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Conserved domains on  [gi|2024517785|ref|XP_040534742|]
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probable guanine nucleotide exchange factor MCF2L2 isoform X9 [Gallus gallus]

Protein Classification

guanine nucleotide exchange factor DBS; FYVE, RhoGEF and PH domain-containing protein( domain architecture ID 11271240)

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| FYVE, RhoGEF and PH domain-containing protein activates CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP, and also plays a role in regulating the actin cytoskeleton and cell shape

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 778-909 2.58e-65

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd01227:

Pssm-ID: 473070 [Multi-domain]  Cd Length: 126  Bit Score: 216.68  E-value: 2.58e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  778 AITGYEGDVSELGKLLMQGSFNVWTDHKKGHNKvkDLARFKPMQRHLFLYTKMLLFCKKREENTDghekTASYSFKNSLK 857
Cdd:cd01227      1 AITGYDGNLGDLGKLLMQGSFNVWTEHKKGHTK--KLARFKPMQRHIFLYEKAVLFCKKRGENGE----APSYSYKNSLN 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024517785  858 MSTVGITENVKGDNKKFEIWYNGREEVYIIQASSVELKNTWISEIRKVLTGQ 909
Cdd:cd01227     75 TTAVGLTENVKGDTKKFEIWLNGREEVFIIQAPTPEIKAAWVKAIRQVLLSQ 126
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 594-771 1.56e-51

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: 179.42  E-value: 1.56e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  594 RSHIINELIETERVYVEELQSIIEGYASEMDNPSLlhlipSVLQNKKDILFGNLPEIYEFHnRIFLKELENCIEN----P 669
Cdd:cd00160      1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELL-----PLSPEEVELLFGNIEEIYEFH-RIFLKSLEERVEEwdksG 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  670 ELLARCFLKRKEDLQIYEKYCQNKPRSEALWRQC-GDSIFFQECQRKLD---HKLSLDAYLLKPVQRITKYQLLLKEMLK 745
Cdd:cd00160     75 PRIGDVFLKLAPFFKIYSEYCSNHPDALELLKKLkKFNKFFQEFLEKAEsecGRLKLESLLLKPVQRLTKYPLLLKELLK 154

                          170       180
                   ....*....|....*....|....*..
gi 2024517785  746 CSK-NSEGTAELEEALATVLDIIKSVN 771
Cdd:cd00160    155 HTPdGHEDREDLKKALEAIKEVASQVN 181
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 24-162 4.46e-22

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: 93.90  E-value: 4.46e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785    24 LSGGRG--KDGAPIITFP--EFAGFSEIPDEDFLNVVTYLTSIPSLEAASI---GFIIIIDRRRDKWSAVKASLTRIA-- 94
Cdd:smart00516    9 IPGGRGydKDGRPVLIERagRFDLKSVTLEELLRYLVYVLEKILQEEKKTGgieGFTVIFDLKGLSMSNPDLSVLRKIlk 88

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024517785    95 ---GAFPGNLQLVFVLRPSRFIqRAIADIGIKLYRDDFKMKVPIIMLNSVSDLHGYIDKCQLTRELGGTLE 162
Cdd:smart00516   89 ilqDHYPERLGKVYIINPPWFF-RVLWKIIKPFLDEKTREKIRFVGNDSKEELLEYIDKEQLPEELGGTLD 158
SH3_DBS cd11857
Src homology 3 domain of DBL's Big Sister (DBS), a guanine nucleotide exchange factor; DBS, ...
 1134-1188 6.23e-21

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: 86.96  E-value: 6.23e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2024517785 1134 LFRVEGSFDSCFPDSLTLEDGDLVQFVQEGENGQWLVKKLVSEKSEWVPSSILQP 1188
Cdd:cd11857      1 KYTVVADYEKGGPDDLTVKSGDLVQLIHEGDEGQWLVKNLSTRKEGWVPAANLQP 55
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 293-495 1.61e-14

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: 74.02  E-value: 1.61e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  293 QLRHFEHDFREVKLTLDNlMEAQAGFSDVGDSVTRVEHLLREQKQLEEKGQEPLEKAQTLALHGEQLIQNNHYAVDSIRP 372
Cdd:cd00176      1 KLQQFLRDADELEAWLSE-KEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  373 KCVELRRICDDFTNETKKKYDILGKSLELHKQLDKAS---QWCEAGIYLLASQavDKCQSQEGAETALVEIEKFLAT--A 447
Cdd:cd00176     80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADdleQWLEEKEAALASE--DLGKDLESVEELLKKHKELEEEleA 157

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024517785  448 KEHQLSNPKEFYNQFDTILTP----EIKANAQRILQKLEDVQEMFDKRQVSL 495
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 ...
 778-909 2.58e-65

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: 216.68  E-value: 2.58e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  778 AITGYEGDVSELGKLLMQGSFNVWTDHKKGHNKvkDLARFKPMQRHLFLYTKMLLFCKKREENTDghekTASYSFKNSLK 857
Cdd:cd01227      1 AITGYDGNLGDLGKLLMQGSFNVWTEHKKGHTK--KLARFKPMQRHIFLYEKAVLFCKKRGENGE----APSYSYKNSLN 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024517785  858 MSTVGITENVKGDNKKFEIWYNGREEVYIIQASSVELKNTWISEIRKVLTGQ 909
Cdd:cd01227     75 TTAVGLTENVKGDTKKFEIWLNGREEVFIIQAPTPEIKAAWVKAIRQVLLSQ 126
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 594-771 1.56e-51

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: 179.42  E-value: 1.56e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  594 RSHIINELIETERVYVEELQSIIEGYASEMDNPSLlhlipSVLQNKKDILFGNLPEIYEFHnRIFLKELENCIEN----P 669
Cdd:cd00160      1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELL-----PLSPEEVELLFGNIEEIYEFH-RIFLKSLEERVEEwdksG 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  670 ELLARCFLKRKEDLQIYEKYCQNKPRSEALWRQC-GDSIFFQECQRKLD---HKLSLDAYLLKPVQRITKYQLLLKEMLK 745
Cdd:cd00160     75 PRIGDVFLKLAPFFKIYSEYCSNHPDALELLKKLkKFNKFFQEFLEKAEsecGRLKLESLLLKPVQRLTKYPLLLKELLK 154

                          170       180
                   ....*....|....*....|....*..
gi 2024517785  746 CSK-NSEGTAELEEALATVLDIIKSVN 771
Cdd:cd00160    155 HTPdGHEDREDLKKALEAIKEVASQVN 181
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 597-772 2.31e-48

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: 170.17  E-value: 2.31e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785   597 IINELIETERVYVEELQSIIEGYASEMDNPSLLhlipsVLQNKKDILFGNLPEIYEFHnRIFLKELENCIEN----PELL 672
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELKL-----LSPNELETLFGNIEEIYEFH-RDFLDELEERIEEwddsVERI 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785   673 ARCFLKRKEDLQIYEKYCQNKPRSEALWRQCGDSIFFQECQRKLDHK-----LSLDAYLLKPVQRITKYQLLLKEMLKCS 747
Cdd:smart00325   75 GDVFLKLEEFFKIYSEYCSNHPDALELLKKLKKNPRFQKFLKEIESSpqcrrLTLESLLLKPVQRLTKYPLLLKELLKHT 154

                           170       180
                    ....*....|....*....|....*.
gi 2024517785   748 K-NSEGTAELEEALATVLDIIKSVND 772
Cdd:smart00325  155 PeDHEDREDLKKALKAIKELANQVNE 180
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 597-771 1.08e-45

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: 162.47  E-value: 1.08e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  597 IINELIETERVYVEELQSIIEGYASEMDNPSllhlipSVLQNKKDILFGNLPEIYEFHNRIFLKELENCIENPELLARCF 676
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKPL------SESEEEIKTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIF 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  677 LKRKEDLQIYEKYCQNKPRSEALWRQCGDSI-----FFQECQ-RKLDHKLSLDAYLLKPVQRITKYQLLLKEMLK-CSKN 749
Cdd:pfam00621   75 LKFAPGFKVYSTYCSNYPKALKLLKKLLKKNpkfraFLEELEaNPECRGLDLNSFLIKPVQRIPRYPLLLKELLKhTPPD 154

                          170       180
                   ....*....|....*....|..
gi 2024517785  750 SEGTAELEEALATVLDIIKSVN 771
Cdd:pfam00621  155 HPDYEDLKKALEAIKEVAKQIN 176
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 24-162 4.46e-22

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: 93.90  E-value: 4.46e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785    24 LSGGRG--KDGAPIITFP--EFAGFSEIPDEDFLNVVTYLTSIPSLEAASI---GFIIIIDRRRDKWSAVKASLTRIA-- 94
Cdd:smart00516    9 IPGGRGydKDGRPVLIERagRFDLKSVTLEELLRYLVYVLEKILQEEKKTGgieGFTVIFDLKGLSMSNPDLSVLRKIlk 88

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024517785    95 ---GAFPGNLQLVFVLRPSRFIqRAIADIGIKLYRDDFKMKVPIIMLNSVSDLHGYIDKCQLTRELGGTLE 162
Cdd:smart00516   89 ilqDHYPERLGKVYIINPPWFF-RVLWKIIKPFLDEKTREKIRFVGNDSKEELLEYIDKEQLPEELGGTLD 158
SH3_DBS cd11857
Src homology 3 domain of DBL's Big Sister (DBS), a guanine nucleotide exchange factor; DBS, ...
 1134-1188 6.23e-21

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: 86.96  E-value: 6.23e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2024517785 1134 LFRVEGSFDSCFPDSLTLEDGDLVQFVQEGENGQWLVKKLVSEKSEWVPSSILQP 1188
Cdd:cd11857      1 KYTVVADYEKGGPDDLTVKSGDLVQLIHEGDEGQWLVKNLSTRKEGWVPAANLQP 55
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 32-163 1.07e-17

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: 80.83  E-value: 1.07e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785   32 GAPIITFPE-FAGFSEIPDEDFLNVVTYLTSIPSLEAASIGFIIIIDRR------RDKWSAVKASLTRIAGAFPGNLQLV 104
Cdd:pfam13716    1 GRPVLVFISkLLPSRPASLDDLDRLLFYLLKTLSEKLKGKPFVVVVDHTgvtsenFPSLSFLKKAYDLLPRAFKKNLKAV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024517785  105 FVLRPSRFIQRAIADIGIKLYRDDFKMKVpiIMLNSVSDLHGYIDKCQLTRELGGTLEY 163
Cdd:pfam13716   81 YVVHPSTFLRTFLKTLGSLLGSKKLRKKV--HYVSSLSELWEGIDREQLPTELPGVLSY 137
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 293-495 1.61e-14

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: 74.02  E-value: 1.61e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  293 QLRHFEHDFREVKLTLDNlMEAQAGFSDVGDSVTRVEHLLREQKQLEEKGQEPLEKAQTLALHGEQLIQNNHYAVDSIRP 372
Cdd:cd00176      1 KLQQFLRDADELEAWLSE-KEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  373 KCVELRRICDDFTNETKKKYDILGKSLELHKQLDKAS---QWCEAGIYLLASQavDKCQSQEGAETALVEIEKFLAT--A 447
Cdd:cd00176     80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADdleQWLEEKEAALASE--DLGKDLESVEELLKKHKELEEEleA 157

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024517785  448 KEHQLSNPKEFYNQFDTILTP----EIKANAQRILQKLEDVQEMFDKRQVSL 495
Cdd:cd00176    158 HEPRLKSLNELAEELLEEGHPdadeEIEEKLEELNERWEELLELAEERQKKL 209
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 11-160 2.43e-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: 71.60  E-value: 2.43e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785   11 VDIIEQLHRQFAILsGGRGKDGAPIITFPEFAGFSEIPD-EDFLNVVTYL--TSIPSLEAASIGFIIIIDRRRDKWS--- 84
Cdd:cd00170      1 LEELLELLGGIGYL-GGRDKEGRPVLVFRAGWDPPKLLDlEELLRYLVYLleKALRELEEQVEGFVVIIDLKGFSLSnls 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024517785   85 ---AVKASLTRIAGAFPGNLQLVFVLRPSRFIqRAIADIGIKLYRDDFKMKVpIIMLNSVSDLHGYIDKCQLTRELGGT 160
Cdd:cd00170     80 dlsLLKKLLKILQDHYPERLKKIYIVNAPWIF-SALWKIVKPFLSEKTRKKI-VFLGSDLEELLEYIDPDQLPKELGGT 156
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 792-906 5.32e-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: 63.34  E-value: 5.32e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785   792 LLMQGSFNVWTDHKKGHNKvkdlarfkpmQRHLFLYTKMLLFCKKREENTDghektasYSFKNSLKMSTVGITENVKGDN 871
Cdd:smart00233    1 VIKEGWLYKKSGGGKKSWK----------KRYFVLFNSTLLYYKSKKDKKS-------YKPKGSIDLSGCTVREAPDPDS 63

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 2024517785   872 KK----FEIWYNGREeVYIIQASSVELKNTWISEIRKVL 906
Cdd:smart00233   64 SKkphcFEIKTSDRK-TLLLQAESEEEREKWVEALRKAI 101
SPEC smart00150
Spectrin repeats;
295-391 3.89e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 52.33  E-value: 3.89e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785   295 RHFEHDFREVKLTLDNlMEAQAGFSDVGDSVTRVEHLLREQKQLEEKGQEPLEKAQTLALHGEQLIQNNHYAVDSIRPKC 374
Cdd:smart00150    1 QQFLRDADELEAWLEE-KEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79

                            90
                    ....*....|....*..
gi 2024517785   375 VELRRICDDFTNETKKK 391
Cdd:smart00150   80 EELNERWEELKELAEER 96
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 804-906 1.47e-07

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 50.64  E-value: 1.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  804 HKKGHNKVKdlaRFKPmqRHLFLYTKMLLFCKKREENTDghektasYSFKNSLKMSTVGITENVKGDNKK----FEIWYN 879
Cdd:pfam00169    8 LKKGGGKKK---SWKK--RYFVLFDGSLLYYKDDKSGKS-------KEPKGSISLSGCEVVEVVASDSPKrkfcFELRTG 75

                           90       100
                   ....*....|....*....|....*....
gi 2024517785  880 --GREEVYIIQASSVELKNTWISEIRKVL 906
Cdd:pfam00169   76 erTGKRTYLLQAESEEERKDWIKAIQSAI 104
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 290-519 5.82e-04

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 44.36  E-value: 5.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  290 QCLQLRHFEHD---FREVKLTLDNLMEAQAGFSD---VGDSVTRVE-HLLRE--------QKQLEEKGQEPLEKAQTlaL 354
Cdd:pfam07111   71 QLQELRRLEEEvrlLRETSLQQKMRLEAQAMELDalaVAEKAGQAEaEGLRAalagaemvRKNLEEGSQRELEEIQR--L 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  355 HGEQL---IQNNHYAVDSIRPKCVELRRICDDFtnETKKKYDIlgkslelhKQLDKASQWCEagiyLLASQaVDKCQSQE 431
Cdd:pfam07111  149 HQEQLsslTQAHEEALSSLTSKAEGLEKSLNSL--ETKRAGEA--------KQLAEAQKEAE----LLRKQ-LSKTQEEL 213

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  432 GAETALVE-IEKFLAtakeHQLsnPKEFYNQFDTILTPEIKANAQRILQKLEDVQ---EMFDKRQVSLKKLAAKQ----T 503
Cdd:pfam07111  214 EAQVTLVEsLRKYVG----EQV--PPEVHSQTWELERQELLDTMQHLQEDRADLQatvELLQVRVQSLTHMLALQeeelT 287

                          250
                   ....*....|....*.
gi 2024517785  504 RPVQPVAPHPESSPKR 519
Cdd:pfam07111  288 RKIQPSDSLEPEFPKK 303
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 588-862 6.15e-03

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


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 41.03  E-value: 6.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  588 ENLSTR---RSHIINELIETERVYVEELQSIIEGYaseMDNPSLLHLIPS-VLQNKKDILFGNLPEIYEFhNRIFLKELE 663
Cdd:COG5422    476 ESLPKQeikRQEAIYEVIYTERDFVKDLEYLRDTW---IKPLEESNIIPEnARRNFIKHVFANINEIYAV-NSKLLKALT 551

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  664 N--CIEN-PELLARCFLKRKEDLQIYEKYCQNKPRSEALWRQCGDS-----IFFQECQR-KLDHKLSLDAYLLKPVQRIT 734
Cdd:COG5422    552 NrqCLSPiVNGIADIFLDYVPKFEPFIKYGASQPYAKYEFEREKSVnpnfaRFDHEVERlDESRKLELDGYLTKPTTRLA 631

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  735 KYQLLLKEMLKCSKnsEGTAELEEaLATVLDIIKSVNDSMHQIA-ITGYEGDVSELGKLLM-------QGSFNVWTDHK- 805
Cdd:COG5422    632 RYPLLLEEVLKFTD--PDNPDTED-IPKVIDMLREFLSRLNFESgKAENRGDLFHLNQQLLfkpeyvnLGLNDEYRKIIf 708

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024517785  806 KGHNKVKDLARFKPMQR---HLFLYTKMLLFCKKREENT-DGHEKTASYSFKNSLKMSTVG 862
Cdd:COG5422    709 KGVLKRKAKSKTDGSLRgdiQFFLLDNMLLFCKAKAVNKwRQHKVFQRPIPLELLFISPDE 769
 
Name Accession Description Interval E-value
PH_Dbs cd01227
DBL's big sister protein pleckstrin homology (PH) domain; Dbs (also called MCF2-transforming ...
 778-909 2.58e-65

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: 216.68  E-value: 2.58e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  778 AITGYEGDVSELGKLLMQGSFNVWTDHKKGHNKvkDLARFKPMQRHLFLYTKMLLFCKKREENTDghekTASYSFKNSLK 857
Cdd:cd01227      1 AITGYDGNLGDLGKLLMQGSFNVWTEHKKGHTK--KLARFKPMQRHIFLYEKAVLFCKKRGENGE----APSYSYKNSLN 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024517785  858 MSTVGITENVKGDNKKFEIWYNGREEVYIIQASSVELKNTWISEIRKVLTGQ 909
Cdd:cd01227     75 TTAVGLTENVKGDTKKFEIWLNGREEVFIIQAPTPEIKAAWVKAIRQVLLSQ 126
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 594-771 1.56e-51

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: 179.42  E-value: 1.56e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  594 RSHIINELIETERVYVEELQSIIEGYASEMDNPSLlhlipSVLQNKKDILFGNLPEIYEFHnRIFLKELENCIEN----P 669
Cdd:cd00160      1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELL-----PLSPEEVELLFGNIEEIYEFH-RIFLKSLEERVEEwdksG 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  670 ELLARCFLKRKEDLQIYEKYCQNKPRSEALWRQC-GDSIFFQECQRKLD---HKLSLDAYLLKPVQRITKYQLLLKEMLK 745
Cdd:cd00160     75 PRIGDVFLKLAPFFKIYSEYCSNHPDALELLKKLkKFNKFFQEFLEKAEsecGRLKLESLLLKPVQRLTKYPLLLKELLK 154

                          170       180
                   ....*....|....*....|....*..
gi 2024517785  746 CSK-NSEGTAELEEALATVLDIIKSVN 771
Cdd:cd00160    155 HTPdGHEDREDLKKALEAIKEVASQVN 181
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 597-772 2.31e-48

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: 170.17  E-value: 2.31e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785   597 IINELIETERVYVEELQSIIEGYASEMDNPSLLhlipsVLQNKKDILFGNLPEIYEFHnRIFLKELENCIEN----PELL 672
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELKL-----LSPNELETLFGNIEEIYEFH-RDFLDELEERIEEwddsVERI 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785   673 ARCFLKRKEDLQIYEKYCQNKPRSEALWRQCGDSIFFQECQRKLDHK-----LSLDAYLLKPVQRITKYQLLLKEMLKCS 747
Cdd:smart00325   75 GDVFLKLEEFFKIYSEYCSNHPDALELLKKLKKNPRFQKFLKEIESSpqcrrLTLESLLLKPVQRLTKYPLLLKELLKHT 154

                           170       180
                    ....*....|....*....|....*.
gi 2024517785   748 K-NSEGTAELEEALATVLDIIKSVND 772
Cdd:smart00325  155 PeDHEDREDLKKALKAIKELANQVNE 180
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 597-771 1.08e-45

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: 162.47  E-value: 1.08e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  597 IINELIETERVYVEELQSIIEGYASEMDNPSllhlipSVLQNKKDILFGNLPEIYEFHNRIFLKELENCIENPELLARCF 676
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKPL------SESEEEIKTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIF 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  677 LKRKEDLQIYEKYCQNKPRSEALWRQCGDSI-----FFQECQ-RKLDHKLSLDAYLLKPVQRITKYQLLLKEMLK-CSKN 749
Cdd:pfam00621   75 LKFAPGFKVYSTYCSNYPKALKLLKKLLKKNpkfraFLEELEaNPECRGLDLNSFLIKPVQRIPRYPLLLKELLKhTPPD 154

                          170       180
                   ....*....|....*....|..
gi 2024517785  750 SEGTAELEEALATVLDIIKSVN 771
Cdd:pfam00621  155 HPDYEDLKKALEAIKEVAKQIN 176
PH_puratrophin-1 cd13242
Puratrophin-1 pleckstrin homology (PH) domain; Puratrophin-1 (also called Purkinje cell ...
 771-914 1.14e-25

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: 103.53  E-value: 1.14e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  771 NDSMHQIAITGYEGDVSELGKLLMQGSFNVWTDHKKGhnkvkdlarfkpmQRHLFLYTKMLLFCKKREENtDGHEktaSY 850
Cdd:cd13242      8 NDLLAMDSIRGCDVNLKEQGQLLRQDEFLVWQGRKKC-------------LRHVFLFEDLILFSKPKKTP-GGKD---VY 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024517785  851 SFKNSLKMSTVGITENVKGDNKKFEIWYNGRE--EVYIIQASSVELKNTWISEIRKVLTGQleACR 914
Cdd:cd13242     71 IYKHSIKTSDIGLTENVGDSGLKFEIWFRRRKarDTYILQATSPEIKQAWTSDIAKLLWKQ--AIR 134
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 24-162 4.46e-22

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: 93.90  E-value: 4.46e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785    24 LSGGRG--KDGAPIITFP--EFAGFSEIPDEDFLNVVTYLTSIPSLEAASI---GFIIIIDRRRDKWSAVKASLTRIA-- 94
Cdd:smart00516    9 IPGGRGydKDGRPVLIERagRFDLKSVTLEELLRYLVYVLEKILQEEKKTGgieGFTVIFDLKGLSMSNPDLSVLRKIlk 88

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024517785    95 ---GAFPGNLQLVFVLRPSRFIqRAIADIGIKLYRDDFKMKVPIIMLNSVSDLHGYIDKCQLTRELGGTLE 162
Cdd:smart00516   89 ilqDHYPERLGKVYIINPPWFF-RVLWKIIKPFLDEKTREKIRFVGNDSKEELLEYIDKEQLPEELGGTLD 158
SH3_DBS cd11857
Src homology 3 domain of DBL's Big Sister (DBS), a guanine nucleotide exchange factor; DBS, ...
 1134-1188 6.23e-21

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: 86.96  E-value: 6.23e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2024517785 1134 LFRVEGSFDSCFPDSLTLEDGDLVQFVQEGENGQWLVKKLVSEKSEWVPSSILQP 1188
Cdd:cd11857      1 KYTVVADYEKGGPDDLTVKSGDLVQLIHEGDEGQWLVKNLSTRKEGWVPAANLQP 55
PH_Obscurin cd13239
Obscurin pleckstrin homology (PH) domain; Obscurin (also called Obscurin-RhoGEF; ...
 779-905 2.65e-20

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: 87.98  E-value: 2.65e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  779 ITGYEGDVSELGKLLMQGSFNVWtdhkKGHNKVKDLARfkPMQRHLFLYTKMLLFCK-KREENTDghekTASYSFKNSLK 857
Cdd:cd13239      2 IENYPAPLQALGEPIRQGHFTVW----EEAPEVKTSSR--GHHRHVFLFKNCVVICKpKRDSRTD----TVTYVFKNKMK 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2024517785  858 MSTVGITENVKGDNKKFEIWYNGREEV--YIIQASSVELKNTWISEIRKV 905
Cdd:cd13239     72 LSDIDVKDTVEGDDRSFGLWHEHRGSVrkYTLQARSAIIKSSWLKDLRDL 121
PH2_Kalirin_Trio_p63RhoGEF cd13241
p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor ...
 781-910 1.70e-19

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: 86.16  E-value: 1.70e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  781 GYEGDVSELGKLLMQGSFNVwTDHKKGhnkvkdlARFKPMQRHLFLYTKMLLFC----KKREENTDGhektasYSFKNSL 856
Cdd:cd13241      6 GFDGKITAQGKLLLQGTLLV-SEPSAG-------LLQKGKERRVFLFEQIIIFSeilgKKTQFSNPG------YIYKNHI 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024517785  857 KMSTVGITENVKGDNKKFEIW---YNGREEVYIIQASSVELKNTWISEIRKVLTGQL 910
Cdd:cd13241     72 KVNKMSLEENVDGDPLRFALKsrdPNNPSETFILQAASPEVRQEWVDTINQILDTQR 128
PH1_Kalirin_Trio_like cd13240
Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; ...
 779-906 4.47e-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: 81.28  E-value: 4.47e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  779 ITGYEGDVSELGKLLMQGSFNVWtDHKKGHNKVKDlarfkpmqRHLFLYTKMLLFCKKrEENTDGHEKtasYSFKNSLKM 858
Cdd:cd13240      2 LEGCDEDLDSLGEVILQDSFQVW-DPKQLIRKGRE--------RHVFLFELCLVFSKE-VKDSNGKSK---YIYKSRLMT 68

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024517785  859 STVGITENVKGDNKKFEIWyNGREEVY----IIQASSVELKNTWISEIRKVL 906
Cdd:cd13240     69 SEIGVTEHIEGDPCKFALW-TGRVPTSdnkiVLKASSLEVKQTWVKKLREVI 119
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 32-163 1.07e-17

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: 80.83  E-value: 1.07e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785   32 GAPIITFPE-FAGFSEIPDEDFLNVVTYLTSIPSLEAASIGFIIIIDRR------RDKWSAVKASLTRIAGAFPGNLQLV 104
Cdd:pfam13716    1 GRPVLVFISkLLPSRPASLDDLDRLLFYLLKTLSEKLKGKPFVVVVDHTgvtsenFPSLSFLKKAYDLLPRAFKKNLKAV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024517785  105 FVLRPSRFIQRAIADIGIKLYRDDFKMKVpiIMLNSVSDLHGYIDKCQLTRELGGTLEY 163
Cdd:pfam13716   81 YVVHPSTFLRTFLKTLGSLLGSKKLRKKV--HYVSSLSELWEGIDREQLPTELPGVLSY 137
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 293-495 1.61e-14

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: 74.02  E-value: 1.61e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  293 QLRHFEHDFREVKLTLDNlMEAQAGFSDVGDSVTRVEHLLREQKQLEEKGQEPLEKAQTLALHGEQLIQNNHYAVDSIRP 372
Cdd:cd00176      1 KLQQFLRDADELEAWLSE-KEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  373 KCVELRRICDDFTNETKKKYDILGKSLELHKQLDKAS---QWCEAGIYLLASQavDKCQSQEGAETALVEIEKFLAT--A 447
Cdd:cd00176     80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADdleQWLEEKEAALASE--DLGKDLESVEELLKKHKELEEEleA 157

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024517785  448 KEHQLSNPKEFYNQFDTILTP----EIKANAQRILQKLEDVQEMFDKRQVSL 495
Cdd:cd00176    158 HEPRLKSLNELAEELLEEGHPdadeEIEEKLEELNERWEELLELAEERQKKL 209
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 11-160 2.43e-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: 71.60  E-value: 2.43e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785   11 VDIIEQLHRQFAILsGGRGKDGAPIITFPEFAGFSEIPD-EDFLNVVTYL--TSIPSLEAASIGFIIIIDRRRDKWS--- 84
Cdd:cd00170      1 LEELLELLGGIGYL-GGRDKEGRPVLVFRAGWDPPKLLDlEELLRYLVYLleKALRELEEQVEGFVVIIDLKGFSLSnls 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024517785   85 ---AVKASLTRIAGAFPGNLQLVFVLRPSRFIqRAIADIGIKLYRDDFKMKVpIIMLNSVSDLHGYIDKCQLTRELGGT 160
Cdd:cd00170     80 dlsLLKKLLKILQDHYPERLKKIYIVNAPWIF-SALWKIVKPFLSEKTRKKI-VFLGSDLEELLEYIDPDQLPKELGGT 156
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 792-906 5.32e-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: 63.34  E-value: 5.32e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785   792 LLMQGSFNVWTDHKKGHNKvkdlarfkpmQRHLFLYTKMLLFCKKREENTDghektasYSFKNSLKMSTVGITENVKGDN 871
Cdd:smart00233    1 VIKEGWLYKKSGGGKKSWK----------KRYFVLFNSTLLYYKSKKDKKS-------YKPKGSIDLSGCTVREAPDPDS 63

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 2024517785   872 KK----FEIWYNGREeVYIIQASSVELKNTWISEIRKVL 906
Cdd:smart00233   64 SKkphcFEIKTSDRK-TLLLQAESEEEREKWVEALRKAI 101
PH_PLEKHG1_G2_G3 cd13243
Pleckstrin homology domain-containing family G members 1, 2, and 3 pleckstrin homology (PH) ...
 754-906 9.87e-09

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: 55.43  E-value: 9.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  754 AELEEALATVLDIIKSVND-------SMH----QIAITGYEG-DVSELGKLLMQGSFNVwtdhkKGHNKvkdlarfkpmQ 821
Cdd:cd13243      2 SVVEEALDTMTQVAWHINDmkrkhehAVRvqeiQSLLDGWEGpELTTYGDLVLEGTFRM-----AGAKN----------E 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  822 RHLFLYTKMLLFCKKREENtdghektaSYSFKNSLKMSTVGITENVKGDNKKFEIW-YNGREEVYIIQASSVELKNTWIS 900
Cdd:cd13243     67 RLLFLFDKMLLITKKREDG--------ILQYKTHIMCSNLMLSESIPKEPLSFQVLpFDNPKLQYTLQAKNQEQKRLWTQ 138


                   ....*.
gi 2024517785  901 EIRKVL 906
Cdd:cd13243    139 EIKRLI 144
SPEC smart00150
Spectrin repeats;
295-391 3.89e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 52.33  E-value: 3.89e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785   295 RHFEHDFREVKLTLDNlMEAQAGFSDVGDSVTRVEHLLREQKQLEEKGQEPLEKAQTLALHGEQLIQNNHYAVDSIRPKC 374
Cdd:smart00150    1 QQFLRDADELEAWLEE-KEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79

                            90
                    ....*....|....*..
gi 2024517785   375 VELRRICDDFTNETKKK 391
Cdd:smart00150   80 EELNERWEELKELAEER 96
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 804-906 1.47e-07

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 50.64  E-value: 1.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  804 HKKGHNKVKdlaRFKPmqRHLFLYTKMLLFCKKREENTDghektasYSFKNSLKMSTVGITENVKGDNKK----FEIWYN 879
Cdd:pfam00169    8 LKKGGGKKK---SWKK--RYFVLFDGSLLYYKDDKSGKS-------KEPKGSISLSGCEVVEVVASDSPKrkfcFELRTG 75

                           90       100
                   ....*....|....*....|....*....
gi 2024517785  880 --GREEVYIIQASSVELKNTWISEIRKVL 906
Cdd:pfam00169   76 erTGKRTYLLQAESEEERKDWIKAIQSAI 104
SH3_Myosin-I_fungi cd11858
Src homology 3 domain of Type I fungal Myosins; Type I myosins (myosin-I) are actin-dependent ...
 1135-1188 4.47e-06

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: 45.07  E-value: 4.47e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024517785 1135 FRVEGSFDSCFPDSLTLEDGDLVQFVQEGENGQWLVKKLVSEKSEWVPSSILQP 1188
Cdd:cd11858      2 YKALYDFAGSVANELSLKKDDIVYIVQKEDNGWWLAKKLDESKEGWVPAAYLEE 55
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 810-902 5.02e-06

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: 46.00  E-value: 5.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  810 KVKDLARFKPMQRHLFLYTKMLLFCKkreentdgHEKTASYSFKNSLKMS-TVGITENVKGDNK-KFEIWYNGrEEVYII 887
Cdd:cd00821      7 KRGGGGLKSWKKRWFVLFEGVLLYYK--------SKKDSSYKPKGSIPLSgILEVEEVSPKERPhCFELVTPD-GRTYYL 77

                           90
                   ....*....|....*
gi 2024517785  888 QASSVELKNTWISEI 902
Cdd:cd00821     78 QADSEEERQEWLKAL 92
PH_Vav cd01223
Vav pleckstrin homology (PH) domain; Vav acts as a guanosine nucleotide exchange factor (GEF) ...
 810-906 1.32e-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: 45.70  E-value: 1.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  810 KVKDLARFKPMQRHLFLYTKMLLFCKKREENTdghektasYSFKNSLKMSTVGITEN----VKGDNKKFE-IWYNGREE- 883
Cdd:cd01223     26 KIKSHEDQKKKDRYAFLFDKVLLICKSLRGDQ--------YEYKEIINLSEYRIEDDpsrrTLKRDKRWSyQFLLVHKQg 97

                           90       100
                   ....*....|....*....|....*
gi 2024517785  884 --VYIIQASSVELKNTWISEIRKVL 906
Cdd:cd01223     98 ktAYTLYAKTEELKKKWMEAIEMAL 122
PH_unc89 cd13325
unc89 pleckstrin homology (PH) domain; unc89 is a myofibrillar protein. unc89-B the largest ...
 784-904 1.79e-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: 1.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  784 GDVSELGKLLMQGSFNVWTDHKKGHnkvkdlarfkpmQRHLFLYTKMLLFCKKREENTDghekTASYSFKNSLKMSTVGI 863
Cdd:cd13325      1 GNIHKLGRLLRHDWFTVTDGEGKAK------------ERYLFLFKSRILITKVRRISED----RSVFILKDIIRLPEVNV 64

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2024517785  864 tENVKGDNKKFEIWYNG---REEVYIIQASSVELKNTWISEIRK 904
Cdd:cd13325     65 -KQHPDDERTFELQPKLpafGILPIDFKAHKDEIKDYWLNEIEE 107
PH1_FDG_family cd13328
FYVE, RhoGEF and PH domain containing/faciogenital dysplasia family proteins, N-terminal ...
 819-902 3.90e-04

FYVE, RhoGEF and PH domain containing/faciogenital dysplasia family proteins, N-terminal Pleckstrin homology (PH) domain; In general, FGDs have a RhoGEF (DH) domain, followed by an N-terminal PH domain, a FYVE domain and a C-terminal PH domain. All FGDs are guanine nucleotide exchange factors that activates the Rho GTPase Cdc42, an important regulator of membrane trafficking. The RhoGEF domain is responsible for GEF catalytic activity, while the N-terminal PH domain is involved in intracellular targeting of the DH domain. Mutations in the FGD1 gene are responsible for the X-linked disorder known as faciogenital dysplasia (FGDY). 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: 275410  Cd Length: 92  Bit Score: 40.55  E-value: 3.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  819 PMQRHLFLYTKMLLFCKKREENTDghektASYSFKNSLKMSTVGITENVKgDNKKFEIWYNGREEVYIIQASSVELKNTW 898
Cdd:cd13328     15 PQPRYLFLFNDMLLYCVPKLSLVG-----QKFSVRNRLDVAGMKVREPVN-ENYPHTFKISGKERSLELQASSAEEKDEW 88


                   ....
gi 2024517785  899 ISEI 902
Cdd:cd13328     89 IQAI 92
SH3_p47phox_1 cd12021
First or N-terminal Src homology 3 domain of the p47phox subunit of NADPH oxidase, also called ...
 1135-1188 4.20e-04

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: 39.55  E-value: 4.20e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024517785 1135 FRVEGSFDSCFPDSLTLEDGDLVQFVQEGENGQWLVKklVSEKSEWVPSSILQP 1188
Cdd:cd12021      2 YRAIADYEKSSKSEMALKTGDVVEVVEKSENGWWFCQ--LKAKRGWVPASYLEP 53
SH3_p47phox_like cd11856
Src homology 3 domains of the p47phox subunit of NADPH oxidase and similar domains; This ...
 1135-1188 5.17e-04

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: 39.16  E-value: 5.17e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024517785 1135 FRVEGSFDSCFPDSLTLEDGDLVQFVQEGENGQWLVKKLvsEKSEWVPSSILQP 1188
Cdd:cd11856      2 YVAIADYEAQGDDEISLQEGEVVEVLEKNDSGWWYVRKG--DKEGWVPASYLEP 53
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 290-519 5.82e-04

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 44.36  E-value: 5.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  290 QCLQLRHFEHD---FREVKLTLDNLMEAQAGFSD---VGDSVTRVE-HLLRE--------QKQLEEKGQEPLEKAQTlaL 354
Cdd:pfam07111   71 QLQELRRLEEEvrlLRETSLQQKMRLEAQAMELDalaVAEKAGQAEaEGLRAalagaemvRKNLEEGSQRELEEIQR--L 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  355 HGEQL---IQNNHYAVDSIRPKCVELRRICDDFtnETKKKYDIlgkslelhKQLDKASQWCEagiyLLASQaVDKCQSQE 431
Cdd:pfam07111  149 HQEQLsslTQAHEEALSSLTSKAEGLEKSLNSL--ETKRAGEA--------KQLAEAQKEAE----LLRKQ-LSKTQEEL 213

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  432 GAETALVE-IEKFLAtakeHQLsnPKEFYNQFDTILTPEIKANAQRILQKLEDVQ---EMFDKRQVSLKKLAAKQ----T 503
Cdd:pfam07111  214 EAQVTLVEsLRKYVG----EQV--PPEVHSQTWELERQELLDTMQHLQEDRADLQatvELLQVRVQSLTHMLALQeeelT 287

                          250
                   ....*....|....*.
gi 2024517785  504 RPVQPVAPHPESSPKR 519
Cdd:pfam07111  288 RKIQPSDSLEPEFPKK 303
PH_Collybistin_ASEF cd01224
Collybistin/APC-stimulated guanine nucleotide exchange factor pleckstrin homology (PH) domain; ...
 776-904 6.85e-04

Collybistin/APC-stimulated guanine nucleotide exchange factor pleckstrin homology (PH) domain; Collybistin (also called PEM2) is homologous to the Dbl proteins ASEF (also called ARHGEF4/RhoGEF4) and SPATA13 (Spermatogenesis-associated protein 13; also called ASEF2). It activates CDC42 specifically and not any other Rho-family GTPases. Collybistin consists of an SH3 domain, followed by a RhoGEF/DH and PH domain. In Dbl proteins, the DH and PH domains catalyze the exchange of GDP for GTP in Rho GTPases, allowing them to signal to downstream effectors. It induces submembrane clustering of the receptor-associated peripheral membrane protein gephyrin, which is thought to form a scaffold underneath the postsynaptic membrane linking receptors to the cytoskeleton. It also acts as a tumor suppressor that links adenomatous polyposis coli (APC) protein, a negative regulator of the Wnt signaling pathway and promotes the phosphorylation and degradation of beta-catenin, to Cdc42. Autoinhibition of collybistin is accomplished by the binding of its SH3 domain with both the RhoGEF and PH domains to block access of Cdc42 to the GTPase-binding site. Inactivation promotes cancer progression. 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: 269931  Cd Length: 138  Bit Score: 41.09  E-value: 6.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  776 QIAITGYEG-DVSE-LGKLLMQGSFNVWTdhkKGHNKvkdlarfkpmQRHLFLYTKMLLFCKKReentdgHEKTASYSFK 853
Cdd:cd01224     11 QSTVEGWEGeDLSDrSSELIHSGELTKIS---AGRAQ----------ERTFFLFDHQLVYCKKD------LLRRKNYIYK 71

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024517785  854 NSLKMSTVGItENVKgDNKKFEI-------W--YNG-REEVYIIQASSVELKNTWISEIRK 904
Cdd:cd01224     72 GRIDTDNMEI-EDLP-DGKDDESgvtvknaWkiYNAsKNKWYVLCAKSAEEKQRWLEAFAE 130
SH3_Tks_1 cd12015
First Src homology 3 domain of Tyrosine kinase substrate (Tks) proteins; Tks proteins are Src ...
 1146-1188 8.55e-04

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: 38.55  E-value: 8.55e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2024517785 1146 PDSLTLEDGDLVQFVQEGENGQWLVKklVSEKSEWVPSSILQP 1188
Cdd:cd12015     13 PNEISLRAGDVVDVIEKNENGWWFVS--LEDEQGWVPATYLEP 53
SH3_Tks_3 cd12017
Third Src homology 3 domain of Tyrosine kinase substrate (Tks) proteins; Tks proteins are Src ...
 1139-1187 3.89e-03

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: 36.66  E-value: 3.89e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2024517785 1139 GSFDSCFPDSLTLEDGDLVQFVQEGENGQWLVKklVSEKSEWVPSSILQ 1187
Cdd:cd12017      6 GEFQATIQDGISFQKGQKVEVIDKNPSGWWYVK--IDGKEGWAPSSYIE 52
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 588-862 6.15e-03

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


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 41.03  E-value: 6.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  588 ENLSTR---RSHIINELIETERVYVEELQSIIEGYaseMDNPSLLHLIPS-VLQNKKDILFGNLPEIYEFhNRIFLKELE 663
Cdd:COG5422    476 ESLPKQeikRQEAIYEVIYTERDFVKDLEYLRDTW---IKPLEESNIIPEnARRNFIKHVFANINEIYAV-NSKLLKALT 551

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  664 N--CIEN-PELLARCFLKRKEDLQIYEKYCQNKPRSEALWRQCGDS-----IFFQECQR-KLDHKLSLDAYLLKPVQRIT 734
Cdd:COG5422    552 NrqCLSPiVNGIADIFLDYVPKFEPFIKYGASQPYAKYEFEREKSVnpnfaRFDHEVERlDESRKLELDGYLTKPTTRLA 631

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024517785  735 KYQLLLKEMLKCSKnsEGTAELEEaLATVLDIIKSVNDSMHQIA-ITGYEGDVSELGKLLM-------QGSFNVWTDHK- 805
Cdd:COG5422    632 RYPLLLEEVLKFTD--PDNPDTED-IPKVIDMLREFLSRLNFESgKAENRGDLFHLNQQLLfkpeyvnLGLNDEYRKIIf 708

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024517785  806 KGHNKVKDLARFKPMQR---HLFLYTKMLLFCKKREENT-DGHEKTASYSFKNSLKMSTVG 862
Cdd:COG5422    709 KGVLKRKAKSKTDGSLRgdiQFFLLDNMLLFCKAKAVNKwRQHKVFQRPIPLELLFISPDE 769
 
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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