation of F-actin at focal contact sites. Vinexin also promotes keratinocyte migration and wound healing. The SH3 domains of vinexin have been reported to bind a number of ligands including vinculin, WAVE2, DLG5, Abl, and Cbl. 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: 212851 [Multi-domain]  Cd Length: 58  Bit Score: 56.89  E-value: 1.73e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119629966 279 QTLRALFQYKPQNVDELTLSPGDyiFVDPTQQdeASEGWVIGISQRTGCRGFLPENY 335
Cdd:cd11918    2 TPYKAVYQYRPQNEDELELREGD--RVDVMQQ--CDDGWFVGVSRRTQKFGTFPGNY 54
UBA1_spUBP14_like cd14385
UBA1 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
 22-67 1.47e-09

UBA1 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 (spUBP14) and similar proteins; spUBP14, also called deubiquitinating enzyme 14, UBA domain-containing protein 2, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, functions as a deubiquitinating enzyme that is involved in protein degradation in fission yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270568 [Multi-domain]  Cd Length: 47  Bit Score: 53.95  E-value: 1.47e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 119629966  22 PSLLEPLLAMGFPVHTALKALAATGRKTAEEALAWLHDHCNDPSLD 67
Cdd:cd14385    2 AEALAQLLGMGFPEVRCKKALLATGNSDAEAAMNWLFEHMDDPDID 47
SH3_Nebulette_C cd11935
C-terminal Src Homology 3 domain of Nebulette and LIM-nebulette (or Lasp2); Nebulette is a ...
 279-337 2.91e-09

C-terminal Src Homology 3 domain of Nebulette and LIM-nebulette (or Lasp2); Nebulette is a cardiac-specific protein that localizes to the Z-disc. It interacts with tropomyosin and is important in stabilizing actin thin filaments in cardiac muscles. Polymorphisms in the nebulette gene are associated with dilated cardiomyopathy, with some mutations resulting in severe heart failure. Nebulette is a 107kD protein that contains an N-terminal acidic region, multiple nebulin repeats, and a C-terminal SH3 domain. LIM-nebulette, also called Lasp2 (LIM and SH3 domain protein 2), is an alternatively spliced variant of nebulette. Although it shares a gene with nebulette, Lasp2 is not transcribed from a muscle-specific promoter, giving rise to its multiple tissue expression pattern with highest amounts in the brain. It can crosslink actin filaments and it affects cell spreading. Lasp2 is a 34kD protein containing an N-terminal LIM domain, three nebulin repeats, 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: 212868 [Multi-domain]  Cd Length: 58  Bit Score: 53.47  E-value: 2.91e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966 279 QTLRALFQYKPQNVDELTLSPGDYIF-VDPTqqdeaSEGWVIGISQRTGCRGFLPENYTD 337
Cdd:cd11935    1 RTYRAMYDYSAQDEDEVSFRDGDYIVnVQPI-----DEGWMYGTVQRTGRTGMLPANYIE 55
SH3_Nebulin_family_C cd11789
C-terminal Src Homology 3 domain of the Nebulin family of proteins; Nebulin family proteins ...
 280-335 6.07e-09

C-terminal Src Homology 3 domain of the Nebulin family of proteins; Nebulin family proteins contain multiple nebulin repeats, and may contain an N-terminal LIM domain and/or a C-terminal SH3 domain. They have molecular weights ranging from 34 to 900 kD, depending on the number of nebulin repeats, and they all bind actin. They are involved in the regulation of actin filament architecture and function as stabilizers and scaffolds for cytoskeletal structures with which they associate, such as long actin filaments or focal adhesions. Nebulin family proteins that contain a C-terminal SH3 domain include the giant filamentous protein nebulin, nebulette, Lasp1, and Lasp2. Lasp2, also called LIM-nebulette, is an alternatively spliced variant of nebulette. 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: 212723 [Multi-domain]  Cd Length: 55  Bit Score: 52.32  E-value: 6.07e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119629966 280 TLRALFQYKPQNVDELTLSPGDYIfVDPTQQDEaseGWVIGISQRTGCRGFLPENY 335
Cdd:cd11789    1 RYRAMYDYAAADDDEVSFQEGDVI-INVEIIDD---GWMEGTVQRTGQSGMLPANY 52
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 279-335 1.05e-08

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 51.77  E-value: 1.05e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 119629966   279 QTLRALFQYKPQNVDELTLSPGDYIFVDptqqDEASEGWVIGISQRtGCRGFLPENY 335
Cdd:smart00326   3 PQVRALYDYTAQDPDELSFKKGDIITVL----EKSDDGWWKGRLGR-GKEGLFPSNY 54
SH3_Sorbs1_3 cd11916
Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing 1 (Sorbs1), ...
 280-335 2.40e-08

Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing 1 (Sorbs1), also called ponsin; Sorbs1 is also called ponsin, SH3P12, or CAP (c-Cbl associated protein). It is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. It binds Cbl and plays a major role in regulating the insulin signaling pathway by enhancing insulin-induced phosphorylation of Cbl. Sorbs1, like vinexin, localizes at cell-ECM and cell-cell adhesion sites where it binds vinculin, paxillin, and afadin. It may function in the control of cell motility. Other interaction partners of Sorbs1 include c-Abl, Sos, flotillin, Grb4, ataxin-7, filamin C, among others. 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: 212849 [Multi-domain]  Cd Length: 59  Bit Score: 50.76  E-value: 2.40e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119629966 280 TLRALFQYKPQNVDELTLSPGDYIFVdptqQDEASEGWVIGISQRTGCRGFLPENY 335
Cdd:cd11916    3 SYQALYSYAPQNDDELELRDGDIVDV----MEKCDDGWFVGTSRRTKQFGTFPGNY 54
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 282-335 4.13e-08

Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins 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, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.


Pssm-ID: 212690 [Multi-domain]  Cd Length: 51  Bit Score: 49.77  E-value: 4.13e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119629966 282 RALFQYKPQNVDELTLSPGDYIFVDptqqDEASEGWVIGISQRtGCRGFLPENY 335
Cdd:cd00174    3 RALYDYEAQDDDELSFKKGDIITVL----EKDDDGWWEGELNG-GREGLFPANY 51
SH3_Bin1 cd12139
Src Homology 3 domain of Bridging integrator 1 (Bin1), also called Amphiphysin-2; Bin1 ...
 281-338 8.38e-08

Src Homology 3 domain of Bridging integrator 1 (Bin1), also called Amphiphysin-2; Bin1 isoforms are localized in many different tissues and may function in intracellular vesicle trafficking. It plays a role in the organization and maintenance of the T-tubule network in skeletal muscle. Mutations in Bin1 are associated with autosomal recessive centronuclear myopathy. Bin1 contains an N-terminal BAR domain with an additional N-terminal amphipathic helix (an N-BAR) and a C-terminal SH3 domain. The SH3 domain of Bin1 forms transient complexes with actin, myosin filaments, and CDK5, to facilitate sarcomere organization and myofiber maturation. It also binds dynamin and prevents its self-assembly. 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: 213015  Cd Length: 72  Bit Score: 49.53  E-value: 8.38e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119629966 281 LRALFQYKPQNVDELTLSPGDYIFVDPTQQ-DEASEGWVIGISQR--------TGCRGFLPENYTDR 338
Cdd:cd12139    5 VQAQHDYTATDTDELQLKAGDVVLVIPFQNpEEQDEGWLMGVKESdwnqhkklEKCRGVFPENFTER 71
UBA1_atUBP14 cd14295
UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) ...
 21-65 1.12e-07

UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) and similar proteins; atUBP14, also called deubiquitinating enzyme 14, TITAN-6 protein, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is related to the isopeptidase T class of deubiquitinating enzymes that recycle polyubiquitin chains following protein degradation. atUBP14 is essential for early plant development. It can disassemble multi-ubiquitin chains linked internally via epsilon-amino isopeptide bonds using Lys48 and can process some, but not all, translational fusions of ubiquitin linked via alpha-amino peptide bonds. atUBP14 contains two ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270481 [Multi-domain]  Cd Length: 45  Bit Score: 48.52  E-value: 1.12e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 119629966  21 SPSLLEPLLAMGFPVHTALKALAATGRKTAEEALAWLHDHCNDPS 65
Cdd:cd14295    1 DQELVAQLMEMGFPKVRAEKALFFTQNKGLEEAMEWLEEHSEDAD 45
SH3_Sorbs2_3 cd11917
Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing 2 (Sorbs2), ...
 279-338 1.37e-07

Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing 2 (Sorbs2), also called Arg-binding protein 2 (ArgBP2); Sorbs2 or ArgBP2 is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. It regulates actin-dependent processes including cell adhesion, morphology, and migration. It is expressed in many tissues and is abundant in the heart. Like vinexin, it is found in focal adhesion where it interacts with vinculin and afadin. It also localizes in epithelial cell stress fibers and in cardiac muscle cell Z-discs. Sorbs2 has been implicated to play roles in the signaling of c-Arg, Akt, and Pyk2. Other interaction partners of Sorbs2 include c-Abl, flotillin, spectrin, dynamin 1/2, synaptojanin, PTP-PEST, among others. 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: 212850 [Multi-domain]  Cd Length: 61  Bit Score: 48.84  E-value: 1.37e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966 279 QTLRALFQYKPQNVDELTLSPGDYIFVdptqQDEASEGWVIGISQRTGCRGFLPENYTDR 338
Cdd:cd11917    5 EPFQALYNYMPRNEDELELREGDVIDV----MEKCDDGWFVGTSRRTKFFGTFPGNYVKR 60
UBA_PUB_plant cd14290
UBA domain found in plant PNGase/UBA or UBX (PUB) domain-containing proteins; This family ...
 24-67 2.26e-07

UBA domain found in plant PNGase/UBA or UBX (PUB) domain-containing proteins; This family includes some uncharacterized hypothetical proteins found in plants. Although their biological function remain unclear, all family members contain an N-terminal ubiquitin-associated (UBA) domain and a C-terminal PUB domain. UBA domain, along with UBL (ubiquitin-like) domain, has been implicated in proteasomal degradation by associating with substrates destined for degradation as well as with subunits of the proteasome, thus regulating protein turnover. PUB domain functions as a p97 (also known as valosin-containing protein or VCP) adaptor by interacting with the D1 and/or D2 ATPase domains. The type II AAA+ ATPase p97 is involved in a variety of cellular processes such as the deglycosylation of ERAD substrates, membrane fusion, transcription factor activation and cell cycle regulation through differential binding to specific adaptor proteins.


Pssm-ID: 270476 [Multi-domain]  Cd Length: 49  Bit Score: 47.82  E-value: 2.26e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 119629966  24 LLEPLLAMGFPVHTALKALAATGRKTAEEALAWLHDHCNDPSLD 67
Cdd:cd14290    6 LLKELEAMGFPRARAVRALHHTGNTSVEAAVNWIVEHENDPDID 49
SH3_Nebulin_C cd11933
C-terminal Src Homology 3 domain of Nebulin; Nebulin is a giant filamentous protein (600-900 ...
 279-337 2.31e-07

C-terminal Src Homology 3 domain of Nebulin; Nebulin is a giant filamentous protein (600-900 kD) that is expressed abundantly in skeletal muscle. It binds to actin thin filaments and regulates its assembly and function. Nebulin was thought to be part of a molecular ruler complex that is critical in determining the lengths of actin thin filaments in skeletal muscle since its length, which varies due to alternative splicing, correlates with the length of thin filaments in various muscle types. Recent studies indicate that nebulin regulates thin filament length by stabilizing the filaments and preventing depolymerization. Mutations in nebulin can cause nemaline myopathy, characterized by muscle weakness which can be severe and can lead to neonatal lethality. Nebulin contains an N-terminal LIM domain, many nebulin repeats/super repeats, 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: 212866 [Multi-domain]  Cd Length: 58  Bit Score: 48.08  E-value: 2.31e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 119629966 279 QTLRALFQYKPQNVDELTLSPGDYIfVDPTQQDEaseGWVIGISQRTGCRGFLPENYTD 337
Cdd:cd11933    2 KSFRAMYDYRAADDDEVSFKDGDTI-VNVQTIDE---GWMYGTVQRTGKTGMLPANYVE 56
SH3_Lasp1_C cd11934
C-terminal Src Homology 3 domain of LIM and SH3 domain protein 1; Lasp1 is a cytoplasmic ...
 282-337 2.58e-07

C-terminal Src Homology 3 domain of LIM and SH3 domain protein 1; Lasp1 is a cytoplasmic protein that binds focal adhesion proteins and is involved in cell signaling, migration, and proliferation. It is overexpressed in several cancer cells including breast, ovarian, bladder, and liver. In cancer cells, it can be found in the nucleus; its degree of nuclear localization correlates with tumor size and poor prognosis. Lasp1 is a 36kD protein containing an N-terminal LIM domain, two nebulin repeats, 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: 212867 [Multi-domain]  Cd Length: 59  Bit Score: 48.07  E-value: 2.58e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119629966 282 RALFQYKPQNVDELTLSPGDYIfVDPTQQDEaseGWVIGISQRTGCRGFLPENYTD 337
Cdd:cd11934    6 RAVYDYNAADEDEVSFQDGDTI-VNVQQIDD---GWMYGTVERTGDTGMLPANYVE 57
SH3_Intersectin_1 cd11836
First Src homology 3 domain (or SH3A) of Intersectin; Intersectins (ITSNs) are adaptor ...
 282-338 2.86e-07

First Src homology 3 domain (or SH3A) of Intersectin; Intersectins (ITSNs) are adaptor proteins that function in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. They are essential for initiating clathrin-coated pit formation. They bind to many proteins through their multidomain structure and facilitate the assembly of multimeric complexes. Vertebrates contain two ITSN proteins, ITSN1 and ITSN2, which exist in alternatively spliced short and long isoforms. The short isoforms contain two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoforms, in addition, contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. ITSN1 and ITSN2 are both widely expressed, with variations depending on tissue type and stage of development. The first SH3 domain (or SH3A) of ITSN1 has been shown to bind many proteins including Sos1, dynamin1/2, CIN85, c-Cbl, PI3K-C2, SHIP2, N-WASP, and CdGAP, among others. 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: 212770 [Multi-domain]  Cd Length: 55  Bit Score: 47.74  E-value: 2.86e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119629966 282 RALFQYKPQNVDELTLSPGDYIFVDptQQDEASEGWVIGisQRTGCRGFLPENYTDR 338
Cdd:cd11836    3 RALYAFEARNPDEISFQPGDIIQVD--ESQVAEPGWLAG--ELKGKTGWFPANYVEK 55
UBA_UBS3B cd14301
UBA domain found in ubiquitin-associated and SH3 domain-containing protein B (UBS3B) and ...
 23-60 3.08e-07

UBA domain found in ubiquitin-associated and SH3 domain-containing protein B (UBS3B) and similar proteins; UBS3B, or Cbl-interacting protein p70, suppressor of T-cell receptor signaling 1 (Sts-1), T-cell ubiquitin ligand 2 (TULA-2), or tyrosine-protein phosphatase STS1/TULA2, is ubiquitously expressed in mammalian tissues in a variety of cell types. It exhibits high phosphatase activity, but demonstrates no proapoptotic activity. It negatively regulates the tyrosine kinase Zap-70 activation and T cell receptor (TCR) signaling pathways that modulate T cell activation. Moreover, UBS3B acts as a Cbl- and ubiquitin-interacting protein that inhibits endocytosis of epidermal growth factor receptor (EGFR) and platelet-derived growth factor receptor.


Pssm-ID: 270486 [Multi-domain]  Cd Length: 38  Bit Score: 47.05  E-value: 3.08e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 119629966  23 SLLEPLLAMGFPVHTALKALAATGRKTAEEALAWLHDH 60
Cdd:cd14301    1 SALEVLLSMGFPKHRAEKALAATGGRSVQLASDWLLSH 38
SH3_SH3RF_3 cd11783
Third Src Homology 3 domain of SH3 domain containing ring finger 1 (SH3RF1), SH3RF3, and ...
 283-335 5.16e-07

Third Src Homology 3 domain of SH3 domain containing ring finger 1 (SH3RF1), SH3RF3, and similar domains; SH3RF1 (or POSH) and SH3RF3 (or POSH2) are scaffold proteins that function as E3 ubiquitin-protein ligases. They contain an N-terminal RING finger domain and four SH3 domains. This model represents the third SH3 domain, located in the middle of SH3RF1 and SH3RF3, and similar domains. SH3RF1 plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and JNK mediated apoptosis. SH3RF3 interacts with p21-activated kinase 2 (PAK2) and GTP-loaded Rac1. It may play a role in regulating JNK mediated apoptosis in certain conditions. 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: 212717 [Multi-domain]  Cd Length: 55  Bit Score: 47.00  E-value: 5.16e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119629966 283 ALFQYKPQNVDELTLSPGDYIFVDPTQQDeaseGWVIGISQRTGCRGFLPENY 335
Cdd:cd11783    4 ALYPYKPQKPDELELRKGEMYTVTEKCQD----GWFKGTSLRTGQSGVFPGNY 52
SH3_SH3RF3_3 cd11925
Third Src Homology 3 domain of SH3 domain containing ring finger 3, an E3 ubiquitin-protein ...
 283-335 7.02e-07

Third Src Homology 3 domain of SH3 domain containing ring finger 3, an E3 ubiquitin-protein ligase; SH3RF3 is also called POSH2 (Plenty of SH3s 2) or SH3MD4 (SH3 multiple domains protein 4). It is a scaffold protein with E3 ubiquitin-protein ligase activity. It was identified in the screen for interacting partners of p21-activated kinase 2 (PAK2). It may play a role in regulating JNK mediated apoptosis in certain conditions. It also interacts with GTP-loaded Rac1. SH3RF3 is highly homologous to SH3RF1; it also contains an N-terminal RING finger domain and four SH3 domains. This model represents the third SH3 domain, located in the middle, of SH3RF3. 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: 212858  Cd Length: 57  Bit Score: 46.53  E-value: 7.02e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119629966 283 ALFQYKPQNVDELTLSPGDYIFVDPTQQDeaseGWVIGISQRTGCRGFLPENY 335
Cdd:cd11925    5 ALYAYKPQKNDELELRKGEMYRVIEKCQD----GWFKGTSLRTGVSGVFPGNY 53
SH3_Intersectin1_1 cd11987
First Src homology 3 domain (or SH3A) of Intersectin-1; Intersectin-1 (ITSN1) is an adaptor ...
 282-338 7.79e-07

First Src homology 3 domain (or SH3A) of Intersectin-1; Intersectin-1 (ITSN1) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN1 localizes in membranous organelles, CCPs, the Golgi complex, and may be involved in the cell membrane trafficking system. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The first SH3 domain (or SH3A) of ITSN1 has been shown to bind many proteins including Sos1, dynamin1/2, CIN85, c-Cbl, PI3K-C2, SHIP2, N-WASP, and CdGAP, among others. 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: 212920 [Multi-domain]  Cd Length: 55  Bit Score: 46.53  E-value: 7.79e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119629966 282 RALFQYKPQNVDELTLSPGDYIFVDPTQQDEAseGWVIGisQRTGCRGFLPENYTDR 338
Cdd:cd11987    3 RALYPFEARSHDEITIQPGDIVMVDESQTGEP--GWLGG--ELKGKTGWFPANYAEK 55
UBA1_scUBP14_like cd14296
UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ...
 24-60 1.14e-06

UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 (scUBP14) and similar proteins; scUBP14, also called deubiquitinating enzyme 14, glucose-induced degradation protein 6, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is the yeast ortholog of human Isopeptidase T (USP5), a deubiquitinating enzyme known to bind the 29-linked polyubiquitin chains. scUBP14 has been identified as a K29-linked polyubiquitin binding protein as well. It is involved in K29-linked polyubiquitin metabolism by binding to the 29-linked Ub4 resin and serving as an internal positive control in budding yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270482 [Multi-domain]  Cd Length: 39  Bit Score: 45.31  E-value: 1.14e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 119629966  24 LLEPLLAMGFPVHTALKALAATGRKTAEEALAWLHDH 60
Cdd:cd14296    3 AVSQLMSMGFSENAAKRALYYTGNSSVEAAMNWLFEH 39
SH3_SNX9_like cd11763
Src Homology 3 domain of Sorting Nexin 9 and similar proteins; Sorting nexins (SNXs) are Phox ...
 282-335 1.17e-06

Src Homology 3 domain of Sorting Nexin 9 and similar proteins; Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. This subfamily consists of SH3 domain containing SNXs including SNX9, SNX18, SNX33, and similar proteins. SNX9 is localized to plasma membrane endocytic sites and acts primarily in clathrin-mediated endocytosis, while SNX18 is localized to peripheral endosomal structures, and acts in a trafficking pathway that is clathrin-independent but relies on AP-1 and PACS1. 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: 212697 [Multi-domain]  Cd Length: 55  Bit Score: 45.78  E-value: 1.17e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119629966 282 RALFQYKPQNVDELTLSPGDYIFVdpTQQDeASEGWVIGISQRtGCRGFLPENY 335
Cdd:cd11763    3 RALYDFDSQPSGELSLRAGEVLTI--TRQD-VGDGWLEGRNSR-GEVGLFPSSY 52
SH3_Nostrin cd11823
Src homology 3 domain of Nitric Oxide Synthase TRaffic INducer; Nostrin is expressed in ...
 282-337 1.40e-06

Src homology 3 domain of Nitric Oxide Synthase TRaffic INducer; Nostrin is expressed in endothelial and epithelial cells and is involved in the regulation, trafficking and targeting of endothelial NOS (eNOS). It facilitates the endocytosis of eNOS by coordinating the functions of dynamin and the Wiskott-Aldrich syndrome protein (WASP). Increased expression of Nostrin may be correlated to preeclampsia. Nostrin contains an N-terminal F-BAR domain 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: 212757 [Multi-domain]  Cd Length: 53  Bit Score: 45.41  E-value: 1.40e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119629966 282 RALFQYKPQNVDELTLSPGDYIFVdpTQQDEasEGWVIGisQRTGCRGFLPENYTD 337
Cdd:cd11823    3 KALYSYTANREDELSLQPGDIIEV--HEKQD--DGWWLG--ELNGKKGIFPATYVE 52
SH3_D21-like cd12142
Src Homology 3 domain of SH3 domain-containing protein 21 (SH3D21) and similar proteins; ...
 282-335 1.66e-06

Src Homology 3 domain of SH3 domain-containing protein 21 (SH3D21) and similar proteins; N-terminal SH3 domain of the uncharacterized protein SH3 domain-containing protein 21, and similar uncharacterized domains, it belongs to the CD2AP-like_3 subfamily of proteins. The CD2AP-like_3 subfamily is composed of the third SH3 domain (SH3C) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3C of both proteins have been shown to bind to ubiquitin. 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: 213018 [Multi-domain]  Cd Length: 55  Bit Score: 45.53  E-value: 1.66e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119629966 282 RALFQYKPQNVDELTLSPGDYIFVdpTQQDEASEGWVIGisQRTGCRGFLPENY 335
Cdd:cd12142    3 RVLFDYNPVAPDELALKKGDVIEV--ISKETEDEGWWEG--ELNGRRGFFPDNF 52
UBA_UBXN1 cd14302
UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also ...
 23-63 2.37e-06

UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also called SAPK substrate protein 1 (SAKS1) or UBA/UBX 33.3 kDa protein, is a widely expressed protein containing an N-terminal ubiquitin-associated (UBA) domain, a coiled-coil region, and a C-terminal ubiquitin-like (UBX) domain. It binds polyubiquitin and valosin-containing protein (VCP), and has been identified as a substrate for stress-activated protein kinases (SAPKs). Moreover, UBXN1 specifically binds to Homer2b. It may also interact with ubiquitin (Ub) and may be involved in the Ub-proteasome proteolytic pathways. In addition, UBXN1 can associate with autoubiquitinated BRCA1 tumor suppressor and inhibit its enzymatic function through its UBA domain.


Pssm-ID: 270487 [Multi-domain]  Cd Length: 41  Bit Score: 44.59  E-value: 2.37e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 119629966  23 SLLEPLLAMGFPVHTALKALAATGRKTAEEALAWLHDHCND 63
Cdd:cd14302    1 SELQTLIEMGFSRNRAEKALAKTGNQGVEAAMEWLLAHEDD 41
SH3_Intersectin2_1 cd11988
First Src homology 3 domain (or SH3A) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor ...
 280-338 4.43e-06

First Src homology 3 domain (or SH3A) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN2 also functions as a specific GEF for Cdc42 activation in epithelial morphogenesis, and is required in mitotic spindle orientation. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The first SH3 domain (or SH3A) of ITSN2 is expected to bind many protein partners, similar to ITSN1 which has been shown to bind Sos1, dynamin1/2, CIN85, c-Cbl, PI3K-C2, SHIP2, N-WASP, and CdGAP, among others. 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: 212921 [Multi-domain]  Cd Length: 57  Bit Score: 44.48  E-value: 4.43e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 119629966 280 TLRALFQYKPQNVDELTLSPGDYIFVDPTQQDEAseGWVIGISQrtGCRGFLPENYTDR 338
Cdd:cd11988    3 NYRALYPFEARNHDEMSFNAGDIIQVDEKTVGEP--GWLYGSFQ--GNFGWFPCNYVEK 57
SH3_ephexin1_like cd11793
Src homology 3 domain of ephexin-1-like SH3 domain containing Rho guanine nucleotide exchange ...
 283-336 6.01e-06

Src homology 3 domain of ephexin-1-like SH3 domain containing Rho guanine nucleotide exchange factors; Members of this family contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), and C-terminal SH3 domains. They include the Rho guanine nucleotide exchange factors ARHGEF5, ARHGEF16, ARHGEF19, ARHGEF26, ARHGEF27 (also called ephexin-1), and similar proteins, and are also called ephexins because they interact directly with ephrin A receptors. GEFs interact with Rho GTPases via their DH domains to catalyze nucleotide exchange by stabilizing the nucleotide-free GTPase intermediate. They play important roles in neuronal development. The SH3 domains of ARHGEFs play an autoinhibitory role through intramolecular interactions with a proline-rich region N-terminal to the DH 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: 212727 [Multi-domain]  Cd Length: 55  Bit Score: 43.86  E-value: 6.01e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119629966 283 ALFQYKPQNVDELTLSPGDYIFVdpTQQdeASEGWVIGISQRTGCRGFLPENYT 336
Cdd:cd11793    4 CVHAYTAQQPDELTLEEGDVVNV--LRK--MPDGWYEGERLRDGERGWFPSSYT 53
SH3_JIP1_like cd11801
Src homology 3 domain of JNK-interacting proteins 1 and 2, and similar domains; ...
 280-335 7.45e-06

Src homology 3 domain of JNK-interacting proteins 1 and 2, and similar domains; JNK-interacting proteins (JIPs) function as scaffolding proteins for c-Jun N-terminal kinase (JNK) signaling pathways. They bind to components of Mitogen-activated protein kinase (MAPK) pathways such as JNK, MKK, and several MAP3Ks such as MLK and DLK. There are four JIPs (JIP1-4); all contain a JNK binding domain. JIP1 and JIP2 also contain SH3 and Phosphotyrosine-binding (PTB) domains. Both are highly expressed in the brain and pancreatic beta-cells. JIP1 functions as an adaptor linking motor to cargo during axonal transport and also is involved in regulating insulin secretion. JIP2 form complexes with fibroblast growth factor homologous factors (FHFs), which facilitates activation of the p38delta MAPK. The SH3 domain of JIP1 homodimerizes at the interface usually involved in proline-rich ligand recognition, despite the lack of this motif in the domain itself. 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: 212735  Cd Length: 55  Bit Score: 43.45  E-value: 7.45e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119629966 280 TLRALFQYKPQNVDELTLSPGDYIFVdptqQDEASEGWVIGISQRTGCRGFLPENY 335
Cdd:cd11801    1 THRALHKFIPRHEDEIELDIGDPVYV----EQEADDLWCEGTNLRTGQRGIFPAAY 52
SH3_OSTF1 cd11772
Src Homology 3 domain of metazoan osteoclast stimulating factor 1; OSTF1, also named OSF or ...
 282-335 1.07e-05

Src Homology 3 domain of metazoan osteoclast stimulating factor 1; OSTF1, also named OSF or SH3P2, is a signaling protein containing SH3 and ankyrin-repeat domains. It acts through a Src-related pathway to enhance the formation of osteoclasts and bone resorption. It also acts as a negative regulator of cell motility. 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: 212706 [Multi-domain]  Cd Length: 53  Bit Score: 43.06  E-value: 1.07e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119629966 282 RALFQYKPQNVDELTLSPGDYIFVdptqQDEASEGWVIGISQrtGCRGFLPENY 335
Cdd:cd11772    3 RALYDYEAQHPDELSFEEGDLLYI----SDKSDPNWWKATCG--GKTGLIPSNY 50
SH3_Bzz1_2 cd11778
Second Src Homology 3 domain of Bzz1 and similar domains; Bzz1 (or Bzz1p) is a WASP ...
 280-335 1.36e-05

Second Src Homology 3 domain of Bzz1 and similar domains; Bzz1 (or Bzz1p) is a WASP/Las17-interacting protein involved in endocytosis and trafficking to the vacuole. It physically interacts with type I myosins and functions in the early steps of endocytosis. Together with other proteins, it induces membrane scission in yeast. Bzz1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. This model represents the second 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: 212712 [Multi-domain]  Cd Length: 51  Bit Score: 42.87  E-value: 1.36e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119629966 280 TLRALFQYKPQNVDELTLSPGDYIFVdpTQQDEASeGWVIGisQRTGCRGFLPENY 335
Cdd:cd11778    1 YVEALYDYEAQGDDEISIRVGDRIAV--IRGDDGS-GWTYG--EINGVKGLFPTSY 51
SH3_PSTPIP1 cd11824
Src homology 3 domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; PSTPIP1, ...
 282-335 1.39e-05

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: 42.75  E-value: 1.39e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119629966 282 RALFQYKPQNVDELTLSPGDYIFVdptqQDEASEGWviGISQRTGCRGFLPENY 335
Cdd:cd11824    3 SVLYDYTAQEDDELSISKGDVVAV----IEKGEDGW--WTVERNGQKGLVPGTY 50
SH3_SH3RF_C cd11785
C-terminal (Fourth) Src Homology 3 domain of SH3 domain containing ring finger 1 (SH3RF1), ...
 282-337 1.54e-05

C-terminal (Fourth) Src Homology 3 domain of SH3 domain containing ring finger 1 (SH3RF1), SH3RF3, and similar domains; SH3RF1 (or POSH) and SH3RF3 (or POSH2) are scaffold proteins that function as E3 ubiquitin-protein ligases. They contain an N-terminal RING finger domain and four SH3 domains. This model represents the fourth SH3 domain, located at the C-terminus of SH3RF1 and SH3RF3, and similar domains. SH3RF1 plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and JNK mediated apoptosis. SH3RF3 interacts with p21-activated kinase 2 (PAK2) and GTP-loaded Rac1. It may play a role in regulating JNK mediated apoptosis in certain conditions. 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: 212719  Cd Length: 55  Bit Score: 42.84  E-value: 1.54e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119629966 282 RALFQYKPQNVDELTLSPGDYIFVDPTQQDeaseGWVIGISQRTGCRGFLPENYTD 337
Cdd:cd11785    3 RVIVPYPPQSEAELELKEGDIVFVHKKRED----GWFKGTLQRTGKTGLFPGSFVE 54
SH3_JIP2 cd11942
Src homology 3 domain of JNK-interacting protein 2; JNK-interacting protein 2 (JIP2) is also ...
 280-335 1.70e-05

Src homology 3 domain of JNK-interacting protein 2; JNK-interacting protein 2 (JIP2) is also called Mitogen-activated protein kinase 8-interacting protein 2 (MAPK8IP2) or Islet-brain-2 (IB2). It is widely expressed in the brain, where it forms complexes with fibroblast growth factor homologous factors (FHFs), which facilitates activation of the p38delta MAPK. JIP2 is enriched in postsynaptic densities and may play a role in motor and cognitive function. In addition to a JNK binding domain, JIP2 also contains SH3 and Phosphotyrosine-binding (PTB) domains. The SH3 domain of the related protein JIP1 homodimerizes at the interface usually involved in proline-rich ligand recognition, despite the lack of this motif in the domain itself. 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: 212875  Cd Length: 55  Bit Score: 42.61  E-value: 1.70e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119629966 280 TLRALFQYKPQNVDELTLSPGDYIFVDPTQQDEasegWVIGISQRTGCRGFLPENY 335
Cdd:cd11942    1 THRAVFRFIPRHEDELELDVDDPLLVEAEEDDY----WYRGYNMRTGERGIFPAFY 52
SH3_Cortactin_like cd11819
Src homology 3 domain of Cortactin and related proteins; This subfamily includes cortactin, ...
 282-335 2.31e-05

Src homology 3 domain of Cortactin and related proteins; This subfamily includes cortactin, Abp1 (actin-binding protein 1), hematopoietic lineage cell-specific protein 1 (HS1), and similar proteins. These proteins are involved in regulating actin dynamics through direct or indirect interaction with the Arp2/3 complex, which is required to initiate actin polymerization. They all contain at least one C-terminal SH3 domain. Cortactin and HS1 bind Arp2/3 and actin through an N-terminal region that contains an acidic domain and several copies of a repeat domain found in cortactin and HS1. Abp1 binds actin via an N-terminal actin-depolymerizing factor (ADF) homology domain. Yeast Abp1 binds Arp2/3 directly through two acidic domains. Mammalian Abp1 does not directly interact with Arp2/3; instead, it regulates actin dynamics indirectly by interacting with dynamin and WASP family proteins. The C-terminal region of these proteins acts as an adaptor or scaffold that can connect membrane trafficking and signaling proteins that bind the SH3 domain within the actin network. 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: 212753 [Multi-domain]  Cd Length: 54  Bit Score: 42.30  E-value: 2.31e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119629966 282 RALFQYKPQNVDELTLSPGDYIfvdpTQQDEASEGWVIGISqRTGCRGFLPENY 335
Cdd:cd11819    3 KALYDYQAAEDNEISFVEGDII----TQIEQIDEGWWLGVN-AKGQKGLFPANY 51
SH3_PI3K_p85 cd11776
Src Homology 3 domain of the p85 regulatory subunit of Class IA Phosphatidylinositol 3-kinases; ...
 282-337 2.97e-05

Src Homology 3 domain of the p85 regulatory subunit of Class IA Phosphatidylinositol 3-kinases; Class I PI3Ks convert PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. They are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. Class IA PI3Ks associate with the p85 regulatory subunit family, which contains SH3, RhoGAP, and SH2 domains. The p85 subunits recruit the PI3K p110 catalytic subunit to the membrane, where p110 phosphorylates inositol lipids. Vertebrates harbor two p85 isoforms, called alpha and beta. 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: 212710  Cd Length: 72  Bit Score: 42.49  E-value: 2.97e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119629966 282 RALFQYKPQNVDELTLSPGDYIFVD-PTQQD----------EASEGWVIGISQRTGCRGFLPENYTD 337
Cdd:cd11776    4 RALYDYEKERDEDIILKTGDVLVVEnPELLAlgvpdgketvPKPEGWLEGKNERTGERGDFPGTYVE 70
UBA1_UBP5_like cd14294
UBA1 domain found in ubiquitin carboxyl-terminal hydrolase UBP5, UBP13 and similar proteins; ...
 22-64 4.31e-05

UBA1 domain found in ubiquitin carboxyl-terminal hydrolase UBP5, UBP13 and similar proteins; UBP5, also called deubiquitinating enzyme 5, Isopeptidase T (IsoT), ubiquitin thioesterase 5, or ubiquitin-specific-processing protease 5, is a deubiquitinating enzyme largely responsible for the disassembly of the majority of unanchored polyubiquitin in the cell. Zinc is required for its catalytic activity. UBP5 contains four ubiquitin (Ub)-binding sites including an N-terminal zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. ZnF domain binds the proximal ubiquitin. UBP domain forms the active site. UBA domains are involved in binding linear or K48-linked polyubiquitin. UBP13, also called deubiquitinating enzyme 13, Isopeptidase T-3 (isoT3), ubiquitin thioesterase 13, or ubiquitin-specific-processing protease 13, is an ortholog of UBP5. It has similar domain architecture, but functions differently from USP5 in cellular deubiquitination processes. It exhibits a weak deubiquitinating activity preferring to Lys63-linked polyubiquitin in a non-activation manner. Moreover, the zinc finger (ZnF) domain of USP13 cannot bind to Ub. Its tandem UBA domains can bind with different types of diUb but preferentially with K63-linked.USP13 can also regulate the protein level of CD3delta in cells via its UBA domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270480 [Multi-domain]  Cd Length: 44  Bit Score: 41.14  E-value: 4.31e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 119629966  22 PSLLEPLLAMGFPVHTALKALAATGRKTAEEALAWLHDHCNDP 64
Cdd:cd14294    1 EAVVSQLAEMGFPLEACRKAVYHTNNSGLEAAMNWIMEHMDDP 43
SH3_CD2AP_2 cd12054
Second Src Homology 3 domain (SH3B) of CD2-associated protein; CD2AP, also called CMS (Cas ...
 282-335 4.78e-05

Second Src Homology 3 domain (SH3B) of CD2-associated protein; CD2AP, also called CMS (Cas ligand with Multiple SH3 domains) or METS1 (Mesenchyme-to-Epithelium Transition protein with SH3 domains), is a cytosolic adaptor protein that plays a role in regulating the cytoskeleton. It is critical in cell-to-cell union necessary for kidney function. It also stabilizes the contact between a T cell and antigen-presenting cells. It is primarily expressed in podocytes at the cytoplasmic face of the slit diaphragm and serves as a linker anchoring podocin and nephrin to the actin cytoskeleton. CD2AP contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the second SH3 domain (SH3B) of CD2AP. SH3B binds to c-Cbl in a site (TPSSRPLR is the core binding motif) distinct from the c-Cbl/SH3A binding site. 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: 212987 [Multi-domain]  Cd Length: 55  Bit Score: 41.49  E-value: 4.78e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119629966 282 RALFQYKPQNVDELTLSPGDYIFVDptqqDEASEGWVIGisQRTGCRGFLPENY 335
Cdd:cd12054    4 KVLFEYVPQNEDELELKVGDIIDIN----EEVEEGWWSG--TLNGKSGLFPSNF 51
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 434-604 5.77e-05

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 45.74  E-value: 5.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966 434 PCSLPRRSRGIkdfeNDPPLSSCGIFQSRIAGDALLDSGiRISSVFASPALRCVQTAKLILEELKLEkkikIRVEPGIFE 513
Cdd:PRK07238 183 ELSVQRRYSGR----GNPELTEVGRRQAAAAARYLAARG-GIDAVVSSPLQRARDTAAAAAKALGLD----VTVDDDLIE 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966 514 -----W---TKWEAGKTTPtlmsleELKEANFNiDTDYRPafplsalmPA-ESYQEYMDRCTASMVQIVNTCPQDTgvIL 584
Cdd:PRK07238 254 tdfgaWeglTFAEAAERDP------ELHRAWLA-DTSVAP--------PGgESFDAVARRVRRARDRLIAEYPGAT--VL 316

                        170       180
                 ....*....|....*....|
gi 119629966 585 IVSHGSTLDSCTRPLLGLPP 604
Cdd:PRK07238 317 VVSHVTPIKTLLRLALDAGP 336
SH3_Irsp53_BAIAP2L cd11779
Src Homology 3 domain of Insulin Receptor tyrosine kinase Substrate p53, Brain-specific ...
 279-336 6.55e-05

Src Homology 3 domain of Insulin Receptor tyrosine kinase Substrate p53, Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2 (BAIAP2)-Like proteins, and similar proteins; Proteins in this family include IRSp53, BAIAP2L1, BAIAP2L2, and similar proteins. They all contain an Inverse-Bin/Amphiphysin/Rvs (I-BAR) or IMD domain in addition to the SH3 domain. IRSp53, also known as BAIAP2, is a scaffolding protein that takes part in many signaling pathways including Cdc42-induced filopodia formation, Rac-mediated lamellipodia extension, and spine morphogenesis. IRSp53 exists as multiple splicing variants that differ mainly at the C-termini. BAIAP2L1, also called IRTKS (Insulin Receptor Tyrosine Kinase Substrate), serves as a substrate for the insulin receptor and binds the small GTPase Rac. It plays a role in regulating the actin cytoskeleton and colocalizes with F-actin, cortactin, VASP, and vinculin. IRSp53 and IRTKS also mediate the recruitment of effector proteins Tir and EspFu, which regulate host cell actin reorganization, to bacterial attachment sites. BAIAP2L2 co-localizes with clathrin plaques but its function has not been determined. The SH3 domains of IRSp53 and IRTKS have been shown to bind the proline-rich C-terminus of EspFu. 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: 212713 [Multi-domain]  Cd Length: 57  Bit Score: 41.15  E-value: 6.55e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 119629966 279 QTLRALFQYKPQNVDELTLSPGDYIFVdptQQDEASEGWVIGISQRTGCRGFLPENYT 336
Cdd:cd11779    1 PRVKALYPHAAGGETQLSFEEGDVITL---LGPEPRDGWHYGENERSGRRGWFPIAYT 55
SH3_Bem1p_1 cd11878
First Src Homology 3 domain of Bud emergence protein 1 and similar domains; Members of this ...
 281-335 8.43e-05

First Src Homology 3 domain of Bud emergence protein 1 and similar domains; Members of this subfamily bear similarity to Saccharomyces cerevisiae Bem1p, containing two Src Homology 3 (SH3) domains at the N-terminus, a central PX domain, and a C-terminal PB1 domain. Bem1p is a scaffolding protein that is critical for proper Cdc42p activation during bud formation in yeast. During budding and mating, Bem1p migrates to the plasma membrane where it can serve as an adaptor for Cdc42p and some other proteins. Bem1p also functions as an effector of the G1 cyclin Cln3p and the cyclin-dependent kinase Cdc28p in promoting vacuolar fusion. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212811 [Multi-domain]  Cd Length: 54  Bit Score: 40.73  E-value: 8.43e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119629966 281 LRALFQYKPQNVDELTLSPGDYIFVdptQQDEASEGWVIGISQRTGCRGFLPENY 335
Cdd:cd11878    2 IRALYDYRAQTPGELSFSKGDFFHV---IGEEDQGEWYEATNPVTGKRGLVPKSY 53
SH3_GRAF-like cd11882
Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase and similar ...
 280-335 8.91e-05

Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase and similar proteins; This subfamily is composed of Rho GTPase activating proteins (GAPs) with similarity to GRAF. Members contain an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, a Rho GAP domain, and a C-terminal SH3 domain. Although vertebrates harbor four Rho GAPs in the GRAF subfamily including GRAF, GRAF2, GRAF3, and Oligophrenin-1 (OPHN1), only three are included in this model. OPHN1 contains the BAR, PH and GAP domains, but not the C-terminal SH3 domain. GRAF and GRAF2 show GAP activity towards RhoA and Cdc42. GRAF influences Rho-mediated cytoskeletal rearrangements and binds focal adhesion kinase. GRAF2 regulates caspase-activated p21-activated protein kinase-2. The SH3 domain of GRAF and GRAF2 binds PKNbeta, a target of the small GTPase Rho. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212815 [Multi-domain]  Cd Length: 54  Bit Score: 40.35  E-value: 8.91e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119629966 280 TLRALFQYKPQNVDELTLSPGDyIFVDPTQQDEasEGWVIGISQrtGCRGFLPENY 335
Cdd:cd11882    1 RARALYACKAEDESELSFEPGQ-IITNVQPSDE--PGWLEGTLN--GRTGLIPENY 51
SH3_JIP1 cd11943
Src homology 3 domain of JNK-interacting protein 1; JNK-interacting protein 1 (JIP1) is also ...
 280-335 1.01e-04

Src homology 3 domain of JNK-interacting protein 1; JNK-interacting protein 1 (JIP1) is also called Islet-brain 1 (IB1) or Mitogen-activated protein kinase 8-interacting protein 1 (MAPK8IP1). It is highly expressed in neurons, where it functions as an adaptor linking motor to cargo during axonal transport. It also affects microtubule dynamics in neurons. JIP1 is also found in pancreatic beta-cells, where it is involved in regulating insulin secretion. In addition to a JNK binding domain, JIP1 also contains SH3 and Phosphotyrosine-binding (PTB) domains. Its SH3 domain homodimerizes at the interface usually involved in proline-rich ligand recognition, despite the lack of this motif in the domain itself. 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: 212876  Cd Length: 55  Bit Score: 40.36  E-value: 1.01e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119629966 280 TLRALFQYKPQNVDELTLSPGDYIFVDPTQQDEasegWVIGISQRTGCRGFLPENY 335
Cdd:cd11943    1 THRAVFRFVPRHPDELELEVDDPLLVEVQAEDY----WYEAYNMRTGARGIFPAYY 52
SH3_PACSIN_like cd11999
Src homology 3 domain of an unknown subfamily of proteins with similarity to Protein kinase C ...
 279-335 1.17e-04

Src homology 3 domain of an unknown subfamily of proteins with similarity to Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins; PACSINs, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. They bind both dynamin and Wiskott-Aldrich syndrome protein (WASP), and may provide direct links between the actin cytoskeletal machinery through WASP and dynamin-dependent endocytosis. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSINs contain an N-terminal F-BAR domain 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: 212932 [Multi-domain]  Cd Length: 56  Bit Score: 40.31  E-value: 1.17e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119629966 279 QTLRALFQYKPQNVDELTLSPGDYIFvdpTQQDEASEGWVIGISQRtGCRGFLPENY 335
Cdd:cd11999    2 VRVRAVYDYTGQEPDELSFKAGEELL---KVEDEDEQGWCKGVTDG-GAVGLYPANY 54
SH3_SH3RF2_3 cd11784
Third Src Homology 3 domain of SH3 domain containing ring finger 2; SH3RF2 is also called ...
 283-335 1.26e-04

Third Src Homology 3 domain of SH3 domain containing ring finger 2; SH3RF2 is also called POSHER (POSH-eliminating RING protein) or HEPP1 (heart protein phosphatase 1-binding protein). It acts as an anti-apoptotic regulator of the JNK pathway by binding to and promoting the degradation of SH3RF1 (or POSH), a scaffold protein that is required for pro-apoptotic JNK activation. It may also play a role in cardiac functions together with protein phosphatase 1. SH3RF2 contains an N-terminal RING finger domain and three SH3 domains. This model represents the third SH3 domain, located in the middle, of SH3RF2. 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: 212718  Cd Length: 55  Bit Score: 40.15  E-value: 1.26e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119629966 283 ALFQYKPQNVDELTLSPGDYIFVDPTQQdeasEGWVIGISQRTGCRGFLPENY 335
Cdd:cd11784    4 ALHSYSAHRPEELELQKGEGVRVLGKFQ----EGWLRGLSLVTGRVGIFPSNY 52
SH3_Stac2_C cd11985
C-terminal Src homology 3 domain of SH3 and cysteine-rich domain-containing protein 2 (Stac2); ...
 283-338 1.31e-04

C-terminal Src homology 3 domain of SH3 and cysteine-rich domain-containing protein 2 (Stac2); Stac proteins are putative adaptor proteins that contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. There are three mammalian members (Stac1, Stac2, and Stac3) of this family. Stac2 contains a single SH3 domain at the C-terminus unlike Stac1 and Stac3, which contain two C-terminal SH3 domains. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. 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: 212918  Cd Length: 53  Bit Score: 39.93  E-value: 1.31e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119629966 283 ALFQYKPQNVDELTLSPGDYIFVdptqQDEASEGWVIGisqRTGCR-GFLPENYTDR 338
Cdd:cd11985    4 ALYKFLPQENNDLPLQPGDRVMV----VDDSNEDWWKG---KSGDRvGFFPANFVQR 53
SH3_FCHSD_1 cd11761
First Src Homology 3 domain of FCH and double SH3 domains proteins; This group is composed of ...
 280-337 1.50e-04

First Src Homology 3 domain of FCH and double SH3 domains proteins; This group is composed of FCH and double SH3 domains protein 1 (FCHSD1) and FCHSD2. These proteins have a common domain structure consisting of an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), two SH3, and C-terminal proline-rich domains. They have only been characterized in silico and their functions remain unknown. This group also includes the insect protein, nervous wreck, which acts as a regulator of synaptic growth signaling. 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: 212695 [Multi-domain]  Cd Length: 57  Bit Score: 40.04  E-value: 1.50e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 119629966 280 TLRALFQYKPQNVDELTLSPGDYIFVdptQQDEASEGWVIGISQRtGCRGFLPENYTD 337
Cdd:cd11761    3 TCKVLYSYEAQRPDELTITEGEELEV---IEDGDGDGWVKARNKS-GEVGYVPENYLQ 56
UBA1_UBP5 cd14383
UBA1 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ...
 23-64 1.60e-04

UBA1 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called deubiquitinating enzyme 5, Isopeptidase T (IsoT), ubiquitin thioesterase 5, or ubiquitin-specific-processing protease 5, is a deubiquitinating enzyme largely responsible for the disassembly of the majority of unanchored polyubiquitin in the cell. Zinc is required for its catalytic activity. UBP5 contains four ubiquitin (Ub)-binding sites including an N-terminal zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. ZnF domain binds the proximal ubiquitin. UBP domain forms the active site. UBA domains are involved in binding linear or K48-linked polyubiquitin. This model corresponds to the UBA1 domain.


Pssm-ID: 270566 [Multi-domain]  Cd Length: 49  Bit Score: 39.65  E-value: 1.60e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 119629966  23 SLLEPLLAMGFPVHTALKALAATGRKTAEEALAWLHDHCNDP 64
Cdd:cd14383    5 SVIIQLVEMGFPMDACRKAVYYTGNSGAEAAMNWVMSHMDDP 46
SH3_CD2AP-like_2 cd11874
Second Src Homology 3 domain (SH3B) of CD2-associated protein and similar proteins; This ...
 282-335 1.73e-04

Second Src Homology 3 domain (SH3B) of CD2-associated protein and similar proteins; This subfamily is composed of the second SH3 domain (SH3B) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3B of both proteins have been shown to bind to Cbl. In the case of CD2AP, its SH3B binds to Cbl at a site distinct from the c-Cbl/SH3A binding site. The CIN85 SH3B also binds ubiquitin. 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: 212807 [Multi-domain]  Cd Length: 53  Bit Score: 39.62  E-value: 1.73e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119629966 282 RALFQYKPQNVDELTLSPGDYIFVdptqQDEASEGWVIGisQRTGCRGFLPENY 335
Cdd:cd11874    3 KVLFSYTPQNEDELELKVGDTIEV----LGEVEEGWWEG--KLNGKVGVFPSNF 50
SH3_CD2AP-like_1 cd11873
First Src Homology 3 domain (SH3A) of CD2-associated protein and similar proteins; This ...
 280-335 1.75e-04

First Src Homology 3 domain (SH3A) of CD2-associated protein and similar proteins; This subfamily is composed of the first SH3 domain (SH3A) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3A of both proteins bind to an atypical PXXXPR motif at the C-terminus of Cbl and the cytoplasmic domain of the cell adhesion protein CD2. CIN85 SH3A binds to internal proline-rich motifs within the proline-rich region; this intramolecular interaction serves as a regulatory mechanism to keep CIN85 in a closed conformation, preventing the recruitment of other proteins. CIN85 SH3A has also been shown to bind ubiquitin. 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: 212806 [Multi-domain]  Cd Length: 53  Bit Score: 39.56  E-value: 1.75e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119629966 280 TLRALFQYKPQNVDELTLSPGDyIFVDPTQQDeasEGWVIGisQRTGCRGFLPENY 335
Cdd:cd11873    1 EVIVEFDYDAEEPDELTLKVGD-IITNVKKME---EGWWEG--TLNGKRGMFPDNF 50
SH3_ARHGEF5_19 cd11940
Src homology 3 domain of the Rho guanine nucleotide exchange factors ARHGEF5 and ARHGEF19; ...
 279-335 1.98e-04

Src homology 3 domain of the Rho guanine nucleotide exchange factors ARHGEF5 and ARHGEF19; ARHGEF5, also called ephexin-3 or TIM (Transforming immortalized mammary oncogene), is a potent activator of RhoA and it plays roles in regulating cell shape, adhesion, and migration. It binds to the SH3 domain of Src and is involved in regulating Src-induced podosome formation. ARHGEF19, also called ephexin-2 or WGEF (weak-similarity GEF), is highly expressed in the intestine, liver, heart and kidney. It activates RhoA, Cdc42, and Rac 1, and has been shown to activate RhoA in the Wnt-PCP (planar cell polarity) pathway. It is involved in the regulation of cell polarity and cytoskeletal reorganization. ARHGEF5 and ARHGEF19 contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), and SH3 domains. The SH3 domains of ARHGEFs play an autoinhibitory role through intramolecular interactions with a proline-rich region N-terminal to the DH 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: 212873  Cd Length: 55  Bit Score: 39.78  E-value: 1.98e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119629966 279 QTLRAlfqYKPQNVDELTLSPGDYIFVdpTQQdeASEGWVIGISQRTGCRGFLPENY 335
Cdd:cd11940    3 QCIRS---YKAQENDELTLEKADIIMV--RQQ--SSDGWLEGVRLSDGERGWFPQSH 52
SH3_MyoIe_If_like cd11827
Src homology 3 domain of Myosins Ie, If, and similar proteins; Myosins Ie (MyoIe) and If ...
 282-338 2.18e-04

Src homology 3 domain of Myosins Ie, If, and similar proteins; Myosins Ie (MyoIe) and If (MyoIf) are nonmuscle, unconventional, long tailed, class I myosins containing an N-terminal motor domain and a myosin tail with TH1, TH2, and SH3 domains. MyoIe interacts with the endocytic proteins, dynamin and synaptojanin-1, through its SH3 domain; it may play a role in clathrin-dependent endocytosis. In the kidney, MyoIe is critical for podocyte function and normal glomerular filtration. Mutations in MyoIe is associated with focal segmental glomerulosclerosis, a disease characterized by massive proteinuria and progression to end-stage kidney disease. MyoIf is predominantly expressed in the immune system; it plays a role in immune cell motility and innate immunity. Mutations in MyoIf may be associated with the loss of hearing. The MyoIf gene has also been found to be fused to the MLL (Mixed lineage leukemia) gene in infant acute myeloid leukemias (AML). 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: 212761 [Multi-domain]  Cd Length: 53  Bit Score: 39.32  E-value: 2.18e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119629966 282 RALFQYKPQNVDELTLSPGDYIfvDPTQQDEAseGWVIGisQRTGCRGFLPENYTDR 338
Cdd:cd11827    3 KALYAYDAQDTDELSFNEGDII--EILKEDPS--GWWTG--RLRGKEGLFPGNYVEK 53
SH3_CD2AP-like_3 cd11875
Third Src Homology 3 domain (SH3C) of CD2-associated protein and similar proteins; This ...
 282-336 2.33e-04

Third Src Homology 3 domain (SH3C) of CD2-associated protein and similar proteins; This subfamily is composed of the third SH3 domain (SH3C) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3C of both proteins have been shown to bind to ubiquitin. 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: 212808 [Multi-domain]  Cd Length: 55  Bit Score: 39.26  E-value: 2.33e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119629966 282 RALFQYKPQNVDELTLSPGDYIFV-DPTQQDeasEGWVIGisQRTGCRGFLPENYT 336
Cdd:cd11875    3 RVLFDYEAENEDELTLREGDIVTIlSKDCED---KGWWKG--ELNGKRGVFPDNFV 53
SH3_Nbp2-like cd11865
Src Homology 3 domain of Saccharomyces cerevisiae Nap1-binding protein 2 and similar fungal ...
 283-335 2.55e-04

Src Homology 3 domain of Saccharomyces cerevisiae Nap1-binding protein 2 and similar fungal proteins; This subfamily includes Saccharomyces cerevisiae Nbp2 (Nucleosome assembly protein 1 (Nap1)-binding protein 2), Schizosaccharomyces pombe Skb5, and similar proteins. Nbp2 interacts with Nap1, which is essential for maintaining proper nucleosome structures in transcription and replication. It is also the binding partner of the yeast type II protein phosphatase Ptc1p and serves as a scaffolding protein that brings seven kinases in close contact to Ptc1p. Nbp2 plays a role many cell processes including organelle inheritance, mating hormone response, cell wall stress, mitotic cell growth at elevated temperatures, and high osmolarity. Skb5 interacts with the p21-activated kinase (PAK) homolog Shk1, which is critical for fission yeast cell viability. Skb5 activates Shk1 and plays a role in regulating cell morphology and growth under hypertonic conditions. Nbp2 and Skb5 contain an 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: 212799  Cd Length: 55  Bit Score: 39.42  E-value: 2.55e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119629966 283 ALFQYKPQNVDELTLSPGDYIFVdptqQDEASEGWVIGISQRTGCRGFLPENY 335
Cdd:cd11865    4 ALYDFEPEHDNELGFAEGQILFI----LYKHGQGWLIAEDESGGKTGLVPEEF 52
SH3_Abi cd11826
Src homology 3 domain of Abl Interactor proteins; Abl interactor (Abi) proteins are adaptor ...
 282-335 3.02e-04

Src homology 3 domain of Abl Interactor proteins; Abl interactor (Abi) proteins are adaptor proteins serving as binding partners and substrates of Abl tyrosine kinases. They are involved in regulating actin cytoskeletal reorganization and play important roles in membrane-ruffling, endocytosis, cell motility, and cell migration. They localize to sites of actin polymerization in epithelial adherens junction and immune synapses, as well as to the leading edge of lamellipodia. Vertebrates contain two Abi proteins, Abi1 and Abi2. Abi1 displays a wide expression pattern while Abi2 is highly expressed in the eye and brain. Abi proteins contain a homeobox homology domain, a proline-rich region, and a SH3 domain. The SH3 domain of Abi binds to a PxxP motif in Abl. 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: 212760 [Multi-domain]  Cd Length: 52  Bit Score: 38.84  E-value: 3.02e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119629966 282 RALFQYKPQNVDELTLSPGDYIFVDPTQQDeaseGWVIGISQrtGCRGFLPENY 335
Cdd:cd11826    3 VALYDYTADKDDELSFQEGDIIYVTKKNDD----GWYEGVLN--GVTGLFPGNY 50
SH3_SH3RF1_3 cd11926
Third Src Homology 3 domain of SH3 domain containing ring finger 1, an E3 ubiquitin-protein ...
 283-335 3.55e-04

Third Src Homology 3 domain of SH3 domain containing ring finger 1, an E3 ubiquitin-protein ligase; SH3RF1 is also called POSH (Plenty of SH3s) or SH3MD2 (SH3 multiple domains protein 2). It is a scaffold protein that acts as an E3 ubiquitin-protein ligase. It plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and JNK mediated apoptosis. SH3RF1 also enhances the ubiquitination of ROMK1 potassium channel resulting in its increased endocytosis. It contains an N-terminal RING finger domain and four SH3 domains. This model represents the third SH3 domain, located in the middle, of SH3RF1. 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: 212859 [Multi-domain]  Cd Length: 55  Bit Score: 38.80  E-value: 3.55e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119629966 283 ALFQYKPQNVDELTLSPGDYIFVDPTQQDeaseGWVIGISQRTGCRGFLPENY 335
Cdd:cd11926    4 AIYPYTPRKEDELELRKGEMFLVFERCQD----GWFKGTSMHTSKIGVFPGNY 52
UBA_AAA_plant cd14389
UBA domain found in plant AAA-type ATPase-like proteins; This family includes some ...
 25-60 3.76e-04

UBA domain found in plant AAA-type ATPase-like proteins; This family includes some uncharacterized AAA-type ATPase-like proteins found in plant. The AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. Members in this family contains an N-terminal ubiquitin-association (UBA) domain, a AAA-type ATPase domain and a C-terminal MgsA AAA+ ATPase domain. This model corresponds to the UBA domain which show a high level of sequence similarity with mammalian ubiquitin-associated and SH3 domain-containing protein A (UBS3A).


Pssm-ID: 270572  Cd Length: 37  Bit Score: 38.49  E-value: 3.76e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 119629966  25 LEPLLAMGFPVHTALKALAATGRKTAEEALAWLHDH 60
Cdd:cd14389    1 MEQLVDMGFSSDLAAEALAATGGKSTQKATEWILSH 36
SH3_Amphiphysin_I cd12140
Src Homology 3 domain of Amphiphysin I; Amphiphysins function primarily in endocytosis and ...
 284-338 5.66e-04

Src Homology 3 domain of Amphiphysin I; Amphiphysins function primarily in endocytosis and other membrane remodeling events. They exist in several isoforms and mammals possess two amphiphysin proteins from distinct genes. Amphiphysin I proteins, enriched in the brain and nervous system, contain domains that bind clathrin, Adaptor Protein complex 2 (AP2), dynamin, and synaptojanin. They function in synaptic vesicle endocytosis. Human autoantibodies to amphiphysin I hinder GABAergic signaling and contribute to the pathogenesis of paraneoplastic stiff-person syndrome. Amphiphysins contain an N-terminal BAR domain with an additional N-terminal amphipathic helix (an N-BAR), a variable central domain, and a C-terminal SH3 domain. The SH3 domain of amphiphysins bind proline-rich motifs present in binding partners such as dynamin, synaptojanin, and nsP3. It also belongs to a subset of SH3 domains that bind ubiquitin in a site that overlaps with the peptide binding site. 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: 213016  Cd Length: 72  Bit Score: 38.72  E-value: 5.66e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119629966 284 LFQYKPQNVDELTLSPGDYIFVDPTQQDEASE-GWVIGISQR--------TGCRGFLPENYTDR 338
Cdd:cd12140    8 LHDFEAANSDELELKRGDIVLVVPSETAADQDaGWLTGVKESdwlqyrdaSAYKGLFPENFTRR 71
PRK06193 PRK06193
hypothetical protein; Provisional
 370-502 5.82e-04

hypothetical protein; Provisional


Pssm-ID: 235734  Cd Length: 206  Bit Score: 41.60  E-value: 5.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966 370 RCSGEFLPQTARSLSSLQALQATvarKSVLVVRHGERVDqifgkawlqqcSTPDgkYYRPDLNfPCSLPRRsrgikdfen 449
Cdd:PRK06193  20 GSGEEAASDEADDKTLLESLQKG---GYVIYFRHAATDR-----------SQAD--QDTSDMD-DCSTQRN--------- 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119629966 450 dppLSSCGIFQSRIAGDALLDSGIRISSVFASPALRCVQTAKLILEELKLEKK 502
Cdd:PRK06193  74 ---LSEEGREQARAIGEAFRALAIPVGKVISSPYCRAWETAQLAFGRHEKEIR 123
SH3_CIN85_2 cd12055
Second Src Homology 3 domain (SH3B) of Cbl-interacting protein of 85 kDa; CIN85, also called ...
 282-336 5.88e-04

Second Src Homology 3 domain (SH3B) of Cbl-interacting protein of 85 kDa; CIN85, also called SH3 domain-containing kinase-binding protein 1 (SH3KBP1) or CD2-binding protein 3 (CD2BP3) or Ruk, is an adaptor protein that is involved in the downregulation of receptor tyrosine kinases by facilitating endocytosis through interaction with endophilin-associated ubiquitin ligase Cbl proteins. It is also important in many other cellular processes including vesicle-mediated transport, cytoskeletal remodelling, apoptosis, cell adhesion and migration, and viral infection, among others. CIN85 exists as multiple variants from alternative splicing; the main variant contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the second SH3 domain (SH3B) of CIN85. SH3B has been shown to bind Cbl proline-rich peptides and ubiquitin. 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: 212988 [Multi-domain]  Cd Length: 53  Bit Score: 38.05  E-value: 5.88e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119629966 282 RALFQYKPQNVDELTLSPGDYIFVdptqQDEASEGWVIGIsqRTGCRGFLPENYT 336
Cdd:cd12055    3 QVAFSYLPQNEDELELKVGDIIEV----VGEVEEGWWEGV--LNGKTGMFPSNFI 51
SH3_PACSIN1-2 cd11998
Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1) ...
 281-337 6.80e-04

Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1) and PACSIN 2; PACSIN 1 or Syndapin I (Synaptic dynamin-associated protein I) is expressed specifically in the brain and is localized in neurites and synaptic boutons. It binds the brain-specific proteins dynamin I, synaptojanin, synapsin I, and neural Wiskott-Aldrich syndrome protein (nWASP), and functions as a link between the cytoskeletal machinery and synaptic vesicle endocytosis. PACSIN 1 interacts with huntingtin and may be implicated in the neuropathology of Huntington's disease. PACSIN 2 or Syndapin II is expressed ubiquitously and is involved in the regulation of tubulin polymerization. It associates with Golgi membranes and forms a complex with dynamin II which is crucial in promoting vesicle formation from the trans-Golgi network. PACSINs act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSINs contain an N-terminal F-BAR domain 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: 212931 [Multi-domain]  Cd Length: 56  Bit Score: 38.01  E-value: 6.80e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119629966 281 LRALFQYKPQNVDELTLSPGDYIfvdPTQQDEASEGWVIGiSQRTGCRGFLPENYTD 337
Cdd:cd11998    3 VRALYDYDGQEQDELSFKAGDEL---TKLEDEDEQGWCKG-RLDSGQVGLYPANYVE 55
SH3_Stac_1 cd11833
First C-terminal Src homology 3 domain of SH3 and cysteine-rich domain-containing (Stac) ...
 283-338 7.31e-04

First C-terminal Src homology 3 domain of SH3 and cysteine-rich domain-containing (Stac) proteins; Stac proteins are putative adaptor proteins that contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. There are three mammalian members (Stac1, Stac2, and Stac3) of this family. Stac1 and Stac3 contain two SH3 domains while Stac2 contains a single SH3 domain at the C-terminus. This model represents the first C-terminal SH3 domain of Stac1 and Stac3, and the single C-terminal SH3 domain of Stac2. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. 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: 212767 [Multi-domain]  Cd Length: 53  Bit Score: 37.87  E-value: 7.31e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119629966 283 ALFQYKPQNVDELTLSPGDYIFVdptqQDEASEGWVIG-ISQRTgcrGFLPENYTDR 338
Cdd:cd11833    4 ALYKFKPQENEDLEMRPGDKITL----LDDSNEDWWKGkIEDRV---GFFPANFVQR 53
SH3_PACSIN cd11843
Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) ...
 282-335 8.21e-04

Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins; PACSINs, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. They bind both dynamin and Wiskott-Aldrich syndrome protein (WASP), and may provide direct links between the actin cytoskeletal machinery through WASP and dynamin-dependent endocytosis. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSINs contain an N-terminal F-BAR domain 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: 212777 [Multi-domain]  Cd Length: 53  Bit Score: 37.78  E-value: 8.21e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119629966 282 RALFQYKPQNVDELTLSPGDyIFVDPTQQDEasEGWVIGisQRTGCRGFLPENY 335
Cdd:cd11843    3 RALYDYEGQESDELSFKAGD-ILTKLEEEDE--QGWCKG--RLDGRVGLYPANY 51
SH3_CIN85_3 cd12057
Third Src Homology 3 domain (SH3C) of Cbl-interacting protein of 85 kDa; CIN85, also called ...
 282-335 8.75e-04

Third Src Homology 3 domain (SH3C) of Cbl-interacting protein of 85 kDa; CIN85, also called SH3 domain-containing kinase-binding protein 1 (SH3KBP1) or CD2-binding protein 3 (CD2BP3) or Ruk, is an adaptor protein that is involved in the downregulation of receptor tyrosine kinases by facilitating endocytosis through interaction with endophilin-associated ubiquitin ligase Cbl proteins. It is also important in many other cellular processes including vesicle-mediated transport, cytoskeletal remodelling, apoptosis, cell adhesion and migration, and viral infection, among others. CIN85 exists as multiple variants from alternative splicing; the main variant contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the third SH3 domain (SH3C) of CIN85. SH3C has been shown to bind ubiquitin. 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: 212990 [Multi-domain]  Cd Length: 56  Bit Score: 37.96  E-value: 8.75e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119629966 282 RALFQYKPQNVDELTLSPGDYIFVdpTQQDEASEGWVIGisQRTGCRGFLPENY 335
Cdd:cd12057    3 KVLFPYEAQNEDELTIKEGDIVTL--ISKDCIDAGWWEG--ELNGRRGVFPDNF 52
SH3_PI3K_p85beta cd11909
Src Homology 3 domain of the p85beta regulatory subunit of Class IA Phosphatidylinositol ...
 282-337 9.03e-04

Src Homology 3 domain of the p85beta regulatory subunit of Class IA Phosphatidylinositol 3-kinases; Class I PI3Ks convert PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. They are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. Class IA PI3Ks associate with the p85 regulatory subunit family, which contains SH3, RhoGAP, and SH2 domains. The p85 subunits recruit the PI3K p110 catalytic subunit to the membrane, where p110 phosphorylates inositol lipids. Vertebrates harbor two p85 isoforms, called alpha and beta. In addition to regulating the p110 subunit, p85beta binds CD28 and may be involved in the activation and differentiation of antigen-stimulated T cells. 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: 212842  Cd Length: 74  Bit Score: 38.27  E-value: 9.03e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119629966 282 RALFQYKPQNVDELTLSPGDYIFVDPT-----------QQDEASEGWVIGISQRTGCRGFLPENYTD 337
Cdd:cd11909    4 RALYPYRKEREEDIDLLPGDVLTVSRAalqalgvkeggEQCPQSIGWILGLNERTKQRGDFPGTYVE 70
SH3_BOI cd11886
Src Homology 3 domain of fungal BOI-like proteins; This subfamily includes the Saccharomyces ...
 280-335 1.07e-03

Src Homology 3 domain of fungal BOI-like proteins; This subfamily includes the Saccharomyces cerevisiae proteins BOI1 and BOI2, and similar proteins. They contain an N-terminal SH3 domain, a Sterile alpha motif (SAM), and a Pleckstrin homology (PH) domain at the C-terminus. BOI1 and BOI2 interact with the SH3 domain of Bem1p, a protein involved in bud formation. They promote polarized cell growth and participates in the NoCut signaling pathway, which is involved in the control of cytokinesis. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212819  Cd Length: 55  Bit Score: 37.70  E-value: 1.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119629966 280 TLRALFQYKPQNVDELTLSPGDYIFVdPTQQDEASEGWVIGISQRTGCRGFLPENY 335
Cdd:cd11886    1 LLIVIHDFNARSEDELTLKPGDKIEL-IEDDEEFGDGWYLGRNLRTGETGLFPVVF 55
SH3_Src_like cd11845
Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members ...
 280-335 1.09e-03

Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, Yes, and Brk. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). However, Brk lacks the N-terminal myristoylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells, and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, Lyn, and Brk show a limited expression pattern. This subfamily also includes Drosophila Src42A, Src oncogene at 42A (also known as Dsrc41) which accumulates at sites of cell-cell or cell-matrix adhesion, and participates in Drosphila development and wound healing. It has been shown to promote tube elongation in the tracheal system, is essential for proper cell-cell matching during dorsal closure, and regulates cell-cell contacts in developing Drosophila eyes. The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. 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: 212779 [Multi-domain]  Cd Length: 52  Bit Score: 37.56  E-value: 1.09e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119629966 280 TLRALFQYKPQNVDELTLSPGDYIFV-DPTQQDeasegWVIGISQRTGCRGFLPENY 335
Cdd:cd11845    1 IYVALYDYEARTDDDLSFKKGDRLQIlDDSDGD-----WWLARHLSTGKEGYIPSNY 52
PTZ00123 PTZ00123
phosphoglycerate mutase like-protein; Provisional
 450-497 1.21e-03

phosphoglycerate mutase like-protein; Provisional


Pssm-ID: 240280  Cd Length: 236  Bit Score: 41.18  E-value: 1.21e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 119629966 450 DPPLSSCGIFQSRIAGDALLDSGIRISSVFASPALRCVQTAKLILEEL 497
Cdd:PTZ00123  12 DVPLSEKGVQEAREAGKLLKEKGFRFDVVYTSVLKRAIKTAWIVLEEL 59
SH3_Abp1_eu cd11960
Src homology 3 domain of eumetazoan Actin-binding protein 1; Abp1, also called drebrin-like ...
 280-335 1.30e-03

Src homology 3 domain of eumetazoan Actin-binding protein 1; Abp1, also called drebrin-like protein, is an adaptor protein that functions in receptor-mediated endocytosis and vesicle trafficking. It contains an N-terminal actin-binding module, the actin-depolymerizing factor (ADF) homology domain, a helical domain, and a C-terminal SH3 domain. Mammalian Abp1, unlike yeast Abp1, does not contain an acidic domain that interacts with the Arp2/3 complex. It regulates actin dynamics indirectly by interacting with dynamin and WASP family proteins. Abp1 deficiency causes abnormal organ structure and function of the spleen, heart, and lung of mice. 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: 212893 [Multi-domain]  Cd Length: 54  Bit Score: 37.38  E-value: 1.30e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119629966 280 TLRALFQYKPQNVDELTLSPGDYIfvdpTQQDEASEGWVIGISQrTGCRGFLPENY 335
Cdd:cd11960    1 RARALYDYQAADDTEISFDPGDII----TDIEQIDEGWWRGTGP-DGTYGLFPANY 51
SH3_CIN85_1 cd12052
First Src Homology 3 domain (SH3A) of Cbl-interacting protein of 85 kDa; CIN85, also called ...
 285-335 1.55e-03

First Src Homology 3 domain (SH3A) of Cbl-interacting protein of 85 kDa; CIN85, also called SH3 domain-containing kinase-binding protein 1 (SH3KBP1) or CD2-binding protein 3 (CD2BP3) or Ruk, is an adaptor protein that is involved in the downregulation of receptor tyrosine kinases by facilitating endocytosis through interaction with endophilin-associated ubiquitin ligase Cbl proteins. It is also important in many other cellular processes including vesicle-mediated transport, cytoskeletal remodelling, apoptosis, cell adhesion and migration, and viral infection, among others. CIN85 exists as multiple variants from alternative splicing; the main variant contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the first SH3 domain (SH3A) of CIN85; SH3A binds to internal proline-rich motifs within the proline-rich region. This intramolecular interaction serves as a regulatory mechanism to keep CIN85 in a closed conformation, preventing the recruitment of other proteins. SH3A has also been shown to bind ubiquitin and to an atypical PXXXPR motif at the C-terminus of Cbl and the cytoplasmic end of the cell adhesion protein CD2. 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: 212985 [Multi-domain]  Cd Length: 53  Bit Score: 37.18  E-value: 1.55e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119629966 285 FQYKPQNVDELTLSPGDyIFVDPTQQDeasEGWVIGisQRTGCRGFLPENY 335
Cdd:cd12052    6 FDYKAQHEDELTITVGD-IITKIKKDD---GGWWEG--EIKGRRGLFPDNF 50
SH3_Sdc25 cd11883
Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors; This subfamily is ...
 280-335 1.93e-03

Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors; This subfamily is composed of the Saccharomyces cerevisiae guanine nucleotide exchange factors (GEFs) Sdc25 and Cdc25, and similar proteins. These GEFs regulate Ras by stimulating the GDP/GTP exchange on Ras. Cdc25 is involved in the Ras/PKA pathway that plays an important role in the regulation of metabolism, stress responses, and proliferation, depending on available nutrients and conditions. Proteins in this subfamily contain an N-terminal SH3 domain as well as REM (Ras exchanger motif) and RasGEF domains at the C-terminus. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212816  Cd Length: 55  Bit Score: 36.88  E-value: 1.93e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119629966 280 TLRALFQYKPQNVDELTLSPGDYIFV---DPTqqdeaseGW---VIGISQRTGCRGFLPENY 335
Cdd:cd11883    1 VVVALYDFTPKSKNQLSFKAGDIIYVlnkDPS-------GWwdgVIISSSGKVKRGWFPSNY 55
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 282-332 1.98e-03

SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 394975 [Multi-domain]  Cd Length: 47  Bit Score: 36.41  E-value: 1.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 119629966  282 RALFQYKPQNVDELTLSPGDYIFVdpTQQDEasEGWVIGISqRTGCRGFLP 332
Cdd:pfam00018   1 VALYDYTAQEPDELSFKKGDIIIV--LEKSE--DGWWKGRN-KGGKEGLIP 46
UBA_VP13D cd14306
UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar ...
 25-61 2.08e-03

UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar proteins; VP13D is a chorea-acanthocytosis (CHAC)-similar protein encoded by gene VPS13D. it contains two putative domains, ubiquitin-associated (UBA) domain and lectin domain of ricin B chain profile (ricin-B-lectin), suggesting it may interact with, and be involved in the trafficking of, proteins modified with ubiquitin and/or carbohydrate molecules. Further investigation is required.


Pssm-ID: 270491  Cd Length: 36  Bit Score: 36.27  E-value: 2.08e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 119629966  25 LEPLLAMGFPVHTALKALAATGRKtAEEALAWLHDHC 61
Cdd:cd14306    1 VAKLMELGFPEEDCIRALRACGGN-VEEAANWLLENA 36
SH3_GRAP_N cd11948
N-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor ...
 283-337 2.43e-03

N-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor protein that is highly expressed in lymphoid tissues. It acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. It has been identified as a regulator of TGFbeta signaling in diabetic kidney tubules and may have a role in the pathogenesis of the disease. GRAP 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: 212881 [Multi-domain]  Cd Length: 54  Bit Score: 36.33  E-value: 2.43e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119629966 283 ALFQYKPQNVDELTLSPGDYIFVDPTQQDEaseGWVIgiSQRTGCRGFLPENYTD 337
Cdd:cd11948    4 ALYSFQATESDELPFQKGDILKILNMEDDQ---NWYK--AELQGREGYIPKNYIK 53
ThpR COG1514
RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA ligase) [Translation, ribosomal structure and ...
 76-166 2.80e-03

RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA ligase) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441123 [Multi-domain]  Cd Length: 181  Bit Score: 39.24  E-value: 2.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629966  76 LFLC--PTGPLLEKLQEFWRESKRQCAKNRAHEVFPHVTLCDFFTCEDQKVECLYEALKRAGDRL---------LGSFPT 144
Cdd:COG1514    3 LFIAlpPPEELREALAALRARLKAAPGGRWVRPENLHLTLAFLGEVDEERLEALAEALARAAAGAppfelrldgLGAFPR 82

                         90       100
                 ....*....|....*....|..
gi 119629966 145 AVPLALhssisYLGffVSGSPA 166
Cdd:COG1514   83 PRPRVL-----WLG--VEPSPE 97
SH3_MLK1-3 cd12059
Src Homology 3 domain of Mixed Lineage Kinases 1, 2, and 3; MLKs 1, 2, and 3 are Serine ...
 283-335 2.92e-03

Src Homology 3 domain of Mixed Lineage Kinases 1, 2, and 3; MLKs 1, 2, and 3 are Serine/Threonine Kinases (STKs), catalyzing the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. Little is known about the specific function of MLK1, also called MAP3K9. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. MLK2, also called MAP3K10, is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK3, also called MAP3K11, is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. It also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and thus, impacts inflammation and immunity. MLKs contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. 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: 212992 [Multi-domain]  Cd Length: 58  Bit Score: 36.28  E-value: 2.92e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119629966 283 ALFQYKPQNVDELTLSPGDYIFVdpTQQDEA---SEGWVIG-ISQRTgcrGFLPENY 335
Cdd:cd12059    4 AVFDYEASAEDELTLRRGDRVEV--LSKDSAvsgDEGWWTGkINDRV---GIFPSNY 55
SH3_Endophilin_A cd11803
Src homology 3 domain of Endophilin-A; Endophilins play roles in synaptic vesicle formation, ...
 282-337 2.99e-03

Src homology 3 domain of Endophilin-A; Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. They are classified into two types, A and B. Vertebrates contain three endophilin-A isoforms (A1, A2, and A3). Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. They tubulate membranes and regulate calcium influx into neurons to trigger the activation of the endocytic machinery. They are also involved in the sorting of plasma membrane proteins, actin filament assembly, and the uncoating of clathrin-coated vesicles for fusion with endosomes. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, 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: 212737 [Multi-domain]  Cd Length: 55  Bit Score: 36.08  E-value: 2.99e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119629966 282 RALFQYKPQNVDELTLSPGDYIfvdpTQQDEASEGWVIGISQrtGCRGFLPENYTD 337
Cdd:cd11803    4 RALYDFEPENEGELGFKEGDII----TLTNQIDENWYEGMVN--GQSGFFPVNYVE 53
SH3_Intersectin_5 cd11840
Fifth Src homology 3 domain (or SH3E) of Intersectin; Intersectins (ITSNs) are adaptor ...
 282-335 4.23e-03

Fifth Src homology 3 domain (or SH3E) of Intersectin; Intersectins (ITSNs) are adaptor proteins that function in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. They are essential for initiating clathrin-coated pit formation. They bind to many proteins through their multidomain structure and facilitate the assembly of multimeric complexes. Vertebrates contain two ITSN proteins, ITSN1 and ITSN2, which exist in alternatively spliced short and long isoforms. The short isoforms contain two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoforms, in addition, contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. ITSN1 and ITSN2 are both widely expressed, with variations depending on tissue type and stage of development. The fifth SH3 domain (or SH3E) of ITSN1 has been shown to bind many protein partners including SGIP1, Sos1, dynamin1/2, CIN85, c-Cbl, SHIP2, N-WASP, and synaptojanin-1, among others. 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: 212774 [Multi-domain]  Cd Length: 53  Bit Score: 35.85  E-value: 4.23e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119629966 282 RALFQYKPQNVDELTLSPGDYIFVdpTQQDEASegWVIGisQRTGCRGFLPENY 335
Cdd:cd11840    3 IALFPYTAQNEDELSFQKGDIINV--LSKDDPD--WWRG--ELNGQTGLFPSNY 50
SH3_Eve1_5 cd11818
Fifth Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 ...
 282-335 4.79e-03

Fifth Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 domain-containing protein 19 (SH3D19) or EEN-binding protein (EBP), exists in multiple alternatively spliced isoforms. The longest isoform contains five SH3 domain in the C-terminal region and seven proline-rich motifs in the N-terminal region. It is abundantly expressed in skeletal muscle and heart, and may be involved in regulating the activity of ADAMs (A disintegrin and metalloproteases). Eve-1 interacts with EEN, an endophilin involved in endocytosis and may be the target of the MLL-EEN fusion protein that is implicated in leukemogenesis. 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: 212752 [Multi-domain]  Cd Length: 50  Bit Score: 35.54  E-value: 4.79e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119629966 282 RALFQYKPQNVDELTLSPGDYIfvdpTQQDEASEGWVIGisQRTGCRGFLPENY 335
Cdd:cd11818    3 RALYDFTGENEDELSFKAGDII----TELESIDEEWMSG--ELRGKSGIFPKNF 50
UBA_LATS cd14322
UBA domain found in serine/threonine-protein kinase LATS and similar proteins; The LATS ...
 22-57 4.86e-03

UBA domain found in serine/threonine-protein kinase LATS and similar proteins; The LATS proteins family consists of two isoforms, LATS1 and LATS2, both of which are mammalian homologs of the Drosophila tumor suppressor gene lats/warts. LATS1, also called large tumor suppressor homolog 1, or WARTS protein kinase (warts), is a serine/threonine-protein kinase that highly conserved from fly to human. LATS2, also called kinase phosphorylated during mitosis protein, or large tumor suppressor homolog 2, or serine/threonine-protein kinase KPM, or Warts-like kinase, inhibits the G1/S transition and is essential for embryonic development, proliferation control and genomic integrity. LATS proteins contain an N-terminal ubiquitin-associated (UBA) domain and a C-terminal protein kinase domain.


Pssm-ID: 270507  Cd Length: 39  Bit Score: 35.14  E-value: 4.86e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 119629966  22 PSLLEPLLAMGFPVHTALKALAATGRKTAEEALAWL 57
Cdd:cd14322    1 NQMLQQLVAAGYSEEISMRALKKSGARTIEAAIEFI 36
SH3_ASPP cd11807
Src homology 3 domain of Apoptosis Stimulating of p53 proteins (ASPP); The ASPP family of ...
 283-335 5.13e-03

Src homology 3 domain of Apoptosis Stimulating of p53 proteins (ASPP); The ASPP family of proteins bind to important regulators of apoptosis (p53, Bcl-2, and RelA) and cell growth (APCL, PP1). They share similarity at their C-termini, where they harbor a proline-rich region, four ankyrin (ANK) repeats, and an SH3 domain. Vertebrates contain three members of the family: ASPP1, ASPP2, and iASPP. ASPP1 and ASPP2 activate the apoptotic function of the p53 family of tumor suppressors (p53, p63, and p73), while iASPP is an oncoprotein that specifically inhibits p53-induced apoptosis. The expression of ASPP proteins is altered in tumors; ASPP1 and ASPP2 are downregulated whereas iASPP is upregulated is some cancer types. ASPP proteins also bind and regulate protein phosphatase 1 (PP1), and this binding is competitive with p53 binding. The SH3 domain and the ANK repeats of ASPP contribute to the p53 binding site; they bind to the DNA binding domain of p53. 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: 212741 [Multi-domain]  Cd Length: 57  Bit Score: 35.82  E-value: 5.13e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119629966 283 ALFQYKPQNVDELTLSPGDYIFVDPTQQDEASEGWVIGISQRtgcRGFLPENY 335
Cdd:cd11807    5 ALFDYEAENGDELSFREGDELTVLRKGDDDETEWWWARLNDK---EGYVPRNL 54
PRK01295 PRK01295
phosphoglyceromutase; Provisional
 450-497 5.45e-03

phosphoglyceromutase; Provisional


Pssm-ID: 167205 [Multi-domain]  Cd Length: 206  Bit Score: 38.90  E-value: 5.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 119629966 450 DPPLSSCGIFQSRIAGDALLDSGIRISSVFASPALRCVQTAKLILEEL 497
Cdd:PRK01295  26 DPDLTEQGVAEAKAAGRKLKAAGLKFDIAFTSALSRAQHTCQLILEEL 73
SH3_CD2AP_3 cd12056
Third Src Homology 3 domain (SH3C) of CD2-associated protein; CD2AP, also called CMS (Cas ...
 282-335 6.08e-03

Third Src Homology 3 domain (SH3C) of CD2-associated protein; CD2AP, also called CMS (Cas ligand with Multiple SH3 domains) or METS1 (Mesenchyme-to-Epithelium Transition protein with SH3 domains), is a cytosolic adaptor protein that plays a role in regulating the cytoskeleton. It is critical in cell-to-cell union necessary for kidney function. It also stabilizes the contact between a T cell and antigen-presenting cells. It is primarily expressed in podocytes at the cytoplasmic face of the slit diaphragm and serves as a linker anchoring podocin and nephrin to the actin cytoskeleton. CD2AP contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the third SH3 domain (SH3C) of CD2AP. SH3C has been shown to bind ubiquitin. 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: 212989 [Multi-domain]  Cd Length: 57  Bit Score: 35.57  E-value: 6.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119629966 282 RALFQYKPQNVDELTLSPGDYIFVdpTQQDEASEGWVIGisQRTGCRGFLPENY 335
Cdd:cd12056    5 KALFHYEGTNEDELDFKEGEIILI--ISKDTGEPGWWKG--ELNGKEGVFPDNF 54
SH3_Nck_2 cd11766
Second Src Homology 3 domain of Nck adaptor proteins; Nck adaptor proteins regulate actin ...
 282-338 6.82e-03

Second Src Homology 3 domain of Nck adaptor proteins; Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2 (also called Nckbeta or Growth factor receptor-bound protein 4, Grb4), which show partly overlapping functions but also bind distinct targets. Their SH3 domains are involved in recruiting downstream effector molecules, such as the N-WASP/Arp2/3 complex, which when activated induces actin polymerization that results in the production of pedestals, or protrusions of the plasma membrane. The second SH3 domain of Nck appears to prefer ligands containing the APxxPxR motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. 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: 212700 [Multi-domain]  Cd Length: 53  Bit Score: 35.32  E-value: 6.82e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119629966 282 RALFQYKPQNVDELTLSPGDYIFVdptqQDEASEGWVIGISQrtGCRGFLPENYTDR 338
Cdd:cd11766    3 VVKFNYEAQREDELSLRKGDRVLV----LEKSSDGWWRGECN--GQVGWFPSNYVTE 53
 
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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