NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|688560287|ref|XP_009300666|]
View 

disks large homolog 1 isoform X6 [Danio rerio]

Protein Classification

SH3_DLG-like and GMPK domain-containing protein( domain architecture ID 12098790)

protein containing domains MAGUK_N_PEST, PDZ_assoc, SH3_DLG-like, and GMPK

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Guanylate_kin pfam00625
Guanylate kinase;
708-886 8.78e-73

Guanylate kinase;


:

Pssm-ID: 395500  Cd Length: 182  Bit Score: 236.89  E-value: 8.78e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287  708 YSRPVIILGPM---KDRINDDLISEFPDKFGSCVPHTTRPKRDYEVDGRDYHFVnSREQMEKDIQDHKFIEAGQYNNHLY 784
Cdd:pfam00625   1 SRRPVVLSGPSgvgKSHIKKALLSEYPDKFGYSVPHTTRPPRKGEVDGKDYYFV-SKEEMERDISANEFLEYAQFSGNMY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287  785 GTSVQSVREVAEKGKHCILDVSGNAIKRLQLAQLYPIAVFIKPKSVENILEMNKRLMEEQGRKTYDRAMKLEQEFLE-HF 863
Cdd:pfam00625  80 GTSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQRRLKGRGKEQEEKINKRMAAAEQEFQHyEF 159
                         170       180
                  ....*....|....*....|...
gi 688560287  864 TAIVQGDTLEEIYNQVKQIIEEQ 886
Cdd:pfam00625 160 DVIIVNDDLEEAYKKLKEALEAE 182
MAGUK_N_PEST pfam10608
Polyubiquitination (PEST) N-terminal domain of MAGUK; The residues upstream of this domain are ...
110-194 4.86e-39

Polyubiquitination (PEST) N-terminal domain of MAGUK; The residues upstream of this domain are the probable palmitoylation sites, particularly two cysteines. The domain has a putative PEST site at the very start that seems to be responsible for poly-ubiquitination. PEST domains are polypeptide sequences enriched in proline (P), glutamic acid (E), serine (S) and threonine (T) that target proteins for rapid destruction. The whole domain, in conjunction with a C-terminal domain of the longer protein, is necessary for dimerization of the whole protein.


:

Pssm-ID: 431391 [Multi-domain]  Cd Length: 85  Bit Score: 139.52  E-value: 4.86e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287  110 KYRYQDEDTtSPPEHSSPHIPGDARPPELVQVSEKNISQIENVHGYVSHSHISPMK-ASPAPVVVNTESLDSSPYVNGTE 188
Cdd:pfam10608   1 KYRYQDEDT-PPQEPSPPHLAGSRGGPELVHVSEKNLSQIENVHGYVPHTHISPMKpANPPPIIVNTDTLDTPPYVNGTE 79

                  ....*.
gi 688560287  189 ADYEYE 194
Cdd:pfam10608  80 GEYEYE 85
SH3_DLG-like cd11861
Src Homology 3 domain of Disks large homolog proteins; The DLG-like proteins are scaffolding ...
558-618 6.23e-37

Src Homology 3 domain of Disks large homolog proteins; The DLG-like proteins are scaffolding proteins that cluster at synapses and are also called PSD (postsynaptic density)-95 proteins or SAPs (synapse-associated proteins). They play important roles in synaptic development and plasticity, cell polarity, migration and proliferation. They are members of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. DLG-like proteins contain three PDZ domains and varying N-terminal regions. All DLG proteins exist as alternatively-spliced isoforms. Vertebrates contain four DLG proteins from different genes, called DLG1-4. DLG4 and DLG2 are found predominantly at postsynaptic sites and they mediate surface ion channel and receptor clustering. DLG3 is found axons and some presynaptic terminals. DLG1 interacts with AMPA-type glutamate receptors and is critical in their maturation and delivery to synapses. The SH3 domain of DLG4 binds and clusters the kainate subgroup of glutamate receptors via two proline-rich sequences in their C-terminal tail. It also binds AKAP79/150 (A-kinase anchoring protein). 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: 212795  Cd Length: 61  Bit Score: 132.45  E-value: 6.23e-37
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688560287 558 YVRALFDYDITKDSGLPSQGLNFRFGDILHVLNASDEEWWQARHVTTDGEMEEMGVIPSKK 618
Cdd:cd11861    1 YVRALFDYDPSRDSGLPSQGLSFKFGDILHVTNASDDEWWQARRVTPNGEEEEVGVIPSKR 61
PDZ_assoc pfam10600
PDZ-associated domain of NMDA receptors; This domain is found in higher eukaryotes between the ...
375-438 9.79e-37

PDZ-associated domain of NMDA receptors; This domain is found in higher eukaryotes between the second and third PDZ domains, pfam00595, of glutamate receptor like proteins. Its exact function is not known.


:

Pssm-ID: 431385  Cd Length: 67  Bit Score: 132.17  E-value: 9.79e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688560287  375 KPTSVFMNDSYAPPDVTSSYSQHMENHISTQSYLSQ---PLTPATPSRYSPVSKGMLGDDEITREPR 438
Cdd:pfam10600   1 KPTSVYLNDSYAPPDITSSYSQHMDNHISHPSYLGGdesVPPPTSPRRYSPVPKHMLGEDDITREPR 67
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
436-520 1.43e-23

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


:

Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 95.14  E-value: 1.43e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287   436 EPRKIVLHRGTTGLGFNIVGGED-GEGIFISFILAGGPADLCGeLRKGDRIVSVNGVDLRSATHEQAAAALKNAGQTVTI 514
Cdd:smart00228   1 EPRLVELEKGGGGLGFSLVGGKDeGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTL 79

                   ....*.
gi 688560287   515 IAQYRP 520
Cdd:smart00228  80 TVLRGG 85
L27_1 pfam09058
L27_1; The L27 domain is a protein interaction module that exists in a large family of ...
7-64 4.41e-22

L27_1; The L27 domain is a protein interaction module that exists in a large family of scaffold proteins, functioning as an organisation centre of large protein assemblies required for the establishment and maintenance of cell polarity. L27 domains form specific heterotetrameric complexes, in which each domain contains three alpha-helices.


:

Pssm-ID: 430389  Cd Length: 59  Bit Score: 90.06  E-value: 4.41e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 688560287    7 DAQRALQLLEEYQTKLSQTGDPHLRLSIERVINIFKSTLFQALVDIQEYYEVSLQDTE 64
Cdd:pfam09058   2 DTERALELLEEYHATLSRPDDEELRRAIERLIIIFKSNLFQALLDIQEFYELTLLSNR 59
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
195-279 2.35e-21

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


:

Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 88.78  E-value: 2.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287 195 EITLERG-NSGLGFSIAGGTDnphigEDPSIFITKIIPGGAAAQdGRLRVNDCILRVNDVDVRDVTHSNAVEALKEAGCI 273
Cdd:cd00992    3 TVTLRKDpGGGLGFSLRGGKD-----SGGGIFVSRVEPGGPAER-GGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDE 76

                 ....*.
gi 688560287 274 VRLYVR 279
Cdd:cd00992   77 VTLTVR 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
288-374 7.57e-20

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


:

Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 84.54  E-value: 7.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287 288 IMDVKLVKGP-KGLGFSIAGGVGNqhipgDNSIYITKIIEGGAAHKdGRLQIGDKLLAVNAVCLEEVTHEDAVAALKNTP 366
Cdd:cd00992    1 VRTVTLRKDPgGGLGFSLRGGKDS-----GGGIFVSRVEPGGPAER-GGLRVGDRILEVNGVSVEGLTHEEAVELLKNSG 74

                 ....*...
gi 688560287 367 DVVYLKVA 374
Cdd:cd00992   75 DEVTLTVR 82
 
Name Accession Description Interval E-value
Guanylate_kin pfam00625
Guanylate kinase;
708-886 8.78e-73

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 236.89  E-value: 8.78e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287  708 YSRPVIILGPM---KDRINDDLISEFPDKFGSCVPHTTRPKRDYEVDGRDYHFVnSREQMEKDIQDHKFIEAGQYNNHLY 784
Cdd:pfam00625   1 SRRPVVLSGPSgvgKSHIKKALLSEYPDKFGYSVPHTTRPPRKGEVDGKDYYFV-SKEEMERDISANEFLEYAQFSGNMY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287  785 GTSVQSVREVAEKGKHCILDVSGNAIKRLQLAQLYPIAVFIKPKSVENILEMNKRLMEEQGRKTYDRAMKLEQEFLE-HF 863
Cdd:pfam00625  80 GTSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQRRLKGRGKEQEEKINKRMAAAEQEFQHyEF 159
                         170       180
                  ....*....|....*....|...
gi 688560287  864 TAIVQGDTLEEIYNQVKQIIEEQ 886
Cdd:pfam00625 160 DVIIVNDDLEEAYKKLKEALEAE 182
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
719-886 7.05e-57

Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to GDP. Structure resembles that of adenylate kinase. So-called membrane-associated guanylate kinase homologues (MAGUKs) do not possess guanylate kinase activities; instead at least some possess protein-binding functions.


Pssm-ID: 214504 [Multi-domain]  Cd Length: 174  Bit Score: 193.28  E-value: 7.05e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287   719 KDRINDDLISEFPDKFGSCVPHTTRPKRDYEVDGRDYHFVnSREQMEKDIQDHKFIEAGQYNNHLYGTSVQSVREVAEKG 798
Cdd:smart00072   5 KGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNGVDYHFV-SKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVAEKG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287   799 KHCILDVSGNAIKRLQLAQLYPIAVFIKPKSVENILEMNKRLMEEQGRKTYDRAMKLEQEF--LEHFTAIVQGDTLEEIY 876
Cdd:smart00072  84 KHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRGTETSERIQKRLAAAQKEAqeYHLFDYVIVNDDLEDAY 163
                          170
                   ....*....|
gi 688560287   877 NQVKQIIEEQ 886
Cdd:smart00072 164 EELKEILEAE 173
MAGUK_N_PEST pfam10608
Polyubiquitination (PEST) N-terminal domain of MAGUK; The residues upstream of this domain are ...
110-194 4.86e-39

Polyubiquitination (PEST) N-terminal domain of MAGUK; The residues upstream of this domain are the probable palmitoylation sites, particularly two cysteines. The domain has a putative PEST site at the very start that seems to be responsible for poly-ubiquitination. PEST domains are polypeptide sequences enriched in proline (P), glutamic acid (E), serine (S) and threonine (T) that target proteins for rapid destruction. The whole domain, in conjunction with a C-terminal domain of the longer protein, is necessary for dimerization of the whole protein.


Pssm-ID: 431391 [Multi-domain]  Cd Length: 85  Bit Score: 139.52  E-value: 4.86e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287  110 KYRYQDEDTtSPPEHSSPHIPGDARPPELVQVSEKNISQIENVHGYVSHSHISPMK-ASPAPVVVNTESLDSSPYVNGTE 188
Cdd:pfam10608   1 KYRYQDEDT-PPQEPSPPHLAGSRGGPELVHVSEKNLSQIENVHGYVPHTHISPMKpANPPPIIVNTDTLDTPPYVNGTE 79

                  ....*.
gi 688560287  189 ADYEYE 194
Cdd:pfam10608  80 GEYEYE 85
SH3_DLG-like cd11861
Src Homology 3 domain of Disks large homolog proteins; The DLG-like proteins are scaffolding ...
558-618 6.23e-37

Src Homology 3 domain of Disks large homolog proteins; The DLG-like proteins are scaffolding proteins that cluster at synapses and are also called PSD (postsynaptic density)-95 proteins or SAPs (synapse-associated proteins). They play important roles in synaptic development and plasticity, cell polarity, migration and proliferation. They are members of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. DLG-like proteins contain three PDZ domains and varying N-terminal regions. All DLG proteins exist as alternatively-spliced isoforms. Vertebrates contain four DLG proteins from different genes, called DLG1-4. DLG4 and DLG2 are found predominantly at postsynaptic sites and they mediate surface ion channel and receptor clustering. DLG3 is found axons and some presynaptic terminals. DLG1 interacts with AMPA-type glutamate receptors and is critical in their maturation and delivery to synapses. The SH3 domain of DLG4 binds and clusters the kainate subgroup of glutamate receptors via two proline-rich sequences in their C-terminal tail. It also binds AKAP79/150 (A-kinase anchoring protein). 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: 212795  Cd Length: 61  Bit Score: 132.45  E-value: 6.23e-37
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688560287 558 YVRALFDYDITKDSGLPSQGLNFRFGDILHVLNASDEEWWQARHVTTDGEMEEMGVIPSKK 618
Cdd:cd11861    1 YVRALFDYDPSRDSGLPSQGLSFKFGDILHVTNASDDEWWQARRVTPNGEEEEVGVIPSKR 61
PDZ_assoc pfam10600
PDZ-associated domain of NMDA receptors; This domain is found in higher eukaryotes between the ...
375-438 9.79e-37

PDZ-associated domain of NMDA receptors; This domain is found in higher eukaryotes between the second and third PDZ domains, pfam00595, of glutamate receptor like proteins. Its exact function is not known.


Pssm-ID: 431385  Cd Length: 67  Bit Score: 132.17  E-value: 9.79e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688560287  375 KPTSVFMNDSYAPPDVTSSYSQHMENHISTQSYLSQ---PLTPATPSRYSPVSKGMLGDDEITREPR 438
Cdd:pfam10600   1 KPTSVYLNDSYAPPDITSSYSQHMDNHISHPSYLGGdesVPPPTSPRRYSPVPKHMLGEDDITREPR 67
PLN02772 PLN02772
guanylate kinase
710-883 5.26e-29

guanylate kinase


Pssm-ID: 215414 [Multi-domain]  Cd Length: 398  Bit Score: 120.33  E-value: 5.26e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287 710 RPVIILGPM---KDRINDDLISEFPDKFGSCVPHTTRPKRDYEVDGRDYHFVnSREQMEKDIQDHKFIEAGQYNNHLYGT 786
Cdd:PLN02772 136 KPIVISGPSgvgKGTLISMLMKEFPSMFGFSVSHTTRAPREMEKDGVHYHFT-ERSVMEKEIKDGKFLEFASVHGNLYGT 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287 787 SVQSVREVAEKGKHCILDVSGNAIKRLQLAQLYPIAVFIKPKSVEnilEMNKRL------MEEQGRKTYDRA-MKLEQ-- 857
Cdd:PLN02772 215 SIEAVEVVTDSGKRCILDIDVQGARSVRASSLEAIFIFICPPSME---ELEKRLrargteTEEQIQKRLRNAeAELEQgk 291
                        170       180
                 ....*....|....*....|....*..
gi 688560287 858 -EFLehFTAIVQGDTLEEIYNQVKQII 883
Cdd:PLN02772 292 sSGI--FDHILYNDNLEECYKNLKKLL 316
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
711-827 5.44e-29

Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.


Pssm-ID: 238026  Cd Length: 137  Bit Score: 112.63  E-value: 5.44e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287 711 PVIILGPM---KDRINDDLISEFPDKFGSCVPHTTRPKRDYEVDGRDYHFVnSREQMEKDIQDHKFIEAGQYNNHLYGTS 787
Cdd:cd00071    1 LIVLSGPSgvgKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVDYHFV-SKEEFERLIENGEFLEWAEFHGNYYGTS 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 688560287 788 VQSVREVAEKGKHCILDVSGNAIKRLQLAQLYPIAVFIKP 827
Cdd:cd00071   80 KAAVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILP 119
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
710-885 6.18e-29

guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP kinase. This enzyme transfers a phosphate from ATP to GMP, yielding ADP and GDP. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 213788  Cd Length: 179  Bit Score: 114.13  E-value: 6.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287  710 RPVIILGPM---KDRINDDLISEFPDKFGScVPHTTRPKRDYEVDGRDYHFVnSREQMEKDIQDHKFIEAGQYNNHLYGT 786
Cdd:TIGR03263   1 LLIVISGPSgagKSTLVKALLEEDPNLKFS-ISATTRKPRPGEVDGVDYFFV-SKEEFEEMIKAGEFLEWAEVHGNYYGT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287  787 SVQSVREVAEKGKHCIL--DVSGnAikrLQLAQLYP--IAVFIKPKSVEnilEMNKRLM------EEQGRKTYDRAMKlE 856
Cdd:TIGR03263  79 PKSPVEEALAAGKDVLLeiDVQG-A---RQVKKKFPdaVSIFILPPSLE---ELERRLRkrgtdsEEVIERRLAKAKK-E 150
                         170       180
                  ....*....|....*....|....*....
gi 688560287  857 QEFLEHFTAIVQGDTLEEIYNQVKQIIEE 885
Cdd:TIGR03263 151 IAHADEFDYVIVNDDLEKAVEELKSIILA 179
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
732-885 3.68e-26

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 223272  Cd Length: 191  Bit Score: 106.46  E-value: 3.68e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287 732 DKFGSCVPHTTRPKRDYEVDGRDYHFVnSREQMEKDIQDHKFIEAGQYNNHLYGTSVQSVREVAEKGKHCILDVSGNAIk 811
Cdd:COG0194   28 DKLRFSVSATTRKPRPGEVDGVDYFFV-TEEEFEELIERDEFLEWAEYHGNYYGTSREPVEQALAEGKDVILDIDVQGA- 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287 812 rLQLAQLYP--IAVFIKPKSVEnilEMNKRLmeeQGRKTYD-----RAMKLEQEFLEH---FTAIVQGDTLEEIYNQVKQ 881
Cdd:COG0194  106 -LQVKKKMPnaVSIFILPPSLE---ELERRL---KGRGTDSeeviaRRLENAKKEISHadeFDYVIVNDDLEKALEELKS 178

                 ....
gi 688560287 882 IIEE 885
Cdd:COG0194  179 IILA 182
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
436-520 1.43e-23

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 95.14  E-value: 1.43e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287   436 EPRKIVLHRGTTGLGFNIVGGED-GEGIFISFILAGGPADLCGeLRKGDRIVSVNGVDLRSATHEQAAAALKNAGQTVTI 514
Cdd:smart00228   1 EPRLVELEKGGGGLGFSLVGGKDeGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTL 79

                   ....*.
gi 688560287   515 IAQYRP 520
Cdd:smart00228  80 TVLRGG 85
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
437-515 2.64e-23

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 94.17  E-value: 2.64e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287 437 PRKIVLHRGTT-GLGFNIVGGED-GEGIFISFILAGGPADLCGeLRKGDRIVSVNGVDLRSATHEQAAAALKNAGQTVTI 514
Cdd:cd00992    1 VRTVTLRKDPGgGLGFSLRGGKDsGGGIFVSRVEPGGPAERGG-LRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVTL 79

                 .
gi 688560287 515 I 515
Cdd:cd00992   80 T 80
L27_1 pfam09058
L27_1; The L27 domain is a protein interaction module that exists in a large family of ...
7-64 4.41e-22

L27_1; The L27 domain is a protein interaction module that exists in a large family of scaffold proteins, functioning as an organisation centre of large protein assemblies required for the establishment and maintenance of cell polarity. L27 domains form specific heterotetrameric complexes, in which each domain contains three alpha-helices.


Pssm-ID: 430389  Cd Length: 59  Bit Score: 90.06  E-value: 4.41e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 688560287    7 DAQRALQLLEEYQTKLSQTGDPHLRLSIERVINIFKSTLFQALVDIQEYYEVSLQDTE 64
Cdd:pfam09058   2 DTERALELLEEYHATLSRPDDEELRRAIERLIIIFKSNLFQALLDIQEFYELTLLSNR 59
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
195-279 2.35e-21

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 88.78  E-value: 2.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287 195 EITLERG-NSGLGFSIAGGTDnphigEDPSIFITKIIPGGAAAQdGRLRVNDCILRVNDVDVRDVTHSNAVEALKEAGCI 273
Cdd:cd00992    3 TVTLRKDpGGGLGFSLRGGKD-----SGGGIFVSRVEPGGPAER-GGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDE 76

                 ....*.
gi 688560287 274 VRLYVR 279
Cdd:cd00992   77 VTLTVR 82
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
195-282 1.32e-20

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 86.66  E-value: 1.32e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287   195 EITLERGNSGLGFSIAGGTDNPHigedpSIFITKIIPGGAAAQDGrLRVNDCILRVNDVDVRDVTHSNAVEALKEAGCIV 274
Cdd:smart00228   4 LVELEKGGGGLGFSLVGGKDEGG-----GVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKV 77

                   ....*...
gi 688560287   275 RLYVRRRK 282
Cdd:smart00228  78 TLTVLRGG 85
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
439-517 6.29e-20

PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 84.64  E-value: 6.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287  439 KIVLHRGTTG-LGFNIVGGEDGE--GIFISFILAGGPADlCGELRKGDRIVSVNGVDLRSATHEQAAAALKNAGQTVTII 515
Cdd:pfam00595   1 QVTLEKDGRGgLGFSLKGGSDQGdpGIFVSEVLPGGAAE-AGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLT 79

                  ..
gi 688560287  516 AQ 517
Cdd:pfam00595  80 IL 81
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
288-374 7.57e-20

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 84.54  E-value: 7.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287 288 IMDVKLVKGP-KGLGFSIAGGVGNqhipgDNSIYITKIIEGGAAHKdGRLQIGDKLLAVNAVCLEEVTHEDAVAALKNTP 366
Cdd:cd00992    1 VRTVTLRKDPgGGLGFSLRGGKDS-----GGGIFVSRVEPGGPAER-GGLRVGDRILEVNGVSVEGLTHEEAVELLKNSG 74

                 ....*...
gi 688560287 367 DVVYLKVA 374
Cdd:cd00992   75 DEVTLTVR 82
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
287-376 3.38e-19

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 82.81  E-value: 3.38e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287   287 KIMDVKLVKGPKGLGFSIAGGVGNqhipgDNSIYITKIIEGGAAHKDGrLQIGDKLLAVNAVCLEEVTHEDAVAALKNTP 366
Cdd:smart00228   1 EPRLVELEKGGGGLGFSLVGGKDE-----GGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAG 74
                           90
                   ....*....|
gi 688560287   367 DVVYLKVAKP 376
Cdd:smart00228  75 GKVTLTVLRG 84
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
195-279 4.50e-19

PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 82.33  E-value: 4.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287  195 EITLER-GNSGLGFSIAGGTDNPhigeDPSIFITKIIPGGAAAQDGrLRVNDCILRVNDVDVRDVTHSNAVEALKEAGCI 273
Cdd:pfam00595   1 QVTLEKdGRGGLGFSLKGGSDQG----DPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGK 75

                  ....*.
gi 688560287  274 VRLYVR 279
Cdd:pfam00595  76 VTLTIL 81
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
296-374 6.42e-18

PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 78.86  E-value: 6.42e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688560287  296 GPKGLGFSIAGGVGNqhipGDNSIYITKIIEGGAAHKDGrLQIGDKLLAVNAVCLEEVTHEDAVAALKNTPDVVYLKVA 374
Cdd:pfam00595   8 GRGGLGFSLKGGSDQ----GDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
558-616 8.52e-09

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: 52.16  E-value: 8.52e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 688560287   558 YVRALFDYDITKDsglpsQGLNFRFGDILHVLNASDEEWWQARHVTtdgemEEMGVIPS 616
Cdd:smart00326   4 QVRALYDYTAQDP-----DELSFKKGDIITVLEKSDDGWWKGRLGR-----GKEGLFPS 52
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
560-616 9.75e-07

SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organisation. 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: 46.04  E-value: 9.75e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 688560287  560 RALFDYDITKDSGLPsqglnFRFGDILHVLNASDEEWWQARhVTTDGEmeemGVIPS 616
Cdd:pfam00018   1 VALYDYTAQEPDELS-----FKKGDIIIVLEKSEDGWWKGR-NKGGKE----GLIPS 47
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
455-514 3.01e-04

periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273938 [Multi-domain]  Cd Length: 428  Bit Score: 44.13  E-value: 3.01e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287  455 GGEDGEGIFISFILAGGPADLCGeLRKGDRIVSVNGVDLRSATHEQAAAALKNAGQTVTI 514
Cdd:TIGR02037 252 GLEKQRGALVAQVLPGSPAEKAG-LKAGDVITSVNGKPISSFADLRRAIGTLKPGKKVTL 310
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
457-514 5.38e-04

C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 223864 [Multi-domain]  Cd Length: 406  Bit Score: 43.47  E-value: 5.38e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 688560287 457 EDGEGIFISFILAGGPADLCGeLRKGDRIVSVNGVDLRSATHEQAAAALKN-AGQTVTI 514
Cdd:COG0793  109 EDIGGVKVVSPIDGSPAAKAG-IKPGDVIIKIDGKSVGGVSLDEAVKLIRGkPGTKVTL 166
L27 smart00569
domain in receptor targeting proteins Lin-2 and Lin-7;
9-64 1.26e-03

domain in receptor targeting proteins Lin-2 and Lin-7;


Pssm-ID: 197794  Cd Length: 53  Bit Score: 37.49  E-value: 1.26e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 688560287     9 QRALQLLEEYQtklSQTGDPHLRLSIERvinIFKSTLFQALVDIQEYYEVSLQDTE 64
Cdd:smart00569   1 QRLLELLEELQ---SLLSPSEDLQELRR---LLQSPHLQALLKIHDKVAETELDPP 50
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
225-373 1.35e-03

periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273938 [Multi-domain]  Cd Length: 428  Bit Score: 42.21  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287  225 FITKIIPGGAAAQDGrLRVNDCILRVNDVDVRDVTH-SNAVEALKEAGCIVRLYVRRRKPLSekiMDVKLVKGPKG---- 299
Cdd:TIGR02037 260 LVAQVLPGSPAEKAG-LKAGDVITSVNGKPISSFADlRRAIGTLKPGKKVTLGILRKGKEKT---ITVTLGASPEEqass 335
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287  300 ----LGFSIA----GGVGNQHIPGD-NSIYITKIIEGGAAHKDGrLQIGDKLLAVNAVCLEEVTH-EDAVAALKNtPDVV 369
Cdd:TIGR02037 336 snpfLGLTVAnlspEIRKELRLKGDvKGVVVTKVVSGSPAARAG-LQPGDVILSVNQQPVSSVAElRKVLARAKK-GGRV 413

                  ....
gi 688560287  370 YLKV 373
Cdd:TIGR02037 414 ALLI 417
 
Name Accession Description Interval E-value
Guanylate_kin pfam00625
Guanylate kinase;
708-886 8.78e-73

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 236.89  E-value: 8.78e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287  708 YSRPVIILGPM---KDRINDDLISEFPDKFGSCVPHTTRPKRDYEVDGRDYHFVnSREQMEKDIQDHKFIEAGQYNNHLY 784
Cdd:pfam00625   1 SRRPVVLSGPSgvgKSHIKKALLSEYPDKFGYSVPHTTRPPRKGEVDGKDYYFV-SKEEMERDISANEFLEYAQFSGNMY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287  785 GTSVQSVREVAEKGKHCILDVSGNAIKRLQLAQLYPIAVFIKPKSVENILEMNKRLMEEQGRKTYDRAMKLEQEFLE-HF 863
Cdd:pfam00625  80 GTSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQRRLKGRGKEQEEKINKRMAAAEQEFQHyEF 159
                         170       180
                  ....*....|....*....|...
gi 688560287  864 TAIVQGDTLEEIYNQVKQIIEEQ 886
Cdd:pfam00625 160 DVIIVNDDLEEAYKKLKEALEAE 182
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
719-886 7.05e-57

Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to GDP. Structure resembles that of adenylate kinase. So-called membrane-associated guanylate kinase homologues (MAGUKs) do not possess guanylate kinase activities; instead at least some possess protein-binding functions.


Pssm-ID: 214504 [Multi-domain]  Cd Length: 174  Bit Score: 193.28  E-value: 7.05e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287   719 KDRINDDLISEFPDKFGSCVPHTTRPKRDYEVDGRDYHFVnSREQMEKDIQDHKFIEAGQYNNHLYGTSVQSVREVAEKG 798
Cdd:smart00072   5 KGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNGVDYHFV-SKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVAEKG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287   799 KHCILDVSGNAIKRLQLAQLYPIAVFIKPKSVENILEMNKRLMEEQGRKTYDRAMKLEQEF--LEHFTAIVQGDTLEEIY 876
Cdd:smart00072  84 KHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRGTETSERIQKRLAAAQKEAqeYHLFDYVIVNDDLEDAY 163
                          170
                   ....*....|
gi 688560287   877 NQVKQIIEEQ 886
Cdd:smart00072 164 EELKEILEAE 173
MAGUK_N_PEST pfam10608
Polyubiquitination (PEST) N-terminal domain of MAGUK; The residues upstream of this domain are ...
110-194 4.86e-39

Polyubiquitination (PEST) N-terminal domain of MAGUK; The residues upstream of this domain are the probable palmitoylation sites, particularly two cysteines. The domain has a putative PEST site at the very start that seems to be responsible for poly-ubiquitination. PEST domains are polypeptide sequences enriched in proline (P), glutamic acid (E), serine (S) and threonine (T) that target proteins for rapid destruction. The whole domain, in conjunction with a C-terminal domain of the longer protein, is necessary for dimerization of the whole protein.


Pssm-ID: 431391 [Multi-domain]  Cd Length: 85  Bit Score: 139.52  E-value: 4.86e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287  110 KYRYQDEDTtSPPEHSSPHIPGDARPPELVQVSEKNISQIENVHGYVSHSHISPMK-ASPAPVVVNTESLDSSPYVNGTE 188
Cdd:pfam10608   1 KYRYQDEDT-PPQEPSPPHLAGSRGGPELVHVSEKNLSQIENVHGYVPHTHISPMKpANPPPIIVNTDTLDTPPYVNGTE 79

                  ....*.
gi 688560287  189 ADYEYE 194
Cdd:pfam10608  80 GEYEYE 85
SH3_DLG-like cd11861
Src Homology 3 domain of Disks large homolog proteins; The DLG-like proteins are scaffolding ...
558-618 6.23e-37

Src Homology 3 domain of Disks large homolog proteins; The DLG-like proteins are scaffolding proteins that cluster at synapses and are also called PSD (postsynaptic density)-95 proteins or SAPs (synapse-associated proteins). They play important roles in synaptic development and plasticity, cell polarity, migration and proliferation. They are members of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. DLG-like proteins contain three PDZ domains and varying N-terminal regions. All DLG proteins exist as alternatively-spliced isoforms. Vertebrates contain four DLG proteins from different genes, called DLG1-4. DLG4 and DLG2 are found predominantly at postsynaptic sites and they mediate surface ion channel and receptor clustering. DLG3 is found axons and some presynaptic terminals. DLG1 interacts with AMPA-type glutamate receptors and is critical in their maturation and delivery to synapses. The SH3 domain of DLG4 binds and clusters the kainate subgroup of glutamate receptors via two proline-rich sequences in their C-terminal tail. It also binds AKAP79/150 (A-kinase anchoring protein). 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: 212795  Cd Length: 61  Bit Score: 132.45  E-value: 6.23e-37
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688560287 558 YVRALFDYDITKDSGLPSQGLNFRFGDILHVLNASDEEWWQARHVTTDGEMEEMGVIPSKK 618
Cdd:cd11861    1 YVRALFDYDPSRDSGLPSQGLSFKFGDILHVTNASDDEWWQARRVTPNGEEEEVGVIPSKR 61
SH3_DLG2 cd12032
Src Homology 3 domain of Disks Large homolog 2; DLG2, also called postsynaptic density-93 ...
552-625 8.77e-37

Src Homology 3 domain of Disks Large homolog 2; DLG2, also called postsynaptic density-93 (PSD93) or Channel-associated protein of synapse-110 (chapsyn 110), is a scaffolding protein that clusters at synapses and plays an important role in synaptic development and plasticity. The DLG2 delta isoform binds inwardly rectifying potassium Kir2 channels, which determine resting membrane potential in neurons. It regulates the spatial and temporal distribution of Kir2 channels within neuronal membranes. DLG2 is a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. DLG2 contains three PDZ domains. 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: 212965  Cd Length: 74  Bit Score: 132.51  E-value: 8.77e-37
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688560287 552 SQKRTLYVRALFDYDITKDSGLPSQGLNFRFGDILHVLNASDEEWWQARHVTTDGEMEEMGVIPSKKRVERKER 625
Cdd:cd12032    1 NQKRSLYVRAMFDYEKSKDSGLPSQGLSFRYGDILHVINASDDEWWQARRVTPDGDSEEMGVIPSKRRVERKER 74
PDZ_assoc pfam10600
PDZ-associated domain of NMDA receptors; This domain is found in higher eukaryotes between the ...
375-438 9.79e-37

PDZ-associated domain of NMDA receptors; This domain is found in higher eukaryotes between the second and third PDZ domains, pfam00595, of glutamate receptor like proteins. Its exact function is not known.


Pssm-ID: 431385  Cd Length: 67  Bit Score: 132.17  E-value: 9.79e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688560287  375 KPTSVFMNDSYAPPDVTSSYSQHMENHISTQSYLSQ---PLTPATPSRYSPVSKGMLGDDEITREPR 438
Cdd:pfam10600   1 KPTSVYLNDSYAPPDITSSYSQHMDNHISHPSYLGGdesVPPPTSPRRYSPVPKHMLGEDDITREPR 67
SH3_DLG1 cd12031
Src Homology 3 domain of Disks Large homolog 1; DLG1, also called synapse-associated protein ...
555-621 2.34e-36

Src Homology 3 domain of Disks Large homolog 1; DLG1, also called synapse-associated protein 97 (SAP97), is a scaffolding protein that clusters at synapses and plays an important role in synaptic development and plasticity. DLG1 plays roles in regulating cell polarity, proliferation, migration, and cycle progression. It interacts with AMPA-type glutamate receptors and is critical in their maturation and delivery to synapses. It also interacts with PKCalpha and promotes wound healing. DLG1 is a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. DLG1 contains three PDZ domains. 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: 212964  Cd Length: 67  Bit Score: 130.97  E-value: 2.34e-36
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688560287 555 RTLYVRALFDYDITKDSGLPSQGLNFRFGDILHVLNASDEEWWQARHVTTDGEMEEMGVIPSKKRVE 621
Cdd:cd12031    1 RSLYVRALFDYDKTKDSGLPSQGLNFKFGDILHVVNASDDEWWQARQVTADGESEEIGVIPSKRRVE 67
SH3_DLG4 cd12030
Src Homology 3 domain of Disks Large homolog 4; DLG4, also called postsynaptic density-95 ...
558-621 2.56e-30

Src Homology 3 domain of Disks Large homolog 4; DLG4, also called postsynaptic density-95 (PSD95) or synapse-associated protein 90 (SAP90), is a scaffolding protein that clusters at synapses and plays an important role in synaptic development and plasticity. It is responsible for the membrane clustering and retention of many transporters and receptors such as potassium channels and PMCA4b, a P-type ion transport ATPase, among others. DLG4 is a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. DLG4 contains three PDZ domains. The SH3 domain of DLG4 binds and clusters the kainate subgroup of glutamate receptors via two proline-rich sequences in their C-terminal tail. It also binds AKAP79/150 (A-kinase anchoring protein). 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: 212963  Cd Length: 66  Bit Score: 113.87  E-value: 2.56e-30
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688560287 558 YVRALFDYDITKDSGLPSQGLNFRFGDILHVLNASDEEWWQARHVTTDGEMEEMGVIPSKKRVE 621
Cdd:cd12030    3 YIRALFDYDKTKDCGFLSQALSFRFGDVLHVIDAGDEEWWQARRVHSDSETEEIGFIPSKRRVE 66
SH3_DLG3 cd12029
Src Homology 3 domain of Disks Large homolog 3; DLG3, also called synapse-associated protein ...
555-621 2.89e-30

Src Homology 3 domain of Disks Large homolog 3; DLG3, also called synapse-associated protein 102 (SAP102), is a scaffolding protein that clusters at synapses and plays an important role in synaptic development and plasticity. Mutations in DLG3 cause midgestational embryonic lethality in mice and may be associated with nonsyndromic X-linked mental retardation in humans. It interacts with the NEDD4 (neural precursor cell-expressed developmentally downregulated 4) family of ubiquitin ligases and promotes apical tight junction formation. DLG3 is a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. DLG3 contains three PDZ domains. 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: 212962  Cd Length: 67  Bit Score: 113.64  E-value: 2.89e-30
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688560287 555 RTLYVRALFDYDITKDSGLPSQGLNFRFGDILHVLNASDEEWWQARHVTTDGEMEEMGVIPSKKRVE 621
Cdd:cd12029    1 RSLYVRALFDYDRTRDSCLPSQGLSFSYGDILHVINASDDEWWQARLVTPHGESEQIGVIPSKKRVE 67
PLN02772 PLN02772
guanylate kinase
710-883 5.26e-29

guanylate kinase


Pssm-ID: 215414 [Multi-domain]  Cd Length: 398  Bit Score: 120.33  E-value: 5.26e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287 710 RPVIILGPM---KDRINDDLISEFPDKFGSCVPHTTRPKRDYEVDGRDYHFVnSREQMEKDIQDHKFIEAGQYNNHLYGT 786
Cdd:PLN02772 136 KPIVISGPSgvgKGTLISMLMKEFPSMFGFSVSHTTRAPREMEKDGVHYHFT-ERSVMEKEIKDGKFLEFASVHGNLYGT 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287 787 SVQSVREVAEKGKHCILDVSGNAIKRLQLAQLYPIAVFIKPKSVEnilEMNKRL------MEEQGRKTYDRA-MKLEQ-- 857
Cdd:PLN02772 215 SIEAVEVVTDSGKRCILDIDVQGARSVRASSLEAIFIFICPPSME---ELEKRLrargteTEEQIQKRLRNAeAELEQgk 291
                        170       180
                 ....*....|....*....|....*..
gi 688560287 858 -EFLehFTAIVQGDTLEEIYNQVKQII 883
Cdd:PLN02772 292 sSGI--FDHILYNDNLEECYKNLKKLL 316
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
711-827 5.44e-29

Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.


Pssm-ID: 238026  Cd Length: 137  Bit Score: 112.63  E-value: 5.44e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287 711 PVIILGPM---KDRINDDLISEFPDKFGSCVPHTTRPKRDYEVDGRDYHFVnSREQMEKDIQDHKFIEAGQYNNHLYGTS 787
Cdd:cd00071    1 LIVLSGPSgvgKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVDYHFV-SKEEFERLIENGEFLEWAEFHGNYYGTS 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 688560287 788 VQSVREVAEKGKHCILDVSGNAIKRLQLAQLYPIAVFIKP 827
Cdd:cd00071   80 KAAVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILP 119
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
710-885 6.18e-29

guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP kinase. This enzyme transfers a phosphate from ATP to GMP, yielding ADP and GDP. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 213788  Cd Length: 179  Bit Score: 114.13  E-value: 6.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287  710 RPVIILGPM---KDRINDDLISEFPDKFGScVPHTTRPKRDYEVDGRDYHFVnSREQMEKDIQDHKFIEAGQYNNHLYGT 786
Cdd:TIGR03263   1 LLIVISGPSgagKSTLVKALLEEDPNLKFS-ISATTRKPRPGEVDGVDYFFV-SKEEFEEMIKAGEFLEWAEVHGNYYGT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287  787 SVQSVREVAEKGKHCIL--DVSGnAikrLQLAQLYP--IAVFIKPKSVEnilEMNKRLM------EEQGRKTYDRAMKlE 856
Cdd:TIGR03263  79 PKSPVEEALAAGKDVLLeiDVQG-A---RQVKKKFPdaVSIFILPPSLE---ELERRLRkrgtdsEEVIERRLAKAKK-E 150
                         170       180
                  ....*....|....*....|....*....
gi 688560287  857 QEFLEHFTAIVQGDTLEEIYNQVKQIIEE 885
Cdd:TIGR03263 151 IAHADEFDYVIVNDDLEKAVEELKSIILA 179
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
732-885 3.68e-26

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 223272  Cd Length: 191  Bit Score: 106.46  E-value: 3.68e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287 732 DKFGSCVPHTTRPKRDYEVDGRDYHFVnSREQMEKDIQDHKFIEAGQYNNHLYGTSVQSVREVAEKGKHCILDVSGNAIk 811
Cdd:COG0194   28 DKLRFSVSATTRKPRPGEVDGVDYFFV-TEEEFEELIERDEFLEWAEYHGNYYGTSREPVEQALAEGKDVILDIDVQGA- 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287 812 rLQLAQLYP--IAVFIKPKSVEnilEMNKRLmeeQGRKTYD-----RAMKLEQEFLEH---FTAIVQGDTLEEIYNQVKQ 881
Cdd:COG0194  106 -LQVKKKMPnaVSIFILPPSLE---ELERRL---KGRGTDSeeviaRRLENAKKEISHadeFDYVIVNDDLEKALEELKS 178

                 ....
gi 688560287 882 IIEE 885
Cdd:COG0194  179 IILA 182
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
436-520 1.43e-23

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 95.14  E-value: 1.43e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287   436 EPRKIVLHRGTTGLGFNIVGGED-GEGIFISFILAGGPADLCGeLRKGDRIVSVNGVDLRSATHEQAAAALKNAGQTVTI 514
Cdd:smart00228   1 EPRLVELEKGGGGLGFSLVGGKDeGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTL 79

                   ....*.
gi 688560287   515 IAQYRP 520
Cdd:smart00228  80 TVLRGG 85
gmk PRK00300
guanylate kinase; Provisional
738-886 2.41e-23

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 98.62  E-value: 2.41e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287 738 VPHTTRPKRDYEVDGRDYHFVnSREQMEKDIQDHKFIEAGQYNNHLYGTSVQSVREVAEKGKHCIL--DVSGnAikrLQL 815
Cdd:PRK00300  36 VSATTRAPRPGEVDGVDYFFV-SKEEFEEMIENGEFLEWAEVFGNYYGTPRSPVEEALAAGKDVLLeiDWQG-A---RQV 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287 816 AQLYP--IAVFIKPKSVEnilEMNKRLmeeQGRKTYD---------RAMKlEQEFLEHFTAIVQGDTLEEIYNQVKQIIE 884
Cdd:PRK00300 111 KKKMPdaVSIFILPPSLE---ELERRL---RGRGTDSeeviarrlaKARE-EIAHASEYDYVIVNDDLDTALEELKAIIR 183

                 ..
gi 688560287 885 EQ 886
Cdd:PRK00300 184 AE 185
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
437-515 2.64e-23

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 94.17  E-value: 2.64e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287 437 PRKIVLHRGTT-GLGFNIVGGED-GEGIFISFILAGGPADLCGeLRKGDRIVSVNGVDLRSATHEQAAAALKNAGQTVTI 514
Cdd:cd00992    1 VRTVTLRKDPGgGLGFSLRGGKDsGGGIFVSRVEPGGPAERGG-LRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVTL 79

                 .
gi 688560287 515 I 515
Cdd:cd00992   80 T 80
L27_1 pfam09058
L27_1; The L27 domain is a protein interaction module that exists in a large family of ...
7-64 4.41e-22

L27_1; The L27 domain is a protein interaction module that exists in a large family of scaffold proteins, functioning as an organisation centre of large protein assemblies required for the establishment and maintenance of cell polarity. L27 domains form specific heterotetrameric complexes, in which each domain contains three alpha-helices.


Pssm-ID: 430389  Cd Length: 59  Bit Score: 90.06  E-value: 4.41e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 688560287    7 DAQRALQLLEEYQTKLSQTGDPHLRLSIERVINIFKSTLFQALVDIQEYYEVSLQDTE 64
Cdd:pfam09058   2 DTERALELLEEYHATLSRPDDEELRRAIERLIIIFKSNLFQALLDIQEFYELTLLSNR 59
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
195-279 2.35e-21

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 88.78  E-value: 2.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287 195 EITLERG-NSGLGFSIAGGTDnphigEDPSIFITKIIPGGAAAQdGRLRVNDCILRVNDVDVRDVTHSNAVEALKEAGCI 273
Cdd:cd00992    3 TVTLRKDpGGGLGFSLRGGKD-----SGGGIFVSRVEPGGPAER-GGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDE 76

                 ....*.
gi 688560287 274 VRLYVR 279
Cdd:cd00992   77 VTLTVR 82
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
195-282 1.32e-20

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 86.66  E-value: 1.32e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287   195 EITLERGNSGLGFSIAGGTDNPHigedpSIFITKIIPGGAAAQDGrLRVNDCILRVNDVDVRDVTHSNAVEALKEAGCIV 274
Cdd:smart00228   4 LVELEKGGGGLGFSLVGGKDEGG-----GVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKV 77

                   ....*...
gi 688560287   275 RLYVRRRK 282
Cdd:smart00228  78 TLTVLRGG 85
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
439-517 6.29e-20

PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 84.64  E-value: 6.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287  439 KIVLHRGTTG-LGFNIVGGEDGE--GIFISFILAGGPADlCGELRKGDRIVSVNGVDLRSATHEQAAAALKNAGQTVTII 515
Cdd:pfam00595   1 QVTLEKDGRGgLGFSLKGGSDQGdpGIFVSEVLPGGAAE-AGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLT 79

                  ..
gi 688560287  516 AQ 517
Cdd:pfam00595  80 IL 81
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
288-374 7.57e-20

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 84.54  E-value: 7.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287 288 IMDVKLVKGP-KGLGFSIAGGVGNqhipgDNSIYITKIIEGGAAHKdGRLQIGDKLLAVNAVCLEEVTHEDAVAALKNTP 366
Cdd:cd00992    1 VRTVTLRKDPgGGLGFSLRGGKDS-----GGGIFVSRVEPGGPAER-GGLRVGDRILEVNGVSVEGLTHEEAVELLKNSG 74

                 ....*...
gi 688560287 367 DVVYLKVA 374
Cdd:cd00992   75 DEVTLTVR 82
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
287-376 3.38e-19

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 82.81  E-value: 3.38e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287   287 KIMDVKLVKGPKGLGFSIAGGVGNqhipgDNSIYITKIIEGGAAHKDGrLQIGDKLLAVNAVCLEEVTHEDAVAALKNTP 366
Cdd:smart00228   1 EPRLVELEKGGGGLGFSLVGGKDE-----GGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAG 74
                           90
                   ....*....|
gi 688560287   367 DVVYLKVAKP 376
Cdd:smart00228  75 GKVTLTVLRG 84
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
195-279 4.50e-19

PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 82.33  E-value: 4.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287  195 EITLER-GNSGLGFSIAGGTDNPhigeDPSIFITKIIPGGAAAQDGrLRVNDCILRVNDVDVRDVTHSNAVEALKEAGCI 273
Cdd:pfam00595   1 QVTLEKdGRGGLGFSLKGGSDQG----DPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGK 75

                  ....*.
gi 688560287  274 VRLYVR 279
Cdd:pfam00595  76 VTLTIL 81
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
296-374 6.42e-18

PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 78.86  E-value: 6.42e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688560287  296 GPKGLGFSIAGGVGNqhipGDNSIYITKIIEGGAAHKDGrLQIGDKLLAVNAVCLEEVTHEDAVAALKNTPDVVYLKVA 374
Cdd:pfam00595   8 GRGGLGFSLKGGSDQ----GDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
SH3_MPP cd11862
Src Homology 3 domain of Membrane Protein, Palmitoylated (or MAGUK p55 subfamily member) ...
558-617 6.97e-18

Src Homology 3 domain of Membrane Protein, Palmitoylated (or MAGUK p55 subfamily member) proteins; The MPP/p55 subfamily of MAGUK (membrane-associated guanylate kinase) proteins includes at least eight vertebrate members (MPP1-7 and CASK), four Drosophila proteins (Stardust, Varicose, CASK and Skiff), and other similar proteins; they all contain one each of the core of three domains characteristic of MAGUK proteins: PDZ, SH3, and guanylate kinase (GuK). In addition, most members except for MPP1 contain N-terminal L27 domains and some also contain a Hook (Protein 4.1 Binding) motif in between the SH3 and GuK domains. CASK has an additional calmodulin-dependent kinase (CaMK)-like domain at the N-terminus. Members of this subfamily are scaffolding proteins that play important roles in regulating and establishing cell polarity, cell adhesion, and synaptic targeting and transmission, among others. The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the 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: 212796  Cd Length: 61  Bit Score: 78.39  E-value: 6.97e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688560287 558 YVRALFDYDITKDSGLPSQ--GLNFRFGDILHVLNASDEEWWQARHVTTDGemEEMGVIPSK 617
Cdd:cd11862    1 FVRALFDYDPEEDPLIPCKeaGLSFKKGDILQIVNQDDPNWWQARKVGDPN--GRAGLIPSQ 60
gmk PRK14738
guanylate kinase; Provisional
701-883 3.22e-14

guanylate kinase; Provisional


Pssm-ID: 237809  Cd Length: 206  Bit Score: 72.46  E-value: 3.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287 701 VTQQEVSYSRPVIILGPM---KDRINDDLiSEFPDKFGSCVPHTTRPKRDYEVDGRDYHFVnSREQMEKDIQDHKFIEAG 777
Cdd:PRK14738   5 WLFNKPAKPLLVVISGPSgvgKDAVLARM-RERKLPFHFVVTATTRPKRPGEIDGVDYHFV-TPEEFREMISQNELLEWA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287 778 QYNNHLYGTSVQSVREVAEKGKHCIL--DVSGNA-IKRLQlaqlyPIAVFI--KPKSVEnilEMNKRLMeeqGRKT---- 848
Cdd:PRK14738  83 EVYGNYYGVPKAPVRQALASGRDVIVkvDVQGAAsIKRLV-----PEAVFIflAPPSMD---ELTRRLE---LRRTespe 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 688560287 849 -YDRAM---KLEQEFLEHFTAIV--QGDTLEEIYNQVKQII 883
Cdd:PRK14738 152 eLERRLataPLELEQLPEFDYVVvnPEDRLDEAVAQIMAII 192
SH3_MPP1-like cd12035
Src Homology 3 domain of Membrane Protein, Palmitoylated 1 (or MAGUK p55 subfamily member 1) ...
558-616 8.12e-14

Src Homology 3 domain of Membrane Protein, Palmitoylated 1 (or MAGUK p55 subfamily member 1)-like proteins; This subfamily includes MPP1, CASK (Calcium/calmodulin-dependent Serine protein Kinase), Caenorhabditis elegans lin-2, and similar proteins. MPP1 and CASK are scaffolding proteins from the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). In addition, they also have the Hook (Protein 4.1 Binding) motif in between the SH3 and GuK domains. The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. CASK and lin-2 also contain an N-terminal calmodulin-dependent kinase (CaMK)-like domain and two L27 domains. MPP1 is ubiquitously-expressed and plays roles in regulating neutrophil polarity, cell shape, hair cell development, and neural development and patterning of the retina. CASK is highly expressed in the mammalian nervous system and plays roles in synaptic protein targeting, neural development, and gene expression regulation. 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: 212968  Cd Length: 62  Bit Score: 66.69  E-value: 8.12e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688560287 558 YVRALFDYDITKDSGLPSQ--GLNFRFGDILHVLNASDEEWWQARHVttDGEMEEMGVIPS 616
Cdd:cd12035    1 YVRAQFDYDPSKDDLIPCQqaGIAFKTGDILQIISKDDHNWWQARKP--GASKEPAGLIPS 59
SH3_MPP7 cd12033
Src Homology 3 domain of Membrane Protein, Palmitoylated 7 (or MAGUK p55 subfamily member 7); ...
558-617 3.32e-13

Src Homology 3 domain of Membrane Protein, Palmitoylated 7 (or MAGUK p55 subfamily member 7); MPP7 is a scaffolding protein that binds to DLG1 and promotes tight junction formation and epithelial cell polarity. Mutations in the MPP7 gene may be associated with the pathogenesis of diabetes and extreme bone mineral density. It is one of seven vertebrate homologs of the Drosophila Stardust protein, which is required in establishing cell polarity, and it contains two L27 domains followed by the core of three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the 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: 212966  Cd Length: 61  Bit Score: 65.04  E-value: 3.32e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688560287 558 YVRALFDYDITKDSGLPSQ--GLNFRFGDILHVLNASDEEWWQARHvTTDGEMEEmGVIPSK 617
Cdd:cd12033    1 FIKALFDYNPNEDKAIPCKeaGLSFKKGDILQIMSQDDATWWQAKH-EGDANPRA-GLIPSK 60
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
447-515 1.32e-12

PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. Heterodimerization through PDZ-PDZ domain interactions adds to the domain's versatility, and PDZ domain-mediated interactions may be modulated dynamically through target phosphorylation. Some PDZ domains play a role in scaffolding supramolecular complexes. PDZ domains are found in diverse signaling proteins in bacteria, archebacteria, and eurkayotes. This CD contains two distinct structural subgroups with either a N- or C-terminal beta-strand forming the peptide-binding groove base. The circular permutation placing the strand on the N-terminus appears to be found in Eumetazoa only, while the C-terminal variant is found in all three kingdoms of life, and seems to co-occur with protease domains. PDZ domains have been named after PSD95(post synaptic density protein), DlgA (Drosophila disc large tumor suppressor), and ZO1, a mammalian tight junction protein.


Pssm-ID: 238080 [Multi-domain]  Cd Length: 70  Bit Score: 63.48  E-value: 1.32e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287 447 TGLGFNIVGGEDGeGIFISFILAGGPADLCGeLRKGDRIVSVNGVDLRSATHEQAAAALKNA-GQTVTII 515
Cdd:cd00136    1 GGLGFSIRGGTEG-GVVVLSVEPGSPAERAG-LQAGDVILAVNGTDVKNLTLEDVAELLKKEvGEKVTLT 68
SH3_MPP5 cd12036
Src Homology 3 domain of Membrane Protein, Palmitoylated 5 (or MAGUK p55 subfamily member 5); ...
558-617 1.49e-12

Src Homology 3 domain of Membrane Protein, Palmitoylated 5 (or MAGUK p55 subfamily member 5); MPP5, also called PALS1 (Protein associated with Lin7) or Nagie oko protein in zebrafish or Stardust in Drosophila, is a scaffolding protein which associates with Crumbs homolog 1 (CRB1), CRB2, or CRB3 through its PDZ domain and with PALS1-associated tight junction protein (PATJ) or multi-PDZ domain protein 1 (MUPP1) through its L27 domain. The resulting tri-protein complexes are core proteins of the Crumb complex, which localizes at tight junctions or subapical regions, and is involved in the maintenance of apical-basal polarity in epithelial cells and the morphogenesis and function of photoreceptor cells. MPP5 is critical for the proper stratification of the retina and is also expressed in T lymphocytes where it is important for TCR-mediated activation of NFkB. Drosophila Stardust exists in several isoforms, some of which show opposing functions in photoreceptor cells, which suggests that the relative ratio of different Crumbs complexes regulates photoreceptor homeostasis. MPP5 contains two L27 domains followed by the core of three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). In addition, it also contains the Hook (Protein 4.1 Binding) motif in between the SH3 and GuK domains. The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the 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: 212969  Cd Length: 63  Bit Score: 63.20  E-value: 1.49e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688560287 558 YVRALFDYDITKDSGLPSQ--GLNFRFGDILHVLNASDEEWWQARHVTTDGEMEEMGVIPSK 617
Cdd:cd12036    1 HVRAHFDYDPEDDPYIPCRelGLSFQKGDILHVISQEDPNWWQAYREGEEDNQSLAGLIPSK 62
SH3_MPP1 cd12080
Src Homology 3 domain of Membrane Protein, Palmitoylated 1 (or MAGUK p55 subfamily member 1); ...
558-616 2.45e-12

Src Homology 3 domain of Membrane Protein, Palmitoylated 1 (or MAGUK p55 subfamily member 1); MPP1, also called 55 kDa erythrocyte membrane protein (p55), is a ubiquitously-expressed scaffolding protein that plays roles in regulating neutrophil polarity, cell shape, hair cell development, and neural development and patterning of the retina. It was originally identified as an erythrocyte protein that stabilizes the actin cytoskeleton to the plasma membrane by forming a complex with 4.1R protein and glycophorin C. MPP1 is one of seven vertebrate homologs of the Drosophila Stardust protein, which is required in establishing cell polarity, and it contains the three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). In addition, it also contains the Hook (Protein 4.1 Binding) motif in between the SH3 and GuK domains. The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the 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: 213013  Cd Length: 62  Bit Score: 62.66  E-value: 2.45e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688560287 558 YVRALFDYDITKDSGLPSQ--GLNFRFGDILHVLNASDEEWWQARhVTTDGEmEEMGVIPS 616
Cdd:cd12080    1 YMRAQFDYDPKKDNLIPCKeaGLKFQTGDIIQIINKDDSNWWQGR-VEGSGE-ESAGLIPS 59
SH3_CASK cd12081
Src Homology 3 domain of Calcium/calmodulin-dependent Serine protein Kinase; CASK is a ...
558-616 8.39e-11

Src Homology 3 domain of Calcium/calmodulin-dependent Serine protein Kinase; CASK is a scaffolding protein that is highly expressed in the mammalian nervous system and plays roles in synaptic protein targeting, neural development, and gene expression regulation. CASK interacts with many different binding partners including parkin, neurexin, syndecans, calcium channel proteins, caskin, among others, to perform specific functions in different subcellular locations. Disruption of the CASK gene in mice results in neonatal lethality while mutations in the human gene have been associated with X-linked mental retardation. Drosophila CASK is associated with both pre- and postsynaptic membranes and is crucial in synaptic transmission and vesicle cycling. CASK contains an N-terminal calmodulin-dependent kinase (CaMK)-like domain, two L27 domains, followed by the core of three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). In addition, it also contains the Hook (Protein 4.1 Binding) motif in between the SH3 and GuK domains. The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the 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: 213014  Cd Length: 62  Bit Score: 58.37  E-value: 8.39e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688560287 558 YVRALFDYDITKDSGLPSQ--GLNFRFGDILHVLNASDEEWWQARHVTTDGemEEMGVIPS 616
Cdd:cd12081    1 YVRAQFEYDPLKDDLIPCKqaGIRFRVGDILQIISKDDHNWWQAKLENSKN--GTAGLIPS 59
SH3_MPP2 cd12037
Src Homology 3 domain of Membrane Protein, Palmitoylated 2 (or MAGUK p55 subfamily member 2); ...
558-617 1.09e-10

Src Homology 3 domain of Membrane Protein, Palmitoylated 2 (or MAGUK p55 subfamily member 2); MPP2 is a scaffolding protein that interacts with the non-receptor tyrosine kinase c-Src in epithelial cells to negatively regulate its activity and morphological function. It is one of seven vertebrate homologs of the Drosophila Stardust protein, which is required in establishing cell polarity, and it contains two L27 domains followed by the core of three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). In addition, it also contains the Hook (Protein 4.1 Binding) motif in between the SH3 and GuK domains. The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the 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: 212970  Cd Length: 59  Bit Score: 57.65  E-value: 1.09e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688560287 558 YVRALFDYDITKDSGLPSQ--GLNFRFGDILHVLNASDEEWWQARHVttdgEMEEMGVIPSK 617
Cdd:cd12037    1 FVKCHFDYDPSSDSLIPCKeaGLKFRAGDLLQIVNQEDPNWWQACHV----EGGSAGLIPSQ 58
SH3_Src_like cd11845
Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members ...
559-616 2.08e-10

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: 56.82  E-value: 2.08e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 688560287 559 VRALFDYD-ITKDSglpsqgLNFRFGDILHVLNASDEEWWQARHVTTDGEmeemGVIPS 616
Cdd:cd11845    2 YVALYDYEaRTDDD------LSFKKGDRLQILDDSDGDWWLARHLSTGKE----GYIPS 50
SH3_MPP3 cd12039
Src Homology 3 domain of Membrane Protein, Palmitoylated 3 (or MAGUK p55 subfamily member 3); ...
558-618 4.01e-10

Src Homology 3 domain of Membrane Protein, Palmitoylated 3 (or MAGUK p55 subfamily member 3); MPP3 is a scaffolding protein that colocalizes with MPP5 and CRB1 at the subdpical region adjacent to adherens junctions and may function in photoreceptor polarity. It interacts with some nectins and regulates their trafficking and processing. Nectins are cell-cell adhesion proteins involved in the establishment apical-basal polarity at cell adhesion sites. It is one of seven vertebrate homologs of the Drosophila Stardust protein, which is required in establishing cell polarity, and it contains two L27 domains followed by the core of three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the 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: 212972  Cd Length: 62  Bit Score: 56.12  E-value: 4.01e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688560287 558 YVRALFDYDITKDSGLPSQ--GLNFRFGDILHVLNASDEEWWQARHVttdGEME-EMGVIPSKK 618
Cdd:cd12039    1 FMRALFDYNPYEDRAIPCQeaGLPFKRRDILEVVSQDDPTWWQAKRV---GDTNlRAGLIPSKQ 61
SH3_MPP4 cd12034
Src Homology 3 domain of Membrane Protein, Palmitoylated 4 (or MAGUK p55 subfamily member 4); ...
558-616 4.41e-10

Src Homology 3 domain of Membrane Protein, Palmitoylated 4 (or MAGUK p55 subfamily member 4); MPP4, also called Disks Large homolog 6 (DLG6) or Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 5 protein (ALS2CR5), is a retina-specific scaffolding protein that plays a role in organizing presynaptic protein complexes in the photoreceptor synapse, where it localizes to the plasma membrane. It is required in the proper localization of calcium ATPases and for maintenance of calcium homeostasis. MPP4 is one of seven vertebrate homologs of the Drosophila Stardust protein, which is required in establishing cell polarity, and it contains two L27 domains followed by the core of three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the 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: 212967  Cd Length: 61  Bit Score: 56.06  E-value: 4.41e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688560287 558 YVRALFDYDITKDSGLP--SQGLNFRFGDILHVLNASDEEWWQARHVTTDGEMEemGVIPS 616
Cdd:cd12034    1 YVRAMVDYWPQQDPSIPcaDAGLPFRKGDILQIVDQNDSLWWQARKLSDLAACA--GLIPS 59
PDZ_CTP_protease cd00988
PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ...
447-514 5.28e-10

PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in posttranslational protein processing, maturation, and disassembly or degradation, in Bacteria, Archaea, and plant chloroplasts. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238488 [Multi-domain]  Cd Length: 85  Bit Score: 56.47  E-value: 5.28e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688560287 447 TGLGFNIvgGEDGEGIFISFILAGGPADLCGeLRKGDRIVSVNGVDLRSATHEQAAAALKN-AGQTVTI 514
Cdd:cd00988    2 GGIGLEL--KYDDGGLVITSVLPGSPAAKAG-IKAGDIIVAIDGEPVDGLSLEDVVKLLRGkAGTKVRL 67
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
203-270 1.92e-09

PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. Heterodimerization through PDZ-PDZ domain interactions adds to the domain's versatility, and PDZ domain-mediated interactions may be modulated dynamically through target phosphorylation. Some PDZ domains play a role in scaffolding supramolecular complexes. PDZ domains are found in diverse signaling proteins in bacteria, archebacteria, and eurkayotes. This CD contains two distinct structural subgroups with either a N- or C-terminal beta-strand forming the peptide-binding groove base. The circular permutation placing the strand on the N-terminus appears to be found in Eumetazoa only, while the C-terminal variant is found in all three kingdoms of life, and seems to co-occur with protease domains. PDZ domains have been named after PSD95(post synaptic density protein), DlgA (Drosophila disc large tumor suppressor), and ZO1, a mammalian tight junction protein.


Pssm-ID: 238080 [Multi-domain]  Cd Length: 70  Bit Score: 54.62  E-value: 1.92e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688560287 203 SGLGFSIAGGTDNPhigedpsIFITKIIPGGAAAQDGrLRVNDCILRVNDVDVRDVTHSNAVEALKEA 270
Cdd:cd00136    1 GGLGFSIRGGTEGG-------VVVLSVEPGSPAERAG-LQAGDVILAVNGTDVKNLTLEDVAELLKKE 60
SH3_MPP6 cd12038
Src Homology 3 domain of Membrane Protein, Palmitoylated 6 (or MAGUK p55 subfamily member 6); ...
558-617 2.07e-09

Src Homology 3 domain of Membrane Protein, Palmitoylated 6 (or MAGUK p55 subfamily member 6); MPP6, also called Veli-associated MAGUK 1 (VAM-1) or PALS2, is a scaffolding protein that binds to Veli-1, a homolog of Caenorhabditis Lin-7. It is one of seven vertebrate homologs of the Drosophila Stardust protein, which is required in establishing cell polarity, and it contains two L27 domains followed by the core of three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). In addition, it also contains the Hook (Protein 4.1 Binding) motif in between the SH3 and GuK domains. The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the 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: 212971  Cd Length: 61  Bit Score: 54.30  E-value: 2.07e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688560287 558 YVRALFDYDITKDSGLPSQ--GLNFRFGDILHVLNASDEEWWQARHVTTDGemeEMGVIPSK 617
Cdd:cd12038    1 FVKCHFDYNPYNDNLIPCKeaGLKFSKGEILQIVNREDPNWWQASHVKEGG---SAGLIPSQ 59
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
558-616 8.52e-09

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: 52.16  E-value: 8.52e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 688560287   558 YVRALFDYDITKDsglpsQGLNFRFGDILHVLNASDEEWWQARHVTtdgemEEMGVIPS 616
Cdd:smart00326   4 QVRALYDYTAQDP-----DELSFKKGDIITVLEKSDDGWWKGRLGR-----GKEGLFPS 52
gmk PRK14737
guanylate kinase; Provisional
714-883 2.58e-08

guanylate kinase; Provisional


Pssm-ID: 173199  Cd Length: 186  Bit Score: 54.61  E-value: 2.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287 714 ILGPMKDRINDDLISEFPDKFGScVPHTTRPKRDYEVDGRDYHFVnSREQMEKDIQDHKFIEAGQYNNHLYGTSVQSVRE 793
Cdd:PRK14737  12 VAGGGKSTIIQALLEEHPDFLFS-ISCTTRAPRPGDEEGKTYFFL-TIEEFKKGIADGEFLEWAEVHDNYYGTPKAFIED 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287 794 VAEKGKHCILDVSGNAIKRLQlaQLYP---IAVFIKPKSVEnilEMNKRLME-----EQGRKTYDRAMKLEQEFLEHFTA 865
Cdd:PRK14737  90 AFKEGRSAIMDIDVQGAKIIK--EKFPeriVTIFIEPPSEE---EWEERLIHrgtdsEESIEKRIENGIIELDEANEFDY 164
                        170
                 ....*....|....*...
gi 688560287 866 IVQGDTLEEIYNQVKQII 883
Cdd:PRK14737 165 KIINDDLEDAIADLEAII 182
SH3_CRK_N cd11758
N-terminal Src Homology 3 domain of Ct10 Regulator of Kinase adaptor proteins; CRK adaptor ...
558-615 4.62e-07

N-terminal Src Homology 3 domain of Ct10 Regulator of Kinase adaptor proteins; CRK adaptor proteins consists of SH2 and SH3 domains, which bind tyrosine-phosphorylated peptides and proline-rich motifs, respectively. They function downstream of protein tyrosine kinases in many signaling pathways started by various extracellular signals, including growth and differentiation factors. Cellular CRK (c-CRK) contains a single SH2 domain, followed by N-terminal and C-terminal SH3 domains. It is involved in the regulation of many cellular processes including cell growth, motility, adhesion, and apoptosis. CRK has been implicated in the malignancy of various human cancers. The N-terminal SH3 domain of CRK binds a number of target proteins including DOCK180, C3G, SOS, and cABL. The CRK family includes two alternatively spliced protein forms, CRKI and CRKII, that are expressed by the CRK gene, and the CRK-like (CRKL) protein, which is expressed by a distinct gene (CRKL). 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: 212692 [Multi-domain]  Cd Length: 55  Bit Score: 47.36  E-value: 4.62e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 688560287 558 YVRALFDYDITKDSGLPsqglnFRFGDILHVLNASDEEWWQARHvtTDGemeEMGVIP 615
Cdd:cd11758    2 YVRALFDFPGNDDEDLP-----FKKGEILTVIRKPEEQWWNARN--SEG---KTGMIP 49
PDZ_CTP_protease cd00988
PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ...
224-283 5.17e-07

PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in posttranslational protein processing, maturation, and disassembly or degradation, in Bacteria, Archaea, and plant chloroplasts. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238488 [Multi-domain]  Cd Length: 85  Bit Score: 47.99  E-value: 5.17e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688560287 224 IFITKIIPGGAAAQDGrLRVNDCILRVNDVDVRDVTHSNAVEALK-EAGCIVRLYVRRRKP 283
Cdd:cd00988   15 LVITSVLPGSPAAKAG-IKAGDIIVAIDGEPVDGLSLEDVVKLLRgKAGTKVRLTLKRGDG 74
SH3_Fyn_Yrk cd12006
Src homology 3 domain of Fyn and Yrk Protein Tyrosine Kinases; Fyn and Yrk (Yes-related kinase) ...
556-616 5.73e-07

Src homology 3 domain of Fyn and Yrk Protein Tyrosine Kinases; Fyn and Yrk (Yes-related kinase) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src kinases 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). 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: 212939 [Multi-domain]  Cd Length: 56  Bit Score: 47.35  E-value: 5.73e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688560287 556 TLYVrALFDYDI-TKDSglpsqgLNFRFGDILHVLNASDEEWWQARHVTTDGEmeemGVIPS 616
Cdd:cd12006    1 TLFV-ALYDYEArTEDD------LSFHKGEKFQILNSSEGDWWEARSLTTGET----GYIPS 51
PDZ_serine_protease cd00987
PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins ...
455-514 5.98e-07

PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins involved in heat-shock response, chaperone function, and apoptosis. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238487 [Multi-domain]  Cd Length: 90  Bit Score: 48.02  E-value: 5.98e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287 455 GGEDGEGIFISFILAGGPADLCGeLRKGDRIVSVNGVDLRSATHEQAAAALKNAGQTVTI 514
Cdd:cd00987   19 GLKDTKGVLVASVDPGSPAAKAG-LKPGDVILAVNGKPVKSVADLRRALAELKPGDKVTL 77
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
558-616 9.36e-07

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: 46.30  E-value: 9.36e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 688560287 558 YVRALFDYDitkdsGLPSQGLNFRFGDILHVLNASDEEWWQARHVTtdgemEEMGVIPS 616
Cdd:cd00174    1 YARALYDYE-----AQDDDELSFKKGDIITVLEKDDDGWWEGELNG-----GREGLFPA 49
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
560-616 9.75e-07

SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organisation. 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: 46.04  E-value: 9.75e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 688560287  560 RALFDYDITKDSGLPsqglnFRFGDILHVLNASDEEWWQARhVTTDGEmeemGVIPS 616
Cdd:pfam00018   1 VALYDYTAQEPDELS-----FKKGDIIIVLEKSEDGWWKGR-NKGGKE----GLIPS 47
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
298-373 2.77e-06

PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. Heterodimerization through PDZ-PDZ domain interactions adds to the domain's versatility, and PDZ domain-mediated interactions may be modulated dynamically through target phosphorylation. Some PDZ domains play a role in scaffolding supramolecular complexes. PDZ domains are found in diverse signaling proteins in bacteria, archebacteria, and eurkayotes. This CD contains two distinct structural subgroups with either a N- or C-terminal beta-strand forming the peptide-binding groove base. The circular permutation placing the strand on the N-terminus appears to be found in Eumetazoa only, while the C-terminal variant is found in all three kingdoms of life, and seems to co-occur with protease domains. PDZ domains have been named after PSD95(post synaptic density protein), DlgA (Drosophila disc large tumor suppressor), and ZO1, a mammalian tight junction protein.


Pssm-ID: 238080 [Multi-domain]  Cd Length: 70  Bit Score: 45.76  E-value: 2.77e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688560287 298 KGLGFSIAGGvgnqhipGDNSIYITKIIEGGAAHKDGrLQIGDKLLAVNAVCLEEVTHEDAVAALKNTP-DVVYLKV 373
Cdd:cd00136    1 GGLGFSIRGG-------TEGGVVVLSVEPGSPAERAG-LQAGDVILAVNGTDVKNLTLEDVAELLKKEVgEKVTLTV 69
SH3_GRAP_C cd11951
C-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor ...
558-600 5.15e-06

C-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 C-terminal SH3 domains (SH3c) of the related proteins, GRB2 and GRAP2, have been shown to bind to classical PxxP motif ligands, as well as to non-classical motifs. GRB2 SH3c binds Gab2 (Grb2-associated binder 2) through epitopes containing RxxK motifs, while the SH3c of GRAP2 binds to the phosphatase-like protein HD-PTP via a RxxxxK motif. SH3 domains are protein interaction domains that typically 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: 212884  Cd Length: 53  Bit Score: 44.41  E-value: 5.15e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 688560287 558 YVRALFDYDITKDSGLPsqglnFRFGDILHVLNASDEEWWQAR 600
Cdd:cd11951    1 FVQAQYDFSAEDPSQLS-----FRRGDIIEVLDCPDPNWWRGR 38
SH3_Sdc25 cd11883
Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors; This subfamily is ...
558-622 5.68e-06

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: 44.19  E-value: 5.68e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688560287 558 YVRALFDYDITKDSGLPsqglnFRFGDILHVLNASDEEWWqarhvttDGEmeemgVIPSKKRVER 622
Cdd:cd11883    1 VVVALYDFTPKSKNQLS-----FKAGDIIYVLNKDPSGWW-------DGV-----IISSSGKVKR 48
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
463-515 6.54e-06

PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 44.06  E-value: 6.54e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 688560287  463 FISFILAGGPADLCGeLRKGDRIVSVNGVDLRSAthEQAAAALKNAGQTVTII 515
Cdd:pfam17820   1 VVTAVVPGSPAERAG-LRVGDVILAVNGKPVRSL--EDVARLLQGSAGESVTL 50
SH3_GRB2_like_C cd11805
C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related ...
558-600 7.45e-06

C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related proteins; This family includes the adaptor protein GRB2 and related proteins including Drosophila melanogaster Downstream of receptor kinase (DRK), Caenorhabditis elegans Sex muscle abnormal protein 5 (Sem-5), GRB2-related adaptor protein (GRAP), GRAP2, and similar proteins. Family members contain an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. GRB2/Sem-5/DRK is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. GRAP2 plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. GRAP acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. The C-terminal SH3 domains (SH3c) of GRB2 and GRAP2 have been shown to bind to classical PxxP motif ligands, as well as to non-classical motifs. GRB2 SH3c binds Gab2 (Grb2-associated binder 2) through epitopes containing RxxK motifs, while the SH3c of GRAP2 binds to the phosphatase-like protein HD-PTP via a RxxxxK motif. SH3 domains are protein interaction domains that typically 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: 212739 [Multi-domain]  Cd Length: 53  Bit Score: 43.77  E-value: 7.45e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 688560287 558 YVRALFDYDITKdsglPSQgLNFRFGDILHVLNASDEEWWQAR 600
Cdd:cd11805    1 RVQALYDFNPQE----PGE-LEFRRGDIITVLDSSDPDWWKGE 38
SH3_GRB2_C cd11949
C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2; GRB2 is a critical ...
558-598 9.87e-06

C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2; GRB2 is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. It is ubiquitously expressed in all tissues throughout development and is important in cell cycle progression, motility, morphogenesis, and angiogenesis. In lymphocytes, GRB2 is associated with antigen receptor signaling components. GRB2 contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The C-terminal SH3 domain of GRB2 binds to Gab2 (Grb2-associated binder 2) through epitopes containing RxxK motifs, as well as to the proline-rich C-terminus of FGRF2. SH3 domains are protein interaction domains that typically 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: 212882 [Multi-domain]  Cd Length: 53  Bit Score: 43.67  E-value: 9.87e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 688560287 558 YVRALFDYDITKDSGLpsqglNFRFGDILHVLNASDEEWWQ 598
Cdd:cd11949    1 YVQALFDFDPQEDGEL-----GFRRGDFIEVMDNSDPNWWK 36
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
225-280 1.57e-05

PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 42.90  E-value: 1.57e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 688560287  225 FITKIIPGGAAAQDGrLRVNDCILRVNDVDVRDVTHsnAVEALKE-AGCIVRLYVRR 280
Cdd:pfam17820   1 VVTAVVPGSPAERAG-LRVGDVILAVNGKPVRSLED--VARLLQGsAGESVTLTVRR 54
SH3_ZO cd11859
Src homology 3 domain of the Tight junction proteins, Zonula occludens (ZO) proteins; ZO ...
558-621 1.97e-05

Src homology 3 domain of the Tight junction proteins, Zonula occludens (ZO) proteins; ZO proteins are scaffolding proteins that associate with each other and with other proteins of the tight junction, zonula adherens, and gap junctions. They play roles in regulating cytoskeletal dynamics at these cell junctions. They are considered members of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. Vertebrates contain three ZO proteins (ZO-1, ZO-2, and ZO-3) with redundant and non-redundant roles. They contain three PDZ domains, followed by SH3 and GuK domains; in addition, ZO-1 and ZO-2 contains a proline-rich (PR) actin binding domain at the C-terminus while ZO-3 contains this PR domain between the second and third PDZ domains. The C-terminal regions of the three ZO proteins are unique. The SH3 domain of ZO-1 has been shown to bind ZONAB, ZAK, afadin, and Galpha12. 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: 212793  Cd Length: 62  Bit Score: 43.05  E-value: 1.97e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688560287 558 YVRALFDYDitkdsGLPSQGLNFRFGDILHVLNASDEE---WWQARHVTTDGEMEEMGVIPSKKRVE 621
Cdd:cd11859    1 YIRTHFDYE-----KPAKGELSFKKGEVFHVVDTLYQGtvgSWQAVRVGRNHQELERGVIPNKSRAE 62
SH3_STAM cd11820
Src homology 3 domain of Signal Transducing Adaptor Molecules; STAMs were discovered as ...
559-598 2.70e-05

Src homology 3 domain of Signal Transducing Adaptor Molecules; STAMs were discovered as proteins that are highly phosphorylated following cytokine and growth factor stimulation. They function in cytokine signaling and surface receptor degradation, as well as regulate Golgi morphology. They associate with many proteins including Jak2 and Jak3 tyrosine kinases, Hrs, AMSH, and UBPY. STAM adaptor proteins contain VHS (Vps27, Hrs, STAM homology), ubiquitin interacting (UIM), and SH3 domains. There are two vertebrate STAMs, STAM1 and STAM2, which may be functionally redundant; vertebrate STAMs contain ITAM motifs. They are part of the endosomal sorting complex required for transport (ESCRT-0). STAM2 deficiency in mice did not cause any obvious abnormality, while STAM1 deficiency resulted in growth retardation. Loss of both STAM1 and STAM2 in mice proved lethal, indicating that STAMs are important for embryonic development. 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: 212754 [Multi-domain]  Cd Length: 54  Bit Score: 42.45  E-value: 2.70e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 688560287 559 VRALFDYDITKDSGLpsqglNFRFGDILHVLNASDEEWWQ 598
Cdd:cd11820    3 VRALYDFEAAEDNEL-----TFKAGEIITVLDDSDPNWWK 37
SH3_Yes cd12007
Src homology 3 domain of Yes Protein Tyrosine Kinase; Yes (or c-Yes) is a member of the Src ...
556-616 6.03e-05

Src homology 3 domain of Yes Protein Tyrosine Kinase; Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases 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). 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: 212940 [Multi-domain]  Cd Length: 58  Bit Score: 41.56  E-value: 6.03e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688560287 556 TLYVrALFDYDitkdsGLPSQGLNFRFGDILHVLNASDEEWWQARHVTTDgemeEMGVIPS 616
Cdd:cd12007    1 TIFV-ALYDYE-----ARTTEDLSFKKGERFQIINNTEGDWWEARSIATG----KNGYIPS 51
SH3_DLG5 cd11860
Src homology 3 domain of Disks Large homolog 5; DLG5 is a multifunctional scaffold protein ...
558-621 6.29e-05

Src homology 3 domain of Disks Large homolog 5; DLG5 is a multifunctional scaffold protein that is located at sites of cell-cell contact and is involved in the maintenance of cell shape and polarity. Mutations in the DLG5 gene are associated with Crohn's disease (CD) and inflammatory bowel disease (IBD). DLG5 is a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. DLG5 contains 4 PDZ domains as well as an N-terminal domain of unknown function. 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: 212794  Cd Length: 63  Bit Score: 41.56  E-value: 6.29e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287 558 YVRALFDYditkdSGLPSQGLNFRFGDILHV----LNASDEEW--WQARHvttDGEMEEMGVIPSKKRVE 621
Cdd:cd11860    1 YVRALFDR-----SAENEDELSFKKDDILYVdntmFNGVFGQWraWLVDE---EGRKRKCGIIPSKYKVE 62
PDZ_CTP_protease cd00988
PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ...
306-378 6.86e-05

PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in posttranslational protein processing, maturation, and disassembly or degradation, in Bacteria, Archaea, and plant chloroplasts. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238488 [Multi-domain]  Cd Length: 85  Bit Score: 42.21  E-value: 6.86e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688560287 306 GGVGNQHIPGDNSIYITKIIEGGAAHKDGrLQIGDKLLAVNAVCLEEVTHEDAVAALKNTP-DVVYLKVAKPTS 378
Cdd:cd00988    2 GGIGLELKYDDGGLVITSVLPGSPAAKAG-IKAGDIIVAIDGEPVDGLSLEDVVKLLRGKAgTKVRLTLKRGDG 74
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
558-621 7.56e-05

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


Pssm-ID: 429575 [Multi-domain]  Cd Length: 54  Bit Score: 41.04  E-value: 7.56e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688560287  558 YVRALFDYDitkdsGLPSQGLNFRFGDILHVLNASDEEWWQARhvttdgEMEEMGVIPSKKRVE 621
Cdd:pfam07653   1 YGRVIFDYV-----GTDKNGLTLKKGDVVKVLGKDNDGWWEGE------TGGRVGLVPSTAVEE 53
SH3_STAM1 cd11964
Src homology 3 domain of Signal Transducing Adaptor Molecule 1; STAM1 is part of the endosomal ...
559-616 9.32e-05

Src homology 3 domain of Signal Transducing Adaptor Molecule 1; STAM1 is part of the endosomal sorting complex required for transport (ESCRT-0) and is involved in sorting ubiquitinated cargo proteins from the endosome. It may also be involved in the regulation of IL2 and GM-CSF mediated signaling, and has been implicated in neural cell survival. STAMs were discovered as proteins that are highly phosphorylated following cytokine and growth factor stimulation. They function in cytokine signaling and surface receptor degradation, as well as regulate Golgi morphology. They associate with many proteins including Jak2 and Jak3 tyrosine kinases, Hrs, AMSH, and UBPY. STAM adaptor proteins contain VHS (Vps27, Hrs, STAM homology), ubiquitin interacting (UIM), and SH3 domains. 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: 212897 [Multi-domain]  Cd Length: 55  Bit Score: 40.70  E-value: 9.32e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 688560287 559 VRALFDYDITKDSGLpsqglNFRFGDILHVLNASDEEWWQarhvttdGEMEE-MGVIPS 616
Cdd:cd11964    3 VRAIYDFEAAEDNEL-----TFKAGDIITILDDSDPNWWK-------GETPQgTGLFPS 49
SH3_STAM2 cd11963
Src homology 3 domain of Signal Transducing Adaptor Molecule 2; STAM2, also called EAST ...
559-601 1.11e-04

Src homology 3 domain of Signal Transducing Adaptor Molecule 2; STAM2, also called EAST (Epidermal growth factor receptor-associated protein with SH3 and TAM domain) or Hbp (Hrs binding protein), is part of the endosomal sorting complex required for transport (ESCRT-0). It plays a role in sorting mono-ubiquinated endosomal cargo for trafficking to the lysosome for degradation. It is also involved in the regulation of exocytosis. STAMs were discovered as proteins that are highly phosphorylated following cytokine and growth factor stimulation. They function in cytokine signaling and surface receptor degradation, as well as regulate Golgi morphology. They associate with many proteins including Jak2 and Jak3 tyrosine kinases, Hrs, AMSH, and UBPY. STAM adaptor proteins contain VHS (Vps27, Hrs, STAM homology), ubiquitin interacting (UIM), and SH3 domains. 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: 212896 [Multi-domain]  Cd Length: 57  Bit Score: 40.77  E-value: 1.11e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 688560287 559 VRALFDYDITKDSGLpsqglNFRFGDILHVLNASDEEWWQARH 601
Cdd:cd11963    4 VRALYDFEAVEDNEL-----TFKHGEIIIVLDDSDANWWKGEN 41
SH3_CACNB cd11863
Src Homology 3 domain of Voltage-dependent L-type calcium channel subunit beta; ...
559-616 1.14e-04

Src Homology 3 domain of Voltage-dependent L-type calcium channel subunit beta; Voltage-dependent calcium channels (Ca(V)s) are multi-protein complexes that regulate the entry of calcium into cells. They impact muscle contraction, neuronal migration, hormone and neurotransmitter release, and the activation of calcium-dependent signaling pathways. They are composed of four subunits: alpha1, alpha2delta, beta, and gamma. The beta subunit is a soluble and intracellular protein that interacts with the transmembrane alpha1 subunit. It facilitates the trafficking and proper localization of the alpha1 subunit to the cellular plasma membrane. Vertebrates contain four different beta subunits from distinct genes (beta1-4); each exists as multiple splice variants. All are expressed in the brain while other tissues show more specific expression patterns. The beta subunits show similarity to MAGUK (membrane-associated guanylate kinase) proteins in that they contain SH3 and inactive guanylate kinase (GuK) domains; however, they do not appear to contain a PDZ 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: 212797  Cd Length: 62  Bit Score: 40.72  E-value: 1.14e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287 559 VRALFDYDITKDSGLPSQGLNFRFG--DILHVLNASDEEWWQARHVttdGEMEEMGVIPS 616
Cdd:cd11863    3 VRTNVGYDGSLDDDSPVPGYAVSFEakDFLHIKEKYNNDWWIGRLV---KEGCDIGFIPS 59
PDZ_serine_protease cd00987
PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins ...
224-280 1.23e-04

PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins involved in heat-shock response, chaperone function, and apoptosis. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238487 [Multi-domain]  Cd Length: 90  Bit Score: 41.47  E-value: 1.23e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 688560287 224 IFITKIIPGGAAAQDGrLRVNDCILRVNDVDVRDVTHSNAVEALKEAGCIVRLYVRR 280
Cdd:cd00987   26 VLVASVDPGSPAAKAG-LKPGDVILAVNGKPVKSVADLRRALAELKPGDKVTLTVLR 81
SH3_ARHGEF9_like cd11828
Src homology 3 domain of ARHGEF9-like Rho guanine nucleotide exchange factors; Members of this ...
558-606 1.62e-04

Src homology 3 domain of ARHGEF9-like Rho guanine nucleotide exchange factors; Members of this family contain a SH3 domain followed by RhoGEF (also called Dbl-homologous or DH) and Pleckstrin Homology (PH) domains. They include the Rho guanine nucleotide exchange factors ARHGEF9, ASEF (also called ARHGEF4), ASEF2, and similar proteins. GEFs activate small GTPases by exchanging bound GDP for free GTP. ARHGEF9 specifically activates Cdc42, while both ASEF and ASEF2 can activate Rac1 and Cdc42. ARHGEF9 is highly expressed in the brain and it interacts with gephyrin, a postsynaptic protein associated with GABA and glycine receptors. ASEF plays a role in angiogenesis and cell migration. ASEF2 is important in cell migration and adhesion dynamics. ASEF exists in an autoinhibited form and is activated upon binding of the tumor suppressor APC (adenomatous polyposis coli), leading to the activation of Rac1 or Cdc42. In its autoinhibited form, the SH3 domain of ASEF forms an extensive interface with the DH and PH domains, blocking the Rac 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: 212762  Cd Length: 53  Bit Score: 40.06  E-value: 1.62e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 688560287 558 YVRALFDYdITKDSglpsQGLNFRFGDILHVLNASDEEWWQARHVTTDG 606
Cdd:cd11828    1 LAEALWDH-VTMDP----EELGFKAGDVIEVLDMSDKDWWWGSIRDEEG 44
SH3_ASEF2 cd11974
Src homology 3 domain of APC-Stimulated guanine nucleotide Exchange Factor 2; ASEF2, also ...
557-600 2.18e-04

Src homology 3 domain of APC-Stimulated guanine nucleotide Exchange Factor 2; ASEF2, also called Spermatogenesis-associated protein 13 (SPATA13), is a GEF that localizes with actin at the leading edge of cells and is important in cell migration and adhesion dynamics. GEFs activate small GTPases by exchanging bound GDP for free GTP. ASEF2 can activate both Rac 1 and Cdc42, but only Rac1 activation is necessary for increased cell migration and adhesion turnover. Together with APC (adenomatous polyposis coli) and Neurabin2, a scaffold protein that binds F-actin, it is involved in regulating HGF-induced cell migration. ASEF2 contains a SH3 domain followed by RhoGEF (also called Dbl-homologous or DH) and Pleckstrin Homology (PH) domains. 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: 212907  Cd Length: 54  Bit Score: 39.66  E-value: 2.18e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 688560287 557 LYVRALFDYdITKDSglpsQGLNFRFGDILHVLNASDEEWWQAR 600
Cdd:cd11974    1 VYAEALWDH-VTMDD----QELAFKAGDVIRVLEASNKDWWWGR 39
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
455-514 3.01e-04

periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273938 [Multi-domain]  Cd Length: 428  Bit Score: 44.13  E-value: 3.01e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287  455 GGEDGEGIFISFILAGGPADLCGeLRKGDRIVSVNGVDLRSATHEQAAAALKNAGQTVTI 514
Cdd:TIGR02037 252 GLEKQRGALVAQVLPGSPAEKAG-LKAGDVITSVNGKPISSFADLRRAIGTLKPGKKVTL 310
SH3_Blk cd12009
Src homology 3 domain of Blk Protein Tyrosine Kinase; Blk is a member of the Src subfamily of ...
558-616 3.99e-04

Src homology 3 domain of Blk Protein Tyrosine Kinase; Blk is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. It is expressed specifically in B-cells and is involved in pre-BCR (B-cell receptor) signaling. Src kinases 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). 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: 212942 [Multi-domain]  Cd Length: 54  Bit Score: 39.03  E-value: 3.99e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 688560287 558 YVRALFDYDITKDSGLPsqglnFRFGDILHVLnASDEEWWQARHVTTDGEmeemGVIPS 616
Cdd:cd12009    1 CVIAQYDFVPSNERDLQ-----LKKGEKLQVL-KSDGEWWLAKSLTTGKE----GYIPS 49
SH3_ASPP cd11807
Src homology 3 domain of Apoptosis Stimulating of p53 proteins (ASPP); The ASPP family of ...
559-601 4.18e-04

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: 38.90  E-value: 4.18e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 688560287 559 VRALFDYDITKDSGLPsqglnFRFGDILHVLNASDE---EWWQARH 601
Cdd:cd11807    3 VYALFDYEAENGDELS-----FREGDELTVLRKGDDdetEWWWARL 43
SH3_Sla1p_1 cd11773
First Src Homology 3 domain of the fungal endocytic adaptor protein Sla1p; Sla1p facilitates ...
559-616 4.65e-04

First Src Homology 3 domain of the fungal endocytic adaptor protein Sla1p; Sla1p facilitates endocytosis by playing a role as an adaptor protein in coupling components of the actin cytoskeleton to the endocytic machinery. It interacts with Abp1p, Las17p and Pan1p, which are activator proteins of actin-related protein 2/3 (Arp2/3). Sla1p contains multiple domains including three SH3 domains, a SAM (sterile alpha motif) domain, and a Sla1 homology domain 1 (SHD1), which binds to the NPFXD motif that is found in many integral membrane proteins such as the Golgi-localized Arf-binding protein Lsb5p and the P4-ATPases, Drs2p and Dnf1p. 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: 212707 [Multi-domain]  Cd Length: 57  Bit Score: 38.94  E-value: 4.65e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688560287 559 VRALFDYDitkdsglpSQG---LNFRFGDILHVLNASDEEWWQAR-HVTTDGEMEEMGVIPS 616
Cdd:cd11773    2 YKALYDYE--------PQTedeLTIQEDDILYLLEKSDDDWWKVKlKVNSSDDDEPVGLVPA 55
SH3_ASEF cd11973
Src homology 3 domain of APC-Stimulated guanine nucleotide Exchange Factor; ASEF, also called ...
552-606 4.84e-04

Src homology 3 domain of APC-Stimulated guanine nucleotide Exchange Factor; ASEF, also called ARHGEF4, exists in an autoinhibited form and is activated upon binding of the tumor suppressor APC (adenomatous polyposis coli). GEFs activate small GTPases by exchanging bound GDP for free GTP. ASEF can activate Rac1 or Cdc42. Truncated ASEF, which is found in colorectal cancers, is constitutively active and has been shown to promote angiogenesis and cancer cell migration. ASEF contains a SH3 domain followed by RhoGEF (also called Dbl-homologous or DH) and Pleckstrin Homology (PH) domains. In its autoinhibited form, the SH3 domain of ASEF forms an extensive interface with the DH and PH domains, blocking the Rac 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: 212906 [Multi-domain]  Cd Length: 73  Bit Score: 39.62  E-value: 4.84e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 688560287 552 SQKRTLYVRALFDYdITKDSglpsQGLNFRFGDILHVLNASDEEWWQARHVTTDG 606
Cdd:cd11973   13 SDGSVVCAEALWDH-VTMDD----QELGFKAGDVIEVMDATNKEWWWGRVLDSEG 62
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
457-514 5.38e-04

C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 223864 [Multi-domain]  Cd Length: 406  Bit Score: 43.47  E-value: 5.38e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 688560287 457 EDGEGIFISFILAGGPADLCGeLRKGDRIVSVNGVDLRSATHEQAAAALKN-AGQTVTI 514
Cdd:COG0793  109 EDIGGVKVVSPIDGSPAAKAG-IKPGDVIIKIDGKSVGGVSLDEAVKLIRGkPGTKVTL 166
SH3_srGAP4 cd11956
Src homology 3 domain of Slit-Robo GTPase Activating Protein 4; srGAP4, also called ARHGAP4, ...
561-617 6.08e-04

Src homology 3 domain of Slit-Robo GTPase Activating Protein 4; srGAP4, also called ARHGAP4, is highly expressed in hematopoietic cells and may play a role in lymphocyte differentiation. It is able to stimulate the GTPase activity of Rac1, Cdc42, and RhoA. In the nervous system, srGAP4 has been detected in differentiating neurites and may be involved in axon and dendritic growth. srGAPs are Rho GAPs that interact with Robo1, the transmembrane receptor of Slit proteins. Slit proteins are secreted proteins that control axon guidance and the migration of neurons and leukocytes. srGAPs contain an N-terminal F-BAR domain, a Rho GAP 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: 212889  Cd Length: 55  Bit Score: 38.67  E-value: 6.08e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 688560287 561 ALFDYditkdSGLPSQGLNFRFGDILHVLNASDEEWWQARHVTTdgemeeMGVIPSK 617
Cdd:cd11956    6 ACFDY-----TGRTAQELSFKRGDVLLLHSKASSDWWRGEHNGM------RGLIPHK 51
SH3_GRAP2_C cd11950
C-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS ...
559-600 7.11e-04

C-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS (GRB2-related adapter downstream of Shc), GrpL, GRB2L, Mona, or GRID (Grb2-related protein with insert domain). It is expressed specifically in the hematopoietic system. It plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. It also has roles in antigen-receptor and tyrosine kinase mediated signaling. GRAP2 is unique from other GRB2-like adaptor proteins in that it can be regulated by caspase cleavage. It contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The C-terminal SH3 domain of GRAP2 binds to different motifs found in substrate peptides including the typical PxxP motif in hematopoietic progenitor kinase 1 (HPK1), the RxxK motif in SLP-76 and HPK1, and the RxxxxK motif in phosphatase-like protein HD-PTP. SH3 domains are protein interaction domains that typically 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: 212883  Cd Length: 53  Bit Score: 38.27  E-value: 7.11e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 688560287 559 VRALFDYDITKDSGLpsqglNFRFGDILHVLNASDEEWWQAR 600
Cdd:cd11950    2 VRALYDFEALEDDEL-----GFNSGDVIEVLDSSNPSWWKGR 38
SH3_OSTF1 cd11772
Src Homology 3 domain of metazoan osteoclast stimulating factor 1; OSTF1, also named OSF or ...
559-616 7.88e-04

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: 38.05  E-value: 7.88e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 688560287 559 VRALFDYDitkdsGLPSQGLNFRFGDILHVLNASDEEWWQArhvTTDGemeEMGVIPS 616
Cdd:cd11772    2 FRALYDYE-----AQHPDELSFEEGDLLYISDKSDPNWWKA---TCGG---KTGLIPS 48
SH3_SH3BP4 cd11757
Src Homology 3 domain of SH3 domain-binding protein 4; SH3 domain-binding protein 4 (SH3BP4) ...
578-616 1.04e-03

Src Homology 3 domain of SH3 domain-binding protein 4; SH3 domain-binding protein 4 (SH3BP4) is also called transferrin receptor trafficking protein (TTP). SH3BP4 is an endocytic accessory protein that interacts with endocytic proteins including clathrin and dynamin, and regulates the internalization of the transferrin receptor (TfR). 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: 212691  Cd Length: 52  Bit Score: 37.69  E-value: 1.04e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 688560287 578 LNFRFGDILHVLNASDEEWWQARHVTtdgemeEMGVIPS 616
Cdd:cd11757   16 LKFSKGDHLYVLDTSGGEWWYAHNTT------EMGYIPS 48
SH3_RUSC1 cd11958
Src homology 3 domain of RUN and SH3 domain-containing protein 1; RUSC1, also called NESCA ...
559-615 1.10e-03

Src homology 3 domain of RUN and SH3 domain-containing protein 1; RUSC1, also called NESCA (New molecule containing SH3 at the carboxy-terminus), is highly expressed in the brain and is translocated to the nuclear membrane from the cytoplasm upon stimulation with neurotrophin. It plays a role in facilitating neurotrophin-dependent neurite outgrowth. It also interacts with NEMO (or IKKgamma) and may function in NEMO-mediated activation of NF-kB. RUSC proteins are adaptor proteins consisting of RUN, leucine zipper, and SH3 domains. 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: 212891  Cd Length: 51  Bit Score: 37.89  E-value: 1.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 688560287 559 VRALFDYDITKDsglpsqGLNFRFGDILHVLNASDEEWWQARHvttdGEMEemGVIP 615
Cdd:cd11958    2 VRALCDHAGSES------QLSFRKGEELQVLGTVDEDWIRCRR----GDRE--GLVP 46
L27 smart00569
domain in receptor targeting proteins Lin-2 and Lin-7;
9-64 1.26e-03

domain in receptor targeting proteins Lin-2 and Lin-7;


Pssm-ID: 197794  Cd Length: 53  Bit Score: 37.49  E-value: 1.26e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 688560287     9 QRALQLLEEYQtklSQTGDPHLRLSIERvinIFKSTLFQALVDIQEYYEVSLQDTE 64
Cdd:smart00569   1 QRLLELLEELQ---SLLSPSEDLQELRR---LLQSPHLQALLKIHDKVAETELDPP 50
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
398-514 1.31e-03

Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 223343 [Multi-domain]  Cd Length: 347  Bit Score: 41.80  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287 398 MENHISTQSYLSQPLTPATPS-RYSPVSKGMLGDDEITREPRKIVLHRGTTGLGFNIvggEDGEGIFISFILAGGPADLC 476
Cdd:COG0265  210 INTAIIAPSGGSSGIGFAIPVnLVAPVLDELISKGKVVRGYLGVIGEPLTADIALGL---PVAAGAVVLGVLPGSPAAKA 286
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 688560287 477 GeLRKGDRIVSVNGVDLRSATHEQAAAALKNAGQTVTI 514
Cdd:COG0265  287 G-IKAGDIITAVNGKPVASLSDLVAAVASNRPGDEVAL 323
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
225-373 1.35e-03

periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273938 [Multi-domain]  Cd Length: 428  Bit Score: 42.21  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287  225 FITKIIPGGAAAQDGrLRVNDCILRVNDVDVRDVTH-SNAVEALKEAGCIVRLYVRRRKPLSekiMDVKLVKGPKG---- 299
Cdd:TIGR02037 260 LVAQVLPGSPAEKAG-LKAGDVITSVNGKPISSFADlRRAIGTLKPGKKVTLGILRKGKEKT---ITVTLGASPEEqass 335
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688560287  300 ----LGFSIA----GGVGNQHIPGD-NSIYITKIIEGGAAHKDGrLQIGDKLLAVNAVCLEEVTH-EDAVAALKNtPDVV 369
Cdd:TIGR02037 336 snpfLGLTVAnlspEIRKELRLKGDvKGVVVTKVVSGSPAARAG-LQPGDVILSVNQQPVSSVAElRKVLARAKK-GGRV 413

                  ....
gi 688560287  370 YLKV 373
Cdd:TIGR02037 414 ALLI 417
SH3_Tec_like cd11768
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed ...
559-616 1.50e-03

Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed in hepatocellular carcinoma) subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) tyr kinases containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Most Tec subfamily members (except Rlk) also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. The function of Tec kinases in lymphoid cells have been studied extensively. They play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and 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: 212702 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 1.50e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 688560287 559 VRALFDYDITKDSGLPsqglnFRFGDILHVLNASDEEWWQARhvttDGEMEEmGVIPS 616
Cdd:cd11768    2 VVALYDFQPIEPGDLP-----LEKGEEYVVLDDSNEHWWRAR----DKNGNE-GYIPS 49
SH3_ARHGAP9_like cd11888
Src Homology 3 domain of Rho GTPase-activating protein 9 and similar proteins; This subfamily ...
558-600 2.37e-03

Src Homology 3 domain of Rho GTPase-activating protein 9 and similar proteins; This subfamily is composed of Rho GTPase-activating proteins including mammalian ARHGAP9, and vertebrate ARHGAPs 12 and 27. RhoGAPs (or ARHGAPs) bind to Rho proteins and enhance the hydrolysis rates of bound GTP. ARHGAP9 functions as a GAP for Rac and Cdc42, but not for RhoA. It negatively regulates cell migration and adhesion. It also acts as a docking protein for the MAP kinases Erk2 and p38alpha, and may facilitate cross-talk between the Rho GTPase and MAPK pathways to control actin remodeling. ARHGAP27, also called CAMGAP1, shows GAP activity towards Rac1 and Cdc42. It binds the adaptor protein CIN85 and may play a role in clathrin-mediated endocytosis. ARHGAP12 has been shown to display GAP activity towards Rac1. It plays a role in regulating HFG-driven cell growth and invasiveness. ARHGAPs in this subfamily contain SH3, WW, Pleckstin homology (PH), and RhoGAP domains. 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: 212821  Cd Length: 54  Bit Score: 36.96  E-value: 2.37e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 688560287 558 YVRALFDYDITKDSGlpsQGLNFRFGDILHVLNASDEEWWQAR 600
Cdd:cd11888    1 YVVVLYPFEYTGKDG---RKVSIKEGERFLLLKKSNDDWWQVR 40
SH3_Abi cd11826
Src homology 3 domain of Abl Interactor proteins; Abl interactor (Abi) proteins are adaptor ...
558-598 2.89e-03

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: 36.53  E-value: 2.89e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 688560287 558 YVRALFDYDITKDSGLpsqglNFRFGDILHVLNASDEEWWQ 598
Cdd:cd11826    1 KVVALYDYTADKDDEL-----SFQEGDIIYVTKKNDDGWYE 36
COG3975 COG3975
Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];
456-521 3.06e-03

Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];


Pssm-ID: 226483 [Multi-domain]  Cd Length: 558  Bit Score: 41.27  E-value: 3.06e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688560287 456 GEDGEGIFISFILAGGPADLCGeLRKGDRIVSVNGVDLRSATHEqaaaalknAGQTVTIIAQYRPE 521
Cdd:COG3975  458 KSEGGHEKITFVFPGGPAYKAG-LSPGDKIVAINGISDQLDRYK--------VNDKIQVHVFREGR 514
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
320-375 4.90e-03

PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 35.97  E-value: 4.90e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 688560287  320 YITKIIEGGAAHKDGrLQIGDKLLAVNAVCLEEVthEDAVAALKNTPD-VVYLKVAK 375
Cdd:pfam17820   1 VVTAVVPGSPAERAG-LRVGDVILAVNGKPVRSL--EDVARLLQGSAGeSVTLTVRR 54
PDZ_metalloprotease cd00989
PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or ...
467-514 5.90e-03

PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or integral membrane proteases, which may be involved in signalling and regulatory mechanisms. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238489 [Multi-domain]  Cd Length: 79  Bit Score: 36.44  E-value: 5.90e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 688560287 467 ILAGGPADLCGeLRKGDRIVSVNGVDLRSAthEQAAAAL-KNAGQTVTI 514
Cdd:cd00989   19 VVPGSPAAKAG-LKAGDRILAINGQKIKSW--EDLVDAVqENPGKPLTL 64
SH3_ZO-3 cd12028
Src homology 3 domain of the Tight junction protein, Zonula occludens protein 3; ZO-3 is a ...
556-621 7.90e-03

Src homology 3 domain of the Tight junction protein, Zonula occludens protein 3; ZO-3 is a scaffolding protein that associates with other ZO proteins and other proteins of the tight junction, zonula adherens, and gap junctions. ZO proteins play roles in regulating cytoskeletal dynamics at these cell junctions. ZO-3 is critical for epidermal barrier function. It regulates cyclin D1-dependent cell proliferation. It is considered a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. The C-terminal region of ZO-3 is the smallest of the three ZO proteins. The SH3 domain of the related protein ZO-1 has been shown to bind ZONAB, ZAK, afadin, and Galpha12. 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: 212961  Cd Length: 65  Bit Score: 35.62  E-value: 7.90e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688560287 556 TLYVRALFDYDITkdsglPSQGLNFRFGDILHVLNASDEE---WWQARHVTTDGEMEEMGVIPSKKRVE 621
Cdd:cd12028    2 SFYIRTHFDYEPD-----PPSGLSFTRGEVFHVLDTMHRGklgSWLAVRMGRDLREMEKGIIPNQSRAE 65
SH3_PRMT2 cd11806
Src homology 3 domain of Protein arginine N-methyltransferase 2; PRMT2, also called HRMT1L1, ...
561-601 9.13e-03

Src homology 3 domain of Protein arginine N-methyltransferase 2; PRMT2, also called HRMT1L1, belongs to the arginine methyltransferase protein family. It functions as a coactivator to both estrogen receptor alpha (ER-alpha) and androgen receptor (AR), presumably through arginine methylation. The ER-alpha transcription factor is involved in cell proliferation, differentiation, morphogenesis, and apoptosis, and is also implicated in the development and progression of breast cancer. PRMT2 and its variants are upregulated in breast cancer cells and may be involved in modulating the ER-alpha signaling pathway during formation of breast cancer. PRMT2 also plays a role in regulating the function of E2F transcription factors, which are critical cell cycle regulators, by binding to the retinoblastoma gene product (RB). It contains an N-terminal SH3 domain and an AdoMet binding 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: 212740  Cd Length: 53  Bit Score: 35.06  E-value: 9.13e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 688560287 561 ALFDYDITKDSGLpsqglNFRFGDILHVLNASDEEWWQARH 601
Cdd:cd11806    4 AIADFVATDDSQL-----SFESGDKLLVLRKPSVDWWWAEH 39
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH