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Conserved domains on  [gi|564389920|ref|XP_006253485|]
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guanine nucleotide exchange factor DBS isoform X9 [Rattus norvegicus]

Protein Classification

guanine nucleotide exchange factor DBS( domain architecture ID 11271215)

guanine nucleotide exchange factor DBS, similar to Mus musculus guanine nucleotide exchange factor OSTIII; contains spectrin repeats, a rhoGEF (DH) domain and a PH domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH_Dbs cd01227
DBL's big sister protein pleckstrin homology (PH) domain; Dbs (also called MCF2-transforming ...
 791-922 5.36e-77

DBL's big sister protein pleckstrin homology (PH) domain; Dbs (also called MCF2-transforming sequence-like protein 2) is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a rhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 269934 [Multi-domain]  Cd Length: 126  Bit Score: 249.42  E-value: 5.36e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  791 AITGYDGNLGDLGKLLMQGSFSVWTDHKKGHTKvkELARFKPMQRHLFLHEKAVLFCKKREENGEgyekAPSYSYKQSLN 870
Cdd:cd01227     1 AITGYDGNLGDLGKLLMQGSFNVWTEHKKGHTK--KLARFKPMQRHIFLYEKAVLFCKKRGENGE----APSYSYKNSLN 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564389920  871 MTAVGITENVKGDTKKFEIWYNAREEVYIIQAPTPEIKAAWVNEIRKVLTSQ 922
Cdd:cd01227    75 TTAVGLTENVKGDTKKFEIWLNGREEVFIIQAPTPEIKAAWVKAIRQVLLSQ 126
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 607-784 2.28e-55

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


:

Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 190.20  E-value: 2.28e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  607 RRHVMNELLDTERAYVEELLCVLEGYAAEMDNPLMahlisTGLQNKKNILFGNMEEIYHFHnRIFLRELESCIDC----P 682
Cdd:cd00160     1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELL-----PLSPEEVELLFGNIEEIYEFH-RIFLKSLEERVEEwdksG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  683 ELVGRCFLERMEEFQIYEKYCQNKPRSESLWRQC-SDCPFFQECQKKLD---HKLSLDSYLLKPVQRITKYQLLLKEMLK 758
Cdd:cd00160    75 PRIGDVFLKLAPFFKIYSEYCSNHPDALELLKKLkKFNKFFQEFLEKAEsecGRLKLESLLLKPVQRLTKYPLLLKELLK 154

                         170       180
                  ....*....|....*....|....*..
gi 564389920  759 YSKH-CEGAEDLQEALSSILGILKAVN 784
Cdd:cd00160   155 HTPDgHEDREDLKKALEAIKEVASQVN 181
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 50-195 7.23e-28

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


:

Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 110.47  E-value: 7.23e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920     50 LKKRFAYLSGGRGQD--GSPVITFPDY--PAFSEIPDKEFQNVMTYLTSIPSLQDAGI---GFILVIDRRQDKWTSVKAS 122
Cdd:smart00516    2 LELLKAYIPGGRGYDkdGRPVLIERAGrfDLKSVTLEELLRYLVYVLEKILQEEKKTGgieGFTVIFDLKGLSMSNPDLS 81

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564389920    123 VLRIAAS-----FPANLQLVLVLRPTGFFqRTLSDIAFKFNRDEFKMKVPVMMLSSVPELHGYIDKSQLTEDLGGTLD 195
Cdd:smart00516   82 VLRKILKilqdhYPERLGKVYIINPPWFF-RVLWKIIKPFLDEKTREKIRFVGNDSKEELLEYIDKEQLPEELGGTLD 158
SH3_DBS cd11857
Src homology 3 domain of DBL's Big Sister (DBS), a guanine nucleotide exchange factor; DBS, ...
 1089-1141 6.95e-22

Src homology 3 domain of DBL's Big Sister (DBS), a guanine nucleotide exchange factor; DBS, also called MCF2L (MCF2-transforming sequence-like protein) or OST, is a Rho GTPase guanine nucleotide exchange factor (RhoGEF), facilitating the exchange of GDP and GTP. It was originally isolated from a cDNA screen for sequences that cause malignant growth. It plays roles in regulating clathrin-mediated endocytosis and cell migration through its activation of Rac1 and Cdc42. Depending on cell type, DBS can also activate RhoA and RhoG. DBS contains a Sec14-like domain, spectrin-like repeats, a RhoGEF [or Dbl homology (DH)] domain, a Pleckstrin homology (PH) domain, and an SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


:

Pssm-ID: 212791  Cd Length: 55  Bit Score: 89.65  E-value: 6.95e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564389920 1089 KYTVLMDGEKGGSDTLAMRSGDMVEVVEEGTEGLWYVRDLTSSKEGWVPASSL 1141
Cdd:cd11857     1 KYTVVADYEKGGPDDLTVKSGDLVQLIHEGDEGQWLVKNLSTRKEGWVPAANL 53
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 326-528 4.86e-16

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 78.26  E-value: 4.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  326 QLRHFEQGFREVKTALDSMSQKIAAfTDVGNSLAHVQHLLKDLTTFEEKSSVAVDKARALSLEGQQLIENRHYAVDSIHP 405
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  406 KCEELQHLCDHFASEVTRRRDLLSKSLELHSLLETS---MKWSDEGIFLLASQPVDKcqSQDGAEAALQEIEKFLET--G 480
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAddlEQWLEEKEAALASEDLGK--DLESVEELLKKHKELEEEleA 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564389920  481 AENKIQELNKIYKEYECILNQDLLEHVQKVF----QKQESTEEMFHRRQASL 528
Cdd:cd00176   158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLeelnERWEELLELAEERQKKL 209
 
Name Accession Description Interval E-value
PH_Dbs cd01227
DBL's big sister protein pleckstrin homology (PH) domain; Dbs (also called MCF2-transforming ...
 791-922 5.36e-77

DBL's big sister protein pleckstrin homology (PH) domain; Dbs (also called MCF2-transforming sequence-like protein 2) is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a rhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269934 [Multi-domain]  Cd Length: 126  Bit Score: 249.42  E-value: 5.36e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  791 AITGYDGNLGDLGKLLMQGSFSVWTDHKKGHTKvkELARFKPMQRHLFLHEKAVLFCKKREENGEgyekAPSYSYKQSLN 870
Cdd:cd01227     1 AITGYDGNLGDLGKLLMQGSFNVWTEHKKGHTK--KLARFKPMQRHIFLYEKAVLFCKKRGENGE----APSYSYKNSLN 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564389920  871 MTAVGITENVKGDTKKFEIWYNAREEVYIIQAPTPEIKAAWVNEIRKVLTSQ 922
Cdd:cd01227    75 TTAVGLTENVKGDTKKFEIWLNGREEVFIIQAPTPEIKAAWVKAIRQVLLSQ 126
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 607-784 2.28e-55

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 190.20  E-value: 2.28e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  607 RRHVMNELLDTERAYVEELLCVLEGYAAEMDNPLMahlisTGLQNKKNILFGNMEEIYHFHnRIFLRELESCIDC----P 682
Cdd:cd00160     1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELL-----PLSPEEVELLFGNIEEIYEFH-RIFLKSLEERVEEwdksG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  683 ELVGRCFLERMEEFQIYEKYCQNKPRSESLWRQC-SDCPFFQECQKKLD---HKLSLDSYLLKPVQRITKYQLLLKEMLK 758
Cdd:cd00160    75 PRIGDVFLKLAPFFKIYSEYCSNHPDALELLKKLkKFNKFFQEFLEKAEsecGRLKLESLLLKPVQRLTKYPLLLKELLK 154

                         170       180
                  ....*....|....*....|....*..
gi 564389920  759 YSKH-CEGAEDLQEALSSILGILKAVN 784
Cdd:cd00160   155 HTPDgHEDREDLKKALEAIKEVASQVN 181
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 610-785 1.23e-52

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 182.50  E-value: 1.23e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920    610 VMNELLDTERAYVEELLCVLEGYAAEMDNPLMahLIStglQNKKNILFGNMEEIYHFHnRIFLRELESCIDC----PELV 685
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELK--LLS---PNELETLFGNIEEIYEFH-RDFLDELEERIEEwddsVERI 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920    686 GRCFLERMEEFQIYEKYCQNKPRSESLWRQCSDCPFFQECQKKLDHK-----LSLDSYLLKPVQRITKYQLLLKEMLKYS 760
Cdd:smart00325   75 GDVFLKLEEFFKIYSEYCSNHPDALELLKKLKKNPRFQKFLKEIESSpqcrrLTLESLLLKPVQRLTKYPLLLKELLKHT 154

