NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568990429|ref|XP_006520117|]
View 

triple functional domain protein isoform X8 [Mus musculus]

Protein Classification

kalirin; RhoGEF family protein( domain architecture ID 11271282)

kalirin is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal serine/threonine-protein kinase that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates; it also functions as a GEF, activating Rac1, RhoA, and RhoG| RhoGEF (rho guanine nucleotide exchange factor) family protein similar to RhoGEF and PH (pleckstrin homology) domain regions of Homo sapiens phosphatidylinositol 3,4,5-trisphosphate-dependent RAC exchanger 1 protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SH3-RhoG_link super family cl24983
SH3-RhoGEF linking unstructured region; This family of natively unstructured but conserved ...
 1715-1889 2.71e-96

SH3-RhoGEF linking unstructured region; This family of natively unstructured but conserved residues from higher eukaryotes is found to lie between an SH3 pfam00018 and the RhoGEF, pfam00621, domains. It is serine-rich and likely to be acidic and natively unstructured.


The actual alignment was detected with superfamily member pfam16609:

Pssm-ID: 465196  Cd Length: 261  Bit Score: 311.74  E-value: 2.71e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  1715 SLCIAHSRSSMEMEGIFNHKDSLSVSSNDASPPASVASLQP-HMIGAQSSPGPKRPGNTLRKWLTSPVRRLSSGKADGHA 1793
Cdd:pfam16609    1 MLCIAHSRSSMEMEGIFNHKDTLSVYSNDSIMPGSSATLQPgHGISSHASPGPKRPGNTLRKWLTSPVRRLSSGKADGHV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  1794 KKLAHKHKKSREVRKS--ADAGSQKDSDDSAATPQDETIEERGRNEGLSSGTLSKSSSSGMQSCGEEEGEEGADAVPLPP 1871
Cdd:pfam16609   81 KKLAHKHKKSREVRKSreITAGSQKDSDDSAATPQDETVEERVRNEGLSSGTLSKSSSSGMQSCGEEEGEEGADSVPLPP 160

                          170
                   ....*....|....*...
gi 568990429  1872 PMAIQQHSLLQPDSQDDK 1889
Cdd:pfam16609  161 PMAIQQHSLLQPDSQDDK 178
PH1_Kalirin_Trio_like cd13240
Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; ...
 1472-1594 2.14e-71

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: 234.20  E-value: 2.14e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429 1472 MLEGFDENIESQGELILQESFQVWDPKTLIRKGRERHLFLFEMSLVFSKEVKDSSGRSKYLYKSKLFTSELGVTEHVEGD 1551
Cdd:cd13240     1 LLEGCDEDLDSLGEVILQDSFQVWDPKQLIRKGRERHVFLFELCLVFSKEVKDSNGKSKYIYKSRLMTSEIGVTEHIEGD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568990429 1552 PCKFALWVGRTPTSDNKIVLKASSIENKQDWIKHIREVIQERT 1594
Cdd:cd13240    81 PCKFALWTGRVPTSDNKIVLKASSLEVKQTWVKKLREVIQERI 123
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 1295-1465 4.04e-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: 155.92  E-value: 4.04e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429 1295 FIMAELIQTEKAYVRDLRECMDTYLWEMTSGVEEIPPGIVNkelIIFGNMQEIYEFHNnIFLKELEKY----EQLPEDVG 1370
Cdd:cd00160     3 EVIKELLQTERNYVRDLKLLVEVFLKPLDKELLPLSPEEVE---LLFGNIEEIYEFHR-IFLKSLEERveewDKSGPRIG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429 1371 HCFVTWADKFQMYVTYCKNKPDSTQLILEHAG--SYFDEIQQRHGLAN---SISSYLIKPVQRITKYQLLLKELLTCCEE 1445
Cdd:cd00160    79 DVFLKLAPFFKIYSEYCSNHPDALELLKKLKKfnKFFQEFLEKAESECgrlKLESLLLKPVQRLTKYPLLLKELLKHTPD 158

                         170       180
                  ....*....|....*....|...
gi 568990429 1446 G---KGEIKDGLEVMLSVPKRAN 1465
Cdd:cd00160   159 GhedREDLKKALEAIKEVASQVN 181
SH3_Kalirin_1 cd11852
First Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or ...
 1659-1718 2.81e-32

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: 120.19  E-value: 2.81e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568990429 1659 ELTVVIHDFTACNSNELTIRRGQTVEVLERPHDKPDWCLVRTT--DRSPAAEGLVPCGSLCI 1718
Cdd:cd11852     1 ELTVVIEDFEATSSQELTVSKGQTVEVLERPSSRPDWCLVRTLeqDNSPPQEGLVPSSILCI 62
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 567-783 8.48e-23

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: 98.67  E-value: 8.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  567 QLCVFQQDVQQVLDWIENHGEAFLSkhTGVGKSLHRARALQKRHEDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIY 646
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  647 QAAHQLEDRIQDFVRRVEQRKILLDMSV---SFHTHVKELWTWLEELQKELLDDVYAESVEAVQDLIKRFgqqqqttlQV 723
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALdlqQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKH--------KE 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  724 TVNVIKEGEDLIQQLRDSAISSNKTPHNSSINHIETVLQQLDEAQSQMEELFQERKIKLE 783
Cdd:cd00176   151 LEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 69-204 3.44e-22

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


:

Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 95.06  E-value: 3.44e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429     69 LKEKVAYLSGGR--DKRGGPILTFPARS--NHDRIRQEDLRRLISYLACIPSEE---VCKRGFTVIVDMRGSK-----WD 136
Cdd:smart00516    2 LELLKAYIPGGRgyDKDGRPVLIERAGRfdLKSVTLEELLRYLVYVLEKILQEEkktGGIEGFTVIFDLKGLSmsnpdLS 81

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568990429    137 SIKPLLKILQESFPCCIHIALIIKPDNFWQ---KQRTNFGSSKFEFETNMVSL---EGLTKVVDPSQLTPEFDG 204
Cdd:smart00516   82 VLRKILKILQDHYPERLGKVYIINPPWFFRvlwKIIKPFLDEKTREKIRFVGNdskEELLEYIDKEQLPEELGG 155
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 908-1137 1.25e-16

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 80.57  E-value: 1.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  908 QLRHLQAEVKQVLGWIRNGESMLNAGLiTASSLQEAEQLQREHEQFQHAIEKTHQSALQVQQKAEAMLQANHYDMDMIRD 987
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  988 CAEKVASHWQQLMLKMEDRLKLVNASVAFYKTSEQVCSVlesleqeykreEDWCGGADKLGPNSETDHVTPMISKHLEQK 1067
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL-----------EQWLEEKEAALASEDLGKDLESVEELLKKH 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429 1068 EAFLKACTlarrNADVFLKYLHRNSVSMPGmvTHIKAPEQQVKNILNELFQRENRVLHYWTMRKRRLDQC 1137
Cdd:cd00176   149 KELEEELE----AHEPRLKSLNELAEELLE--EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 341-566 1.53e-15

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: 77.49  E-value: 1.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  341 QLRLFEQDAEKMFDWITHNKGLFLNsyTEIGTSHPHAMELQTQHNHFAMNCMNVYVNINRIMSVANRLVESGHYASQQIK 420
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  421 QIANQLEQEWKAFAAALDERSTLLDMSSIFHQKAEKyMSNVDSWCKACGEV----DLPSELQDLEDAIHHHQGIYEHITL 496
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAAlaseDLGKDLESVEELLKKHKELEEELEA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  497 AysevSQDGKSLLDKLQRPLTPGSSDSLTasanyskavhHVLDVIHEVLHHQRQLENIWQHRKVRLHQRL 566
Cdd:cd00176   158 H----EPRLKSLNELAEELLEEGHPDADE----------EIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 787-1014 3.33e-14

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 73.63  E-value: 3.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  787 QLRIFERDAidiiSDLESWNDELSQQMNDFDT-EDLTIAEQRLQHHADKALTMNNltfdviHQGQdllqyVNEVQASGvE 865
Cdd:cd00176     1 KLQQFLRDA----DELEAWLSEKEELLSSTDYgDDLESVEALLKKHEALEAELAA------HEER-----VEALNELG-E 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  866 LLCDRDVDMATRVQDLLEFLHEKQQELDLAAEQHRKHLEQCVQLRHLQAEVKQVLGWIRNGESMLNAGLITaSSLQEAEQ 945
Cdd:cd00176    65 QLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLG-KDLESVEE 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  946 LQREHEQFQHAIEKTHQSALQVQQKAEAMLQANHYDMDM-IRDCAEKVASHWQQLMLKMEDRLKLVNASV 1014
Cdd:cd00176   144 LLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEeIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 220-445 5.07e-13

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: 70.17  E-value: 5.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  220 FEEYISNAAHMLSRLEELQDVLAKKELPQDLEGARNMIDEHSQLKK--KVIKAPIEDLDLEGQKLLQriqssdsfpkknS 297
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAelAAHEERVEALNELGEQLIE------------E 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  298 GSGNADlqnllpKVSTMLDRLHSTRQHLHQMWHVRKLKLDQCFQLRLFEQDAEKMFDWIThNKGLFLNSyTEIGTSHPHA 377
Cdd:cd00176    70 GHPDAE------EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLE-EKEAALAS-EDLGKDLESV 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568990429  378 MELQTQHNHFAMNCMNVYVNINRIMSVANRLVESGHYASQ-QIKQIANQLEQEWKAFAAALDERSTLLD 445
Cdd:cd00176   142 EELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC smart00150
Spectrin repeats;
1143-1243 1.40e-12

Spectrin repeats;


:

Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 65.43  E-value: 1.40e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   1143 FERSAKQALEWIHDNGEfyLSTHTSTGSSIQHTQELLKEHEEFQITAKQTKERVKLLIQLADGFCEKGHAHAAEIKKCVT 1222
Cdd:smart00150    3 FLRDADELEAWLEEKEQ--LLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 568990429   1223 AVDKRYRDFSLRMEKYRTSLE 1243
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
 
Name Accession Description Interval E-value
SH3-RhoG_link pfam16609
SH3-RhoGEF linking unstructured region; This family of natively unstructured but conserved ...
 1715-1889 2.71e-96

SH3-RhoGEF linking unstructured region; This family of natively unstructured but conserved residues from higher eukaryotes is found to lie between an SH3 pfam00018 and the RhoGEF, pfam00621, domains. It is serine-rich and likely to be acidic and natively unstructured.


Pssm-ID: 465196  Cd Length: 261  Bit Score: 311.74  E-value: 2.71e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  1715 SLCIAHSRSSMEMEGIFNHKDSLSVSSNDASPPASVASLQP-HMIGAQSSPGPKRPGNTLRKWLTSPVRRLSSGKADGHA 1793
Cdd:pfam16609    1 MLCIAHSRSSMEMEGIFNHKDTLSVYSNDSIMPGSSATLQPgHGISSHASPGPKRPGNTLRKWLTSPVRRLSSGKADGHV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  1794 KKLAHKHKKSREVRKS--ADAGSQKDSDDSAATPQDETIEERGRNEGLSSGTLSKSSSSGMQSCGEEEGEEGADAVPLPP 1871
Cdd:pfam16609   81 KKLAHKHKKSREVRKSreITAGSQKDSDDSAATPQDETVEERVRNEGLSSGTLSKSSSSGMQSCGEEEGEEGADSVPLPP 160

                          170
                   ....*....|....*...
gi 568990429  1872 PMAIQQHSLLQPDSQDDK 1889
Cdd:pfam16609  161 PMAIQQHSLLQPDSQDDK 178
PH1_Kalirin_Trio_like cd13240
Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; ...
 1472-1594 2.14e-71

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: 234.20  E-value: 2.14e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429 1472 MLEGFDENIESQGELILQESFQVWDPKTLIRKGRERHLFLFEMSLVFSKEVKDSSGRSKYLYKSKLFTSELGVTEHVEGD 1551
Cdd:cd13240     1 LLEGCDEDLDSLGEVILQDSFQVWDPKQLIRKGRERHVFLFELCLVFSKEVKDSNGKSKYIYKSRLMTSEIGVTEHIEGD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568990429 1552 PCKFALWVGRTPTSDNKIVLKASSIENKQDWIKHIREVIQERT 1594
Cdd:cd13240    81 PCKFALWTGRVPTSDNKIVLKASSLEVKQTWVKKLREVIQERI 123
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 1295-1465 4.04e-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: 155.92  E-value: 4.04e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429 1295 FIMAELIQTEKAYVRDLRECMDTYLWEMTSGVEEIPPGIVNkelIIFGNMQEIYEFHNnIFLKELEKY----EQLPEDVG 1370
Cdd:cd00160     3 EVIKELLQTERNYVRDLKLLVEVFLKPLDKELLPLSPEEVE---LLFGNIEEIYEFHR-IFLKSLEERveewDKSGPRIG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429 1371 HCFVTWADKFQMYVTYCKNKPDSTQLILEHAG--SYFDEIQQRHGLAN---SISSYLIKPVQRITKYQLLLKELLTCCEE 1445
Cdd:cd00160    79 DVFLKLAPFFKIYSEYCSNHPDALELLKKLKKfnKFFQEFLEKAESECgrlKLESLLLKPVQRLTKYPLLLKELLKHTPD 158

                         170       180
                  ....*....|....*....|...
gi 568990429 1446 G---KGEIKDGLEVMLSVPKRAN 1465
Cdd:cd00160   159 GhedREDLKKALEAIKEVASQVN 181
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 1296-1466 1.02e-40

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: 148.99  E-value: 1.02e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   1296 IMAELIQTEKAYVRDLRECMDTYLWEMTSGVEEIPPgivNKELIIFGNMQEIYEFHNnIFLKELEKY----EQLPEDVGH 1371
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELKLLSP---NELETLFGNIEEIYEFHR-DFLDELEERieewDDSVERIGD 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   1372 CFVTWADKFQMYVTYCKNKPDSTQLI--LEHAGSYFDEIQQRHGLAN----SISSYLIKPVQRITKYQLLLKELLTCCEE 1445
Cdd:smart00325   77 VFLKLEEFFKIYSEYCSNHPDALELLkkLKKNPRFQKFLKEIESSPQcrrlTLESLLLKPVQRLTKYPLLLKELLKHTPE 156

                           170       180
                    ....*....|....*....|....
gi 568990429   1446 G---KGEIKDGLEVMLSVPKRAND 1466
Cdd:smart00325  157 DhedREDLKKALKAIKELANQVNE 180
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 1296-1465 6.98e-40

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: 146.29  E-value: 6.98e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  1296 IMAELIQTEKAYVRDLRECMDTYLWEMTSGVEEIPpgivnKEL-IIFGNMQEIYEFHNNIFLKELEKYEQLPEDVGHCFV 1374
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESE-----EEIkTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIFL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  1375 TWADKFQMYVTYCKNKPDSTQLI------LEHAGSYFDEIQQR---HGLanSISSYLIKPVQRITKYQLLLKELLTCCEE 1445
Cdd:pfam00621   76 KFAPGFKVYSTYCSNYPKALKLLkkllkkNPKFRAFLEELEANpecRGL--DLNSFLIKPVQRIPRYPLLLKELLKHTPP 153

                          170       180
                   ....*....|....*....|...
gi 568990429  1446 G---KGEIKDGLEVMLSVPKRAN 1465
Cdd:pfam00621  154 DhpdYEDLKKALEAIKEVAKQIN 176
SH3_Kalirin_1 cd11852
First Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or ...
 1659-1718 2.81e-32

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: 120.19  E-value: 2.81e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568990429 1659 ELTVVIHDFTACNSNELTIRRGQTVEVLERPHDKPDWCLVRTT--DRSPAAEGLVPCGSLCI 1718
Cdd:cd11852     1 ELTVVIEDFEATSSQELTVSKGQTVEVLERPSSRPDWCLVRTLeqDNSPPQEGLVPSSILCI 62
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 567-783 8.48e-23

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: 98.67  E-value: 8.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  567 QLCVFQQDVQQVLDWIENHGEAFLSkhTGVGKSLHRARALQKRHEDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIY 646
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  647 QAAHQLEDRIQDFVRRVEQRKILLDMSV---SFHTHVKELWTWLEELQKELLDDVYAESVEAVQDLIKRFgqqqqttlQV 723
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALdlqQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKH--------KE 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  724 TVNVIKEGEDLIQQLRDSAISSNKTPHNSSINHIETVLQQLDEAQSQMEELFQERKIKLE 783
Cdd:cd00176   151 LEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 69-204 3.44e-22

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


Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 95.06  E-value: 3.44e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429     69 LKEKVAYLSGGR--DKRGGPILTFPARS--NHDRIRQEDLRRLISYLACIPSEE---VCKRGFTVIVDMRGSK-----WD 136
Cdd:smart00516    2 LELLKAYIPGGRgyDKDGRPVLIERAGRfdLKSVTLEELLRYLVYVLEKILQEEkktGGIEGFTVIFDLKGLSmsnpdLS 81

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568990429    137 SIKPLLKILQESFPCCIHIALIIKPDNFWQ---KQRTNFGSSKFEFETNMVSL---EGLTKVVDPSQLTPEFDG 204
Cdd:smart00516   82 VLRKILKILQDHYPERLGKVYIINPPWFFRvlwKIIKPFLDEKTREKIRFVGNdskEELLEYIDKEQLPEELGG 155
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 908-1137 1.25e-16

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 80.57  E-value: 1.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  908 QLRHLQAEVKQVLGWIRNGESMLNAGLiTASSLQEAEQLQREHEQFQHAIEKTHQSALQVQQKAEAMLQANHYDMDMIRD 987
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  988 CAEKVASHWQQLMLKMEDRLKLVNASVAFYKTSEQVCSVlesleqeykreEDWCGGADKLGPNSETDHVTPMISKHLEQK 1067
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL-----------EQWLEEKEAALASEDLGKDLESVEELLKKH 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429 1068 EAFLKACTlarrNADVFLKYLHRNSVSMPGmvTHIKAPEQQVKNILNELFQRENRVLHYWTMRKRRLDQC 1137
Cdd:cd00176   149 KELEEELE----AHEPRLKSLNELAEELLE--EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 341-566 1.53e-15

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: 77.49  E-value: 1.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  341 QLRLFEQDAEKMFDWITHNKGLFLNsyTEIGTSHPHAMELQTQHNHFAMNCMNVYVNINRIMSVANRLVESGHYASQQIK 420
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  421 QIANQLEQEWKAFAAALDERSTLLDMSSIFHQKAEKyMSNVDSWCKACGEV----DLPSELQDLEDAIHHHQGIYEHITL 496
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAAlaseDLGKDLESVEELLKKHKELEEELEA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  497 AysevSQDGKSLLDKLQRPLTPGSSDSLTasanyskavhHVLDVIHEVLHHQRQLENIWQHRKVRLHQRL 566
Cdd:cd00176   158 H----EPRLKSLNELAEELLEEGHPDADE----------EIEEKLEELNERWEELLELAEERQKKLEEAL 213
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 74-204 2.40e-15

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: 75.06  E-value: 2.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   74 AYLSGGRDKRGGPILTFPAR-SNHDRIRQEDLRRLISYL--ACIPSEEVCKRGFTVIVDMRGSKW------DSIKPLLKI 144
Cdd:cd00170    11 IGYLGGRDKEGRPVLVFRAGwDPPKLLDLEELLRYLVYLleKALRELEEQVEGFVVIIDLKGFSLsnlsdlSLLKKLLKI 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  145 LQESFPCCIHIALIIKPDNF----WQ------KQRTnfgSSKFEFETNmvSLEGLTKVVDPSQLTPEFDG 204
Cdd:cd00170    91 LQDHYPERLKKIYIVNAPWIfsalWKivkpflSEKT---RKKIVFLGS--DLEELLEYIDPDQLPKELGG 155
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 787-1014 3.33e-14

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 73.63  E-value: 3.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  787 QLRIFERDAidiiSDLESWNDELSQQMNDFDT-EDLTIAEQRLQHHADKALTMNNltfdviHQGQdllqyVNEVQASGvE 865
Cdd:cd00176     1 KLQQFLRDA----DELEAWLSEKEELLSSTDYgDDLESVEALLKKHEALEAELAA------HEER-----VEALNELG-E 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  866 LLCDRDVDMATRVQDLLEFLHEKQQELDLAAEQHRKHLEQCVQLRHLQAEVKQVLGWIRNGESMLNAGLITaSSLQEAEQ 945
Cdd:cd00176    65 QLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLG-KDLESVEE 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  946 LQREHEQFQHAIEKTHQSALQVQQKAEAMLQANHYDMDM-IRDCAEKVASHWQQLMLKMEDRLKLVNASV 1014
Cdd:cd00176   144 LLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEeIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 220-445 5.07e-13

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: 70.17  E-value: 5.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  220 FEEYISNAAHMLSRLEELQDVLAKKELPQDLEGARNMIDEHSQLKK--KVIKAPIEDLDLEGQKLLQriqssdsfpkknS 297
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAelAAHEERVEALNELGEQLIE------------E 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  298 GSGNADlqnllpKVSTMLDRLHSTRQHLHQMWHVRKLKLDQCFQLRLFEQDAEKMFDWIThNKGLFLNSyTEIGTSHPHA 377
Cdd:cd00176    70 GHPDAE------EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLE-EKEAALAS-EDLGKDLESV 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568990429  378 MELQTQHNHFAMNCMNVYVNINRIMSVANRLVESGHYASQ-QIKQIANQLEQEWKAFAAALDERSTLLD 445
Cdd:cd00176   142 EELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC smart00150
Spectrin repeats;
1143-1243 1.40e-12

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 65.43  E-value: 1.40e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   1143 FERSAKQALEWIHDNGEfyLSTHTSTGSSIQHTQELLKEHEEFQITAKQTKERVKLLIQLADGFCEKGHAHAAEIKKCVT 1222
Cdd:smart00150    3 FLRDADELEAWLEEKEQ--LLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 568990429   1223 AVDKRYRDFSLRMEKYRTSLE 1243
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
571-671 2.71e-12

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 64.66  E-value: 2.71e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429    571 FQQDVQQVLDWIENHgEAFLSkHTGVGKSLHRARALQKRHEDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIYQAAH 650
Cdd:smart00150    3 FLRDADELEAWLEEK-EQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 568990429    651 QLEDRIQDFVRRVEQRKILLD 671
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 1139-1246 1.16e-11

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: 66.32  E-value: 1.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429 1139 QYVVFERSAKQALEWIHDNGEFYLSThtSTGSSIQHTQELLKEHEEFQITAKQTKERVKLLIQLADGFCEKGHAHAAEIK 1218
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSST--DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                          90       100
                  ....*....|....*....|....*...
gi 568990429 1219 KCVTAVDKRYRDFSLRMEKYRTSLEKAL 1246
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEAL 106
SPEC smart00150
Spectrin repeats;
910-1008 1.82e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 59.65  E-value: 1.82e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429    910 RHLQAEVKQVLGWIRNGESMLNAgLITASSLQEAEQLQREHEQFQHAIEKTHQSALQVQQKAEAMLQANHYDMDMIRDCA 989
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79

                            90
                    ....*....|....*....
gi 568990429    990 EKVASHWQQLMLKMEDRLK 1008
Cdd:smart00150   80 EELNERWEELKELAEERRQ 98
SPEC smart00150
Spectrin repeats;
345-445 2.13e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 59.27  E-value: 2.13e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429    345 FEQDAEKMFDWITHNKGLFlnSYTEIGTSHPHAMELQTQHNHFAMNCMNVYVNINRIMSVANRLVESGHYASQQIKQIAN 424
Cdd:smart00150    3 FLRDADELEAWLEEKEQLL--ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 568990429    425 QLEQEWKAFAAALDERSTLLD 445
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 84-211 2.79e-10

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: 60.03  E-value: 2.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429    84 GGPILTFPARS-NHDRIRQEDLRRLISYLACIPSEEVCKRGFTVIVDMRGSKWDS------IKPLLKILQESFPCCIHIA 156
Cdd:pfam13716    1 GRPVLVFISKLlPSRPASLDDLDRLLFYLLKTLSEKLKGKPFVVVVDHTGVTSENfpslsfLKKAYDLLPRAFKKNLKAV 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   157 LIIKPDNFWQKQ----RTNFGSSKFEFETNMVS-LEGLTKVVDPSQLTPEFDGCLEYNHE 211
Cdd:pfam13716   81 YVVHPSTFLRTFlktlGSLLGSKKLRKKVHYVSsLSELWEGIDREQLPTELPGVLSYDEE 140
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 1505-1590 1.24e-07

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 51.41  E-value: 1.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  1505 RERHLFLFEMSLVFSKevkDSSGRSKYLYKSKLFTSELGVTEHVEGD----PCKFALWVGrTPTSDNKIVLKASSIENKQ 1580
Cdd:pfam00169   19 KKRYFVLFDGSLLYYK---DDKSGKSKEPKGSISLSGCEVVEVVASDspkrKFCFELRTG-ERTGKRTYLLQAESEEERK 94

                           90
                   ....*....|
gi 568990429  1581 DWIKHIREVI 1590
Cdd:pfam00169   95 DWIKAIQSAI 104
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 1662-1713 1.59e-07

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: 49.46  E-value: 1.59e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 568990429   1662 VVIHDFTACNSNELTIRRGQTVEVLERPHDkpDWCLVRTTDRspaAEGLVPC 1713
Cdd:smart00326    6 RALYDYTAQDPDELSFKKGDIITVLEKSDD--GWWKGRLGRG---KEGLFPS 52
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 1483-1591 1.94e-07

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: 51.01  E-value: 1.94e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   1483 QGELILQEsfqvwdpKTLIRKGRERHLFLFEMSLVFSKevkDSSGRSKYLYKSKLFTSELGVTEHVEGD----PCKFALW 1558
Cdd:smart00233    4 EGWLYKKS-------GGGKKSWKKRYFVLFNSTLLYYK---SKKDKKSYKPKGSIDLSGCTVREAPDPDsskkPHCFEIK 73

                            90       100       110
                    ....*....|....*....|....*....|...
gi 568990429   1559 VGRTPTsdnkIVLKASSIENKQDWIKHIREVIQ 1591
Cdd:smart00233   74 TSDRKT----LLLQAESEEEREKWVEALRKAIA 102
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 1280-1457 6.36e-07

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


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 54.90  E-value: 6.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429 1280 HELNEEKRKSARRKEFIMAELIQTEKAYVRDLRECMDTY---LWEMTsgveeIPPGIVNKELI--IFGNMQEIYEFhNNI 1354
Cdd:COG5422   472 KEVWESLPKQEIKRQEAIYEVIYTERDFVKDLEYLRDTWikpLEESN-----IIPENARRNFIkhVFANINEIYAV-NSK 545

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429 1355 FLKELEK---YEQLPEDVGHCFVTWADKFQMYVTYCKNKPDSTQLIlEHAGS-------YFDEIQ-----QRHGlansIS 1419
Cdd:COG5422   546 LLKALTNrqcLSPIVNGIADIFLDYVPKFEPFIKYGASQPYAKYEF-EREKSvnpnfarFDHEVErldesRKLE----LD 620

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 568990429 1420 SYLIKPVQRITKYQLLLKELLTCCEEGKGEIKDGLEVM 1457
Cdd:COG5422   621 GYLTKPTTRLARYPLLLEEVLKFTDPDNPDTEDIPKVI 658
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 908-999 7.10e-07

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 49.24  E-value: 7.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   908 QLRHLQAEVKQVLGWIRNGESMLNAGLItASSLQEAEQLQREHEQFQHAIEkTHQSALQ-VQQKAEAMLQANHYDMDMIR 986
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEALLSSEDY-GKDLESVQALLKKHKALEAELA-AHQDRVEaLNELAEKLIDEGHYASEEIQ 79

                           90
                   ....*....|...
gi 568990429   987 DCAEKVASHWQQL 999
Cdd:pfam00435   80 ERLEELNERWEQL 92
SPEC smart00150
Spectrin repeats;
221-337 2.11e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 48.09  E-value: 2.11e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429    221 EEYISNAAHMLSRLEELQDVLAKKELPQDLEGARNMIDEHSQLKKKV--IKAPIEDLDLEGQKLLQriqssdsfpkknSG 298
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELeaHEERVEALNELGEQLIE------------EG 68

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 568990429    299 SGNAdlqnllPKVSTMLDRLHSTRQHLHQMWHVRKLKLD 337
Cdd:smart00150   69 HPDA------EEIEERLEELNERWEELKELAEERRQKLE 101
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 1662-1713 3.17e-06

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


Pssm-ID: 394975 [Multi-domain]  Cd Length: 47  Bit Score: 45.66  E-value: 3.17e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568990429  1662 VVIHDFTACNSNELTIRRGQTVEVLERPHDkpDWCLVRTTDRSpaaEGLVPC 1713
Cdd:pfam00018    1 VALYDYTAQEPDELSFKKGDIIIVLEKSED--GWWKGRNKGGK---EGLIPS 47
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 1143-1243 3.50e-06

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 47.31  E-value: 3.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  1143 FERSAKQALEWIHDNGEFYLSThtSTGSSIQHTQELLKEHEEFQITAKQTKERVKLLIQLADGFCEKGHAHAAEIKKCVT 1222
Cdd:pfam00435    6 FFRDADDLESWIEEKEALLSSE--DYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83

                           90       100
                   ....*....|....*....|.
gi 568990429  1223 AVDKRYRDFSLRMEKYRTSLE 1243
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLE 104
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 341-444 2.80e-05

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 45.00  E-value: 2.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   341 QLRLFEQDAEKMFDWIThNKGLFLNSyTEIGTSHPHAMELQTQHNHFAMNcMNVY-VNINRIMSVANRLVESGHYASQQI 419
Cdd:pfam00435    2 LLQQFFRDADDLESWIE-EKEALLSS-EDYGKDLESVQALLKKHKALEAE-LAAHqDRVEALNELAEKLIDEGHYASEEI 78

                           90       100
                   ....*....|....*....|....*
gi 568990429   420 KQIANQLEQEWKAFAAALDERSTLL 444
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKL 103
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 571-670 6.35e-05

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 43.85  E-value: 6.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   571 FQQDVQQVLDWIENHgEAFLSKhTGVGKSLHRARALQKRHEDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIYQAAH 650
Cdd:pfam00435    6 FFRDADDLESWIEEK-EALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83

                           90       100
                   ....*....|....*....|
gi 568990429   651 QLEDRIQDFVRRVEQRKILL 670
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKL 103
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 733-1039 1.04e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 1.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   733 DLIQQLRDSAISSNKTPHNSSINHIETVLQQLDEAQSQMEEL---FQERKIKLElFLQLRIFERDaiDIISDLESWNDEL 809
Cdd:TIGR02168  217 ELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELtaeLQELEEKLE-ELRLEVSELE--EEIEELQKELYAL 293

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   810 SQQMNDFdtedltiaEQRLQHHADKALTMNNLTFDVIHQGQDLLQYVNEVQASGVELLCDRDVDMA--TRVQDLLEFLHE 887
Cdd:TIGR02168  294 ANEISRL--------EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEelESLEAELEELEA 365

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   888 KQQELDLAAEQHRKHLEQcvqlrhLQAEVKQvlgwIRNGESMLNAGLITASSlqEAEQLQREHEQFQHAIEkTHQSALQV 967
Cdd:TIGR02168  366 ELEELESRLEELEEQLET------LRSKVAQ----LELQIASLNNEIERLEA--RLERLEDRRERLQQEIE-ELLKKLEE 432

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568990429   968 QQKAEAMLQANHYDMdMIRDCAEKVASHWQQLMLKMEDRLKLVNASVAFYKTSEQVCSVLESLEQEYKREED 1039
Cdd:TIGR02168  433 AELKELQAELEELEE-ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 766-977 5.70e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 5.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  766 EAQSQMEELfQERKIKLeLFLQLRIFERDAIDIISDLESWNDELSQQMNDFDTEDLTIAEQRLQHHAdkaltmnnLTFDV 845
Cdd:COG1196   214 RYRELKEEL-KELEAEL-LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE--------LELEL 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  846 IHQGQDLLQYVNEVQA--SGVELLCDRDVDMATRVQDLLEFLHEKQQELDLAAEQHRKHLEQCVQLRHLQAEVKQVLgwI 923
Cdd:COG1196   284 EEAQAEEYELLAELARleQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL--A 361

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568990429  924 RNGESMLNAGLITASSLQEAEQLQREHEQFQHAIEKTHQSALQVQQKAEAMLQA 977
Cdd:COG1196   362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 574-914 1.39e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 43.79  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  574 DVQQVLDwienhgeaflSKHTgvgkslhraRALQkrhedfeevaqntYTNADKLLEAAEQLAQTGECDPEEI--YQAAHQ 651
Cdd:COG3096   400 DYQQALD----------VQQT---------RAIQ-------------YQQAVQALEKARALCGLPDLTPENAedYLAAFR 447

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  652 L-EDRIQDFVRRVEQRKILLDMSVSFHTHVKELwtwleeLQKeLLDDVYAESV-EAVQDLIKRFgqqqqttlQVTVNVIK 729
Cdd:COG3096   448 AkEQQATEEVLELEQKLSVADAARRQFEKAYEL------VCK-IAGEVERSQAwQTARELLRRY--------RSQQALAQ 512

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  730 EGEDLIQQLRDsaissnktphnssinhIETVLQQLDEAQSQMEELFQERKIKLELFLQLRiferdaiDIISDLESWNDEL 809
Cdd:COG3096   513 RLQQLRAQLAE----------------LEQRLRQQQNAERLLEEFCQRIGQQLDAAEELE-------ELLAELEAQLEEL 569

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  810 SQQMNDFdTEDLTIAEQRLQHHADKaltMNNLTFD--VIHQGQDLLQYVNEvqASGVELLCDRDVdMATRvQDLLEFLHE 887
Cdd:COG3096   570 EEQAAEA-VEQRSELRQQLEQLRAR---IKELAARapAWLAAQDALERLRE--QSGEALADSQEV-TAAM-QQLLERERE 641

                         330       340
                  ....*....|....*....|....*..
gi 568990429  888 KQQELDLAAEQhRKHLEQcvQLRHLQA 914
Cdd:COG3096   642 ATVERDELAAR-KQALES--QIERLSQ 665
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 220-338 4.35e-03

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 38.45  E-value: 4.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   220 FEEYISNAAHMLSRLEELQDVLAKKELPQDLEGARNMIDEHSQLKK--KVIKAPIEDLDLEGQKLLQRiQSSDSfpkkns 297
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAelAAHQDRVEALNELAEKLIDE-GHYAS------ 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 568990429   298 gsgnadlqnllPKVSTMLDRLHSTRQHLHQMWHVRKLKLDQ 338
Cdd:pfam00435   76 -----------EEIQERLEELNERWEQLLELAAERKQKLEE 105
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 544-846 4.63e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 4.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   544 VLHHQRQLENIWQHRKVRLHQRLQLCVFQQDVQQVLDWIENHGEAFLSKHTGVGKSLHRARALQKRHEDFEEVAQNTYTN 623
Cdd:TIGR02168  672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   624 ADKLLEAAEQLAQTGECDPEEIYQAAHQLEDRIQDFVRRVEQRKILLdmsvsfhthvKELWTWLEELQKEL--LDDVYAE 701
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL----------KALREALDELRAELtlLNEEAAN 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   702 SVEAVQDLIKRfgqqqqttlqvTVNVIKEGEDLIQQLRDSAissnktphnssiNHIETVLQQLDEAQSQMEELFQERKIK 781
Cdd:TIGR02168  822 LRERLESLERR-----------IAATERRLEDLEEQIEELS------------EDIESLAAEIEELEELIEELESELEAL 878

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568990429   782 LELF----LQLRIFERDAIDIISDLESWN----------DELSQQMNDFDTEdLTIAEQRLQHHADKALTMNNLTFDVI 846
Cdd:TIGR02168  879 LNERasleEALALLRSELEELSEELRELEskrselrrelEELREKLAQLELR-LEGLEVRIDNLQERLSEEYSLTLEEA 956
 
Name Accession Description Interval E-value
SH3-RhoG_link pfam16609
SH3-RhoGEF linking unstructured region; This family of natively unstructured but conserved ...
 1715-1889 2.71e-96

SH3-RhoGEF linking unstructured region; This family of natively unstructured but conserved residues from higher eukaryotes is found to lie between an SH3 pfam00018 and the RhoGEF, pfam00621, domains. It is serine-rich and likely to be acidic and natively unstructured.


Pssm-ID: 465196  Cd Length: 261  Bit Score: 311.74  E-value: 2.71e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  1715 SLCIAHSRSSMEMEGIFNHKDSLSVSSNDASPPASVASLQP-HMIGAQSSPGPKRPGNTLRKWLTSPVRRLSSGKADGHA 1793
Cdd:pfam16609    1 MLCIAHSRSSMEMEGIFNHKDTLSVYSNDSIMPGSSATLQPgHGISSHASPGPKRPGNTLRKWLTSPVRRLSSGKADGHV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  1794 KKLAHKHKKSREVRKS--ADAGSQKDSDDSAATPQDETIEERGRNEGLSSGTLSKSSSSGMQSCGEEEGEEGADAVPLPP 1871
Cdd:pfam16609   81 KKLAHKHKKSREVRKSreITAGSQKDSDDSAATPQDETVEERVRNEGLSSGTLSKSSSSGMQSCGEEEGEEGADSVPLPP 160

                          170
                   ....*....|....*...
gi 568990429  1872 PMAIQQHSLLQPDSQDDK 1889
Cdd:pfam16609  161 PMAIQQHSLLQPDSQDDK 178
PH1_Kalirin_Trio_like cd13240
Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; ...
 1472-1594 2.14e-71

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: 234.20  E-value: 2.14e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429 1472 MLEGFDENIESQGELILQESFQVWDPKTLIRKGRERHLFLFEMSLVFSKEVKDSSGRSKYLYKSKLFTSELGVTEHVEGD 1551
Cdd:cd13240     1 LLEGCDEDLDSLGEVILQDSFQVWDPKQLIRKGRERHVFLFELCLVFSKEVKDSNGKSKYIYKSRLMTSEIGVTEHIEGD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568990429 1552 PCKFALWVGRTPTSDNKIVLKASSIENKQDWIKHIREVIQERT 1594
Cdd:cd13240    81 PCKFALWTGRVPTSDNKIVLKASSLEVKQTWVKKLREVIQERI 123
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 1295-1465 4.04e-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: 155.92  E-value: 4.04e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429 1295 FIMAELIQTEKAYVRDLRECMDTYLWEMTSGVEEIPPGIVNkelIIFGNMQEIYEFHNnIFLKELEKY----EQLPEDVG 1370
Cdd:cd00160     3 EVIKELLQTERNYVRDLKLLVEVFLKPLDKELLPLSPEEVE---LLFGNIEEIYEFHR-IFLKSLEERveewDKSGPRIG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429 1371 HCFVTWADKFQMYVTYCKNKPDSTQLILEHAG--SYFDEIQQRHGLAN---SISSYLIKPVQRITKYQLLLKELLTCCEE 1445
Cdd:cd00160    79 DVFLKLAPFFKIYSEYCSNHPDALELLKKLKKfnKFFQEFLEKAESECgrlKLESLLLKPVQRLTKYPLLLKELLKHTPD 158

                         170       180
                  ....*....|....*....|...
gi 568990429 1446 G---KGEIKDGLEVMLSVPKRAN 1465
Cdd:cd00160   159 GhedREDLKKALEAIKEVASQVN 181
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 1296-1466 1.02e-40

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: 148.99  E-value: 1.02e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   1296 IMAELIQTEKAYVRDLRECMDTYLWEMTSGVEEIPPgivNKELIIFGNMQEIYEFHNnIFLKELEKY----EQLPEDVGH 1371
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELKLLSP---NELETLFGNIEEIYEFHR-DFLDELEERieewDDSVERIGD 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   1372 CFVTWADKFQMYVTYCKNKPDSTQLI--LEHAGSYFDEIQQRHGLAN----SISSYLIKPVQRITKYQLLLKELLTCCEE 1445
Cdd:smart00325   77 VFLKLEEFFKIYSEYCSNHPDALELLkkLKKNPRFQKFLKEIESSPQcrrlTLESLLLKPVQRLTKYPLLLKELLKHTPE 156

                           170       180
                    ....*....|....*....|....
gi 568990429   1446 G---KGEIKDGLEVMLSVPKRAND 1466
Cdd:smart00325  157 DhedREDLKKALKAIKELANQVNE 180
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 1296-1465 6.98e-40

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: 146.29  E-value: 6.98e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  1296 IMAELIQTEKAYVRDLRECMDTYLWEMTSGVEEIPpgivnKEL-IIFGNMQEIYEFHNNIFLKELEKYEQLPEDVGHCFV 1374
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESE-----EEIkTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIFL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  1375 TWADKFQMYVTYCKNKPDSTQLI------LEHAGSYFDEIQQR---HGLanSISSYLIKPVQRITKYQLLLKELLTCCEE 1445
Cdd:pfam00621   76 KFAPGFKVYSTYCSNYPKALKLLkkllkkNPKFRAFLEELEANpecRGL--DLNSFLIKPVQRIPRYPLLLKELLKHTPP 153

                          170       180
                   ....*....|....*....|...
gi 568990429  1446 G---KGEIKDGLEVMLSVPKRAN 1465
Cdd:pfam00621  154 DhpdYEDLKKALEAIKEVAKQIN 176
SH3_Kalirin_1 cd11852
First Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or ...
 1659-1718 2.81e-32

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: 120.19  E-value: 2.81e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568990429 1659 ELTVVIHDFTACNSNELTIRRGQTVEVLERPHDKPDWCLVRTT--DRSPAAEGLVPCGSLCI 1718
Cdd:cd11852     1 ELTVVIEDFEATSSQELTVSKGQTVEVLERPSSRPDWCLVRTLeqDNSPPQEGLVPSSILCI 62
PH2_Kalirin_Trio_p63RhoGEF cd13241
p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor ...
 1470-1605 5.60e-27

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: 108.12  E-value: 5.60e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429 1470 LSMLEGFDENIESQGELILQESFQVWDPK-TLIRKGRERHLFLFEMSLVFSKEVKDSSGRSK--YLYKSKLFTSELGVTE 1546
Cdd:cd13241     1 VGRLQGFDGKITAQGKLLLQGTLLVSEPSaGLLQKGKERRVFLFEQIIIFSEILGKKTQFSNpgYIYKNHIKVNKMSLEE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429 1547 HVEGDPCKFALWvGRTP-TSDNKIVLKASSIENKQDWIKHIREVIQERTVHLRgALKEPI 1605
Cdd:cd13241    81 NVDGDPLRFALK-SRDPnNPSETFILQAASPEVRQEWVDTINQILDTQRDFLK-ALQSPI 138
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 567-783 8.48e-23

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: 98.67  E-value: 8.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  567 QLCVFQQDVQQVLDWIENHGEAFLSkhTGVGKSLHRARALQKRHEDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIY 646
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  647 QAAHQLEDRIQDFVRRVEQRKILLDMSV---SFHTHVKELWTWLEELQKELLDDVYAESVEAVQDLIKRFgqqqqttlQV 723
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALdlqQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKH--------KE 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  724 TVNVIKEGEDLIQQLRDSAISSNKTPHNSSINHIETVLQQLDEAQSQMEELFQERKIKLE 783
Cdd:cd00176   151 LEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 69-204 3.44e-22

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


Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 95.06  E-value: 3.44e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429     69 LKEKVAYLSGGR--DKRGGPILTFPARS--NHDRIRQEDLRRLISYLACIPSEE---VCKRGFTVIVDMRGSK-----WD 136
Cdd:smart00516    2 LELLKAYIPGGRgyDKDGRPVLIERAGRfdLKSVTLEELLRYLVYVLEKILQEEkktGGIEGFTVIFDLKGLSmsnpdLS 81

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568990429    137 SIKPLLKILQESFPCCIHIALIIKPDNFWQ---KQRTNFGSSKFEFETNMVSL---EGLTKVVDPSQLTPEFDG 204
Cdd:smart00516   82 VLRKILKILQDHYPERLGKVYIINPPWFFRvlwKIIKPFLDEKTREKIRFVGNdskEELLEYIDKEQLPEELGG 155
PH_puratrophin-1 cd13242
Puratrophin-1 pleckstrin homology (PH) domain; Puratrophin-1 (also called Purkinje cell ...
 1462-1598 3.35e-21

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: 91.20  E-value: 3.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429 1462 KRANDAMHLSMLEGFDENIESQGELILQESFQVWDPktliRKGRERHLFLFEMSLVFSKEVKDSSGRSKYLYKSKLFTSE 1541
Cdd:cd13242     5 RHGNDLLAMDSIRGCDVNLKEQGQLLRQDEFLVWQG----RKKCLRHVFLFEDLILFSKPKKTPGGKDVYIYKHSIKTSD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568990429 1542 LGVTEHVEGDPCKFALWVgRTPTSDNKIVLKASSIENKQDWIKHIREVIQERTVHLR 1598
Cdd:cd13242    81 IGLTENVGDSGLKFEIWF-RRRKARDTYILQATSPEIKQAWTSDIAKLLWKQAIRNR 136
PH_Dbs cd01227
DBL's big sister protein pleckstrin homology (PH) domain; Dbs (also called MCF2-transforming ...
 1475-1590 5.10e-21

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: 90.33  E-value: 5.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429 1475 GFDENIESQGELILQESFQVW------DPKTLIR-KGRERHLFLFEMSLVFSKEVKDSSGRSKYLYKSKLFTSELGVTEH 1547
Cdd:cd01227     4 GYDGNLGDLGKLLMQGSFNVWtehkkgHTKKLARfKPMQRHIFLYEKAVLFCKKRGENGEAPSYSYKNSLNTTAVGLTEN 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568990429 1548 VEGDPCKFALWV-GRTPTsdnkIVLKASSIENKQDWIKHIREVI 1590
Cdd:cd01227    84 VKGDTKKFEIWLnGREEV----FIIQAPTPEIKAAWVKAIRQVL 123
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 908-1137 1.25e-16

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 80.57  E-value: 1.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  908 QLRHLQAEVKQVLGWIRNGESMLNAGLiTASSLQEAEQLQREHEQFQHAIEKTHQSALQVQQKAEAMLQANHYDMDMIRD 987
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  988 CAEKVASHWQQLMLKMEDRLKLVNASVAFYKTSEQVCSVlesleqeykreEDWCGGADKLGPNSETDHVTPMISKHLEQK 1067
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL-----------EQWLEEKEAALASEDLGKDLESVEELLKKH 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429 1068 EAFLKACTlarrNADVFLKYLHRNSVSMPGmvTHIKAPEQQVKNILNELFQRENRVLHYWTMRKRRLDQC 1137
Cdd:cd00176   149 KELEEELE----AHEPRLKSLNELAEELLE--EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 341-566 1.53e-15

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: 77.49  E-value: 1.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  341 QLRLFEQDAEKMFDWITHNKGLFLNsyTEIGTSHPHAMELQTQHNHFAMNCMNVYVNINRIMSVANRLVESGHYASQQIK 420
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  421 QIANQLEQEWKAFAAALDERSTLLDMSSIFHQKAEKyMSNVDSWCKACGEV----DLPSELQDLEDAIHHHQGIYEHITL 496
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAAlaseDLGKDLESVEELLKKHKELEEELEA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  497 AysevSQDGKSLLDKLQRPLTPGSSDSLTasanyskavhHVLDVIHEVLHHQRQLENIWQHRKVRLHQRL 566
Cdd:cd00176   158 H----EPRLKSLNELAEELLEEGHPDADE----------EIEEKLEELNERWEELLELAEERQKKLEEAL 213
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 74-204 2.40e-15

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: 75.06  E-value: 2.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   74 AYLSGGRDKRGGPILTFPAR-SNHDRIRQEDLRRLISYL--ACIPSEEVCKRGFTVIVDMRGSKW------DSIKPLLKI 144
Cdd:cd00170    11 IGYLGGRDKEGRPVLVFRAGwDPPKLLDLEELLRYLVYLleKALRELEEQVEGFVVIIDLKGFSLsnlsdlSLLKKLLKI 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  145 LQESFPCCIHIALIIKPDNF----WQ------KQRTnfgSSKFEFETNmvSLEGLTKVVDPSQLTPEFDG 204
Cdd:cd00170    91 LQDHYPERLKKIYIVNAPWIfsalWKivkpflSEKT---RKKIVFLGS--DLEELLEYIDPDQLPKELGG 155
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 787-1014 3.33e-14

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 73.63  E-value: 3.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  787 QLRIFERDAidiiSDLESWNDELSQQMNDFDT-EDLTIAEQRLQHHADKALTMNNltfdviHQGQdllqyVNEVQASGvE 865
Cdd:cd00176     1 KLQQFLRDA----DELEAWLSEKEELLSSTDYgDDLESVEALLKKHEALEAELAA------HEER-----VEALNELG-E 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  866 LLCDRDVDMATRVQDLLEFLHEKQQELDLAAEQHRKHLEQCVQLRHLQAEVKQVLGWIRNGESMLNAGLITaSSLQEAEQ 945
Cdd:cd00176    65 QLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLG-KDLESVEE 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  946 LQREHEQFQHAIEKTHQSALQVQQKAEAMLQANHYDMDM-IRDCAEKVASHWQQLMLKMEDRLKLVNASV 1014
Cdd:cd00176   144 LLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEeIEEKLEELNERWEELLELAEERQKKLEEAL 213
PH_Obscurin cd13239
Obscurin pleckstrin homology (PH) domain; Obscurin (also called Obscurin-RhoGEF; ...
 1472-1593 3.75e-14

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: 71.04  E-value: 3.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429 1472 MLEGFDENIESQGELILQESFQVWDPKTLIR---KGRERHLFLFEMSLVFSKEVKDSSGRSK-YLYKSKLFTSELGVTEH 1547
Cdd:cd13239     1 LIENYPAPLQALGEPIRQGHFTVWEEAPEVKtssRGHHRHVFLFKNCVVICKPKRDSRTDTVtYVFKNKMKLSDIDVKDT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568990429 1548 VEGDPCKFALWVGRTpTSDNKIVLKASSIENKQDWIKHIREvIQER 1593
Cdd:cd13239    81 VEGDDRSFGLWHEHR-GSVRKYTLQARSAIIKSSWLKDLRD-LQQR 124
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 220-445 5.07e-13

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: 70.17  E-value: 5.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  220 FEEYISNAAHMLSRLEELQDVLAKKELPQDLEGARNMIDEHSQLKK--KVIKAPIEDLDLEGQKLLQriqssdsfpkknS 297
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAelAAHEERVEALNELGEQLIE------------E 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  298 GSGNADlqnllpKVSTMLDRLHSTRQHLHQMWHVRKLKLDQCFQLRLFEQDAEKMFDWIThNKGLFLNSyTEIGTSHPHA 377
Cdd:cd00176    70 GHPDAE------EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLE-EKEAALAS-EDLGKDLESV 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568990429  378 MELQTQHNHFAMNCMNVYVNINRIMSVANRLVESGHYASQ-QIKQIANQLEQEWKAFAAALDERSTLLD 445
Cdd:cd00176   142 EELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC smart00150
Spectrin repeats;
1143-1243 1.40e-12

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 65.43  E-value: 1.40e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   1143 FERSAKQALEWIHDNGEfyLSTHTSTGSSIQHTQELLKEHEEFQITAKQTKERVKLLIQLADGFCEKGHAHAAEIKKCVT 1222
Cdd:smart00150    3 FLRDADELEAWLEEKEQ--LLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 568990429   1223 AVDKRYRDFSLRMEKYRTSLE 1243
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
571-671 2.71e-12

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 64.66  E-value: 2.71e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429    571 FQQDVQQVLDWIENHgEAFLSkHTGVGKSLHRARALQKRHEDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIYQAAH 650
Cdd:smart00150    3 FLRDADELEAWLEEK-EQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 568990429    651 QLEDRIQDFVRRVEQRKILLD 671
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 1139-1246 1.16e-11

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: 66.32  E-value: 1.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429 1139 QYVVFERSAKQALEWIHDNGEFYLSThtSTGSSIQHTQELLKEHEEFQITAKQTKERVKLLIQLADGFCEKGHAHAAEIK 1218
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSST--DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                          90       100
                  ....*....|....*....|....*...
gi 568990429 1219 KCVTAVDKRYRDFSLRMEKYRTSLEKAL 1246
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEAL 106
SPEC smart00150
Spectrin repeats;
910-1008 1.82e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 59.65  E-value: 1.82e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429    910 RHLQAEVKQVLGWIRNGESMLNAgLITASSLQEAEQLQREHEQFQHAIEKTHQSALQVQQKAEAMLQANHYDMDMIRDCA 989
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79

                            90
                    ....*....|....*....
gi 568990429    990 EKVASHWQQLMLKMEDRLK 1008
Cdd:smart00150   80 EELNERWEELKELAEERRQ 98
SPEC smart00150
Spectrin repeats;
345-445 2.13e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 59.27  E-value: 2.13e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429    345 FEQDAEKMFDWITHNKGLFlnSYTEIGTSHPHAMELQTQHNHFAMNCMNVYVNINRIMSVANRLVESGHYASQQIKQIAN 424
Cdd:smart00150    3 FLRDADELEAWLEEKEQLL--ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 568990429    425 QLEQEWKAFAAALDERSTLLD 445
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 84-211 2.79e-10

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: 60.03  E-value: 2.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429    84 GGPILTFPARS-NHDRIRQEDLRRLISYLACIPSEEVCKRGFTVIVDMRGSKWDS------IKPLLKILQESFPCCIHIA 156
Cdd:pfam13716    1 GRPVLVFISKLlPSRPASLDDLDRLLFYLLKTLSEKLKGKPFVVVVDHTGVTSENfpslsfLKKAYDLLPRAFKKNLKAV 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   157 LIIKPDNFWQKQ----RTNFGSSKFEFETNMVS-LEGLTKVVDPSQLTPEFDGCLEYNHE 211
Cdd:pfam13716   81 YVVHPSTFLRTFlktlGSLLGSKKLRKKVHYVSsLSELWEGIDREQLPTELPGVLSYDEE 140
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 676-907 3.85e-10

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: 61.69  E-value: 3.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  676 FHTHVKELWTWLEELQKELLDDVYAESVEAVQDLIKR---FGQQQQTTLQVTVNVIKEGEDLIQQLRDSAissnktphns 752
Cdd:cd00176     5 FLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKheaLEAELAAHEERVEALNELGEQLIEEGHPDA---------- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  753 siNHIETVLQQLDEAQSQMEELFQERKIKLELFLQLRIFERDAidiiSDLESWNDELSQQMNDFDT-EDLTIAEQRLQHH 831
Cdd:cd00176    75 --EEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA----DDLEQWLEEKEAALASEDLgKDLESVEELLKKH 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568990429  832 ADKALTMNNltfdviHQGQdllqyVNEVQASGVELLCDRDVDMATRVQDLLEFLHEKQQELDLAAEQHRKHLEQCV 907
Cdd:cd00176   149 KELEEELEA------HEPR-----LKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
PH_PLEKHG1_G2_G3 cd13243
Pleckstrin homology domain-containing family G members 1, 2, and 3 pleckstrin homology (PH) ...
 1449-1592 5.34e-10

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: 59.67  E-value: 5.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429 1449 EIKDGLEVMLSVPKRAND-------AMHL----SMLEGFDE-NIESQGELILQESFqvwdpkTLIRKGRERHLFLFEMSL 1516
Cdd:cd13243     3 VVEEALDTMTQVAWHINDmkrkhehAVRVqeiqSLLDGWEGpELTTYGDLVLEGTF------RMAGAKNERLLFLFDKML 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568990429 1517 VFSKEVKDSSgrskYLYKSKLFTSELGVTEHVEGDPCKFalWVGRTPTSDNKIVLKASSIENKQDWIKHIREVIQE 1592
Cdd:cd13243    77 LITKKREDGI----LQYKTHIMCSNLMLSESIPKEPLSF--QVLPFDNPKLQYTLQAKNQEQKRLWTQEIKRLILE 146
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 450-671 1.75e-09

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 59.77  E-value: 1.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  450 FHQKAEKYMSNVDSWCKACGEVDLPSELQDLEDAIHHHQGIYEHITLAYSEVSQdgkslLDKLqrpltpgsSDSLTASAN 529
Cdd:cd00176     5 FLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEA-----LNEL--------GEQLIEEGH 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  530 YSKAVHHvlDVIHEVLHHQRQLENIWQHRKVRLHQRLQLCVFQQDVQQVLDWIENHGEAFLSkhTGVGKSLHRARALQKR 609
Cdd:cd00176    72 PDAEEIQ--ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALAS--EDLGKDLESVEELLKK 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568990429  610 HEDFEEVAQNTYTNADKLLEAAEQLAQTGECD-PEEIYQAAHQLEDRIQDFVRRVEQRKILLD 671
Cdd:cd00176   148 HKELEEELEAHEPRLKSLNELAEELLEEGHPDaDEEIEEKLEELNERWEELLELAEERQKKLE 210
CRAL_TRIO pfam00650
CRAL/TRIO domain;
79-204 1.22e-08

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 55.73  E-value: 1.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429    79 GRDKRGGPILTF-PARSNHDRIRQEDLRRLISYLACI---PSEEVCKRGFTVIVDMRGSK--------WDSIKPLLKILQ 146
Cdd:pfam00650    8 GRDKEGRPVLYLrLGRHDPKKSSEEELVRFLVLVLERallLMPEGQVEGLTVIIDLKGLSlsnmdwwsISLLKKIIKILQ 87

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568990429   147 ESFPCCIHIALIIKPD---NFWQKQRTNFGS----SKFEFeTNMVSLEGLTKVVDPSQLTPEFDG 204
Cdd:pfam00650   88 DNYPERLGKILIVNAPwifNTIWKLIKPFLDpktrEKIVF-LKNSNEEELEKYIPPEQLPKEYGG 151
PH_unc89 cd13325
unc89 pleckstrin homology (PH) domain; unc89 is a myofibrillar protein. unc89-B the largest ...
 1479-1592 1.92e-08

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: 54.28  E-value: 1.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429 1479 NIESQGELILQESFQVWDPKTlirKGRERHLFLFEMSLVFSKEVKDSSGRSKYLYKSKLFTSELGVTEHvEGDPCKFALW 1558
Cdd:cd13325     2 NIHKLGRLLRHDWFTVTDGEG---KAKERYLFLFKSRILITKVRRISEDRSVFILKDIIRLPEVNVKQH-PDDERTFELQ 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 568990429 1559 VGRTPTSDNKIVLKASSIENKQDWIKHIREVIQE 1592
Cdd:cd13325    78 PKLPAFGILPIDFKAHKDEIKDYWLNEIEEYAND 111
PH_Collybistin_ASEF cd01224
Collybistin/APC-stimulated guanine nucleotide exchange factor pleckstrin homology (PH) domain; ...
 1469-1593 7.71e-08

Collybistin/APC-stimulated guanine nucleotide exchange factor pleckstrin homology (PH) domain; Collybistin (also called PEM2) is homologous to the Dbl proteins ASEF (also called ARHGEF4/RhoGEF4) and SPATA13 (Spermatogenesis-associated protein 13; also called ASEF2). It activates CDC42 specifically and not any other Rho-family GTPases. Collybistin consists of an SH3 domain, followed by a RhoGEF/DH and PH domain. In Dbl proteins, the DH and PH domains catalyze the exchange of GDP for GTP in Rho GTPases, allowing them to signal to downstream effectors. It induces submembrane clustering of the receptor-associated peripheral membrane protein gephyrin, which is thought to form a scaffold underneath the postsynaptic membrane linking receptors to the cytoskeleton. It also acts as a tumor suppressor that links adenomatous polyposis coli (APC) protein, a negative regulator of the Wnt signaling pathway and promotes the phosphorylation and degradation of beta-catenin, to Cdc42. Autoinhibition of collybistin is accomplished by the binding of its SH3 domain with both the RhoGEF and PH domains to block access of Cdc42 to the GTPase-binding site. Inactivation promotes cancer progression. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269931  Cd Length: 138  Bit Score: 53.03  E-value: 7.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429 1469 HLSMLEGFDENIES-QGELILQESFQVWDPKTL--IRKGR--ERHLFLFEMSLVFSKevKDSSGRSKYLYKSKLFTSELG 1543
Cdd:cd01224     3 NLEKLAAWQSTVEGwEGEDLSDRSSELIHSGELtkISAGRaqERTFFLFDHQLVYCK--KDLLRRKNYIYKGRIDTDNME 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568990429 1544 V------TEHVEGDPCKFALWVGRtpTSDNK-IVLKASSIENKQDWIKHIREviqER 1593
Cdd:cd01224    81 IedlpdgKDDESGVTVKNAWKIYN--ASKNKwYVLCAKSAEEKQRWLEAFAE---ER 132
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 1662-1712 1.11e-07

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


Pssm-ID: 212690 [Multi-domain]  Cd Length: 51  Bit Score: 49.77  E-value: 1.11e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568990429 1662 VVIHDFTACNSNELTIRRGQTVEVLERPHDkpDWCLVRTTDRSpaaEGLVP 1712
Cdd:cd00174     3 RALYDYEAQDDDELSFKKGDIITVLEKDDD--GWWEGELNGGR---EGLFP 48
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 1505-1590 1.24e-07

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 51.41  E-value: 1.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  1505 RERHLFLFEMSLVFSKevkDSSGRSKYLYKSKLFTSELGVTEHVEGD----PCKFALWVGrTPTSDNKIVLKASSIENKQ 1580
Cdd:pfam00169   19 KKRYFVLFDGSLLYYK---DDKSGKSKEPKGSISLSGCEVVEVVASDspkrKFCFELRTG-ERTGKRTYLLQAESEEERK 94

                           90
                   ....*....|
gi 568990429  1581 DWIKHIREVI 1590
Cdd:pfam00169   95 DWIKAIQSAI 104
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 1662-1713 1.59e-07

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: 49.46  E-value: 1.59e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 568990429   1662 VVIHDFTACNSNELTIRRGQTVEVLERPHDkpDWCLVRTTDRspaAEGLVPC 1713
Cdd:smart00326    6 RALYDYTAQDPDELSFKKGDIITVLEKSDD--GWWKGRLGRG---KEGLFPS 52
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 1483-1591 1.94e-07

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: 51.01  E-value: 1.94e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   1483 QGELILQEsfqvwdpKTLIRKGRERHLFLFEMSLVFSKevkDSSGRSKYLYKSKLFTSELGVTEHVEGD----PCKFALW 1558
Cdd:smart00233    4 EGWLYKKS-------GGGKKSWKKRYFVLFNSTLLYYK---SKKDKKSYKPKGSIDLSGCTVREAPDPDsskkPHCFEIK 73

                            90       100       110
                    ....*....|....*....|....*....|...
gi 568990429   1559 VGRTPTsdnkIVLKASSIENKQDWIKHIREVIQ 1591
Cdd:smart00233   74 TSDRKT----LLLQAESEEEREKWVEALRKAIA 102
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 1501-1586 3.26e-07

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


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 49.85  E-value: 3.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429 1501 IRKGRERHLFLFEMSLVFSKEVKDSSGRSKYLYKsklFTSELGVTEHVEGD-PCKFALWVgrtpTSDNKIVLKASSIENK 1579
Cdd:cd00821    13 LKSWKKRWFVLFEGVLLYYKSKKDSSYKPKGSIP---LSGILEVEEVSPKErPHCFELVT----PDGRTYYLQADSEEER 85


                  ....*..
gi 568990429 1580 QDWIKHI 1586
Cdd:cd00821    86 QEWLKAL 92
SH3_Eps8 cd11764
Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar ...
 1660-1713 5.69e-07

Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar proteins; This group is composed of Eps8 and Eps8-like proteins including Eps8-like 1-3, among others. These proteins contain N-terminal Phosphotyrosine-binding (PTB), central SH3, and C-terminal effector domains. Eps8 binds either Abi1 (also called E3b1) or Rab5 GTPase activating protein RN-tre through its SH3 domain. With Abi1 and Sos1, it becomes part of a trimeric complex that is required to activate Rac. Together with RN-tre, it inhibits the internalization of EGFR. The SH3 domains of Eps8 and similar proteins recognize peptides containing a PxxDY motif, instead of the classical PxxP motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity. 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: 212698 [Multi-domain]  Cd Length: 54  Bit Score: 48.03  E-value: 5.69e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568990429 1660 LTVVIHDFTACNSNELTIRRGQTVEVLErphDKPDWCLVRTtdrSPAAEGLVPC 1713
Cdd:cd11764     1 YVRVLYDFTARNSKELSVLKGEYLEVLD---DSRQWWKVRN---SRGQVGYVPH 48
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 1280-1457 6.36e-07

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


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 54.90  E-value: 6.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429 1280 HELNEEKRKSARRKEFIMAELIQTEKAYVRDLRECMDTY---LWEMTsgveeIPPGIVNKELI--IFGNMQEIYEFhNNI 1354
Cdd:COG5422   472 KEVWESLPKQEIKRQEAIYEVIYTERDFVKDLEYLRDTWikpLEESN-----IIPENARRNFIkhVFANINEIYAV-NSK 545

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429 1355 FLKELEK---YEQLPEDVGHCFVTWADKFQMYVTYCKNKPDSTQLIlEHAGS-------YFDEIQ-----QRHGlansIS 1419
Cdd:COG5422   546 LLKALTNrqcLSPIVNGIADIFLDYVPKFEPFIKYGASQPYAKYEF-EREKSvnpnfarFDHEVErldesRKLE----LD 620

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 568990429 1420 SYLIKPVQRITKYQLLLKELLTCCEEGKGEIKDGLEVM 1457
Cdd:COG5422   621 GYLTKPTTRLARYPLLLEEVLKFTDPDNPDTEDIPKVI 658
SH3_p47phox_like cd11856
Src homology 3 domains of the p47phox subunit of NADPH oxidase and similar domains; This ...
 1662-1713 6.79e-07

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


Pssm-ID: 212790 [Multi-domain]  Cd Length: 53  Bit Score: 47.63  E-value: 6.79e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568990429 1662 VVIHDFTACNSNELTIRRGQTVEVLERphDKPDWCLVRTTDRspaaEGLVPC 1713
Cdd:cd11856     3 VAIADYEAQGDDEISLQEGEVVEVLEK--NDSGWWYVRKGDK----EGWVPA 48
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 908-999 7.10e-07

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 49.24  E-value: 7.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   908 QLRHLQAEVKQVLGWIRNGESMLNAGLItASSLQEAEQLQREHEQFQHAIEkTHQSALQ-VQQKAEAMLQANHYDMDMIR 986
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEALLSSEDY-GKDLESVQALLKKHKALEAELA-AHQDRVEaLNELAEKLIDEGHYASEEIQ 79

                           90
                   ....*....|...
gi 568990429   987 DCAEKVASHWQQL 999
Cdd:pfam00435   80 ERLEELNERWEQL 92
SPEC smart00150
Spectrin repeats;
221-337 2.11e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 48.09  E-value: 2.11e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429    221 EEYISNAAHMLSRLEELQDVLAKKELPQDLEGARNMIDEHSQLKKKV--IKAPIEDLDLEGQKLLQriqssdsfpkknSG 298
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELeaHEERVEALNELGEQLIE------------EG 68

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 568990429    299 SGNAdlqnllPKVSTMLDRLHSTRQHLHQMWHVRKLKLD 337
Cdd:smart00150   69 HPDA------EEIEERLEELNERWEELKELAEERRQKLE 101
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 1662-1713 3.17e-06

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


Pssm-ID: 394975 [Multi-domain]  Cd Length: 47  Bit Score: 45.66  E-value: 3.17e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568990429  1662 VVIHDFTACNSNELTIRRGQTVEVLERPHDkpDWCLVRTTDRSpaaEGLVPC 1713
Cdd:pfam00018    1 VALYDYTAQEPDELSFKKGDIIIVLEKSED--GWWKGRNKGGK---EGLIPS 47
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 1143-1243 3.50e-06

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 47.31  E-value: 3.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  1143 FERSAKQALEWIHDNGEFYLSThtSTGSSIQHTQELLKEHEEFQITAKQTKERVKLLIQLADGFCEKGHAHAAEIKKCVT 1222
Cdd:pfam00435    6 FFRDADDLESWIEEKEALLSSE--DYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83

                           90       100
                   ....*....|....*....|.
gi 568990429  1223 AVDKRYRDFSLRMEKYRTSLE 1243
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLE 104
SPEC smart00150
Spectrin repeats;
676-783 5.64e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 46.55  E-value: 5.64e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429    676 FHTHVKELWTWLEELQKELLDDVYAESVEAVQDLIKR---FGQQQQTTLQVTVNVIKEGEDLIQQlrdsaissnktpHNS 752
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKheaFEAELEAHEERVEALNELGEQLIEE------------GHP 70

                            90       100       110
                    ....*....|....*....|....*....|.
gi 568990429    753 SINHIETVLQQLDEAQSQMEELFQERKIKLE 783
Cdd:smart00150   71 DAEEIEERLEELNERWEELKELAEERRQKLE 101
SH3_Fus1p cd11854
Src homology 3 domain of yeast cell fusion protein Fus1p; Fus1p is required at the cell ...
 1660-1719 1.06e-05

Src homology 3 domain of yeast cell fusion protein Fus1p; Fus1p is required at the cell surface for cell fusion during the mating response in yeast. It requires Bch1p and Bud7p, which are Chs5p-Arf1p binding proteins, for localization to the plasma membrane. It acts as a scaffold protein to assemble a cell surface complex which is involved in septum degradation and inhibition of the NOG pathway to promote cell fusion. The SH3 domain of Fus1p interacts with Bin1p, a formin that controls the assembly of actin cables in response to Cdc42 signaling. It has been shown to bind the motif, R(S/T)(S/T)SL, instead of PxxP motifs. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. 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: 212788 [Multi-domain]  Cd Length: 56  Bit Score: 44.62  E-value: 1.06e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429 1660 LTVVIHDFTACNSNELTIRRGQTVEVLERPHDkpDWCLVRTTDRSPAAEGLVPCgsLCIA 1719
Cdd:cd11854     1 LMTVISTFEPSLDDELLIKVGETVRVLAEYDD--GWCLVERADGLNGDRGMVPG--ECLQ 56
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 341-444 2.80e-05

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 45.00  E-value: 2.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   341 QLRLFEQDAEKMFDWIThNKGLFLNSyTEIGTSHPHAMELQTQHNHFAMNcMNVY-VNINRIMSVANRLVESGHYASQQI 419
Cdd:pfam00435    2 LLQQFFRDADDLESWIE-EKEALLSS-EDYGKDLESVQALLKKHKALEAE-LAAHqDRVEALNELAEKLIDEGHYASEEI 78

                           90       100
                   ....*....|....*....|....*
gi 568990429   420 KQIANQLEQEWKAFAAALDERSTLL 444
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKL 103
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 571-670 6.35e-05

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 43.85  E-value: 6.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   571 FQQDVQQVLDWIENHgEAFLSKhTGVGKSLHRARALQKRHEDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIYQAAH 650
Cdd:pfam00435    6 FFRDADDLESWIEEK-EALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83

                           90       100
                   ....*....|....*....|
gi 568990429   651 QLEDRIQDFVRRVEQRKILL 670
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKL 103
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 733-1039 1.04e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 1.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   733 DLIQQLRDSAISSNKTPHNSSINHIETVLQQLDEAQSQMEEL---FQERKIKLElFLQLRIFERDaiDIISDLESWNDEL 809
Cdd:TIGR02168  217 ELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELtaeLQELEEKLE-ELRLEVSELE--EEIEELQKELYAL 293

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   810 SQQMNDFdtedltiaEQRLQHHADKALTMNNLTFDVIHQGQDLLQYVNEVQASGVELLCDRDVDMA--TRVQDLLEFLHE 887
Cdd:TIGR02168  294 ANEISRL--------EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEelESLEAELEELEA 365

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   888 KQQELDLAAEQHRKHLEQcvqlrhLQAEVKQvlgwIRNGESMLNAGLITASSlqEAEQLQREHEQFQHAIEkTHQSALQV 967
Cdd:TIGR02168  366 ELEELESRLEELEEQLET------LRSKVAQ----LELQIASLNNEIERLEA--RLERLEDRRERLQQEIE-ELLKKLEE 432

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568990429   968 QQKAEAMLQANHYDMdMIRDCAEKVASHWQQLMLKMEDRLKLVNASVAFYKTSEQVCSVLESLEQEYKREED 1039
Cdd:TIGR02168  433 AELKELQAELEELEE-ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
SH3_DNMBP_C2_like cd11800
Second C-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba, and ...
 1666-1698 1.92e-04

Second C-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba, and similar domains; DNMBP or Tuba is a cdc42-specific guanine nucleotide exchange factor (GEF) that contains four N-terminal SH3 domains, a central RhoGEF [or Dbl homology (DH)] domain followed by a Bin/Amphiphysin/Rvs (BAR) domain, and two C-terminal SH3 domains. It provides a functional link between dynamin, Rho GTPase signaling, and actin dynamics. It plays an important role in regulating cell junction configuration. The C-terminal SH3 domains of DNMBP bind to N-WASP and Ena/VASP proteins, which are key regulatory proteins of the actin cytoskeleton. Also included in this subfamily is the second C-terminal SH3 domain of Rho guanine nucleotide exchange factor 37 (ARHGEF37), whose function is still unknown. 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: 212734 [Multi-domain]  Cd Length: 57  Bit Score: 40.82  E-value: 1.92e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 568990429 1666 DFTACNSNELTIRRGQTVEVLErPHDK---PDWCLV 1698
Cdd:cd11800     7 TFEARSPGELSVTEGQVVTVLE-KHDLkgnPEWWLV 41
SH3_Bzz1_1 cd11912
First Src Homology 3 domain of Bzz1 and similar domains; Bzz1 (or Bzz1p) is a WASP ...
 1663-1712 2.42e-04

First Src Homology 3 domain of Bzz1 and similar domains; Bzz1 (or Bzz1p) is a WASP/Las17-interacting protein involved in endocytosis and trafficking to the vacuole. It physically interacts with type I myosins and functions in the early steps of endocytosis. Together with other proteins, it induces membrane scission in yeast. Bzz1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. This model represents the first C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212845 [Multi-domain]  Cd Length: 55  Bit Score: 40.67  E-value: 2.42e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568990429 1663 VIHDFTACNSNELTIRRGQTVEVLErPHDKPDWCLVRTTDrspAAEGLVP 1712
Cdd:cd11912     4 VLYDYTASGDDEVSISEGEEVTVLE-PDDGSGWTKVRNGS---GEEGLVP 49
SH3_ARHGEF37_C2 cd11941
Second C-terminal Src homology 3 domain of Rho guanine nucleotide exchange factor 37; ARHGEF37 ...
 1662-1718 2.70e-04

Second C-terminal Src homology 3 domain of Rho guanine nucleotide exchange factor 37; ARHGEF37 contains a RhoGEF [or Dbl homology (DH)] domain followed by a Bin/Amphiphysin/Rvs (BAR) domain, and two C-terminal SH3 domains. Its specific function is unknown. Its domain architecture is similar to the C-terminal half of DNMBP or Tuba, a cdc42-specific GEF that provides a functional link between dynamin, Rho GTPase signaling, and actin dynamics, and plays an important role in regulating cell junction configuration. GEFs activate small GTPases by exchanging bound GDP for free GTP. 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: 212874  Cd Length: 57  Bit Score: 40.67  E-value: 2.70e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429 1662 VVIHDFTACNSNELTIRRGQTVEVLErPHDK---PDWCLVRTTDRspaaEGLVPCGSLCI 1718
Cdd:cd11941     3 VAAYPFTARSKHEVSLQAGQPVTVLE-PHDKkgsPEWSLVEVNGQ----RGYVPSSYLAR 57
SH3_Nck1_3 cd11904
Third Src Homology 3 domain of Nck1 adaptor protein; Nck1 (also called Nckalpha) plays a ...
 1664-1712 3.03e-04

Third Src Homology 3 domain of Nck1 adaptor protein; Nck1 (also called Nckalpha) plays a crucial role in connecting signaling pathways of tyrosine kinase receptors and important effectors in actin dynamics and cytoskeletal remodeling. It binds and activates RasGAP, resulting in the downregulation of Ras. It is also involved in the signaling of endothilin-mediated inhibition of cell migration. Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2, which show partly overlapping functions but also bind distinct targets. The third SH3 domain of Nck appears to prefer ligands with a PxAPxR motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212837 [Multi-domain]  Cd Length: 57  Bit Score: 40.40  E-value: 3.03e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568990429 1664 IHDFTACNSNELTIRRGQTVEVLERPHDKPDWCLVRTTDrspAAEGLVP 1712
Cdd:cd11904     6 LYPFSSSNDEELNFEKGEVMDVIEKPENDPEWWKCRKAN---GQVGLVP 51
SH3_Sla1p_3 cd11775
Third Src Homology 3 domain of the fungal endocytic adaptor protein Sla1p; Sla1p facilitates ...
 1659-1712 3.30e-04

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: 40.38  E-value: 3.30e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568990429 1659 ELTVVIHDFTACNSNELTIRRGQTVEVLERPHDKpDWCLVRttDRSPAAEGLVP 1712
Cdd:cd11775     1 KRGKVLYDFDAQSDDELTVKEGDVVYILDDKKSK-DWWMVE--NVSTGKEGVVP 51
SH3_Nck2_3 cd11903
Third Src Homology 3 domain of Nck2 adaptor protein; Nck2 (also called Nckbeta or Growth ...
 1664-1712 4.64e-04

Third Src Homology 3 domain of Nck2 adaptor protein; Nck2 (also called Nckbeta or Growth factor receptor-bound protein 4, Grb4) plays a crucial role in connecting signaling pathways of tyrosine kinase receptors and important effectors in actin dynamics and cytoskeletal remodeling. It binds neuronal signaling proteins such as ephrinB and Disabled-1 (Dab-1) exclusively. Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2, which show partly overlapping functions but also bind distinct targets. The third SH3 domain of Nck appears to prefer ligands with a PxAPxR motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212836 [Multi-domain]  Cd Length: 59  Bit Score: 40.04  E-value: 4.64e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568990429 1664 IHDFTACNSNELTIRRGQTVEVLERPHDKPDWCLVRTtdrSPAAEGLVP 1712
Cdd:cd11903     6 LYPFSSVTEEELNFEKGETMEVIEKPENDPEWWKCKN---SRGQVGLVP 51
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 766-977 5.70e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 5.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  766 EAQSQMEELfQERKIKLeLFLQLRIFERDAIDIISDLESWNDELSQQMNDFDTEDLTIAEQRLQHHAdkaltmnnLTFDV 845
Cdd:COG1196   214 RYRELKEEL-KELEAEL-LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE--------LELEL 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  846 IHQGQDLLQYVNEVQA--SGVELLCDRDVDMATRVQDLLEFLHEKQQELDLAAEQHRKHLEQCVQLRHLQAEVKQVLgwI 923
Cdd:COG1196   284 EEAQAEEYELLAELARleQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL--A 361

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568990429  924 RNGESMLNAGLITASSLQEAEQLQREHEQFQHAIEKTHQSALQVQQKAEAMLQA 977
Cdd:COG1196   362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
SH3_GRB2_like_N cd11804
N-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related ...
 1662-1713 8.50e-04

N-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related proteins; This family includes the adaptor protein GRB2 and related proteins including Drosophila melanogaster Downstream of receptor kinase (DRK), Caenorhabditis elegans Sex muscle abnormal protein 5 (Sem-5), GRB2-related adaptor protein (GRAP), GRAP2, and similar proteins. Family members contain an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. GRB2/Sem-5/DRK is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. GRAP2 plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. GRAP acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. The N-terminal SH3 domain of GRB2 binds to Sos and Sos-derived proline-rich peptides. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212738 [Multi-domain]  Cd Length: 52  Bit Score: 38.88  E-value: 8.50e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568990429 1662 VVIHDFTACNSNELTIRRGQTVEVLERPHDkPDWCLVRTTDRspaaEGLVPC 1713
Cdd:cd11804     3 VAKHDFKATAEDELSFKKGSILKVLNMEDD-PNWYKAELDGK----EGLIPK 49
SH3_Abl cd11850
Src homology 3 domain of the Protein Tyrosine Kinase, Abelson kinase; Abl (or c-Abl) is a ...
 1660-1712 8.79e-04

Src homology 3 domain of the Protein Tyrosine Kinase, Abelson kinase; Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212784  Cd Length: 56  Bit Score: 38.93  E-value: 8.79e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568990429 1660 LTVVIHDFTACNSNELTIRRGQTVEVLERPHDKpDWCLVRTtdRSPAAEGLVP 1712
Cdd:cd11850     1 LFVALYDFVASGENQLSIKKGEQLRVLGYNKNG-EWCEAES--KSTGGQGWVP 50
SH3_PSTPIP1 cd11824
Src homology 3 domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; PSTPIP1, ...
 1662-1718 1.03e-03

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


Pssm-ID: 212758 [Multi-domain]  Cd Length: 53  Bit Score: 38.89  E-value: 1.03e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568990429 1662 VVIHDFTACNSNELTIRRGQTVEVLERPHDkpDWCLVrttDRSpAAEGLVPCGSLCI 1718
Cdd:cd11824     3 SVLYDYTAQEDDELSISKGDVVAVIEKGED--GWWTV---ERN-GQKGLVPGTYLEK 53
SH3_Kalirin_2 cd11853
Second Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or ...
 1662-1712 1.04e-03

Second 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: 212787  Cd Length: 59  Bit Score: 38.96  E-value: 1.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568990429 1662 VVIHDFTACNSNELTIRRGQTVEVLERphDKPDWCLVR--TTDRSPAAEGLVP 1712
Cdd:cd11853     3 PVIQDYYALKEDEICVSQGEVVQILAA--NQQNMFLVYrpATDQSPAAEGWIP 53
SH3_PEX13_eumet cd11864
Src Homology 3 domain of eumetazoan Peroxisomal biogenesis factor 13; PEX13 is a peroxin and ...
 1660-1712 1.34e-03

Src Homology 3 domain of eumetazoan Peroxisomal biogenesis factor 13; PEX13 is a peroxin and is required for protein import into the peroxisomal matrix and membrane. It is an integral membrane protein that is essential for the localization of PEX14 and the import of proteins containing the peroxisome matrix targeting signals, PTS1 and PTS2. Mutations of the PEX13 gene in humans lead to a wide range of peroxisome biogenesis disorders (PBDs), the most severe of which is known as Zellweger syndrome (ZS), a severe multisystem disorder characterized by hypotonia, psychomotor retardation, and neuronal migration defects. PEX13 contains two transmembrane regions and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212798  Cd Length: 58  Bit Score: 38.77  E-value: 1.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568990429 1660 LTVVIHDFTACNSNELTIRRGQTVEVLER---PHdKPDWCLVRTTDRSPaaeGLVP 1712
Cdd:cd11864     1 VARAEYDFVAESEDELSFRAGDKLRLAPKelqPR-VRGWLLATVDGQKI---GLVP 52
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 574-914 1.39e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 43.79  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  574 DVQQVLDwienhgeaflSKHTgvgkslhraRALQkrhedfeevaqntYTNADKLLEAAEQLAQTGECDPEEI--YQAAHQ 651
Cdd:COG3096   400 DYQQALD----------VQQT---------RAIQ-------------YQQAVQALEKARALCGLPDLTPENAedYLAAFR 447

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  652 L-EDRIQDFVRRVEQRKILLDMSVSFHTHVKELwtwleeLQKeLLDDVYAESV-EAVQDLIKRFgqqqqttlQVTVNVIK 729
Cdd:COG3096   448 AkEQQATEEVLELEQKLSVADAARRQFEKAYEL------VCK-IAGEVERSQAwQTARELLRRY--------RSQQALAQ 512

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  730 EGEDLIQQLRDsaissnktphnssinhIETVLQQLDEAQSQMEELFQERKIKLELFLQLRiferdaiDIISDLESWNDEL 809
Cdd:COG3096   513 RLQQLRAQLAE----------------LEQRLRQQQNAERLLEEFCQRIGQQLDAAEELE-------ELLAELEAQLEEL 569

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429  810 SQQMNDFdTEDLTIAEQRLQHHADKaltMNNLTFD--VIHQGQDLLQYVNEvqASGVELLCDRDVdMATRvQDLLEFLHE 887
Cdd:COG3096   570 EEQAAEA-VEQRSELRQQLEQLRAR---IKELAARapAWLAAQDALERLRE--QSGEALADSQEV-TAAM-QQLLERERE 641

                         330       340
                  ....*....|....*....|....*..
gi 568990429  888 KQQELDLAAEQhRKHLEQcvQLRHLQA 914
Cdd:COG3096   642 ATVERDELAAR-KQALES--QIERLSQ 665
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 220-338 4.35e-03

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 38.45  E-value: 4.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   220 FEEYISNAAHMLSRLEELQDVLAKKELPQDLEGARNMIDEHSQLKK--KVIKAPIEDLDLEGQKLLQRiQSSDSfpkkns 297
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAelAAHQDRVEALNELAEKLIDE-GHYAS------ 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 568990429   298 gsgnadlqnllPKVSTMLDRLHSTRQHLHQMWHVRKLKLDQ 338
Cdd:pfam00435   76 -----------EEIQERLEELNERWEQLLELAAERKQKLEE 105
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 544-846 4.63e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 4.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   544 VLHHQRQLENIWQHRKVRLHQRLQLCVFQQDVQQVLDWIENHGEAFLSKHTGVGKSLHRARALQKRHEDFEEVAQNTYTN 623
Cdd:TIGR02168  672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   624 ADKLLEAAEQLAQTGECDPEEIYQAAHQLEDRIQDFVRRVEQRKILLdmsvsfhthvKELWTWLEELQKEL--LDDVYAE 701
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL----------KALREALDELRAELtlLNEEAAN 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   702 SVEAVQDLIKRfgqqqqttlqvTVNVIKEGEDLIQQLRDSAissnktphnssiNHIETVLQQLDEAQSQMEELFQERKIK 781
Cdd:TIGR02168  822 LRERLESLERR-----------IAATERRLEDLEEQIEELS------------EDIESLAAEIEELEELIEELESELEAL 878

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568990429   782 LELF----LQLRIFERDAIDIISDLESWN----------DELSQQMNDFDTEdLTIAEQRLQHHADKALTMNNLTFDVI 846
Cdd:TIGR02168  879 LNERasleEALALLRSELEELSEELRELEskrselrrelEELREKLAQLELR-LEGLEVRIDNLQERLSEEYSLTLEEA 956
SH3_Nck_3 cd11767
Third Src Homology 3 domain of Nck adaptor proteins; This group contains the third SH3 domain ...
 1667-1712 4.79e-03

Third Src Homology 3 domain of Nck adaptor proteins; This group contains the third SH3 domain of Nck, the first SH3 domain of Caenorhabditis elegans Ced-2 (Cell death abnormality protein 2), and similar domains. Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2 (also called Nckbeta or Growth factor receptor-bound protein 4, Grb4), which show partly overlapping functions but also bind distinct targets. Their SH3 domains are involved in recruiting downstream effector molecules, such as the N-WASP/Arp2/3 complex, which when activated induces actin polymerization that results in the production of pedestals, or protrusions of the plasma membrane. The third SH3 domain of Nck appears to prefer ligands with a PxAPxR motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. Ced-2 is a cell corpse engulfment protein that interacts with Ced-5 in a pathway that regulates the activation of Ced-10, a Rac small GTPase.


Pssm-ID: 212701 [Multi-domain]  Cd Length: 56  Bit Score: 36.91  E-value: 4.79e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 568990429 1667 FTACNSNELTIRRGQTVEVLERPHDKPDWCLVRttdRSPAAEGLVP 1712
Cdd:cd11767     8 FTGENDEELSFEKGERLEIIEKPEDDPDWWKAR---NALGTTGLVP 50
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 676-783 6.12e-03

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 38.07  E-value: 6.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990429   676 FHTHVKELWTWLEELQKELLDDVYAESVEAVQDLIKRFGQQQQTTLQVTVNViKEGEDLIQQLRDSAISSNKtphnssin 755
Cdd:pfam00435    6 FFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRV-EALNELAEKLIDEGHYASE-------- 76

                           90       100
                   ....*....|....*....|....*...
gi 568990429   756 HIETVLQQLDEAQSQMEELFQERKIKLE 783
Cdd:pfam00435   77 EIQERLEELNERWEQLLELAAERKQKLE 104
SH3_CIP4-like cd11911
Src Homology 3 domain of Cdc42-Interacting Protein 4; This subfamily is composed of ...
 1662-1712 7.04e-03

Src Homology 3 domain of Cdc42-Interacting Protein 4; This subfamily is composed of Cdc42-Interacting Protein 4 (CIP4), Formin Binding Protein 17 (FBP17), FormiN Binding Protein 1-Like (FNBP1L), and similar proteins. CIP4 and FNBP1L are Cdc42 effectors that bind Wiskott-Aldrich syndrome protein (WASP) and function in endocytosis. CIP4 and FBP17 bind to the Fas ligand and may be implicated in the inflammatory response. CIP4 may also play a role in phagocytosis. It functions downstream of Cdc42 in PDGF-dependent actin reorganization and cell migration, and also regulates the activity of PDGFRbeta. It uses Src as a substrate in regulating the invasiveness of breast tumor cells. CIP4 may also play a role in the pathogenesis of Huntington's disease. Members of this subfamily typically contain an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain, a central Cdc42-binding HR1 domain, and a C-terminal SH3 domain. The SH3 domain of CIP4 associates with Gapex-5, a Rab31 GEF. 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: 212844 [Multi-domain]  Cd Length: 55  Bit Score: 36.47  E-value: 7.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568990429 1662 VVIHDFTACNSNELTIRRGQTVEVLErpHDKPD-WCLVRttdRSPAAEGLVP 1712
Cdd:cd11911     3 TALYDFDGTSEGTLSMEEGEILLVLE--EDGGDgWTRVR---KNNGDEGYVP 49
SH3_AHI-1 cd11812
Src Homology 3 domain of Abelson helper integration site-1 (AHI-1); AHI-1, also called ...
 1661-1695 7.51e-03

Src Homology 3 domain of Abelson helper integration site-1 (AHI-1); AHI-1, also called Jouberin, is expressed in high levels in the brain, gonad tissues, and skeletal muscle. It is an adaptor protein that interacts with the small GTPase Rab8a and regulates it distribution and function, affecting cilium formation and vesicle transport. Mutations in the AHI-1 gene can cause Joubert syndrome, a disorder characterized by brainstem malformations, cerebellar aplasia/hypoplasia, and retinal dystrophy. AHI-1 variation is also associated with susceptibility to schizophrenia and type 2 diabetes mellitus progression. AHI-1 contains WD40 and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212746 [Multi-domain]  Cd Length: 52  Bit Score: 36.33  E-value: 7.51e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 568990429 1661 TVV-IHDFTACNSNELTIRRGQTVEVLERphDKPDW 1695
Cdd:cd11812     1 TVVaLYDYTANRSDELTIHRGDIIRVLYK--DNDNW 34
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH