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Conserved domains on  [gi|71987133|ref|NP_001021496|]
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CRAL-TRIO domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH2_Kalirin_Trio_p63RhoGEF cd13241
p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor ...
 1990-2128 1.75e-66

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: 221.37  E-value: 1.75e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 1990 VGRLQNFDKSLSAQGKLIHQGTLQISESIAGNVQKPKDRRIFLFEQSAIIADHIPPKKEFGNPTYIFKSQFMVNKMVFEP 2069
Cdd:cd13241    1 VGRLQGFDGKITAQGKLLLQGTLLVSEPSAGLLQKGKERRVFLFEQIIIFSEILGKKTQFSNPGYIYKNHIKVNKMSLEE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 2070 NVPDDPLRFVIKSSDPTQP-TSFIANAQSQEEKDEWNRKMSELLDQQKRLLAALVDPRRY 2128
Cdd:cd13241   81 NVDGDPLRFALKSRDPNNPsETFILQAASPEVRQEWVDTINQILDTQRDFLKALQSPIAY 140
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 1813-1985 5.32e-43

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: 155.54  E-value: 5.32e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133   1813 VLMELVETEQDYVKDLTSVVEGYIGNLNK--MDLPADLvgkdKIIFANIVNILEFHKTNFLKEIEKCSENYEAAGAAFVK 1890
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKplSESEEEI----KTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIFLK 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133   1891 YERRLHtLYVTYCQNKPKSDYLLAQ-----DDFEAFFADTKA-KLGHKVALCDLLIKPVQRIMKYQLLLKDILKFTERAK 1964
Cdd:pfam00621   77 FAPGFK-VYSTYCSNYPKALKLLKKllkknPKFRAFLEELEAnPECRGLDLNSFLIKPVQRIPRYPLLLKELLKHTPPDH 155

                          170       180
                   ....*....|....*....|.
gi 71987133   1965 DKTDTLKKALQVMHVVPKACD 1985
Cdd:pfam00621  156 PDYEDLKKALEAIKEVAKQIN 176
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 1208-1383 1.98e-38

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: 142.82  E-value: 1.98e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 1208 EPMRELIQSERDYIKDLERCVNIYVKEFDQAAKNGTIPTLNplkyEIFGNIEKIFKFHNDKLLHELIKYENQ---PEAVG 1284
Cdd:cd00160    3 EVIKELLQTERNYVRDLKLLVEVFLKPLDKELLPLSPEEVE----LLFGNIEEIYEFHRIFLKSLEERVEEWdksGPRIG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 1285 ASFIVWIDLLnELYTEYCVNKEQKNHVIATPDAV-SFFTGIRERHGLEINN-EIASLLIKPVQRITRYRLLIEQLMRSCT 1362
Cdd:cd00160   79 DVFLKLAPFF-KIYSEYCSNHPDALELLKKLKKFnKFFQEFLEKAESECGRlKLESLLLKPVQRLTKYPLLLKELLKHTP 157

                        170       180
                 ....*....|....*....|....
gi 71987133 1363 DKTND---LKEAYEVVCSVPRKVN 1383
Cdd:cd00160  158 DGHEDredLKKALEAIKEVASQVN 181
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 1391-1509 1.71e-34

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 cd13240:

Pssm-ID: 473070  Cd Length: 123  Bit Score: 129.04  E-value: 1.71e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 1391 LDLKDFKVDELGPFVTQDTLTFWEPRAYFKgRGKERQVFLFDISIVFAKRIEVSPKNIKYVIKGKpLPLSEVSIVEHVEG 1470
Cdd:cd13240    2 LEGCDEDLDSLGEVILQDSFQVWDPKQLIR-KGRERHVFLFELCLVFSKEVKDSNGKSKYIYKSR-LMTSEIGVTEHIEG 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 71987133 1471 DTCRFGLRVGTVSSNDNRIDLKANNHHTKVKWVQKIRDL 1509
Cdd:cd13240   80 DPCKFALWTGRVPTSDNKIVLKASSLEVKQTWVKKLREV 118
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 19-156 1.60e-17

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: 81.96  E-value: 1.60e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133      19 LRDGIAVLPGGRC--RAGQAVIVCPSREQPVNQDNLRNVFLYLFEVTSKMAREK-------GFLVVIDMRGKQ----TWT 85
Cdd:smart00516    2 LELLKAYIPGGRGydKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEKILQEEkktggieGFTVIFDLKGLSmsnpDLS 81

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71987133      86 NVRHILKALSSIESSSTVQVFIIKPEKFWE---KQKAQMSLGTWDFEVEMIS---FESLIKIIDSSHLPKTVGGSYP 156
Cdd:smart00516   82 VLRKILKILQDHYPERLGKVYIINPPWFFRvlwKIIKPFLDEKTREKIRFVGndsKEELLEYIDKEQLPEELGGTLD 158
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 2395-2473 1.89e-10

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


:

Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 59.17  E-value: 1.89e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133    2395 PDPPTDFTVKISGDHEVRLKWKA---ESGLKYCIEYRILDDSSPENWLIASTNIEKTHVSLRNFARNS-YSFRVFAYNQR 2470
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPppdDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTeYEFRVRAVNGA 80


                    ...
gi 71987133    2471 VRS 2473
Cdd:smart00060   81 GEG 83
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 2305-2391 9.57e-08

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 51.87  E-value: 9.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133   2305 PVVVEDMKDIEVVEGNDVEMCPIISSHTDFTVIWH---GPAVDSKRARIQTNQLNSRLLIKHVKKCDAGAYSVIAKNSFG 2381
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFkdgQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                           90
                   ....*....|
gi 71987133   2382 VTSTVAFLSV 2391
Cdd:pfam07679   81 EAEASAELTV 90
SH3 super family cl17036
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 1575-1634 5.55e-04

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.


The actual alignment was detected with superfamily member cd11852:

Pssm-ID: 473055  Cd Length: 62  Bit Score: 40.07  E-value: 5.55e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71987133 1575 EVWIVTADFDGQVEGHLTVHKGDRVEIVEdQATDCAEYVQVVLCDQ---PTKHGLVPASIIAP 1634
Cdd:cd11852    1 ELTVVIEDFEATSSQELTVSKGQTVEVLE-RPSSRPDWCLVRTLEQdnsPPQEGLVPSSILCI 62
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 422-568 1.34e-03

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


The actual alignment was detected with superfamily member cd00176:

Pssm-ID: 413338 [Multi-domain]  Cd Length: 213  Bit Score: 42.43  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133  422 ESLEEAIRKHDAFWAQVEEvYAQAYDDASKVTRALKEADAEDNVA-REHSSRLQRAHKQLMEKWKERQVLLHHMLAMIAF 500
Cdd:cd00176   33 ESVEALLKKHEALEAELAA-HEERVEALNELGEQLIEEGHPDAEEiQERLEELNQRWEELRELAEERRQRLEEALDLQQF 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71987133  501 ETDVRLVVDWLEQHgEPYLRRNIHiGENVNQARSFQRNHTNFQRVAANTYGNVQKLHQVYQDVTKSGS 568
Cdd:cd00176  112 FRDADDLEQWLEEK-EAALASEDL-GKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGH 177
 
Name Accession Description Interval E-value
PH2_Kalirin_Trio_p63RhoGEF cd13241
p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor ...
 1990-2128 1.75e-66

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: 221.37  E-value: 1.75e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 1990 VGRLQNFDKSLSAQGKLIHQGTLQISESIAGNVQKPKDRRIFLFEQSAIIADHIPPKKEFGNPTYIFKSQFMVNKMVFEP 2069
Cdd:cd13241    1 VGRLQGFDGKITAQGKLLLQGTLLVSEPSAGLLQKGKERRVFLFEQIIIFSEILGKKTQFSNPGYIYKNHIKVNKMSLEE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 2070 NVPDDPLRFVIKSSDPTQP-TSFIANAQSQEEKDEWNRKMSELLDQQKRLLAALVDPRRY 2128
Cdd:cd13241   81 NVDGDPLRFALKSRDPNNPsETFILQAASPEVRQEWVDTINQILDTQRDFLKALQSPIAY 140
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 1813-1985 5.32e-43

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: 155.54  E-value: 5.32e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133   1813 VLMELVETEQDYVKDLTSVVEGYIGNLNK--MDLPADLvgkdKIIFANIVNILEFHKTNFLKEIEKCSENYEAAGAAFVK 1890
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKplSESEEEI----KTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIFLK 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133   1891 YERRLHtLYVTYCQNKPKSDYLLAQ-----DDFEAFFADTKA-KLGHKVALCDLLIKPVQRIMKYQLLLKDILKFTERAK 1964
Cdd:pfam00621   77 FAPGFK-VYSTYCSNYPKALKLLKKllkknPKFRAFLEELEAnPECRGLDLNSFLIKPVQRIPRYPLLLKELLKHTPPDH 155

                          170       180
                   ....*....|....*....|.
gi 71987133   1965 DKTDTLKKALQVMHVVPKACD 1985
Cdd:pfam00621  156 PDYEDLKKALEAIKEVAKQIN 176
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 1810-1985 6.12e-43

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: 155.53  E-value: 6.12e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 1810 RSYVLMELVETEQDYVKDLTSVVEGYIGNLNKMDLPADLvGKDKIIFANIVNILEFHKtNFLKEIEKCSEN----YEAAG 1885
Cdd:cd00160    1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLPLSP-EEVELLFGNIEEIYEFHR-IFLKSLEERVEEwdksGPRIG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 1886 AAFVKYERRLHTlYVTYCQNKPKSDYLLAQ-DDFEAFFADTKAKLG---HKVALCDLLIKPVQRIMKYQLLLKDILKFTE 1961
Cdd:cd00160   79 DVFLKLAPFFKI-YSEYCSNHPDALELLKKlKKFNKFFQEFLEKAEsecGRLKLESLLLKPVQRLTKYPLLLKELLKHTP 157

                        170       180
                 ....*....|....*....|....
gi 71987133 1962 RAKDKTDTLKKALQVMHVVPKACD 1985
Cdd:cd00160  158 DGHEDREDLKKALEAIKEVASQVN 181
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 1813-1986 3.68e-42

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: 153.23  E-value: 3.68e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133    1813 VLMELVETEQDYVKDLTSVVEGYIGNLNKMD--LPADLVgkdKIIFANIVNILEFHkTNFLKEIEKCSEN----YEAAGA 1886
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELklLSPNEL---ETLFGNIEEIYEFH-RDFLDELEERIEEwddsVERIGD 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133    1887 AFVKYERRLHTlYVTYCQNKPKSDYLLAQ----DDFEAFFADTKAKLGH-KVALCDLLIKPVQRIMKYQLLLKDILKFTE 1961
Cdd:smart00325   77 VFLKLEEFFKI-YSEYCSNHPDALELLKKlkknPRFQKFLKEIESSPQCrRLTLESLLLKPVQRLTKYPLLLKELLKHTP 155

                           170       180
                    ....*....|....*....|....*
gi 71987133    1962 RAKDKTDTLKKALQVMHVVPKACDD 1986
Cdd:smart00325  156 EDHEDREDLKKALKAIKELANQVNE 180
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 1208-1383 1.98e-38

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: 142.82  E-value: 1.98e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 1208 EPMRELIQSERDYIKDLERCVNIYVKEFDQAAKNGTIPTLNplkyEIFGNIEKIFKFHNDKLLHELIKYENQ---PEAVG 1284
Cdd:cd00160    3 EVIKELLQTERNYVRDLKLLVEVFLKPLDKELLPLSPEEVE----LLFGNIEEIYEFHRIFLKSLEERVEEWdksGPRIG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 1285 ASFIVWIDLLnELYTEYCVNKEQKNHVIATPDAV-SFFTGIRERHGLEINN-EIASLLIKPVQRITRYRLLIEQLMRSCT 1362
Cdd:cd00160   79 DVFLKLAPFF-KIYSEYCSNHPDALELLKKLKKFnKFFQEFLEKAESECGRlKLESLLLKPVQRLTKYPLLLKELLKHTP 157

                        170       180
                 ....*....|....*....|....
gi 71987133 1363 DKTND---LKEAYEVVCSVPRKVN 1383
Cdd:cd00160  158 DGHEDredLKKALEAIKEVASQVN 181
PH1_Kalirin_Trio_like cd13240
Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; ...
 1391-1509 1.71e-34

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: 129.04  E-value: 1.71e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 1391 LDLKDFKVDELGPFVTQDTLTFWEPRAYFKgRGKERQVFLFDISIVFAKRIEVSPKNIKYVIKGKpLPLSEVSIVEHVEG 1470
Cdd:cd13240    2 LEGCDEDLDSLGEVILQDSFQVWDPKQLIR-KGRERHVFLFELCLVFSKEVKDSNGKSKYIYKSR-LMTSEIGVTEHIEG 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 71987133 1471 DTCRFGLRVGTVSSNDNRIDLKANNHHTKVKWVQKIRDL 1509
Cdd:cd13240   80 DPCKFALWTGRVPTSDNKIVLKASSLEVKQTWVKKLREV 118
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 1210-1384 2.32e-32

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: 125.11  E-value: 2.32e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133    1210 MRELIQSERDYIKDLERCVNIYVKEFDQAAKngtiPTLNPLKYEIFGNIEKIFKFHNDkLLHELIKY----ENQPEAVGA 1285
Cdd:smart00325    2 LKELLQTERNYVRDLKLLVEVFLKPLKKELK----LLSPNELETLFGNIEEIYEFHRD-FLDELEERieewDDSVERIGD 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133    1286 SFIVWIDLLnELYTEYCVNKEQKNHVIAT-PDAVSFFTGIRERHGLEINN--EIASLLIKPVQRITRYRLLIEQLMRSCT 1362
Cdd:smart00325   77 VFLKLEEFF-KIYSEYCSNHPDALELLKKlKKNPRFQKFLKEIESSPQCRrlTLESLLLKPVQRLTKYPLLLKELLKHTP 155

                           170       180
                    ....*....|....*....|....*
gi 71987133    1363 DKTND---LKEAYEVVCSVPRKVND 1384
Cdd:smart00325  156 EDHEDredLKKALKAIKELANQVNE 180
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 1210-1383 3.69e-30

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: 118.94  E-value: 3.69e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133   1210 MRELIQSERDYIKDLERCVNIYVKEFDQAakngtIPTLNPLKYEIFGNIEKIFKFHNDKLLHELIKYENQPEAVGASFIV 1289
Cdd:pfam00621    2 IKELLQTERSYVRDLEILVEVFLPPNSKP-----LSESEEEIKTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIFLK 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133   1290 WIDLLnELYTEYCVNKEQKNHVIAT-----PDAVSFFTGIRER---HGLEINneiaSLLIKPVQRITRYRLLIEQLMRSC 1361
Cdd:pfam00621   77 FAPGF-KVYSTYCSNYPKALKLLKKllkknPKFRAFLEELEANpecRGLDLN----SFLIKPVQRIPRYPLLLKELLKHT 151

                          170       180
                   ....*....|....*....|....*
gi 71987133   1362 TDKTND---LKEAYEVVCSVPRKVN 1383
Cdd:pfam00621  152 PPDHPDyedLKKALEAIKEVAKQIN 176
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 19-156 1.60e-17

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: 81.96  E-value: 1.60e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133      19 LRDGIAVLPGGRC--RAGQAVIVCPSREQPVNQDNLRNVFLYLFEVTSKMAREK-------GFLVVIDMRGKQ----TWT 85
Cdd:smart00516    2 LELLKAYIPGGRGydKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEKILQEEkktggieGFTVIFDLKGLSmsnpDLS 81

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71987133      86 NVRHILKALSSIESSSTVQVFIIKPEKFWE---KQKAQMSLGTWDFEVEMIS---FESLIKIIDSSHLPKTVGGSYP 156
Cdd:smart00516   82 VLRKILKILQDHYPERLGKVYIINPPWFFRvlwKIIKPFLDEKTREKIRFVGndsKEELLEYIDKEQLPEELGGTLD 158
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 2395-2473 1.89e-10

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 59.17  E-value: 1.89e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133    2395 PDPPTDFTVKISGDHEVRLKWKA---ESGLKYCIEYRILDDSSPENWLIASTNIEKTHVSLRNFARNS-YSFRVFAYNQR 2470
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPppdDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTeYEFRVRAVNGA 80


                    ...
gi 71987133    2471 VRS 2473
Cdd:smart00060   81 GEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 2395-2481 5.62e-10

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 58.28  E-value: 5.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 2395 PDPPTDFTVKISGDHEVRLKWKAESG-----LKYCIEYRILDDSSPENwlIASTNIEKTHVSLRNFARNS-YSFRVFAYN 2468
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDdggpiTGYVVEYREKGSGDWKE--VEVTPGSETSYTLTGLKPGTeYEFRVRAVN 78

                         90
                 ....*....|...
gi 71987133 2469 QRVRSAPSQCICI 2481
Cdd:cd00063   79 GGGESPPSESVTV 91
I-set pfam07679
Immunoglobulin I-set domain;
2305-2391 9.57e-08

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 51.87  E-value: 9.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133   2305 PVVVEDMKDIEVVEGNDVEMCPIISSHTDFTVIWH---GPAVDSKRARIQTNQLNSRLLIKHVKKCDAGAYSVIAKNSFG 2381
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFkdgQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                           90
                   ....*....|
gi 71987133   2382 VTSTVAFLSV 2391
Cdd:pfam07679   81 EAEASAELTV 90
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
 2314-2392 3.54e-07

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 49.90  E-value: 3.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 2314 IEVVEGNDVEMCPIISSHTDFTVIWH---GPAVDSKRARIQTNQLNSRLLIKHVKKCDAGAYSVIAKNSFGVTStvAFLS 2390
Cdd:cd05748    2 IVVRAGESLRLDIPIKGRPTPTVTWSkdgQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKS--ATIN 79


                 ..
gi 71987133 2391 VI 2392
Cdd:cd05748   80 VK 81
fn3 pfam00041
Fibronectin type III domain;
2396-2476 7.72e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 46.25  E-value: 7.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133   2396 DPPTDFTVKISGDHEVRLKWKAESG-----LKYCIEYRILDDSSPENWLIASTNieKTHVSLRNF-ARNSYSFRVFAYNQ 2469
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDgngpiTGYEVEYRPKNSGEPWNEITVPGT--TTSVTLTGLkPGTEYEVRVQAVNG 78


                   ....*..
gi 71987133   2470 RVRSAPS 2476
Cdd:pfam00041   79 GGEGPPS 85
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 1407-1511 8.56e-06

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: 46.77  E-value: 8.56e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133    1407 QDTLTFWEPRayFKGRGKERQVFLFDISIVFAKRievSPKNIKYVIKGKpLPLSEVSIVEHVEGDTC--RFGLRVgtVSS 1484
Cdd:smart00233    4 EGWLYKKSGG--GKKSWKKRYFVLFNSTLLYYKS---KKDKKSYKPKGS-IDLSGCTVREAPDPDSSkkPHCFEI--KTS 75

                            90       100
                    ....*....|....*....|....*..
gi 71987133    1485 NDNRIDLKANNHHTKVKWVQKIRDLTA 1511
Cdd:smart00233   76 DRKTLLLQAESEEEREKWVEALRKAIA 102
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
2372-2477 1.30e-05

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 50.39  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 2372 YSVIAKNSFGVTS---TVAFLSVISIPDPPTDFTVKISGDHEVRLKWKA--ESGLKYcieYRIL-DDSSPENW-LIASTN 2444
Cdd:COG3401  207 YRVAATDTGGESApsnEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPvtESDATG---YRVYrSNSGDGPFtKVATVT 283

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 71987133 2445 ieKTHVSLRNFARN-SYSFRVFAYNQR-VRSAPSQ 2477
Cdd:COG3401  284 --TTSYTDTGLTNGtTYYYRVTAVDAAgNESAPSN 316
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 34-160 3.55e-04

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: 43.08  E-value: 3.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133     34 GQAVIVCPSR---EQPVNQDNLRNVFLYLFEVTSKMAREKGFLVVIDMRGKQTWTNVR--HILKALSSIESSSTVQ---V 105
Cdd:pfam13716    1 GRPVLVFISKllpSRPASLDDLDRLLFYLLKTLSEKLKGKPFVVVVDHTGVTSENFPSlsFLKKAYDLLPRAFKKNlkaV 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133    106 FIIKPEKFWEK-----QKAQMSLGTWDFEVEMISFESLIKIIDSSHLPKTVGGSYPYDHD 160
Cdd:pfam13716   81 YVVHPSTFLRTflktlGSLLGSKKLRKKVHYVSSLSELWEGIDREQLPTELPGVLSYDEE 140
SH3_Kalirin_1 cd11852
First Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or ...
 1575-1634 5.55e-04

First Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or TRAD, is a large neuronal dual Rho guanine nucleotide exchange factor (RhoGEF) that activates Rac1, RhoA, and RhoG using two RhoGEF domains. Kalirin exists in many isoforms generated by alternative splicing and the use of multiple promoters; the major isoforms are kalirin-7, -9, and -12, which differ at their C-terminal ends. Kalirin-12, the longest isoform, contains an N-terminal Sec14p domain, spectrin-like repeats, two RhoGEF domains, two SH3 domains, as well as Ig, FNIII, and kinase domains at the C-terminal end. Kalirin-7 contains only a single RhoGEF domain and does not contain an SH3 domain. Kalirin, through its many isoforms, interacts with many different proteins and is able to localize to different locations within the cell. It influences neurite initiation, axon growth, dendritic morphogenesis, vesicle trafficking, neuronal maintenance, and neurodegeneration. 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: 212786  Cd Length: 62  Bit Score: 40.07  E-value: 5.55e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71987133 1575 EVWIVTADFDGQVEGHLTVHKGDRVEIVEdQATDCAEYVQVVLCDQ---PTKHGLVPASIIAP 1634
Cdd:cd11852    1 ELTVVIEDFEATSSQELTVSKGQTVEVLE-RPSSRPDWCLVRTLEQdnsPPQEGLVPSSILCI 62
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 1573-1633 5.67e-04

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: 39.83  E-value: 5.67e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71987133    1573 SSEVWIVTADFDGQVEGHLTVHKGDRVEIVEDqatDCAEYVQVVLCDQptKHGLVPASIIA 1633
Cdd:smart00326    1 EGPQVRALYDYTAQDPDELSFKKGDIITVLEK---SDDGWWKGRLGRG--KEGLFPSNYVE 56
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 2312-2391 7.63e-04

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 40.57  E-value: 7.63e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133    2312 KDIEVVEGNDVEM-CPIiSSHTDFTVIWH----GPAVDSKRARIQTNQLNSRLLIKHVKKCDAGAYSVIAKNSFGVTSTV 2386
Cdd:smart00410    2 PSVTVKEGESVTLsCEA-SGSPPPEVTWYkqggKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80


                    ....*
gi 71987133    2387 AFLSV 2391
Cdd:smart00410   81 TTLTV 85
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 422-568 1.34e-03

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: 42.43  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133  422 ESLEEAIRKHDAFWAQVEEvYAQAYDDASKVTRALKEADAEDNVA-REHSSRLQRAHKQLMEKWKERQVLLHHMLAMIAF 500
Cdd:cd00176   33 ESVEALLKKHEALEAELAA-HEERVEALNELGEQLIEEGHPDAEEiQERLEELNQRWEELRELAEERRQRLEEALDLQQF 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71987133  501 ETDVRLVVDWLEQHgEPYLRRNIHiGENVNQARSFQRNHTNFQRVAANTYGNVQKLHQVYQDVTKSGS 568
Cdd:cd00176  112 FRDADDLEQWLEEK-EAALASEDL-GKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGH 177
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 20-154 1.87e-03

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: 41.17  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133   20 RDGIAVLPGGRCRAGQAVIVCPSREQP---VNQDNLRNVFLYLFEVTSKMAREK--GFLVVIDMRG-----KQTWTNVRH 89
Cdd:cd00170    7 LLGGIGYLGGRDKEGRPVLVFRAGWDPpklLDLEELLRYLVYLLEKALRELEEQveGFVVIIDLKGfslsnLSDLSLLKK 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133   90 ILKALSS-----------IESSSTVQVF--IIKP---EKFWEKqkaqmslgtwdfeVEMIS--FESLIKIIDSSHLPKTV 151
Cdd:cd00170   87 LLKILQDhyperlkkiyiVNAPWIFSALwkIVKPflsEKTRKK-------------IVFLGsdLEELLEYIDPDQLPKEL 153


                 ...
gi 71987133  152 GGS 154
Cdd:cd00170  154 GGT 156
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 1419-1511 5.53e-03

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 38.70  E-value: 5.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133   1419 FKGRGKERQVFLFDISIVFAKRievSPKNIKYVIKGKpLPLSEVSIVEHVEGDT----CRFGLRVGTvSSNDNRIDLKAN 1494
Cdd:pfam00169   14 KKKSWKKRYFVLFDGSLLYYKD---DKSGKSKEPKGS-ISLSGCEVVEVVASDSpkrkFCFELRTGE-RTGKRTYLLQAE 88

                           90
                   ....*....|....*..
gi 71987133   1495 NHHTKVKWVQKIRDLTA 1511
Cdd:pfam00169   89 SEEERKDWIKAIQSAIR 105
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 2006-2113 7.41e-03

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: 38.30  E-value: 7.41e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133    2006 LIHQGTLQISESiaGNVQKPKDRRIFLFEQSAIIAdhippKKEFGNPTYIFKSQFMVNKMVFEPNV----PDDPLRFVIK 2081
Cdd:smart00233    1 VIKEGWLYKKSG--GGKKSWKKRYFVLFNSTLLYY-----KSKKDKKSYKPKGSIDLSGCTVREAPdpdsSKKPHCFEIK 73

                            90       100       110
                    ....*....|....*....|....*....|..
gi 71987133    2082 SSDPTqptSFIANAQSQEEKDEWNRKMSELLD 2113
Cdd:smart00233   74 TSDRK---TLLLQAESEEEREKWVEALRKAIA 102
 
Name Accession Description Interval E-value
PH2_Kalirin_Trio_p63RhoGEF cd13241
p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor ...
 1990-2128 1.75e-66

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: 221.37  E-value: 1.75e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 1990 VGRLQNFDKSLSAQGKLIHQGTLQISESIAGNVQKPKDRRIFLFEQSAIIADHIPPKKEFGNPTYIFKSQFMVNKMVFEP 2069
Cdd:cd13241    1 VGRLQGFDGKITAQGKLLLQGTLLVSEPSAGLLQKGKERRVFLFEQIIIFSEILGKKTQFSNPGYIYKNHIKVNKMSLEE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 2070 NVPDDPLRFVIKSSDPTQP-TSFIANAQSQEEKDEWNRKMSELLDQQKRLLAALVDPRRY 2128
Cdd:cd13241   81 NVDGDPLRFALKSRDPNNPsETFILQAASPEVRQEWVDTINQILDTQRDFLKALQSPIAY 140
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 1813-1985 5.32e-43

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: 155.54  E-value: 5.32e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133   1813 VLMELVETEQDYVKDLTSVVEGYIGNLNK--MDLPADLvgkdKIIFANIVNILEFHKTNFLKEIEKCSENYEAAGAAFVK 1890
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKplSESEEEI----KTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIFLK 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133   1891 YERRLHtLYVTYCQNKPKSDYLLAQ-----DDFEAFFADTKA-KLGHKVALCDLLIKPVQRIMKYQLLLKDILKFTERAK 1964
Cdd:pfam00621   77 FAPGFK-VYSTYCSNYPKALKLLKKllkknPKFRAFLEELEAnPECRGLDLNSFLIKPVQRIPRYPLLLKELLKHTPPDH 155

                          170       180
                   ....*....|....*....|.
gi 71987133   1965 DKTDTLKKALQVMHVVPKACD 1985
Cdd:pfam00621  156 PDYEDLKKALEAIKEVAKQIN 176
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 1810-1985 6.12e-43

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: 155.53  E-value: 6.12e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 1810 RSYVLMELVETEQDYVKDLTSVVEGYIGNLNKMDLPADLvGKDKIIFANIVNILEFHKtNFLKEIEKCSEN----YEAAG 1885
Cdd:cd00160    1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLPLSP-EEVELLFGNIEEIYEFHR-IFLKSLEERVEEwdksGPRIG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 1886 AAFVKYERRLHTlYVTYCQNKPKSDYLLAQ-DDFEAFFADTKAKLG---HKVALCDLLIKPVQRIMKYQLLLKDILKFTE 1961
Cdd:cd00160   79 DVFLKLAPFFKI-YSEYCSNHPDALELLKKlKKFNKFFQEFLEKAEsecGRLKLESLLLKPVQRLTKYPLLLKELLKHTP 157

                        170       180
                 ....*....|....*....|....
gi 71987133 1962 RAKDKTDTLKKALQVMHVVPKACD 1985
Cdd:cd00160  158 DGHEDREDLKKALEAIKEVASQVN 181
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 1813-1986 3.68e-42

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: 153.23  E-value: 3.68e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133    1813 VLMELVETEQDYVKDLTSVVEGYIGNLNKMD--LPADLVgkdKIIFANIVNILEFHkTNFLKEIEKCSEN----YEAAGA 1886
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELklLSPNEL---ETLFGNIEEIYEFH-RDFLDELEERIEEwddsVERIGD 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133    1887 AFVKYERRLHTlYVTYCQNKPKSDYLLAQ----DDFEAFFADTKAKLGH-KVALCDLLIKPVQRIMKYQLLLKDILKFTE 1961
Cdd:smart00325   77 VFLKLEEFFKI-YSEYCSNHPDALELLKKlkknPRFQKFLKEIESSPQCrRLTLESLLLKPVQRLTKYPLLLKELLKHTP 155

                           170       180
                    ....*....|....*....|....*
gi 71987133    1962 RAKDKTDTLKKALQVMHVVPKACDD 1986
Cdd:smart00325  156 EDHEDREDLKKALKAIKELANQVNE 180
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 1208-1383 1.98e-38

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: 142.82  E-value: 1.98e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 1208 EPMRELIQSERDYIKDLERCVNIYVKEFDQAAKNGTIPTLNplkyEIFGNIEKIFKFHNDKLLHELIKYENQ---PEAVG 1284
Cdd:cd00160    3 EVIKELLQTERNYVRDLKLLVEVFLKPLDKELLPLSPEEVE----LLFGNIEEIYEFHRIFLKSLEERVEEWdksGPRIG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 1285 ASFIVWIDLLnELYTEYCVNKEQKNHVIATPDAV-SFFTGIRERHGLEINN-EIASLLIKPVQRITRYRLLIEQLMRSCT 1362
Cdd:cd00160   79 DVFLKLAPFF-KIYSEYCSNHPDALELLKKLKKFnKFFQEFLEKAESECGRlKLESLLLKPVQRLTKYPLLLKELLKHTP 157

                        170       180
                 ....*....|....*....|....
gi 71987133 1363 DKTND---LKEAYEVVCSVPRKVN 1383
Cdd:cd00160  158 DGHEDredLKKALEAIKEVASQVN 181
PH1_Kalirin_Trio_like cd13240
Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; ...
 1391-1509 1.71e-34

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: 129.04  E-value: 1.71e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 1391 LDLKDFKVDELGPFVTQDTLTFWEPRAYFKgRGKERQVFLFDISIVFAKRIEVSPKNIKYVIKGKpLPLSEVSIVEHVEG 1470
Cdd:cd13240    2 LEGCDEDLDSLGEVILQDSFQVWDPKQLIR-KGRERHVFLFELCLVFSKEVKDSNGKSKYIYKSR-LMTSEIGVTEHIEG 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 71987133 1471 DTCRFGLRVGTVSSNDNRIDLKANNHHTKVKWVQKIRDL 1509
Cdd:cd13240   80 DPCKFALWTGRVPTSDNKIVLKASSLEVKQTWVKKLREV 118
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 1210-1384 2.32e-32

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: 125.11  E-value: 2.32e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133    1210 MRELIQSERDYIKDLERCVNIYVKEFDQAAKngtiPTLNPLKYEIFGNIEKIFKFHNDkLLHELIKY----ENQPEAVGA 1285
Cdd:smart00325    2 LKELLQTERNYVRDLKLLVEVFLKPLKKELK----LLSPNELETLFGNIEEIYEFHRD-FLDELEERieewDDSVERIGD 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133    1286 SFIVWIDLLnELYTEYCVNKEQKNHVIAT-PDAVSFFTGIRERHGLEINN--EIASLLIKPVQRITRYRLLIEQLMRSCT 1362
Cdd:smart00325   77 VFLKLEEFF-KIYSEYCSNHPDALELLKKlKKNPRFQKFLKEIESSPQCRrlTLESLLLKPVQRLTKYPLLLKELLKHTP 155

                           170       180
                    ....*....|....*....|....*
gi 71987133    1363 DKTND---LKEAYEVVCSVPRKVND 1384
Cdd:smart00325  156 EDHEDredLKKALKAIKELANQVNE 180
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 1210-1383 3.69e-30

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: 118.94  E-value: 3.69e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133   1210 MRELIQSERDYIKDLERCVNIYVKEFDQAakngtIPTLNPLKYEIFGNIEKIFKFHNDKLLHELIKYENQPEAVGASFIV 1289
Cdd:pfam00621    2 IKELLQTERSYVRDLEILVEVFLPPNSKP-----LSESEEEIKTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIFLK 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133   1290 WIDLLnELYTEYCVNKEQKNHVIAT-----PDAVSFFTGIRER---HGLEINneiaSLLIKPVQRITRYRLLIEQLMRSC 1361
Cdd:pfam00621   77 FAPGF-KVYSTYCSNYPKALKLLKKllkknPKFRAFLEELEANpecRGLDLN----SFLIKPVQRIPRYPLLLKELLKHT 151

                          170       180
                   ....*....|....*....|....*
gi 71987133   1362 TDKTND---LKEAYEVVCSVPRKVN 1383
Cdd:pfam00621  152 PPDHPDyedLKKALEAIKEVAKQIN 176
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 19-156 1.60e-17

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: 81.96  E-value: 1.60e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133      19 LRDGIAVLPGGRC--RAGQAVIVCPSREQPVNQDNLRNVFLYLFEVTSKMAREK-------GFLVVIDMRGKQ----TWT 85
Cdd:smart00516    2 LELLKAYIPGGRGydKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEKILQEEkktggieGFTVIFDLKGLSmsnpDLS 81

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71987133      86 NVRHILKALSSIESSSTVQVFIIKPEKFWE---KQKAQMSLGTWDFEVEMIS---FESLIKIIDSSHLPKTVGGSYP 156
Cdd:smart00516   82 VLRKILKILQDHYPERLGKVYIINPPWFFRvlwKIIKPFLDEKTREKIRFVGndsKEELLEYIDKEQLPEELGGTLD 158
PH1_Kalirin_Trio_like cd13240
Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; ...
 1993-2112 1.72e-14

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: 72.03  E-value: 1.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 1993 LQNFDKSLSAQGKLIHQGTLQISESIAgNVQKPKDRRIFLFEQSAIIADHIppKKEFGNPTYIFKSQFMVNKMVFEPNVP 2072
Cdd:cd13240    2 LEGCDEDLDSLGEVILQDSFQVWDPKQ-LIRKGRERHVFLFELCLVFSKEV--KDSNGKSKYIYKSRLMTSEIGVTEHIE 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 71987133 2073 DDPLRFVIKS-SDPTQPTSFIANAQSQEEKDEWNRKMSELL 2112
Cdd:cd13240   79 GDPCKFALWTgRVPTSDNKIVLKASSLEVKQTWVKKLREVI 119
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 2395-2473 1.89e-10

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 59.17  E-value: 1.89e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133    2395 PDPPTDFTVKISGDHEVRLKWKA---ESGLKYCIEYRILDDSSPENWLIASTNIEKTHVSLRNFARNS-YSFRVFAYNQR 2470
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPppdDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTeYEFRVRAVNGA 80


                    ...
gi 71987133    2471 VRS 2473
Cdd:smart00060   81 GEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 2395-2481 5.62e-10

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 58.28  E-value: 5.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 2395 PDPPTDFTVKISGDHEVRLKWKAESG-----LKYCIEYRILDDSSPENwlIASTNIEKTHVSLRNFARNS-YSFRVFAYN 2468
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDdggpiTGYVVEYREKGSGDWKE--VEVTPGSETSYTLTGLKPGTeYEFRVRAVN 78

                         90
                 ....*....|...
gi 71987133 2469 QRVRSAPSQCICI 2481
Cdd:cd00063   79 GGGESPPSESVTV 91
PH2_Kalirin_Trio_p63RhoGEF cd13241
p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor ...
 1393-1509 3.64e-09

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: 57.27  E-value: 3.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 1393 LKDF--KVDELGPFVTQDTLTFWEPRAYFKGRGKERQVFLFDISIVFA-----KRIEVSPKNI-KYVIKgkplpLSEVSI 1464
Cdd:cd13241    4 LQGFdgKITAQGKLLLQGTLLVSEPSAGLLQKGKERRVFLFEQIIIFSeilgkKTQFSNPGYIyKNHIK-----VNKMSL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 71987133 1465 VEHVEGDTCRFGLRVGTVSSNDNRIDLKANNHHTKVKWVQKIRDL 1509
Cdd:cd13241   79 EENVDGDPLRFALKSRDPNNPSETFILQAASPEVRQEWVDTINQI 123
PH_Obscurin cd13239
Obscurin pleckstrin homology (PH) domain; Obscurin (also called Obscurin-RhoGEF; ...
 1401-1509 9.34e-09

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: 55.63  E-value: 9.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 1401 LGPFVTQDTLTFWE--PRAYFKGRGKERQVFLFDISIVFAK-RIEVSPKNIKYVIKGKpLPLSEVSIVEHVEGDTCRFGL 1477
Cdd:cd13239   12 LGEPIRQGHFTVWEeaPEVKTSSRGHHRHVFLFKNCVVICKpKRDSRTDTVTYVFKNK-MKLSDIDVKDTVEGDDRSFGL 90

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 71987133 1478 ---RVGTVssndNRIDLKANNHHTKVKWVQKIRDL 1509
Cdd:cd13239   91 wheHRGSV----RKYTLQARSAIIKSSWLKDLRDL 121
I-set pfam07679
Immunoglobulin I-set domain;
2305-2391 9.57e-08

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 51.87  E-value: 9.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133   2305 PVVVEDMKDIEVVEGNDVEMCPIISSHTDFTVIWH---GPAVDSKRARIQTNQLNSRLLIKHVKKCDAGAYSVIAKNSFG 2381
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFkdgQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                           90
                   ....*....|
gi 71987133   2382 VTSTVAFLSV 2391
Cdd:pfam07679   81 EAEASAELTV 90
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
 2314-2392 3.54e-07

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 49.90  E-value: 3.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 2314 IEVVEGNDVEMCPIISSHTDFTVIWH---GPAVDSKRARIQTNQLNSRLLIKHVKKCDAGAYSVIAKNSFGVTStvAFLS 2390
Cdd:cd05748    2 IVVRAGESLRLDIPIKGRPTPTVTWSkdgQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKS--ATIN 79


                 ..
gi 71987133 2391 VI 2392
Cdd:cd05748   80 VK 81
PH_puratrophin-1 cd13242
Puratrophin-1 pleckstrin homology (PH) domain; Puratrophin-1 (also called Purkinje cell ...
 1986-2115 5.18e-07

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: 51.14  E-value: 5.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 1986 DMMQVGRLQNFDKSLSAQGKLIHQGTLQISESIagnvqKPKDRRIFLFEQSAIIADhiPPKKEFGNPTYIFKSQFMVNKM 2065
Cdd:cd13242    9 DLLAMDSIRGCDVNLKEQGQLLRQDEFLVWQGR-----KKCLRHVFLFEDLILFSK--PKKTPGGKDVYIYKHSIKTSDI 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 71987133 2066 VFEPNVPDDPLRFVI-----KSSDptqptSFIANAQSQEEKDEWNRKMSELLDQQ 2115
Cdd:cd13242   82 GLTENVGDSGLKFEIwfrrrKARD-----TYILQATSPEIKQAWTSDIAKLLWKQ 131
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 2305-2391 1.22e-06

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 48.65  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 2305 PVVVEDMKDIEVVEGNDVEMCPIISSHTDFTVIW----HGPAVDSKRARIQTNQLNSRLLIKHVKKCDAGAYSVIAKNSF 2380
Cdd:cd05744    1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWqlngKPVRPDSAHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRA 80

                         90
                 ....*....|.
gi 71987133 2381 GVTSTVAFLSV 2391
Cdd:cd05744   81 GENSFNAELVV 91
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 2305-2391 2.97e-06

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 47.80  E-value: 2.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 2305 PVVVEDMKDIEVVEGNDVEMCPIISSHTDFTVIWH------GPAVDSKRARIQTNQLNSRLLIKHVKKCDAGAYSVIAKN 2378
Cdd:cd20951    1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYkngvpiDPSSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80

                         90
                 ....*....|...
gi 71987133 2379 SFGVTSTVAFLSV 2391
Cdd:cd20951   81 IHGEASSSASVVV 93
fn3 pfam00041
Fibronectin type III domain;
2396-2476 7.72e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 46.25  E-value: 7.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133   2396 DPPTDFTVKISGDHEVRLKWKAESG-----LKYCIEYRILDDSSPENWLIASTNieKTHVSLRNF-ARNSYSFRVFAYNQ 2469
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDgngpiTGYEVEYRPKNSGEPWNEITVPGT--TTSVTLTGLkPGTEYEVRVQAVNG 78


                   ....*..
gi 71987133   2470 RVRSAPS 2476
Cdd:pfam00041   79 GGEGPPS 85
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 1407-1511 8.56e-06

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: 46.77  E-value: 8.56e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133    1407 QDTLTFWEPRayFKGRGKERQVFLFDISIVFAKRievSPKNIKYVIKGKpLPLSEVSIVEHVEGDTC--RFGLRVgtVSS 1484
Cdd:smart00233    4 EGWLYKKSGG--GKKSWKKRYFVLFNSTLLYYKS---KKDKKSYKPKGS-IDLSGCTVREAPDPDSSkkPHCFEI--KTS 75

                            90       100
                    ....*....|....*....|....*..
gi 71987133    1485 NDNRIDLKANNHHTKVKWVQKIRDLTA 1511
Cdd:smart00233   76 DRKTLLLQAESEEEREKWVEALRKAIA 102
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
2372-2477 1.30e-05

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 50.39  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 2372 YSVIAKNSFGVTS---TVAFLSVISIPDPPTDFTVKISGDHEVRLKWKA--ESGLKYcieYRIL-DDSSPENW-LIASTN 2444
Cdd:COG3401  207 YRVAATDTGGESApsnEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPvtESDATG---YRVYrSNSGDGPFtKVATVT 283

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 71987133 2445 ieKTHVSLRNFARN-SYSFRVFAYNQR-VRSAPSQ 2477
Cdd:COG3401  284 --TTSYTDTGLTNGtTYYYRVTAVDAAgNESAPSN 316
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 2304-2378 3.61e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 44.09  E-value: 3.61e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71987133   2304 RPVVVEDMKDIEVVEGNDVEMCPIISSHTDFTVIWH---GPAVDSKRARIQTNQLNSRLLIKHVKKCDAGAYSVIAKN 2378
Cdd:pfam13927    1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYkngEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
 2309-2398 9.92e-05

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 43.40  E-value: 9.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 2309 EDMKdieVVEGNDVEMCPIISSHTDFTVIW---HGPAVDSKRARIQTNQLNSRLLIKHVKKCDAGAYSVIAKNSFGVTST 2385
Cdd:cd05762    9 EDMK---VRAGESVELFCKVTGTQPITCTWmkfRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQA 85

                         90
                 ....*....|...
gi 71987133 2386 VAFLSVISIPDPP 2398
Cdd:cd05762   86 QVNLTVVDKPDPP 98
PH_Dbs cd01227
DBL's big sister protein pleckstrin homology (PH) domain; Dbs (also called MCF2-transforming ...
 1996-2115 1.03e-04

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: 44.11  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 1996 FDKSLSAQGKLIHQGTLQI------SESIAGNVQKPKDRRIFLFEQSAIIAdhippkKEFG----NPTYIFKSQFMVNKM 2065
Cdd:cd01227    5 YDGNLGDLGKLLMQGSFNVwtehkkGHTKKLARFKPMQRHIFLYEKAVLFC------KKRGengeAPSYSYKNSLNTTAV 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 71987133 2066 VFEPNVPDDPLRFVIKSSDPTQptSFIANAQSQEEKDEWNRKMSELLDQQ 2115
Cdd:cd01227   79 GLTENVKGDTKKFEIWLNGREE--VFIIQAPTPEIKAAWVKAIRQVLLSQ 126
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
2372-2477 1.33e-04

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 47.30  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 2372 YSVIAKNSFGVTS----TVAFLSVISIPDPPTDFTVKISGDHEVRLKWKAESGL---KYCIEYRILDDSSPEnwLIASTn 2444
Cdd:COG3401  300 YRVTAVDAAGNESapsnVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDAdvtGYNVYRSTSGGGTYT--KIAET- 376

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 71987133 2445 IEKTHVSLRNFARN-SYSFRVFAYNQR-VRSAPSQ 2477
Cdd:COG3401  377 VTTTSYTDTGLTPGtTYYYKVTAVDAAgNESAPSE 411
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
 2305-2391 2.55e-04

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 42.06  E-value: 2.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 2305 PVVVEDMKDIEVVEGNDVEMCPIISSHTDFTVIW--HGPAVDSKRARIQTNQLNS---RLLIKHVKKCDAGAYSVIAKNS 2379
Cdd:cd05892    1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWkkNNEMLQYNTDRISLYQDNCgriCLLIQNANKKDAGWYTVSAVNE 80

                         90
                 ....*....|..
gi 71987133 2380 FGVTSTVAFLSV 2391
Cdd:cd05892   81 AGVVSCNARLDV 92
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 34-160 3.55e-04

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: 43.08  E-value: 3.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133     34 GQAVIVCPSR---EQPVNQDNLRNVFLYLFEVTSKMAREKGFLVVIDMRGKQTWTNVR--HILKALSSIESSSTVQ---V 105
Cdd:pfam13716    1 GRPVLVFISKllpSRPASLDDLDRLLFYLLKTLSEKLKGKPFVVVVDHTGVTSENFPSlsFLKKAYDLLPRAFKKNlkaV 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133    106 FIIKPEKFWEK-----QKAQMSLGTWDFEVEMISFESLIKIIDSSHLPKTVGGSYPYDHD 160
Cdd:pfam13716   81 YVVHPSTFLRTflktlGSLLGSKKLRKKVHYVSSLSELWEGIDREQLPTELPGVLSYDEE 140
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 1417-1506 3.92e-04

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: 41.76  E-value: 3.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 1417 AYFKGRGKERQVFLFDISIVFAKrievSPKNIKYVIKGKpLPLSEVSIVEHVEGDTCRFGLRVgtVSSNDNRIDLKANNH 1496
Cdd:cd00821   10 GGGLKSWKKRWFVLFEGVLLYYK----SKKDSSYKPKGS-IPLSGILEVEEVSPKERPHCFEL--VTPDGRTYYLQADSE 82

                         90
                 ....*....|
gi 71987133 1497 HTKVKWVQKI 1506
Cdd:cd00821   83 EERQEWLKAL 92
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 2312-2391 4.35e-04

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 41.22  E-value: 4.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 2312 KDIEVVEGNDVEM-CPIISSHTDfTVIW-H-GPAVDSKRARIQTNQlnSRLLIKHVKKCDAGAYSVIAKNSFGVTSTVAF 2388
Cdd:cd20978    9 KNVVVKGGQDVTLpCQVTGVPQP-KITWlHnGKPLQGPMERATVED--GTLTIINVQPEDTGYYGCVATNEIGDIYTETL 85


                 ...
gi 71987133 2389 LSV 2391
Cdd:cd20978   86 LHV 88
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 2312-2391 4.84e-04

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 41.23  E-value: 4.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 2312 KDIEVVEGNDVEM-CPIISSHTDFTVIW--HGPAVDSKRARIQTNQlNSRLLIKHVKKCDAGAYSVIAKNSFGV-TSTVA 2387
Cdd:cd05724    5 SDTQVAVGEMAVLeCSPPRGHPEPTVSWrkDGQPLNLDNERVRIVD-DGNLLIAEARKSDEGTYKCVATNMVGErESRAA 83


                 ....
gi 71987133 2388 FLSV 2391
Cdd:cd05724   84 RLSV 87
SH3_Kalirin_1 cd11852
First Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or ...
 1575-1634 5.55e-04

First Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or TRAD, is a large neuronal dual Rho guanine nucleotide exchange factor (RhoGEF) that activates Rac1, RhoA, and RhoG using two RhoGEF domains. Kalirin exists in many isoforms generated by alternative splicing and the use of multiple promoters; the major isoforms are kalirin-7, -9, and -12, which differ at their C-terminal ends. Kalirin-12, the longest isoform, contains an N-terminal Sec14p domain, spectrin-like repeats, two RhoGEF domains, two SH3 domains, as well as Ig, FNIII, and kinase domains at the C-terminal end. Kalirin-7 contains only a single RhoGEF domain and does not contain an SH3 domain. Kalirin, through its many isoforms, interacts with many different proteins and is able to localize to different locations within the cell. It influences neurite initiation, axon growth, dendritic morphogenesis, vesicle trafficking, neuronal maintenance, and neurodegeneration. 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: 212786  Cd Length: 62  Bit Score: 40.07  E-value: 5.55e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71987133 1575 EVWIVTADFDGQVEGHLTVHKGDRVEIVEdQATDCAEYVQVVLCDQ---PTKHGLVPASIIAP 1634
Cdd:cd11852    1 ELTVVIEDFEATSSQELTVSKGQTVEVLE-RPSSRPDWCLVRTLEQdnsPPQEGLVPSSILCI 62
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 1573-1633 5.67e-04

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: 39.83  E-value: 5.67e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71987133    1573 SSEVWIVTADFDGQVEGHLTVHKGDRVEIVEDqatDCAEYVQVVLCDQptKHGLVPASIIA 1633
Cdd:smart00326    1 EGPQVRALYDYTAQDPDELSFKKGDIITVLEK---SDDGWWKGRLGRG--KEGLFPSNYVE 56
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 2312-2391 7.63e-04

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 40.57  E-value: 7.63e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133    2312 KDIEVVEGNDVEM-CPIiSSHTDFTVIWH----GPAVDSKRARIQTNQLNSRLLIKHVKKCDAGAYSVIAKNSFGVTSTV 2386
Cdd:smart00410    2 PSVTVKEGESVTLsCEA-SGSPPPEVTWYkqggKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80


                    ....*
gi 71987133    2387 AFLSV 2391
Cdd:smart00410   81 TTLTV 85
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 422-568 1.34e-03

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: 42.43  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133  422 ESLEEAIRKHDAFWAQVEEvYAQAYDDASKVTRALKEADAEDNVA-REHSSRLQRAHKQLMEKWKERQVLLHHMLAMIAF 500
Cdd:cd00176   33 ESVEALLKKHEALEAELAA-HEERVEALNELGEQLIEEGHPDAEEiQERLEELNQRWEELRELAEERRQRLEEALDLQQF 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71987133  501 ETDVRLVVDWLEQHgEPYLRRNIHiGENVNQARSFQRNHTNFQRVAANTYGNVQKLHQVYQDVTKSGS 568
Cdd:cd00176  112 FRDADDLEQWLEEK-EAALASEDL-GKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGH 177
PH_PLEKHG1_G2_G3 cd13243
Pleckstrin homology domain-containing family G members 1, 2, and 3 pleckstrin homology (PH) ...
 1968-2112 1.54e-03

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: 41.18  E-value: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 1968 DTLKKALQVMHVVPKACDDM-------MQVGRLQNF-----DKSLSAQGKLIHQGTLQISesiagnvQKPKDRRIFLFEQ 2035
Cdd:cd13243    2 SVVEEALDTMTQVAWHINDMkrkhehaVRVQEIQSLldgweGPELTTYGDLVLEGTFRMA-------GAKNERLLFLFDK 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71987133 2036 SAIIAdhippKKEFGNPtYIFKSQFMV-NKMVFEpNVPDDPLRF-VIKSSDPTQPTSFiaNAQSQEEKDEWNRKMSELL 2112
Cdd:cd13243   75 MLLIT-----KKREDGI-LQYKTHIMCsNLMLSE-SIPKEPLSFqVLPFDNPKLQYTL--QAKNQEQKRLWTQEIKRLI 144
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 2325-2388 1.58e-03

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 39.23  E-value: 1.58e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71987133 2325 CPIiSSHTDFTVIWH---GPAVDSKRARIQTNQLNSRLLIKHVKKCDAGAYSVIAKNSFGVTSTVAF 2388
Cdd:cd00096    5 CSA-SGNPPPTITWYkngKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 2305-2391 1.59e-03

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 39.93  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 2305 PVVVEDMKDIEVVEGND-VEMCPIISSHT-DFTVIWHGPAVDSKRARIQTNQLNSRLLIKHVKKCDAGAYSVIAKNSFGV 2382
Cdd:cd20976    2 PSFSSVPKDLEAVEGQDfVAQCSARGKPVpRITWIRNAQPLQYAADRSTCEAGVGELHIQDVLPEDHGTYTCLAKNAAGQ 81


                 ....*....
gi 71987133 2383 TSTVAFLSV 2391
Cdd:cd20976   82 VSCSAWVTV 90
PH_Dbs cd01227
DBL's big sister protein pleckstrin homology (PH) domain; Dbs (also called MCF2-transforming ...
 1400-1507 1.60e-03

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: 40.64  E-value: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 1400 ELGPFVTQDTLTFW------EPRAYFKGRGKERQVFLFDISIVFAKRIEVSPKNIKYVIKgKPLPLSEVSIVEHVEGDTC 1473
Cdd:cd01227   11 DLGKLLMQGSFNVWtehkkgHTKKLARFKPMQRHIFLYEKAVLFCKKRGENGEAPSYSYK-NSLNTTAVGLTENVKGDTK 89

                         90       100       110
                 ....*....|....*....|....*....|....
gi 71987133 1474 RFGLRVGtvsSNDNRIDLKANNHHTKVKWVQKIR 1507
Cdd:cd01227   90 KFEIWLN---GREEVFIIQAPTPEIKAAWVKAIR 120
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
 2314-2391 1.77e-03

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 39.62  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 2314 IEVVEGNDVE-MCPIISSHTDfTVIWH-------GPAVDSKRARIqtnqLNSRLLIKHVKKCDAGAYSVIAKNSFGVTST 2385
Cdd:cd20949    9 TTVKEGQSATiLCEVKGEPQP-NVTWHfngqpisASVADMSKYRI----LADGLLINKVTQDDTGEYTCRAYQVNSIASD 83


                 ....*.
gi 71987133 2386 VAFLSV 2391
Cdd:cd20949   84 MQERTV 89
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 20-154 1.87e-03

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: 41.17  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133   20 RDGIAVLPGGRCRAGQAVIVCPSREQP---VNQDNLRNVFLYLFEVTSKMAREK--GFLVVIDMRG-----KQTWTNVRH 89
Cdd:cd00170    7 LLGGIGYLGGRDKEGRPVLVFRAGWDPpklLDLEELLRYLVYLLEKALRELEEQveGFVVIIDLKGfslsnLSDLSLLKK 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133   90 ILKALSS-----------IESSSTVQVF--IIKP---EKFWEKqkaqmslgtwdfeVEMIS--FESLIKIIDSSHLPKTV 151
Cdd:cd00170   87 LLKILQDhyperlkkiyiVNAPWIFSALwkIVKPflsEKTRKK-------------IVFLGsdLEELLEYIDPDQLPKEL 153


                 ...
gi 71987133  152 GGS 154
Cdd:cd00170  154 GGT 156
SH3_Sla1p_3 cd11775
Third Src Homology 3 domain of the fungal endocytic adaptor protein Sla1p; Sla1p facilitates ...
 1578-1634 4.35e-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: 37.68  E-value: 4.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 71987133 1578 IVTADFDGQVEGHLTVHKGDRVEIVEDQATDCAEYVQVVlcdQPTKHGLVPASIIAP 1634
Cdd:cd11775    4 KVLYDFDAQSDDELTVKEGDVVYILDDKKSKDWWMVENV---STGKEGVVPASYIEI 57
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 1419-1511 5.53e-03

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 38.70  E-value: 5.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133   1419 FKGRGKERQVFLFDISIVFAKRievSPKNIKYVIKGKpLPLSEVSIVEHVEGDT----CRFGLRVGTvSSNDNRIDLKAN 1494
Cdd:pfam00169   14 KKKSWKKRYFVLFDGSLLYYKD---DKSGKSKEPKGS-ISLSGCEVVEVVASDSpkrkFCFELRTGE-RTGKRTYLLQAE 88

                           90
                   ....*....|....*..
gi 71987133   1495 NHHTKVKWVQKIRDLTA 1511
Cdd:pfam00169   89 SEEERKDWIKAIQSAIR 105
PH_13 pfam16652
Pleckstrin homology domain;
1376-1508 6.84e-03

Pleckstrin homology domain;


Pssm-ID: 465218  Cd Length: 143  Bit Score: 39.30  E-value: 6.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133   1376 CSVPRKvndLIHYNCLdlkdFKV---DELGPFVTQDTLTFWEPRAYFKGRGKErqvFLFDisivfakrievSPKNIKYVI 1452
Cdd:pfam16652   18 CLGPRK---LLHSGKL----YKVksnKELVGFLFNDFLLLTQPVKPLSSAGTD---KLFS-----------SKSNIQYKM 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 71987133   1453 KGKPLPLSEVSIVEHVEGDTCRFglrVGTVSSNDNRIDLKANNHHTKVKWVQKIRD 1508
Cdd:pfam16652   77 YKTPIFLNEVMVKLPTDPSSSEP---TFQLSHIDRVYTLKAESPNERTAWVKKIKE 129
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 1578-1630 7.36e-03

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: 36.67  E-value: 7.36e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 71987133 1578 IVTADFDGQVEGHLTVHKGDRVEIVEDQATDCAEyvqVVLCDQptKHGLVPAS 1630
Cdd:cd00174    3 RALYDYEAQDDDELSFKKGDIITVLEKDDDGWWE---GELNGG--REGLFPAN 50
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 2006-2113 7.41e-03

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: 38.30  E-value: 7.41e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133    2006 LIHQGTLQISESiaGNVQKPKDRRIFLFEQSAIIAdhippKKEFGNPTYIFKSQFMVNKMVFEPNV----PDDPLRFVIK 2081
Cdd:smart00233    1 VIKEGWLYKKSG--GGKKSWKKRYFVLFNSTLLYY-----KSKKDKKSYKPKGSIDLSGCTVREAPdpdsSKKPHCFEIK 73

                            90       100       110
                    ....*....|....*....|....*....|..
gi 71987133    2082 SSDPTqptSFIANAQSQEEKDEWNRKMSELLD 2113
Cdd:smart00233   74 TSDRK---TLLLQAESEEEREKWVEALRKAIA 102
PH_unc89 cd13325
unc89 pleckstrin homology (PH) domain; unc89 is a myofibrillar protein. unc89-B the largest ...
 1401-1507 9.67e-03

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: 38.10  E-value: 9.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987133 1401 LGPFVTQDTLTFWEPRayfkGRGKERQVFLFDISIVFAKRIEVS-PKNIkYVIKgKPLPLSEVSIVEHvEGDTCRFGLRV 1479
Cdd:cd13325    6 LGRLLRHDWFTVTDGE----GKAKERYLFLFKSRILITKVRRISeDRSV-FILK-DIIRLPEVNVKQH-PDDERTFELQP 78

                         90       100
                 ....*....|....*....|....*...
gi 71987133 1480 GTVSSNDNRIDLKANNHHTKVKWVQKIR 1507
Cdd:cd13325   79 KLPAFGILPIDFKAHKDEIKDYWLNEIE 106
 
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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