                           170       180
                    ....*....|....*....|....*.
gi 564389920    761 KH-CEGAEDLQEALSSILGILKAVND 785
Cdd:smart00325  155 PEdHEDREDLKKALKAIKELANQVNE 180
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 610-784 2.02e-47

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 167.48  E-value: 2.02e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920   610 VMNELLDTERAYVEELLCVLEGYAAEMDNPLMAHlistglQNKKNILFGNMEEIYHFHNRIFLRELESCIDCPELVGRCF 689
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSES------EEEIKTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIF 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920   690 LERMEEFQIYEKYCQNKPRSESLWRQCSD-----CPFFQECQK-KLDHKLSLDSYLLKPVQRITKYQLLLKEMLKYSKHC 763
Cdd:pfam00621   75 LKFAPGFKVYSTYCSNYPKALKLLKKLLKknpkfRAFLEELEAnPECRGLDLNSFLIKPVQRIPRYPLLLKELLKHTPPD 154

                          170       180
                   ....*....|....*....|..
gi 564389920   764 -EGAEDLQEALSSILGILKAVN 784
Cdd:pfam00621  155 hPDYEDLKKALEAIKEVAKQIN 176
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 50-195 7.23e-28

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 110.47  E-value: 7.23e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920     50 LKKRFAYLSGGRGQD--GSPVITFPDY--PAFSEIPDKEFQNVMTYLTSIPSLQDAGI---GFILVIDRRQDKWTSVKAS 122
Cdd:smart00516    2 LELLKAYIPGGRGYDkdGRPVLIERAGrfDLKSVTLEELLRYLVYVLEKILQEEKKTGgieGFTVIFDLKGLSMSNPDLS 81

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564389920    123 VLRIAAS-----FPANLQLVLVLRPTGFFqRTLSDIAFKFNRDEFKMKVPVMMLSSVPELHGYIDKSQLTEDLGGTLD 195
Cdd:smart00516   82 VLRKILKilqdhYPERLGKVYIINPPWFF-RVLWKIIKPFLDEKTREKIRFVGNDSKEELLEYIDKEQLPEELGGTLD 158
SH3_DBS cd11857
Src homology 3 domain of DBL's Big Sister (DBS), a guanine nucleotide exchange factor; DBS, ...
 1089-1141 6.95e-22

Src homology 3 domain of DBL's Big Sister (DBS), a guanine nucleotide exchange factor; DBS, also called MCF2L (MCF2-transforming sequence-like protein) or OST, is a Rho GTPase guanine nucleotide exchange factor (RhoGEF), facilitating the exchange of GDP and GTP. It was originally isolated from a cDNA screen for sequences that cause malignant growth. It plays roles in regulating clathrin-mediated endocytosis and cell migration through its activation of Rac1 and Cdc42. Depending on cell type, DBS can also activate RhoA and RhoG. DBS contains a Sec14-like domain, spectrin-like repeats, a RhoGEF [or Dbl homology (DH)] domain, a Pleckstrin homology (PH) domain, and an SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212791  Cd Length: 55  Bit Score: 89.65  E-value: 6.95e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564389920 1089 KYTVLMDGEKGGSDTLAMRSGDMVEVVEEGTEGLWYVRDLTSSKEGWVPASSL 1141
Cdd:cd11857     1 KYTVVADYEKGGPDDLTVKSGDLVQLIHEGDEGQWLVKNLSTRKEGWVPAANL 53
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 65-198 8.07e-18

Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain family. This family includes ECM25 that contains a divergent CRAL-TRIO domain identified by Gallego and colleagues.


Pssm-ID: 463965 [Multi-domain]  Cd Length: 140  Bit Score: 81.22  E-value: 8.07e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920    65 GSPVITFPDYPAFSE-IPDKEFQNVMTYLTSIPSLQDAGIGFILVIDRRQDKWTS------VKASVLRIAASFPANLQLV 137
Cdd:pfam13716    1 GRPVLVFISKLLPSRpASLDDLDRLLFYLLKTLSEKLKGKPFVVVVDHTGVTSENfpslsfLKKAYDLLPRAFKKNLKAV 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564389920   138 LVLRPTGFFQRTLSDIAFKFNRDEFKMKVpvMMLSSVPELHGYIDKSQLTEDLGGTLDYCH 198
Cdd:pfam13716   81 YVVHPSTFLRTFLKTLGSLLGSKKLRKKV--HYVSSLSELWEGIDREQLPTELPGVLSYDE 139
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 326-528 4.86e-16

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 78.26  E-value: 4.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  326 QLRHFEQGFREVKTALDSMSQKIAAfTDVGNSLAHVQHLLKDLTTFEEKSSVAVDKARALSLEGQQLIENRHYAVDSIHP 405
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  406 KCEELQHLCDHFASEVTRRRDLLSKSLELHSLLETS---MKWSDEGIFLLASQPVDKcqSQDGAEAALQEIEKFLET--G 480
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAddlEQWLEEKEAALASEDLGK--DLESVEELLKKHKELEEEleA 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564389920  481 AENKIQELNKIYKEYECILNQDLLEHVQKVF----QKQESTEEMFHRRQASL 528
Cdd:cd00176   158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLeelnERWEELLELAEERQKKL 209
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 45-193 6.77e-14

Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 469559 [Multi-domain]  Cd Length: 156  Bit Score: 70.44  E-value: 6.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920   45 DIQEQLKKrfAYLSGGRGQDGSPVITFPDYPAFSEIPDKE--FQNVMTYLTSIPSLQDAGI-GFILVIDRRQDKWTS--- 118
Cdd:cd00170     3 ELLELLGG--IGYLGGRDKEGRPVLVFRAGWDPPKLLDLEelLRYLVYLLEKALRELEEQVeGFVVIIDLKGFSLSNlsd 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564389920  119 ---VKASVLRIAASFPANLQLVLVLRPTGFFqRTLSDIAFKFNRDEFKMKVpVMMLSSVPELHGYIDKSQLTEDLGGT 193
Cdd:cd00170    81 lslLKKLLKILQDHYPERLKKIYIVNAPWIF-SALWKIVKPFLSEKTRKKI-VFLGSDLEELLEYIDPDQLPKELGGT 156
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 805-919 8.79e-12

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 62.57  E-value: 8.79e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920    805 LLMQGSFSVWTDHKKGHTKvkelarfkpmQRHLFLHEKAVLFCKKREENgegyekaPSYSYKQSLNMTAVGITENVKGDT 884
Cdd:smart00233    1 VIKEGWLYKKSGGGKKSWK----------KRYFVLFNSTLLYYKSKKDK-------KSYKPKGSIDLSGCTVREAPDPDS 63

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 564389920    885 KK----FEIWYNAREeVYIIQAPTPEIKAAWVNEIRKVL 919
Cdd:smart00233   64 SKkphcFEIKTSDRK-TLLLQAESEEEREKWVEALRKAI 101
SPEC smart00150
Spectrin repeats;
328-428 7.91e-11

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 60.04  E-value: 7.91e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920    328 RHFEQGFREVKTALDSMsQKIAAFTDVGNSLAHVQHLLKDLTTFEEKSSVAVDKARALSLEGQQLIENRHYAVDSIHPKC 407
Cdd:smart00150    1 QQFLRDADELEAWLEEK-EQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79

                            90       100
                    ....*....|....*....|.
gi 564389920    408 EELQHLCDHFASEVTRRRDLL 428
Cdd:smart00150   80 EELNERWEELKELAEERRQKL 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 805-919 5.30e-07

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 49.10  E-value: 5.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920   805 LLMQGSFSVWTDHKKGHTKvkelarfkpmQRHLFLHEKAVLFCKKREengegyeKAPSYSYKQSLNMTAVGITENVKGDT 884
Cdd:pfam00169    1 VVKEGWLLKKGGGKKKSWK----------KRYFVLFDGSLLYYKDDK-------SGKSKEPKGSISLSGCEVVEVVASDS 63

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 564389920   885 KK----FEIWYNAR--EEVYIIQAPTPEIKAAWVNEIRKVL 919
Cdd:pfam00169   64 PKrkfcFELRTGERtgKRTYLLQAESEEERKDWIKAIQSAI 104
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 328-428 4.10e-06

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 46.54  E-value: 4.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920   328 RHFEQGFREVKTALDSMSQKIAAFT--DVGNSLAHVQHLLKDLTTFEEKSSVAVDKARALSLEGQQLIENRHYAVDSIHP 405
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSseDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80

                           90       100
                   ....*....|....*....|...
gi 564389920   406 KCEELQHLCDHFASEVTRRRDLL 428
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKL 103
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 1086-1142 1.95e-05

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: 43.30  E-value: 1.95e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 564389920   1086 VPGKYTVLMDGEKGGSDTLAMRSGDMVEVVEEGTEGLWYVRdLTSSKEGWVPASSLA 1142
Cdd:smart00326    1 EGPQVRALYDYTAQDPDELSFKKGDIITVLEKSDDGWWKGR-LGRGKEGLFPSNYVE 56
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 605-853 2.72e-05

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 48.73  E-value: 2.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  605 ILRRHVMNELLDTERAYVEELlcvlEGYAAEMDNPLMA-HLISTglQNKKNIL---FGNMEEIYHFHNRIF--LRELESC 678
Cdd:COG5422   483 IKRQEAIYEVIYTERDFVKDL----EYLRDTWIKPLEEsNIIPE--NARRNFIkhvFANINEIYAVNSKLLkaLTNRQCL 556

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  679 IDCPELVGRCFLERMEEFQIYEKYCQNKPRSE-SLWRQCSDCPFFqecqKKLDH---------KLSLDSYLLKPVQRITK 748
Cdd:COG5422   557 SPIVNGIADIFLDYVPKFEPFIKYGASQPYAKyEFEREKSVNPNF----ARFDHeverldesrKLELDGYLTKPTTRLAR 632

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  749 YQLLLKEMLKYSKhcEGAEDLQEalssILGILKAVNDSMHLIAI-TGYDGNLGDLGKLLMQGSFSvwTDH---------- 817
Cdd:COG5422   633 YPLLLEEVLKFTD--PDNPDTED----IPKVIDMLREFLSRLNFeSGKAENRGDLFHLNQQLLFK--PEYvnlglndeyr 704

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 564389920  818 ---KKGHTKVKELARFKPMQR---HLFLHEKAVLFCKKREEN 853
Cdd:COG5422   705 kiiFKGVLKRKAKSKTDGSLRgdiQFFLLDNMLLFCKAKAVN 746
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 1091-1138 1.95e-04

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


Pssm-ID: 394975 [Multi-domain]  Cd Length: 47  Bit Score: 39.88  E-value: 1.95e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 564389920  1091 TVLMDGEKGGSDTLAMRSGDMVEVVEEGTEGLWYVRDLTsSKEGWVPA 1138
Cdd:pfam00018    1 VALYDYTAQEPDELSFKKGDIIIVLEKSEDGWWKGRNKG-GKEGLIPS 47
 
Name Accession Description Interval E-value
PH_Dbs cd01227
DBL's big sister protein pleckstrin homology (PH) domain; Dbs (also called MCF2-transforming ...
 791-922 5.36e-77

DBL's big sister protein pleckstrin homology (PH) domain; Dbs (also called MCF2-transforming sequence-like protein 2) is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a rhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269934 [Multi-domain]  Cd Length: 126  Bit Score: 249.42  E-value: 5.36e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  791 AITGYDGNLGDLGKLLMQGSFSVWTDHKKGHTKvkELARFKPMQRHLFLHEKAVLFCKKREENGEgyekAPSYSYKQSLN 870
Cdd:cd01227     1 AITGYDGNLGDLGKLLMQGSFNVWTEHKKGHTK--KLARFKPMQRHIFLYEKAVLFCKKRGENGE----APSYSYKNSLN 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564389920  871 MTAVGITENVKGDTKKFEIWYNAREEVYIIQAPTPEIKAAWVNEIRKVLTSQ 922
Cdd:cd01227    75 TTAVGLTENVKGDTKKFEIWLNGREEVFIIQAPTPEIKAAWVKAIRQVLLSQ 126
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 607-784 2.28e-55

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 190.20  E-value: 2.28e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  607 RRHVMNELLDTERAYVEELLCVLEGYAAEMDNPLMahlisTGLQNKKNILFGNMEEIYHFHnRIFLRELESCIDC----P 682
Cdd:cd00160     1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELL-----PLSPEEVELLFGNIEEIYEFH-RIFLKSLEERVEEwdksG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  683 ELVGRCFLERMEEFQIYEKYCQNKPRSESLWRQC-SDCPFFQECQKKLD---HKLSLDSYLLKPVQRITKYQLLLKEMLK 758
Cdd:cd00160    75 PRIGDVFLKLAPFFKIYSEYCSNHPDALELLKKLkKFNKFFQEFLEKAEsecGRLKLESLLLKPVQRLTKYPLLLKELLK 154

                         170       180
                  ....*....|....*....|....*..
gi 564389920  759 YSKH-CEGAEDLQEALSSILGILKAVN 784
Cdd:cd00160   155 HTPDgHEDREDLKKALEAIKEVASQVN 181
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 610-785 1.23e-52

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 182.50  E-value: 1.23e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920    610 VMNELLDTERAYVEELLCVLEGYAAEMDNPLMahLIStglQNKKNILFGNMEEIYHFHnRIFLRELESCIDC----PELV 685
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELK--LLS---PNELETLFGNIEEIYEFH-RDFLDELEERIEEwddsVERI 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920    686 GRCFLERMEEFQIYEKYCQNKPRSESLWRQCSDCPFFQECQKKLDHK-----LSLDSYLLKPVQRITKYQLLLKEMLKYS 760
Cdd:smart00325   75 GDVFLKLEEFFKIYSEYCSNHPDALELLKKLKKNPRFQKFLKEIESSpqcrrLTLESLLLKPVQRLTKYPLLLKELLKHT 154

                           170       180
                    ....*....|....*....|....*.
gi 564389920    761 KH-CEGAEDLQEALSSILGILKAVND 785
Cdd:smart00325  155 PEdHEDREDLKKALKAIKELANQVNE 180
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 610-784 2.02e-47

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 167.48  E-value: 2.02e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920   610 VMNELLDTERAYVEELLCVLEGYAAEMDNPLMAHlistglQNKKNILFGNMEEIYHFHNRIFLRELESCIDCPELVGRCF 689
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSES------EEEIKTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIF 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920   690 LERMEEFQIYEKYCQNKPRSESLWRQCSD-----CPFFQECQK-KLDHKLSLDSYLLKPVQRITKYQLLLKEMLKYSKHC 763
Cdd:pfam00621   75 LKFAPGFKVYSTYCSNYPKALKLLKKLLKknpkfRAFLEELEAnPECRGLDLNSFLIKPVQRIPRYPLLLKELLKHTPPD 154

                          170       180
                   ....*....|....*....|..
gi 564389920   764 -EGAEDLQEALSSILGILKAVN 784
Cdd:pfam00621  155 hPDYEDLKKALEAIKEVAKQIN 176
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 50-195 7.23e-28

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 110.47  E-value: 7.23e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920     50 LKKRFAYLSGGRGQD--GSPVITFPDY--PAFSEIPDKEFQNVMTYLTSIPSLQDAGI---GFILVIDRRQDKWTSVKAS 122
Cdd:smart00516    2 LELLKAYIPGGRGYDkdGRPVLIERAGrfDLKSVTLEELLRYLVYVLEKILQEEKKTGgieGFTVIFDLKGLSMSNPDLS 81

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564389920    123 VLRIAAS-----FPANLQLVLVLRPTGFFqRTLSDIAFKFNRDEFKMKVPVMMLSSVPELHGYIDKSQLTEDLGGTLD 195
Cdd:smart00516   82 VLRKILKilqdhYPERLGKVYIINPPWFF-RVLWKIIKPFLDEKTREKIRFVGNDSKEELLEYIDKEQLPEELGGTLD 158
PH_puratrophin-1 cd13242
Puratrophin-1 pleckstrin homology (PH) domain; Puratrophin-1 (also called Purkinje cell ...
 784-927 1.98e-27

Puratrophin-1 pleckstrin homology (PH) domain; Puratrophin-1 (also called Purkinje cell atrophy-associated protein 1 or PLEKHG4/Pleckstrin homology domain-containing family G member 4) contains a spectrin repeat, a RhoGEF (DH) domain, and a PH domain. It is thought to function in intracellular signaling and cytoskeleton dynamics at the Golgi. Puratrophin-1 is expressed in kidney, Leydig cells in the testis, epithelial cells in the prostate gland and Langerhans islet in the pancreas. A single nucleotide substitution in the puratrophin-1 gene were once thought to result in autosomal dominant cerebellar ataxia (ADCA), but now it has been demonstrated that this ataxia is a result of defects in the BEAN gene. Puratrophin contains a domain architecture similar to that of Dbl family members Dbs and Trio. Dbs is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a RhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Trio is a multidomain signaling protein that contains two RhoGEF(DH)-PH domains in tandem. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270062  Cd Length: 136  Bit Score: 108.53  E-value: 1.98e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  784 NDSMHLIAITGYDGNLGDLGKLLMQGSFSVWTDHKKGhtkvkelarfkpmQRHLFLHEKAVLFCKKReengegyeKAPS- 862
Cdd:cd13242     8 NDLLAMDSIRGCDVNLKEQGQLLRQDEFLVWQGRKKC-------------LRHVFLFEDLILFSKPK--------KTPGg 66

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  863 ---YSYKQSLNMTAVGITENVKGDTKKFEIWYNARE--EVYIIQAPTPEIKAAWVNEIRKVLTSqlQACR 927
Cdd:cd13242    67 kdvYIYKHSIKTSDIGLTENVGDSGLKFEIWFRRRKarDTYILQATSPEIKQAWTSDIAKLLWK--QAIR 134
SH3_DBS cd11857
Src homology 3 domain of DBL's Big Sister (DBS), a guanine nucleotide exchange factor; DBS, ...
 1089-1141 6.95e-22

Src homology 3 domain of DBL's Big Sister (DBS), a guanine nucleotide exchange factor; DBS, also called MCF2L (MCF2-transforming sequence-like protein) or OST, is a Rho GTPase guanine nucleotide exchange factor (RhoGEF), facilitating the exchange of GDP and GTP. It was originally isolated from a cDNA screen for sequences that cause malignant growth. It plays roles in regulating clathrin-mediated endocytosis and cell migration through its activation of Rac1 and Cdc42. Depending on cell type, DBS can also activate RhoA and RhoG. DBS contains a Sec14-like domain, spectrin-like repeats, a RhoGEF [or Dbl homology (DH)] domain, a Pleckstrin homology (PH) domain, and an SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212791  Cd Length: 55  Bit Score: 89.65  E-value: 6.95e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564389920 1089 KYTVLMDGEKGGSDTLAMRSGDMVEVVEEGTEGLWYVRDLTSSKEGWVPASSL 1141
Cdd:cd11857     1 KYTVVADYEKGGPDDLTVKSGDLVQLIHEGDEGQWLVKNLSTRKEGWVPAANL 53
PH2_Kalirin_Trio_p63RhoGEF cd13241
p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor ...
 794-923 7.41e-21

p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor p63RhoGEF is an effector of the heterotrimeric G protein, Galphaq and linking Galphaq-coupled receptors (GPCRs) to the activation of RhoA. The Dbl(DH) and PH domains of p63RhoGEF interact with the effector-binding site and the C-terminal region of Galphaq and appear to relieve autoinhibition of the catalytic DH domain by the PH domain. Trio, Duet, and p63RhoGEF are shown to constitute a family of Galphaq effectors that appear to activate RhoA both in vitro and in intact cells. Dbs is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a rhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Trio is a multidomain signaling protein that contains two RhoGEF(DH)-PH domains in tandem. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270061  Cd Length: 140  Bit Score: 90.01  E-value: 7.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  794 GYDGNLGDLGKLLMQGSFSVwtdhkkghTKVKELARFKPMQRHLFLHEKAVLFC----KKREENGegyekaPSYSYKQSL 869
Cdd:cd13241     6 GFDGKITAQGKLLLQGTLLV--------SEPSAGLLQKGKERRVFLFEQIIIFSeilgKKTQFSN------PGYIYKNHI 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 564389920  870 NMTAVGITENVKGDTKKFEIW---YNAREEVYIIQAPTPEIKAAWVNEIRKVLTSQL 923
Cdd:cd13241    72 KVNKMSLEENVDGDPLRFALKsrdPNNPSETFILQAASPEVRQEWVDTINQILDTQR 128
PH1_Kalirin_Trio_like cd13240
Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; ...
 792-919 3.96e-18

Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; RhoGEFs, Kalirin and Trio, the mammalian homologs of Drosophila Trio and Caenorhabditis elegans UNC-73 regulate a novel step in secretory granule maturation. Their signaling modulates the extent to which regulated cargo enter and remain in the regulated secretory pathway. This allows for fine tuning of peptides released by a single secretory cell type with impaired signaling leading to pathological states. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Kalirin and Trio are encoded by separate genes in mammals and by a single one in invertebrates. Kalirin and Trio share the same complex multidomain structure and display several splice variants. The longest Kalirin and Trio proteins have a Sec14 domain, a stretch of spectrin repeats, a RhoGEF(DH)/PH cassette (also called GEF1), an SH3 domain, a second RhoGEF(DH)/PH cassette (also called GEF2), a second SH3 domain, Ig/FNIII domains, and a kinase domain. The first RhoGEF(DH)/PH cassette catalyzes exchange on Rac1 and RhoG while the second RhoGEF(DH)/PH cassette is specific for RhoA. Kalirin and Trio are closely related to p63RhoGEF and have PH domains of similar function. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains.


Pssm-ID: 270060  Cd Length: 123  Bit Score: 81.66  E-value: 3.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  792 ITGYDGNLGDLGKLLMQGSFSVWtDHKKGHTKVKElarfkpmqRHLFLHEKAVLFCKKrEENGEGYEKapsYSYKQSLNM 871
Cdd:cd13240     2 LEGCDEDLDSLGEVILQDSFQVW-DPKQLIRKGRE--------RHVFLFELCLVFSKE-VKDSNGKSK---YIYKSRLMT 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564389920  872 TAVGITENVKGDTKKFEIW---YNAREEVYIIQAPTPEIKAAWVNEIRKVL 919
Cdd:cd13240    69 SEIGVTEHIEGDPCKFALWtgrVPTSDNKIVLKASSLEVKQTWVKKLREVI 119
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 65-198 8.07e-18

Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain family. This family includes ECM25 that contains a divergent CRAL-TRIO domain identified by Gallego and colleagues.


Pssm-ID: 463965 [Multi-domain]  Cd Length: 140  Bit Score: 81.22  E-value: 8.07e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920    65 GSPVITFPDYPAFSE-IPDKEFQNVMTYLTSIPSLQDAGIGFILVIDRRQDKWTS------VKASVLRIAASFPANLQLV 137
Cdd:pfam13716    1 GRPVLVFISKLLPSRpASLDDLDRLLFYLLKTLSEKLKGKPFVVVVDHTGVTSENfpslsfLKKAYDLLPRAFKKNLKAV 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564389920   138 LVLRPTGFFQRTLSDIAFKFNRDEFKMKVpvMMLSSVPELHGYIDKSQLTEDLGGTLDYCH 198
Cdd:pfam13716   81 YVVHPSTFLRTFLKTLGSLLGSKKLRKKV--HYVSSLSELWEGIDREQLPTELPGVLSYDE 139
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 326-528 4.86e-16

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 78.26  E-value: 4.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  326 QLRHFEQGFREVKTALDSMSQKIAAfTDVGNSLAHVQHLLKDLTTFEEKSSVAVDKARALSLEGQQLIENRHYAVDSIHP 405
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  406 KCEELQHLCDHFASEVTRRRDLLSKSLELHSLLETS---MKWSDEGIFLLASQPVDKcqSQDGAEAALQEIEKFLET--G 480
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAddlEQWLEEKEAALASEDLGK--DLESVEELLKKHKELEEEleA 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564389920  481 AENKIQELNKIYKEYECILNQDLLEHVQKVF----QKQESTEEMFHRRQASL 528
Cdd:cd00176   158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLeelnERWEELLELAEERQKKL 209
PH_Obscurin cd13239
Obscurin pleckstrin homology (PH) domain; Obscurin (also called Obscurin-RhoGEF; ...
 792-918 5.71e-16

Obscurin pleckstrin homology (PH) domain; Obscurin (also called Obscurin-RhoGEF; Obscurin-myosin light chain kinase/Obscurin-MLCK) is a giant muscle protein that is concentrated at the peripheries of Z-disks and M-lines. It binds small ankyrin I, a component of the sarcoplasmic reticulum (SR) membrane. It is associated with the contractile apparatus through binding with titin and sarcomeric myosin. It plays important roles in the organization and assembly of the myofibril and the SR. Obscurin has been observed as alternatively-spliced isoforms. The major isoform in sleletal muscle, approximately 800 kDa in size, is composed of many adhesion modules and signaling domains. It harbors 49 Ig and 2 FNIII repeats at the N-terminues, a complex middle region with additional Ig domains, an IQ motif, and a conserved SH3 domain near RhoGEF and PH domains, and a non-modular C-terminus with phosphorylation motifs. The obscurin gene also encodes two kinase domains, which are not part of the 800 kDa form of the protein, but is part of smaller spliced products that present in heart muscle. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270059  Cd Length: 125  Bit Score: 75.27  E-value: 5.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  792 ITGYDGNLGDLGKLLMQGSFSVWtdhkKGHTKVKELARfkPMQRHLFLHEKAVLFCKKREENGEGYEkapSYSYKQSLNM 871
Cdd:cd13239     2 IENYPAPLQALGEPIRQGHFTVW----EEAPEVKTSSR--GHHRHVFLFKNCVVICKPKRDSRTDTV---TYVFKNKMKL 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 564389920  872 TAVGITENVKGDTKKFEIWYNAREEV--YIIQAPTPEIKAAWVNEIRKV 918
Cdd:cd13239    73 SDIDVKDTVEGDDRSFGLWHEHRGSVrkYTLQARSAIIKSSWLKDLRDL 121
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 45-193 6.77e-14

Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 469559 [Multi-domain]  Cd Length: 156  Bit Score: 70.44  E-value: 6.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920   45 DIQEQLKKrfAYLSGGRGQDGSPVITFPDYPAFSEIPDKE--FQNVMTYLTSIPSLQDAGI-GFILVIDRRQDKWTS--- 118
Cdd:cd00170     3 ELLELLGG--IGYLGGRDKEGRPVLVFRAGWDPPKLLDLEelLRYLVYLLEKALRELEEQVeGFVVIIDLKGFSLSNlsd 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564389920  119 ---VKASVLRIAASFPANLQLVLVLRPTGFFqRTLSDIAFKFNRDEFKMKVpVMMLSSVPELHGYIDKSQLTEDLGGT 193
Cdd:cd00170    81 lslLKKLLKILQDHYPERLKKIYIVNAPWIF-SALWKIVKPFLSEKTRKKI-VFLGSDLEELLEYIDPDQLPKELGGT 156
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 805-919 8.79e-12

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 62.57  E-value: 8.79e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920    805 LLMQGSFSVWTDHKKGHTKvkelarfkpmQRHLFLHEKAVLFCKKREENgegyekaPSYSYKQSLNMTAVGITENVKGDT 884
Cdd:smart00233    1 VIKEGWLYKKSGGGKKSWK----------KRYFVLFNSTLLYYKSKKDK-------KSYKPKGSIDLSGCTVREAPDPDS 63

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 564389920    885 KK----FEIWYNAREeVYIIQAPTPEIKAAWVNEIRKVL 919
Cdd:smart00233   64 SKkphcFEIKTSDRK-TLLLQAESEEEREKWVEALRKAI 101
SPEC smart00150
Spectrin repeats;
328-428 7.91e-11

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 60.04  E-value: 7.91e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920    328 RHFEQGFREVKTALDSMsQKIAAFTDVGNSLAHVQHLLKDLTTFEEKSSVAVDKARALSLEGQQLIENRHYAVDSIHPKC 407
Cdd:smart00150    1 QQFLRDADELEAWLEEK-EQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79

                            90       100
                    ....*....|....*....|.
gi 564389920    408 EELQHLCDHFASEVTRRRDLL 428
Cdd:smart00150   80 EELNERWEELKELAEERRQKL 100
SH3_p47phox_like cd11856
Src homology 3 domains of the p47phox subunit of NADPH oxidase and similar domains; This ...
 1089-1141 5.48e-09

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


Pssm-ID: 212790 [Multi-domain]  Cd Length: 53  Bit Score: 53.02  E-value: 5.48e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564389920 1089 KYTVLMDGEKGGSDTLAMRSGDMVEVVEEGTEGLWYVRdlTSSKEGWVPASSL 1141
Cdd:cd11856     1 SYVAIADYEAQGDDEISLQEGEVVEVLEKNDSGWWYVR--KGDKEGWVPASYL 51
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 229-432 6.73e-09

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 57.46  E-value: 6.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  229 LAETELPNDVQSTSLVLSAHtekkakvkEDLQLALTEGNSILESLREpLAESIVhsvnQDQLDNQATVKRLLTQLNETEA 308
Cdd:cd00176    23 LSSTDYGDDLESVEALLKKH--------EALEAELAAHEERVEALNE-LGEQLI----EEGHPDAEEIQERLEELNQRWE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  309 AFDEFWAKHQQKLEQCLQLRHFEQGFREVKTALDSMSQKIAAfTDVGNSLAHVQHLLKDLTTFEEKSSVAVDKARALSLE 388
Cdd:cd00176    90 ELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNEL 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 564389920  389 GQQLIENRHYAV-DSIHPKCEELQHLCDHFASEVTRRRDLLSKSL 432
Cdd:cd00176   169 AEELLEEGHPDAdEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SH3_p47phox_1 cd12021
First or N-terminal Src homology 3 domain of the p47phox subunit of NADPH oxidase, also called ...
 1090-1141 4.96e-08

First or N-terminal Src homology 3 domain of the p47phox subunit of NADPH oxidase, also called Neutrophil Cytosolic Factor 1; p47phox, or NCF1, is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox), which plays a key role in the ability of phagocytes to defend against bacterial infections. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p47phox is required for activation of NADH oxidase and plays a role in translocation. It contains an N-terminal Phox homology (PX) domain, tandem SH3 domains (N-SH3 and C-SH3), a polybasic/autoinhibitory region, and a C-terminal proline-rich region (PRR). This model characterizes the first SH3 domain (or N-SH3) of p47phox. In its inactive state, the tandem SH3 domains interact intramolecularly with the autoinhibitory region; upon activation, the tandem SH3 domains are exposed through a conformational change, resulting in their binding to the PRR of p22phox and the activation of NADPH oxidase. 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: 212954 [Multi-domain]  Cd Length: 53  Bit Score: 50.34  E-value: 4.96e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564389920 1090 YTVLMDGEKGGSDTLAMRSGDMVEVVEEGTEGLWYVRdlTSSKEGWVPASSL 1141
Cdd:cd12021     2 YRAIADYEKSSKSEMALKTGDVVEVVEKSENGWWFCQ--LKAKRGWVPASYL 51
SH3_Tks5_1 cd12074
First Src homology 3 domain of Tyrosine kinase substrate with five SH3 domains; Tks5, also ...
 1089-1141 5.37e-08

First Src homology 3 domain of Tyrosine kinase substrate with five SH3 domains; Tks5, also called SH3 and PX domain-containing protein 2A (SH3PXD2A) or Five SH (FISH), is a scaffolding protein and Src substrate that is localized in podosomes, which are electron-dense structures found in Src-transformed fibroblasts, osteoclasts, macrophages, and some invasive cancer cells. It binds and regulates some members of the ADAMs family of transmembrane metalloproteases, which function as sheddases and mediators of cell and matrix interactions. It is required for podosome formation, degradation of the extracellular matrix, and cancer cell invasion. Tks5 contains an N-terminal Phox homology (PX) domain and five SH3 domains. This model characterizes the first SH3 domain of Tks5. 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: 213007 [Multi-domain]  Cd Length: 53  Bit Score: 50.48  E-value: 5.37e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564389920 1089 KYTVLMDGEKGGSDTLAMRSGDMVEVVEEGTEGLWYVRdlTSSKEGWVPASSL 1141
Cdd:cd12074     1 QYVVVSNYEKQENSEISLQAGEVVDVIEKNESGWWFVS--TAEEQGWVPATYL 51
SH3_Tks5_2 cd12077
Second Src homology 3 domain of Tyrosine kinase substrate with five SH3 domains; Tks5, also ...
 1089-1141 9.40e-08

Second Src homology 3 domain of Tyrosine kinase substrate with five SH3 domains; Tks5, also called SH3 and PX domain-containing protein 2A (SH3PXD2A) or Five SH (FISH), is a scaffolding protein and Src substrate that is localized in podosomes, which are electron-dense structures found in Src-transformed fibroblasts, osteoclasts, macrophages, and some invasive cancer cells. It binds and regulates some members of the ADAMs family of transmembrane metalloproteases, which function as sheddases and mediators of cell and matrix interactions. It is required for podosome formation, degradation of the extracellular matrix, and cancer cell invasion. Tks5 contains an N-terminal Phox homology (PX) domain and five SH3 domains. This model characterizes the second SH3 domain of Tks5. 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: 213010  Cd Length: 54  Bit Score: 49.65  E-value: 9.40e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564389920 1089 KYTVLMDGEKGGSDTLAMRSGDMVEVVEEGTEGLWYVRDLtsSKEGWVPASSL 1141
Cdd:cd12077     2 KYVTVQPYTSQGKDEIGFEKGVTVEVIQKNLEGWWYIRYL--GKEGWAPASYL 52
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 818-915 1.74e-07

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 50.23  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  818 KKGH-TKVKELARFKPMQRHLFLHEKAVLFCKKREENgegyekapSYSYKQSLNMTA-VGITENVKGDTK-KFEIWyNAR 894
Cdd:cd00821     1 KEGYlLKRGGGGLKSWKKRWFVLFEGVLLYYKSKKDS--------SYKPKGSIPLSGiLEVEEVSPKERPhCFELV-TPD 71

                          90       100
                  ....*....|....*....|.
gi 564389920  895 EEVYIIQAPTPEIKAAWVNEI 915
Cdd:cd00821    72 GRTYYLQADSEEERQEWLKAL 92
SH3_Tks_1 cd12015
First Src homology 3 domain of Tyrosine kinase substrate (Tks) proteins; Tks proteins are Src ...
 1089-1141 2.06e-07

First Src homology 3 domain of Tyrosine kinase substrate (Tks) proteins; Tks proteins are Src substrates and scaffolding proteins that play important roles in the formation of podosomes and invadopodia, the dynamic actin-rich structures that are related to cell migration and cancer cell invasion. Vertebrates contain two Tks proteins, Tks4 (Tyr kinase substrate with four SH3 domains) and Tks5 (Tyr kinase substrate with five SH3 domains), which display partially overlapping but non-redundant functions. Both associate with the ADAMs family of transmembrane metalloproteases, which function as sheddases and mediators of cell and matrix interactions. Tks5 interacts with N-WASP and Nck, while Tks4 is essential for the localization of MT1-MMP (membrane-type 1 matrix metalloproteinase) to invadopodia. Tks proteins contain an N-terminal Phox homology (PX) domain and four or five SH3 domains. This model characterizes the first SH3 domain of Tks proteins. 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: 212948  Cd Length: 53  Bit Score: 48.57  E-value: 2.06e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564389920 1089 KYTVLMDGEKGGSDTLAMRSGDMVEVVEEGTEGLWYVRdlTSSKEGWVPASSL 1141
Cdd:cd12015     1 QYVVVADYKKQQPNEISLRAGDVVDVIEKNENGWWFVS--LEDEQGWVPATYL 51
SH3_Myosin-I_fungi cd11858
Src homology 3 domain of Type I fungal Myosins; Type I myosins (myosin-I) are actin-dependent ...
 1090-1141 2.55e-07

Src homology 3 domain of Type I fungal Myosins; Type I myosins (myosin-I) are actin-dependent motors in endocytic actin structures and actin patches. They play roles in membrane traffic in endocytic and secretory pathways, cell motility, and mechanosensing. Saccharomyces cerevisiae has two myosins-I, Myo3 and Myo5, which are involved in endocytosis and the polarization of the actin cytoskeleton. Myosin-I contains an N-terminal actin-activated ATPase, a phospholipid-binding TH1 (tail homology 1) domain, and a C-terminal extension which includes an F-actin-binding TH2 domain, an SH3 domain, and an acidic peptide that participates in activating the Arp2/3complex. The SH3 domain of myosin-I is required for myosin-I-induced actin polymerization. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212792 [Multi-domain]  Cd Length: 55  Bit Score: 48.54  E-value: 2.55e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564389920 1090 YTVLMDGEKGGSDTLAMRSGDMVEVVEEGTEGLWYVRDLTSSKEGWVPASSL 1141
Cdd:cd11858     2 YKALYDFAGSVANELSLKKDDIVYIVQKEDNGWWLAKKLDESKEGWVPAAYL 53
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 805-919 5.30e-07

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 49.10  E-value: 5.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920   805 LLMQGSFSVWTDHKKGHTKvkelarfkpmQRHLFLHEKAVLFCKKREengegyeKAPSYSYKQSLNMTAVGITENVKGDT 884
Cdd:pfam00169    1 VVKEGWLLKKGGGKKKSWK----------KRYFVLFDGSLLYYKDDK-------SGKSKEPKGSISLSGCEVVEVVASDS 63

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 564389920   885 KK----FEIWYNAR--EEVYIIQAPTPEIKAAWVNEIRKVL 919
Cdd:pfam00169   64 PKrkfcFELRTGERtgKRTYLLQAESEEERKDWIKAIQSAI 104
SH3_Tks4_1 cd12075
First Src homology 3 domain of Tyrosine kinase substrate with four SH3 domains; Tks4, also ...
 1089-1141 1.26e-06

First Src homology 3 domain of Tyrosine kinase substrate with four SH3 domains; Tks4, also called SH3 and PX domain-containing protein 2B (SH3PXD2B) or HOFI, is a Src substrate and scaffolding protein that plays an important role in the formation of podosomes and invadopodia, the dynamic actin-rich structures that are related to cell migration and cancer cell invasion. It is required in the formation of functional podosomes, EGF-induced membrane ruffling, and lamellipodia generation. It plays an important role in cellular attachment and cell spreading. Tks4 is essential for the localization of MT1-MMP (membrane-type 1 matrix metalloproteinase) to invadopodia. It contains an N-terminal Phox homology (PX) domain and four SH3 domains. This model characterizes the first SH3 domain of Tks4. 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: 213008  Cd Length: 55  Bit Score: 46.61  E-value: 1.26e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564389920 1089 KYTVLMDGEKGGSDTLAMRSGDMVEVVEEGTEGLWYVRdlTSSKEGWVPASSL 1141
Cdd:cd12075     2 QYVVVANYQKQESSEISLYVGQVVDIIEKNESGWWFVS--TADEQGWVPATCL 52
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 328-428 4.10e-06

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 46.54  E-value: 4.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920   328 RHFEQGFREVKTALDSMSQKIAAFT--DVGNSLAHVQHLLKDLTTFEEKSSVAVDKARALSLEGQQLIENRHYAVDSIHP 405
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSseDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80

                           90       100
                   ....*....|....*....|...
gi 564389920   406 KCEELQHLCDHFASEVTRRRDLL 428
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKL 103
SH3_Tks_3 cd12017
Third Src homology 3 domain of Tyrosine kinase substrate (Tks) proteins; Tks proteins are Src ...
 1090-1141 1.06e-05

Third Src homology 3 domain of Tyrosine kinase substrate (Tks) proteins; Tks proteins are Src substrates and scaffolding proteins that play important roles in the formation of podosomes and invadopodia, the dynamic actin-rich structures that are related to cell migration and cancer cell invasion. Vertebrates contain two Tks proteins, Tks4 (Tyr kinase substrate with four SH3 domains) and Tks5 (Tyr kinase substrate with five SH3 domains), which display partially overlapping but non-redundant functions. Both associate with the ADAMs family of transmembrane metalloproteases, which function as sheddases and mediators of cell and matrix interactions. Tks5 interacts with N-WASP and Nck, while Tks4 is essential for the localization of MT1-MMP (membrane-type 1 matrix metalloproteinase) to invadopodia. Tks proteins contain an N-terminal Phox homology (PX) domain and four or five SH3 domains. This model characterizes the third SH3 domain of Tks proteins. 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: 212950  Cd Length: 53  Bit Score: 43.98  E-value: 1.06e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564389920 1090 YTVLMDGEKGGSDTLAMRSGDMVEVVEEGTEGLWYVRdlTSSKEGWVPASSL 1141
Cdd:cd12017     2 YFTIGEFQATIQDGISFQKGQKVEVIDKNPSGWWYVK--IDGKEGWAPSSYI 51
SH3_Tks4_2 cd12076
Second Src homology 3 domain of Tyrosine kinase substrate with four SH3 domains; Tks4, also ...
 1089-1141 1.19e-05

Second Src homology 3 domain of Tyrosine kinase substrate with four SH3 domains; Tks4, also called SH3 and PX domain-containing protein 2B (SH3PXD2B) or HOFI, is a Src substrate and scaffolding protein that plays an important role in the formation of podosomes and invadopodia, the dynamic actin-rich structures that are related to cell migration and cancer cell invasion. It is required in the formation of functional podosomes, EGF-induced membrane ruffling, and lamellipodia generation. It plays an important role in cellular attachment and cell spreading. Tks4 is essential for the localization of MT1-MMP (membrane-type 1 matrix metalloproteinase) to invadopodia. It contains an N-terminal Phox homology (PX) domain and four SH3 domains. This model characterizes the second SH3 domain of Tks4. 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: 213009 [Multi-domain]  Cd Length: 54  Bit Score: 43.87  E-value: 1.19e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564389920 1089 KYTVLMDGEKGGSDTLAMRSGDMVEVVEEGTEGLWYVRdlTSSKEGWVPASSL 1141
Cdd:cd12076     2 KYTVIYPYTARDQDEINLEKGAVVEVIQKNLEGWWKIR--YQGKEGWAPASYL 52
PH_Vav cd01223
Vav pleckstrin homology (PH) domain; Vav acts as a guanosine nucleotide exchange factor (GEF) ...
 818-919 1.81e-05

Vav pleckstrin homology (PH) domain; Vav acts as a guanosine nucleotide exchange factor (GEF) for Rho/Rac proteins. They control processes including T cell activation, phagocytosis, and migration of cells. The Vav subgroup of Dbl GEFs consists of three family members (Vav1, Vav2, and Vav3) in mammals. Vav1 is preferentially expressed in the hematopoietic system, while Vav2 and Vav3 are described by broader expression patterns. Mammalian Vav proteins consist of a calponin homology (CH) domain, an acidic region, a catalytic Dbl homology (DH) domain, a PH domain, a zinc finger cysteine rich domain (C1/CRD), and an SH2 domain, flanked by two SH3 domains. In invertebrates such as Drosophila and C. elegans, Vav is missing the N-terminal SH3 domain. The DH domain is involved in RhoGTPase recognition and selectivity and stimulates the reorganization of the switch regions for GDP/GTP exchange. The PH domain is implicated in directing membrane localization, allosteric regulation of guanine nucleotide exchange activity, and as a phospholipid- dependent regulator of GEF activity. Vavs bind RhoGTPases including Rac1, RhoA, RhoG, and Cdc42, while other members of the GEF family are specific for a single RhoGTPase. This promiscuity is thought to be a result of its CRD. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.polarized. PH domains also have diverse functions. They are often involved in targeting proteins to the plasma membrane, but only a few (less than 10%) display strong specificity in binding inositol phosphates. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinases, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, cytoskeletal associated molecules, and in lipid associated enzymes.


Pssm-ID: 269930  Cd Length: 127  Bit Score: 45.32  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  818 KKGHTKVKELARFKPMQRHLFLHEKAVLFCKKREENgegyekapSYSYKQSLNMTAVGITEN----VKGDTKKFE-IWYN 892
Cdd:cd01223    21 IDGELKIKSHEDQKKKDRYAFLFDKVLLICKSLRGD--------QYEYKEIINLSEYRIEDDpsrrTLKRDKRWSyQFLL 92

                          90       100       110
                  ....*....|....*....|....*....|
gi 564389920  893 AREE---VYIIQAPTPEIKAAWVNEIRKVL 919
Cdd:cd01223    93 VHKQgktAYTLYAKTEELKKKWMEAIEMAL 122
PH_unc89 cd13325
unc89 pleckstrin homology (PH) domain; unc89 is a myofibrillar protein. unc89-B the largest ...
 797-917 1.89e-05

unc89 pleckstrin homology (PH) domain; unc89 is a myofibrillar protein. unc89-B the largest isoform is composed of 53 immunoglobulin (Ig) domains, 2 Fn3 domains, a triplet of SH3, DH and PH domains at its N-terminus, and 2 protein kinase domains (PK1 and PK2) at its C-terminus. unc-89 mutants display disorganization of muscle A-bands, and usually lack M-lines. The COOH-terminal region of obscurin, the human homolog of unc89, interacts via two specific Ig-like domains with the NH(2)-terminal Z-disk region of titin, a protein that connects the Z line to the M line in the sarcomere and contributes to the contraction of striated muscle. obscurin is also thought to be involved in Ca2+/calmodulin via its IQ domains, as well as G protein-coupled signal transduction in the sarcomere via its RhoGEF/DH domain. The DH-PH region of OBSCN and unc89, the C. elegans homolog, has exchange activity for RhoA and Rho-1 respectively, but not for the small GTPases homologous to Cdc42 or Rac. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270134  Cd Length: 114  Bit Score: 45.03  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  797 GNLGDLGKLLMQGSFSVWTDHKKGHtkvkelarfkpmQRHLFLHEKAVLFCKKRE--ENgegyekaPSYS-YKQSLNMTA 873
Cdd:cd13325     1 GNIHKLGRLLRHDWFTVTDGEGKAK------------ERYLFLFKSRILITKVRRisED-------RSVFiLKDIIRLPE 61

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 564389920  874 VGItENVKGDTKKFEIWYNA---REEVYIIQAPTPEIKAAWVNEIRK 917
Cdd:cd13325    62 VNV-KQHPDDERTFELQPKLpafGILPIDFKAHKDEIKDYWLNEIEE 107
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 1086-1142 1.95e-05

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: 43.30  E-value: 1.95e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 564389920   1086 VPGKYTVLMDGEKGGSDTLAMRSGDMVEVVEEGTEGLWYVRdLTSSKEGWVPASSLA 1142
Cdd:smart00326    1 EGPQVRALYDYTAQDPDELSFKKGDIITVLEKSDDGWWKGR-LGRGKEGLFPSNYVE 56
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 605-853 2.72e-05

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 48.73  E-value: 2.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  605 ILRRHVMNELLDTERAYVEELlcvlEGYAAEMDNPLMA-HLISTglQNKKNIL---FGNMEEIYHFHNRIF--LRELESC 678
Cdd:COG5422   483 IKRQEAIYEVIYTERDFVKDL----EYLRDTWIKPLEEsNIIPE--NARRNFIkhvFANINEIYAVNSKLLkaLTNRQCL 556

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  679 IDCPELVGRCFLERMEEFQIYEKYCQNKPRSE-SLWRQCSDCPFFqecqKKLDH---------KLSLDSYLLKPVQRITK 748
Cdd:COG5422   557 SPIVNGIADIFLDYVPKFEPFIKYGASQPYAKyEFEREKSVNPNF----ARFDHeverldesrKLELDGYLTKPTTRLAR 632

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  749 YQLLLKEMLKYSKhcEGAEDLQEalssILGILKAVNDSMHLIAI-TGYDGNLGDLGKLLMQGSFSvwTDH---------- 817
Cdd:COG5422   633 YPLLLEEVLKFTD--PDNPDTED----IPKVIDMLREFLSRLNFeSGKAENRGDLFHLNQQLLFK--PEYvnlglndeyr 704

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 564389920  818 ---KKGHTKVKELARFKPMQR---HLFLHEKAVLFCKKREEN 853
Cdd:COG5422   705 kiiFKGVLKRKAKSKTDGSLRgdiQFFLLDNMLLFCKAKAVN 746
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 1089-1139 2.78e-05

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: 42.45  E-value: 2.78e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564389920 1089 KYTVLMDGEKGGSDTLAMRSGDMVEVVEEGTEGLWYVRdLTSSKEGWVPAS 1139
Cdd:cd00174     1 YARALYDYEAQDDDELSFKKGDIITVLEKDDDGWWEGE-LNGGREGLFPAN 50
PH_PLEKHG1_G2_G3 cd13243
Pleckstrin homology domain-containing family G members 1, 2, and 3 pleckstrin homology (PH) ...
 767-919 8.03e-05

Pleckstrin homology domain-containing family G members 1, 2, and 3 pleckstrin homology (PH) domain; PLEKHG1 (also called ARHGEF41), PLEKHG2 (also called ARHGEF42 or CLG/common-site lymphoma/leukemia guanine nucleotide exchange factor2), and PLEKHG3 (also called ARHGEF43) have RhoGEF DH/double-homology domains in tandem with a PH domain which is involved in phospholipid binding. They function as a guanine nucleotide exchange factor (GEF) and are involved in the regulation of Rho protein signal transduction. Mutations in PLEKHG1 have been associated panic disorder (PD), an anxiety disorder characterized by panic attacks and anticipatory anxiety. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270063 [Multi-domain]  Cd Length: 147  Bit Score: 43.88  E-value: 8.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  767 EDLQEALSSILGILKAVND-------SMHL----IAITGYDG-NLGDLGKLLMQGSFSVwtdhkkghtkvkelaRFKPMQ 834
Cdd:cd13243     2 SVVEEALDTMTQVAWHINDmkrkhehAVRVqeiqSLLDGWEGpELTTYGDLVLEGTFRM---------------AGAKNE 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389920  835 RHLFLHEKAVLFCKKREENGegyekapsYSYKQSLNMTAVGITENVKGDTKKFEIW-YNAREEVYIIQAPTPEIKAAWVN 913
Cdd:cd13243    67 RLLFLFDKMLLITKKREDGI--------LQYKTHIMCSNLMLSESIPKEPLSFQVLpFDNPKLQYTLQAKNQEQKRLWTQ 138


                  ....*.
gi 564389920  914 EIRKVL 919
Cdd:cd13243   139 EIKRLI 144
SH3_Tks5_3 cd12079
Third Src homology 3 domain of Tyrosine kinase substrate with five SH3 domains; Tks5, also ...
 1089-1139 1.18e-04

Third Src homology 3 domain of Tyrosine kinase substrate with five SH3 domains; Tks5, also called SH3 and PX domain-containing protein 2A (SH3PXD2A) or Five SH (FISH), is a scaffolding protein and Src substrate that is localized in podosomes, which are electron-dense structures found in Src-transformed fibroblasts, osteoclasts, macrophages, and some invasive cancer cells. It binds and regulates some members of the ADAMs family of transmembrane metalloproteases, which function as sheddases and mediators of cell and matrix interactions. It is required for podosome formation, degradation of the extracellular matrix, and cancer cell invasion. Tks5 contains an N-terminal Phox homology (PX) domain and five SH3 domains. This model characterizes the third SH3 domain of Tks5. 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: 213012  Cd Length: 54  Bit Score: 40.80  E-value: 1.18e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564389920 1089 KYTVLMDGEKGGSDTLAMRSGDMVEVVEEGTEGLWYVRdlTSSKEGWVPAS 1139
Cdd:cd12079     2 EYYTIAEFQSCISDGISFRGGQKAEVIEKNSGGWWYVQ--IGEKEGWAPSS 50
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 1091-1138 1.95e-04

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


Pssm-ID: 394975 [Multi-domain]  Cd Length: 47  Bit Score: 39.88  E-value: 1.95e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 564389920  1091 TVLMDGEKGGSDTLAMRSGDMVEVVEEGTEGLWYVRDLTsSKEGWVPA 1138
Cdd:pfam00018    1 VALYDYTAQEPDELSFKKGDIIIVLEKSEDGWWKGRNKG-GKEGLIPS 47
SH3_Tks_2 cd12016
Second Src homology 3 domain of Tyrosine kinase substrate (Tks) proteins; Tks proteins are Src ...
 1088-1141 3.88e-04

Second Src homology 3 domain of Tyrosine kinase substrate (Tks) proteins; Tks proteins are Src substrates and scaffolding proteins that play important roles in the formation of podosomes and invadopodia, the dynamic actin-rich structures that are related to cell migration and cancer cell invasion. Vertebrates contain two Tks proteins, Tks4 (Tyr kinase substrate with four SH3 domains) and Tks5 (Tyr kinase substrate with five SH3 domains), which display partially overlapping but non-redundant functions. Both associate with the ADAMs family of transmembrane metalloproteases, which function as sheddases and mediators of cell and matrix interactions. Tks5 interacts with N-WASP and Nck, while Tks4 is essential for the localization of MT1-MMP (membrane-type 1 matrix metalloproteinase) to invadopodia. Tks proteins contain an N-terminal Phox homology (PX) domain and four or five SH3 domains. This model characterizes the second SH3 domain of Tks proteins. 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: 212949  Cd Length: 54  Bit Score: 39.36  E-value: 3.88e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 564389920 1088 GKYTVLMDGEKGGSDTLAMRSGDMVEVVEEGTEGLWYVRDLtsSKEGWVPASSL 1141
Cdd:cd12016     1 EKYITTQAYKAENEDEIGFETGVVVEVIQKNLDGWWKIRYQ--GKEGWAPATYL 52
SH3_Tks4_3 cd12078
Third Src homology 3 domain of Tyrosine kinase substrate with four SH3 domains; Tks4, also ...
 1089-1139 1.07e-03

Third Src homology 3 domain of Tyrosine kinase substrate with four SH3 domains; Tks4, also called SH3 and PX domain-containing protein 2B (SH3PXD2B) or HOFI, is a Src substrate and scaffolding protein that plays an important role in the formation of podosomes and invadopodia, the dynamic actin-rich structures that are related to cell migration and cancer cell invasion. It is required in the formation of functional podosomes, EGF-induced membrane ruffling, and lamellipodia generation. It plays an important role in cellular attachment and cell spreading. Tks4 is essential for the localization of MT1-MMP (membrane-type 1 matrix metalloproteinase) to invadopodia. It contains an N-terminal Phox homology (PX) domain and four SH3 domains. This model characterizes the third SH3 domain of Tks4. 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: 213011  Cd Length: 53  Bit Score: 38.13  E-value: 1.07e-03
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gi 564389920 1089 KYTVLMDGEKGGSDTLAMRSGDMVEVVEEGTEGLWYVRdlTSSKEGWVPAS 1139
Cdd:cd12078     1 EYYTIADFQTTIPDGISFQAGLKVEVIEKNLSGWWYIQ--IEDKEGWAPAT 49
SH3_Bzz1_1 cd11912
First Src Homology 3 domain of Bzz1 and similar domains; Bzz1 (or Bzz1p) is a WASP ...
 1092-1139 2.81e-03

First Src Homology 3 domain of Bzz1 and similar domains; Bzz1 (or Bzz1p) is a WASP/Las17-interacting protein involved in endocytosis and trafficking to the vacuole. It physically interacts with type I myosins and functions in the early steps of endocytosis. Together with other proteins, it induces membrane scission in yeast. Bzz1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. This model represents the first 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: 212845 [Multi-domain]  Cd Length: 55  Bit Score: 37.20  E-value: 2.81e-03
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gi 564389920 1092 VLMDGEKGGSDTLAMRSGDMVEVVEEGTEGLWYVRDLTSSKEGWVPAS 1139
Cdd:cd11912     4 VLYDYTASGDDEVSISEGEEVTVLEPDDGSGWTKVRNGSGEEGLVPTS 51
SH3_ARHGEF9_like cd11828
Src homology 3 domain of ARHGEF9-like Rho guanine nucleotide exchange factors; Members of this ...
 1092-1139 3.38e-03

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 [Multi-domain]  Cd Length: 53  Bit Score: 36.59  E-value: 3.38e-03
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gi 564389920 1092 VLMDGEKggsdtLAMRSGDMVEVVEEGTEGLWYVRdlTSSKEGWVPAS 1139
Cdd:cd11828     9 VTMDPEE-----LGFKAGDVIEVLDMSDKDWWWGS--IRDEEGWFPAS 49
SH3_PSTPIP1 cd11824
Src homology 3 domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; PSTPIP1, ...
 1089-1141 3.40e-03

Src homology 3 domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; PSTPIP1, also called CD2 Binding Protein 1 (CD2BP1), is mainly expressed in hematopoietic cells. It is a binding partner of the cell surface receptor CD2 and PTP-PEST, a tyrosine phosphatase which functions in cell motility and Rac1 regulation. It also plays a role in the activation of the Wiskott-Aldrich syndrome protein (WASP), which couples actin rearrangement and T cell activation. Mutations in the gene encoding PSTPIP1 cause the autoinflammatory disorder known as PAPA (pyogenic sterile arthritis, pyoderma gangrenosum, and acne) syndrome. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212758 [Multi-domain]  Cd Length: 53  Bit Score: 36.58  E-value: 3.40e-03
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gi 564389920 1089 KYTVLMDGEKGGSDTLAMRSGDMVEVVEEGTEGLWYVRdlTSSKEGWVPASSL 1141
Cdd:cd11824     1 KYSVLYDYTAQEDDELSISKGDVVAVIEKGEDGWWTVE--RNGQKGLVPGTYL 51
SH3_BOI cd11886
Src Homology 3 domain of fungal BOI-like proteins; This subfamily includes the Saccharomyces ...
 1090-1138 5.09e-03

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


Pssm-ID: 212819  Cd Length: 55  Bit Score: 36.16  E-value: 5.09e-03
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gi 564389920 1090 YTVLMDGEKGGSDTLAMRSGDMVEVVEEGTE---GLWYVRDLTSSKEGWVPA 1138
Cdd:cd11886     2 LIVIHDFNARSEDELTLKPGDKIELIEDDEEfgdGWYLGRNLRTGETGLFPV 53
SH3_Src_like cd11845
Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members ...
 1090-1139 7.25e-03

Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, Yes, and Brk. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). However, Brk lacks the N-terminal myristoylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells, and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, Lyn, and Brk show a limited expression pattern. This subfamily also includes Drosophila Src42A, Src oncogene at 42A (also known as Dsrc41) which accumulates at sites of cell-cell or cell-matrix adhesion, and participates in Drosphila development and wound healing. It has been shown to promote tube elongation in the tracheal system, is essential for proper cell-cell matching during dorsal closure, and regulates cell-cell contacts in developing Drosophila eyes. The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212779 [Multi-domain]  Cd Length: 52  Bit Score: 35.64  E-value: 7.25e-03
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gi 564389920 1090 YTVLMDGEKGGSDTLAMRSGDMVEVVEEGTEGLWYVRDLTSSKEGWVPAS 1139
Cdd:cd11845     2 YVALYDYEARTDDDLSFKKGDRLQILDDSDGDWWLARHLSTGKEGYIPSN 51
SH3_Sla1p_3 cd11775
Third Src Homology 3 domain of the fungal endocytic adaptor protein Sla1p; Sla1p facilitates ...
 1091-1139 9.12e-03

Third 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. The third SH3 domain of Sla1p can bind ubiquitin while retaining the ability to bind proline-rich ligands; monoubiquitination of target proteins signals internalization and sorting through the endocytic pathway. 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: 212709 [Multi-domain]  Cd Length: 57  Bit Score: 35.76  E-value: 9.12e-03
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gi 564389920 1091 TVLMDGEKGGSDTLAMRSGDMVEVVEEGTEGLWY-VRDLTSSKEGWVPAS 1139
Cdd:cd11775     4 KVLYDFDAQSDDELTVKEGDVVYILDDKKSKDWWmVENVSTGKEGVVPAS 53
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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