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Conserved domains on  [gi|1958666296|ref|XP_038944590|]
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kalirin isoform X30 [Rattus norvegicus]

Protein Classification

RhoGEF and PH1_Kalirin_Trio_like domain-containing protein( domain architecture ID 11271280)

protein containing domains SEC14, SPEC, RhoGEF, and PH1_Kalirin_Trio_like

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH1_Kalirin_Trio_like cd13240
Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; ...
 1461-1583 5.88e-68

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: 224.19  E-value: 5.88e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296 1461 MLEGFDENLDVQGELILQDAFQVWDPKSLIRKGRERHLFLFEISLVFSKEIKDSSGHTKYVYKNKLLTSELGVTEHVEGD 1540
Cdd:cd13240      1 LLEGCDEDLDSLGEVILQDSFQVWDPKQLIRKGRERHVFLFELCLVFSKEVKDSNGKSKYIYKSRLMTSEIGVTEHIEGD 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1958666296 1541 PCKFALWSGRTPSSDNKTVLKASNIETKQEWIKNIREVIQERI 1583
Cdd:cd13240     81 PCKFALWTGRVPTSDNKIVLKASSLEVKQTWVKKLREVIQERI 123
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 1284-1454 8.02e-44

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: 157.46  E-value: 8.02e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296 1284 FIMAELLQTEKAYVRDLHECLETYLWEMTSGVEEIPPgilNKEHIIFGNIQEIYDFHNnIFLKELEKY----EQLPEDVG 1359
Cdd:cd00160      3 EVIKELLQTERNYVRDLKLLVEVFLKPLDKELLPLSP---EEVELLFGNIEEIYEFHR-IFLKSLEERveewDKSGPRIG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296 1360 HCFVTWADKFQMYVTYCKNKPDSNQLILEHAG--TFFDEIQQRHGLAN---SISSYLIKPVQRVTKYQLLLKELLTCCEE 1434
Cdd:cd00160     79 DVFLKLAPFFKIYSEYCSNHPDALELLKKLKKfnKFFQEFLEKAESECgrlKLESLLLKPVQRLTKYPLLLKELLKHTPD 158

                          170       180
                   ....*....|....*....|...
gi 1958666296 1435 G---KGELKDGLEVMLSVPKKAN 1454
Cdd:cd00160    159 GhedREDLKKALEAIKEVASQVN 181
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 39-177 2.30e-24

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: 100.84  E-value: 2.30e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296    39 LKEKVAFVSGGR--DKRGGPILTFPARS--NHDRIRQEDLRKLVTYLASVPS---EDVCKRGFTVIIDMRGSK-----WD 106
Cdd:smart00516    2 LELLKAYIPGGRgyDKDGRPVLIERAGRfdLKSVTLEELLRYLVYVLEKILQeekKTGGIEGFTVIFDLKGLSmsnpdLS 81

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958666296   107 LIKPLLKTLQEAFPAEIHVALIIKPDNFWQ---KQKTNFGSSKFIFETSMVS---VEGLTKLVDPSQLTEEFDGSLD 177
Cdd:smart00516   82 VLRKILKILQDHYPERLGKVYIINPPWFFRvlwKIIKPFLDEKTREKIRFVGndsKEELLEYIDKEQLPEELGGTLD 158
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 891-1129 3.28e-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: 76.33  E-value: 3.28e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  891 QLRHLQAEVKQVLGWIRNGESMLnASLVNASSLSEAEQLQREHEQFQlaieslfhaTSLQKTHQSALQVQQKAEALLQAG 970
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELL-SSTDYGDDLESVEALLKKHEALE---------AELAAHEERVEALNELGEQLIEEG 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  971 HYDADAIRECAEKVALHWQQLMLKMEDRLKLVNASVAFYKTSEQVCSVlesleqeyrrdEDWCGGRDKLGPAAEMDHVIP 1050
Cdd:cd00176     71 HPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL-----------EQWLEEKEAALASEDLGKDLE 139

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958666296 1051 LLSKHLEQKEAFLKACTlarrNAEVFLKYIHRNNVSMpsVASHTRGPEQQVKAILSELLQRENRVLHFWTLKKRRLDQC 1129
Cdd:cd00176    140 SVEELLKKHKELEEELE----AHEPRLKSLNELAEEL--LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 537-719 6.51e-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: 75.56  E-value: 6.51e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  537 QLCVFQQDVQQVLDWIENHGEAFLSkhTGVGKSLHRARALQKRHDDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIY 616
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  617 KAARHLEVRIQDFVRRVEQRKLLLDMSV---SFHTHTKELWTWMEDLQKEVLEDVCADSVDAVQELIKQFQQQQtATLDA 693
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALdlqQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELE-EELEA 157

                          170       180
                   ....*....|....*....|....*.
gi 1958666296  694 TLNVIKEGEDLIQQLRSAPPSLGEPT 719
Cdd:cd00176    158 HEPRLKSLNELAEELLEEGHPDADEE 183
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 311-536 3.66e-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: 64.39  E-value: 3.66e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  311 QLRLFEQDAEKMFDWISHnKELFLQShTEIGVSYQHALDLQTQHNHFAMNSMNAYVNINRIMSVASRLSEAGHYASQQIK 390
Cdd:cd00176      1 KLQQFLRDADELEAWLSE-KEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  391 QISTQLDQEWKSFAAALDERSTILAMSAVFHQKAEQFLSgVDAWC----KMCSEGGLPSEMQDLELAIHHHQSLYEQVTQ 466
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLeekeAALASEDLGKDLESVEELLKKHKELEEELEA 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  467 AytevSQDGKALLDVLQRPLSPGNSESLTATAnyskavhqvlDVVHEVLHHQRRLESIWQHRKVRLHQRL 536
Cdd:cd00176    158 H----EPRLKSLNELAEELLEEGHPDADEEIE----------EKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 190-410 4.63e-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: 64.39  E-value: 4.63e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  190 LEEFFNSAVHLLSRLEDLQEMLARKEFPVDVEGSRRLIDEHTQLKK--KVLKAPVEELDREGQRLLQcircsdgfsgrnc 267
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAelAAHEERVEALNELGEQLIE------------- 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  268 ipgsaDFQSLVPKITSLLDKLHSTRQHLHQMWHVRKLKLDQCFQLRLFEQDAEKMFDWIShNKELFLQSHtEIGVSYQHA 347
Cdd:cd00176     69 -----EGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLE-EKEAALASE-DLGKDLESV 141

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958666296  348 LDLQTQHNHFaMNSMNAY-VNINRIMSVASRLSEAGHYASQ-QIKQISTQLDQEWKSFAAALDER 410
Cdd:cd00176    142 EELLKKHKEL-EEELEAHePRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEER 205
SPEC smart00150
Spectrin repeats;
1135-1235 2.72e-03

Spectrin repeats;


:

Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 38.85  E-value: 2.72e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  1135 FERSAKQALDWIQETgEYYLSTHTSTGETTEETQeLLKEYGEFRVPAKQTKEKVKLLIQLADSFVEKGHIHATEIRKWVT 1214
Cdd:smart00150    3 FLRDADELEAWLEEK-EQLLASEDLGKDLESVEA-LLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 1958666296  1215 TVDKHYRDFSLRMGKYRYTLE 1235
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 745-991 9.51e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 9.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  745 QQLDDAQVQMEELFHERKIKLDIFLQLRIFEQYTIEVTAELDAWNEDLLRQMNDFNTEDLTLAEQRLQRHTERKLAmNNM 824
Cdd:TIGR02168  698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA-EEE 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  825 TFEVIQQGQDLHQYIMEVQASgIELICEKDVDLAAQVQELLEFLHEKQHELElNAEQTHKRLEQCLQLRHLQAEVKQvlg 904
Cdd:TIGR02168  777 LAEAEAEIEELEAQIEQLKEE-LKALREALDELRAELTLLNEEAANLRERLE-SLERRIAATERRLEDLEEQIEELS--- 851

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  905 wirngESMLNASLVNASSLSEAEQLQREHEQFQLAIESLFHATSLQKTHQSALQVQ-QKAEALLQAGHYDADAIRECAEK 983
Cdd:TIGR02168  852 -----EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEElRELESKRSELRRELEELREKLAQ 926


                   ....*...
gi 1958666296  984 VALHWQQL 991
Cdd:TIGR02168  927 LELRLEGL 934
 
Name Accession Description Interval E-value
PH1_Kalirin_Trio_like cd13240
Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; ...
 1461-1583 5.88e-68

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: 224.19  E-value: 5.88e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296 1461 MLEGFDENLDVQGELILQDAFQVWDPKSLIRKGRERHLFLFEISLVFSKEIKDSSGHTKYVYKNKLLTSELGVTEHVEGD 1540
Cdd:cd13240      1 LLEGCDEDLDSLGEVILQDSFQVWDPKQLIRKGRERHVFLFELCLVFSKEVKDSNGKSKYIYKSRLMTSEIGVTEHIEGD 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1958666296 1541 PCKFALWSGRTPSSDNKTVLKASNIETKQEWIKNIREVIQERI 1583
Cdd:cd13240     81 PCKFALWTGRVPTSDNKIVLKASSLEVKQTWVKKLREVIQERI 123
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 1284-1454 8.02e-44

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: 157.46  E-value: 8.02e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296 1284 FIMAELLQTEKAYVRDLHECLETYLWEMTSGVEEIPPgilNKEHIIFGNIQEIYDFHNnIFLKELEKY----EQLPEDVG 1359
Cdd:cd00160      3 EVIKELLQTERNYVRDLKLLVEVFLKPLDKELLPLSP---EEVELLFGNIEEIYEFHR-IFLKSLEERveewDKSGPRIG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296 1360 HCFVTWADKFQMYVTYCKNKPDSNQLILEHAG--TFFDEIQQRHGLAN---SISSYLIKPVQRVTKYQLLLKELLTCCEE 1434
Cdd:cd00160     79 DVFLKLAPFFKIYSEYCSNHPDALELLKKLKKfnKFFQEFLEKAESECgrlKLESLLLKPVQRLTKYPLLLKELLKHTPD 158

                          170       180
                   ....*....|....*....|...
gi 1958666296 1435 G---KGELKDGLEVMLSVPKKAN 1454
Cdd:cd00160    159 GhedREDLKKALEAIKEVASQVN 181
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 1285-1455 1.48e-41

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: 150.91  E-value: 1.48e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  1285 IMAELLQTEKAYVRDLHECLETYLWEMTSGVEEIPPgilNKEHIIFGNIQEIYDFHNnIFLKELEKY----EQLPEDVGH 1360
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELKLLSP---NELETLFGNIEEIYEFHR-DFLDELEERieewDDSVERIGD 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  1361 CFVTWADKFQMYVTYCKNKPDSNQLI--LEHAGTFFDEIQQRHGLAN----SISSYLIKPVQRVTKYQLLLKELLTCCEE 1434
Cdd:smart00325   77 VFLKLEEFFKIYSEYCSNHPDALELLkkLKKNPRFQKFLKEIESSPQcrrlTLESLLLKPVQRLTKYPLLLKELLKHTPE 156

                           170       180
                    ....*....|....*....|....
gi 1958666296  1435 G---KGELKDGLEVMLSVPKKAND 1455
Cdd:smart00325  157 DhedREDLKKALKAIKELANQVNE 180
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 1285-1454 7.11e-41

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: 148.99  E-value: 7.11e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296 1285 IMAELLQTEKAYVRDLHECLETYLWEMTSGVEEIPPGIlnkeHIIFGNIQEIYDFHNNIFLKELEKYEQLPEDVGHCFVT 1364
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEI----KTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIFLK 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296 1365 WADKFQMYVTYCKNKPDSNQLI------LEHAGTFFDEIQQR---HGLanSISSYLIKPVQRVTKYQLLLKELLTCCEEG 1435
Cdd:pfam00621   77 FAPGFKVYSTYCSNYPKALKLLkkllkkNPKFRAFLEELEANpecRGL--DLNSFLIKPVQRIPRYPLLLKELLKHTPPD 154

                          170       180
                   ....*....|....*....|..
gi 1958666296 1436 ---KGELKDGLEVMLSVPKKAN 1454
Cdd:pfam00621  155 hpdYEDLKKALEAIKEVAKQIN 176
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 39-177 2.30e-24

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: 100.84  E-value: 2.30e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296    39 LKEKVAFVSGGR--DKRGGPILTFPARS--NHDRIRQEDLRKLVTYLASVPS---EDVCKRGFTVIIDMRGSK-----WD 106
Cdd:smart00516    2 LELLKAYIPGGRgyDKDGRPVLIERAGRfdLKSVTLEELLRYLVYVLEKILQeekKTGGIEGFTVIFDLKGLSmsnpdLS 81

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958666296   107 LIKPLLKTLQEAFPAEIHVALIIKPDNFWQ---KQKTNFGSSKFIFETSMVS---VEGLTKLVDPSQLTEEFDGSLD 177
Cdd:smart00516   82 VLRKILKILQDHYPERLGKVYIINPPWFFRvlwKIIKPFLDEKTREKIRFVGndsKEELLEYIDKEQLPEELGGTLD 158
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 891-1129 3.28e-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: 76.33  E-value: 3.28e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  891 QLRHLQAEVKQVLGWIRNGESMLnASLVNASSLSEAEQLQREHEQFQlaieslfhaTSLQKTHQSALQVQQKAEALLQAG 970
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELL-SSTDYGDDLESVEALLKKHEALE---------AELAAHEERVEALNELGEQLIEEG 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  971 HYDADAIRECAEKVALHWQQLMLKMEDRLKLVNASVAFYKTSEQVCSVlesleqeyrrdEDWCGGRDKLGPAAEMDHVIP 1050
Cdd:cd00176     71 HPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL-----------EQWLEEKEAALASEDLGKDLE 139

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958666296 1051 LLSKHLEQKEAFLKACTlarrNAEVFLKYIHRNNVSMpsVASHTRGPEQQVKAILSELLQRENRVLHFWTLKKRRLDQC 1129
Cdd:cd00176    140 SVEELLKKHKELEEELE----AHEPRLKSLNELAEEL--LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 44-175 4.67e-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: 74.29  E-value: 4.67e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296   44 AFVSGGRDKRGGPILTFPAR-SNHDRIRQEDLRKLVTYLASVPSEDVCKR--GFTVIIDMRGSKW------DLIKPLLKT 114
Cdd:cd00170     11 IGYLGGRDKEGRPVLVFRAGwDPPKLLDLEELLRYLVYLLEKALRELEEQveGFVVIIDLKGFSLsnlsdlSLLKKLLKI 90

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958666296  115 LQEAFPAEIHVALIIKPdNFWQKQKTNFGS--------SKFIFETSmvSVEGLTKLVDPSQLTEEFDGS 175
Cdd:cd00170     91 LQDHYPERLKKIYIVNA-PWIFSALWKIVKpflsektrKKIVFLGS--DLEELLEYIDPDQLPKELGGT 156
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 537-719 6.51e-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: 75.56  E-value: 6.51e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  537 QLCVFQQDVQQVLDWIENHGEAFLSkhTGVGKSLHRARALQKRHDDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIY 616
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  617 KAARHLEVRIQDFVRRVEQRKLLLDMSV---SFHTHTKELWTWMEDLQKEVLEDVCADSVDAVQELIKQFQQQQtATLDA 693
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALdlqQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELE-EELEA 157

                          170       180
                   ....*....|....*....|....*.
gi 1958666296  694 TLNVIKEGEDLIQQLRSAPPSLGEPT 719
Cdd:cd00176    158 HEPRLKSLNELAEELLEEGHPDADEE 183
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 311-536 3.66e-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: 64.39  E-value: 3.66e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  311 QLRLFEQDAEKMFDWISHnKELFLQShTEIGVSYQHALDLQTQHNHFAMNSMNAYVNINRIMSVASRLSEAGHYASQQIK 390
Cdd:cd00176      1 KLQQFLRDADELEAWLSE-KEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  391 QISTQLDQEWKSFAAALDERSTILAMSAVFHQKAEQFLSgVDAWC----KMCSEGGLPSEMQDLELAIHHHQSLYEQVTQ 466
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLeekeAALASEDLGKDLESVEELLKKHKELEEELEA 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  467 AytevSQDGKALLDVLQRPLSPGNSESLTATAnyskavhqvlDVVHEVLHHQRRLESIWQHRKVRLHQRL 536
Cdd:cd00176    158 H----EPRLKSLNELAEELLEEGHPDADEEIE----------EKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 190-410 4.63e-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: 64.39  E-value: 4.63e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  190 LEEFFNSAVHLLSRLEDLQEMLARKEFPVDVEGSRRLIDEHTQLKK--KVLKAPVEELDREGQRLLQcircsdgfsgrnc 267
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAelAAHEERVEALNELGEQLIE------------- 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  268 ipgsaDFQSLVPKITSLLDKLHSTRQHLHQMWHVRKLKLDQCFQLRLFEQDAEKMFDWIShNKELFLQSHtEIGVSYQHA 347
Cdd:cd00176     69 -----EGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLE-EKEAALASE-DLGKDLESV 141

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958666296  348 LDLQTQHNHFaMNSMNAY-VNINRIMSVASRLSEAGHYASQ-QIKQISTQLDQEWKSFAAALDER 410
Cdd:cd00176    142 EELLKKHKEL-EEELEAHePRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEER 205
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 54-181 6.81e-11

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: 61.96  E-value: 6.81e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296   54 GGPILTFPARS-NHDRIRQEDLRKLVTYLASVPSEDVCKRGFTVIIDMRGS------KWDLIKPLLKTLQEAFPAEIHVA 126
Cdd:pfam13716    1 GRPVLVFISKLlPSRPASLDDLDRLLFYLLKTLSEKLKGKPFVVVVDHTGVtsenfpSLSFLKKAYDLLPRAFKKNLKAV 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  127 LIIKPDNFWQKQ----KTNFGSSKFIFETSMVS-VEGLTKLVDPSQLTEEFDGSLDYNHE 181
Cdd:pfam13716   81 YVVHPSTFLRTFlktlGSLLGSKKLRKKVHYVSsLSELWEGIDREQLPTELPGVLSYDEE 140
SPEC smart00150
Spectrin repeats;
541-641 3.44e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 58.50  E-value: 3.44e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296   541 FQQDVQQVLDWIENHgEAFLSkHTGVGKSLHRARALQKRHDDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIYKAAR 620
Cdd:smart00150    3 FLRDADELEAWLEEK-EQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 1958666296   621 HLEVRIQDFVRRVEQRKLLLD 641
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
893-1000 2.19e-09

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 56.18  E-value: 2.19e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296   893 RHLQAEVKQVLGWIRNGESMLnASLVNASSLSEAEQLQREHEQFQlaieslfhaTSLQKTHQSALQVQQKAEALLQAGHY 972
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLL-ASEDLGKDLESVEALLKKHEAFE---------AELEAHEERVEALNELGEQLIEEGHP 70

                            90       100
                    ....*....|....*....|....*...
gi 1958666296   973 DADAIRECAEKVALHWQQLMLKMEDRLK 1000
Cdd:smart00150   71 DAEEIEERLEELNERWEELKELAEERRQ 98
SPEC smart00150
Spectrin repeats;
315-414 4.53e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 52.33  E-value: 4.53e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296   315 FEQDAEKMFDWIShNKELFLQShTEIGVSYQHALDLQTQHNHFAMNSMNAYVNINRIMSVASRLSEAGHYASQQIKQIST 394
Cdd:smart00150    3 FLRDADELEAWLE-EKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|
gi 1958666296   395 QLDQEWKSFAAALDERSTIL 414
Cdd:smart00150   81 ELNERWEELKELAEERRQKL 100
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 1226-1446 2.42e-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: 56.05  E-value: 2.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296 1226 RMGKYRYTLEKaLGVNTEDNKDLELDiipASLSDREVKLRDANHEVNEEKRKSARKKEFIMAELLQTEKAYVRDLhECLE 1305
Cdd:COG5422    433 RLEQQARLHLK-LMGGLKRNSSLALD---KFDEEKNLWTLSVPKEVWESLPKQEIKRQEAIYEVIYTERDFVKDL-EYLR 507

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296 1306 TYlWEMTSGVEEIPPGILNKEHI--IFGNIQEIYDFhNNIFLKELEK---YEQLPEDVGHCFVTWADKFQMYVTYCKNKP 1380
Cdd:COG5422    508 DT-WIKPLEESNIIPENARRNFIkhVFANINEIYAV-NSKLLKALTNrqcLSPIVNGIADIFLDYVPKFEPFIKYGASQP 585

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958666296 1381 DSNQLILEHAGT------FFDEIQ-----QRHGlansISSYLIKPVQRVTKYQLLLKELLTCCEEGKGELKDGLEVM 1446
Cdd:COG5422    586 YAKYEFEREKSVnpnfarFDHEVErldesRKLE----LDGYLTKPTTRLARYPLLLEEVLKFTDPDNPDTEDIPKVI 658
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 311-410 4.61e-06

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 46.93  E-value: 4.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  311 QLRLFEQDAEKMFDWIShNKELFLQShTEIGVSYQHALDLQTQHNHFaMNSMNAY-VNINRIMSVASRLSEAGHYASQQI 389
Cdd:pfam00435    2 LLQQFFRDADDLESWIE-EKEALLSS-EDYGKDLESVQALLKKHKAL-EAELAAHqDRVEALNELAEKLIDEGHYASEEI 78

                           90       100
                   ....*....|....*....|.
gi 1958666296  390 KQISTQLDQEWKSFAAALDER 410
Cdd:pfam00435   79 QERLEELNERWEQLLELAAER 99
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 1487-1580 5.72e-06

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


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 46.77  E-value: 5.72e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  1487 KSLIRKGRERHLFLFEISLVFSKeikDSSGHTKYVYKNKLLTSELGVTEHVEGD----PCKFALWSGrtpssDNKT-VLK 1561
Cdd:smart00233   12 GGGKKSWKKRYFVLFNSTLLYYK---SKKDKKSYKPKGSIDLSGCTVREAPDPDsskkPHCFEIKTS-----DRKTlLLQ 83

                            90
                    ....*....|....*....
gi 1958666296  1562 ASNIETKQEWIKNIREVIQ 1580
Cdd:smart00233   84 AESEEEREKWVEALRKAIA 102
SPEC smart00150
Spectrin repeats;
191-307 8.70e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 46.17  E-value: 8.70e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296   191 EEFFNSAVHLLSRLEDLQEMLARKEFPVDVEGSRRLIDEHTQLKKKV--LKAPVEELDREGQRLLQcircsdgfsgrnci 268
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELeaHEERVEALNELGEQLIE-------------- 66

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 1958666296   269 pgSADFQSlvPKITSLLDKLHSTRQHLHQMWHVRKLKLD 307
Cdd:smart00150   67 --EGHPDA--EEIEERLEELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 890-991 1.51e-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: 45.39  E-value: 1.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  890 LQLRHLQAEVKQVLGWIRNGESMLnASLVNASSLSEAEQLQREHEQFQLAIESlfHATSLQkthqsalQVQQKAEALLQA 969
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALL-SSEDYGKDLESVQALLKKHKALEAELAA--HQDRVE-------ALNELAEKLIDE 70

                           90       100
                   ....*....|....*....|..
gi 1958666296  970 GHYDADAIRECAEKVALHWQQL 991
Cdd:pfam00435   71 GHYASEEIQERLEELNERWEQL 92
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 1494-1579 2.67e-05

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 44.86  E-value: 2.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296 1494 RERHLFLFEISLVFSKeikDSSGHTKYVYKNKLLTSELGVTEHVEGD----PCKFALWSGrTPSSDNKTVLKASNIETKQ 1569
Cdd:pfam00169   19 KKRYFVLFDGSLLYYK---DDKSGKSKEPKGSISLSGCEVVEVVASDspkrKFCFELRTG-ERTGKRTYLLQAESEEERK 94

                           90
                   ....*....|
gi 1958666296 1570 EWIKNIREVI 1579
Cdd:pfam00169   95 DWIKAIQSAI 104
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 541-640 2.23e-04

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: 41.92  E-value: 2.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  541 FQQDVQQVLDWIENHgEAFLSKhTGVGKSLHRARALQKRHDDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIYKAAR 620
Cdd:pfam00435    6 FFRDADDLESWIEEK-EALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83

                           90       100
                   ....*....|....*....|
gi 1958666296  621 HLEVRIQDFVRRVEQRKLLL 640
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKL 103
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 190-308 1.62e-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: 39.61  E-value: 1.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  190 LEEFFNSAVHLLSRLEDLQEMLARKEFPVDVEGSRRLIDEHTQLKK--KVLKAPVEELDREGQRLLQcircsdgfsgrnc 267
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAelAAHQDRVEALNELAEKLID------------- 69

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1958666296  268 ipgSADFQSlvPKITSLLDKLHSTRQHLHQMWHVRKLKLDQ 308
Cdd:pfam00435   70 ---EGHYAS--EEIQERLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
1135-1235 2.72e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 38.85  E-value: 2.72e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  1135 FERSAKQALDWIQETgEYYLSTHTSTGETTEETQeLLKEYGEFRVPAKQTKEKVKLLIQLADSFVEKGHIHATEIRKWVT 1214
Cdd:smart00150    3 FLRDADELEAWLEEK-EQLLASEDLGKDLESVEA-LLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 1958666296  1215 TVDKHYRDFSLRMGKYRYTLE 1235
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 1099-1238 6.28e-03

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 40.12  E-value: 6.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296 1099 QQVKAILSELLQRENRVLHFWTLKKRRLDQCQQYVVFERSAKQALDWIQETGEYYLSthTSTGETTEETQELLKEYGEFR 1178
Cdd:cd00176     75 EEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALAS--EDLGKDLESVEELLKKHKELE 152

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958666296 1179 VPAKQTKEKVKLLIQLADSFVEKGHIHAT-EIRKWVTTVDKHYRDFSLRMGKYRYTLEKAL 1238
Cdd:cd00176    153 EELEAHEPRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 745-991 9.51e-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: 40.81  E-value: 9.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  745 QQLDDAQVQMEELFHERKIKLDIFLQLRIFEQYTIEVTAELDAWNEDLLRQMNDFNTEDLTLAEQRLQRHTERKLAmNNM 824
Cdd:TIGR02168  698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA-EEE 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  825 TFEVIQQGQDLHQYIMEVQASgIELICEKDVDLAAQVQELLEFLHEKQHELElNAEQTHKRLEQCLQLRHLQAEVKQvlg 904
Cdd:TIGR02168  777 LAEAEAEIEELEAQIEQLKEE-LKALREALDELRAELTLLNEEAANLRERLE-SLERRIAATERRLEDLEEQIEELS--- 851

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  905 wirngESMLNASLVNASSLSEAEQLQREHEQFQLAIESLFHATSLQKTHQSALQVQ-QKAEALLQAGHYDADAIRECAEK 983
Cdd:TIGR02168  852 -----EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEElRELESKRSELRRELEELREKLAQ 926


                   ....*...
gi 1958666296  984 VALHWQQL 991
Cdd:TIGR02168  927 LELRLEGL 934
 
Name Accession Description Interval E-value
PH1_Kalirin_Trio_like cd13240
Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; ...
 1461-1583 5.88e-68

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: 224.19  E-value: 5.88e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296 1461 MLEGFDENLDVQGELILQDAFQVWDPKSLIRKGRERHLFLFEISLVFSKEIKDSSGHTKYVYKNKLLTSELGVTEHVEGD 1540
Cdd:cd13240      1 LLEGCDEDLDSLGEVILQDSFQVWDPKQLIRKGRERHVFLFELCLVFSKEVKDSNGKSKYIYKSRLMTSEIGVTEHIEGD 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1958666296 1541 PCKFALWSGRTPSSDNKTVLKASNIETKQEWIKNIREVIQERI 1583
Cdd:cd13240     81 PCKFALWTGRVPTSDNKIVLKASSLEVKQTWVKKLREVIQERI 123
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 1284-1454 8.02e-44

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: 157.46  E-value: 8.02e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296 1284 FIMAELLQTEKAYVRDLHECLETYLWEMTSGVEEIPPgilNKEHIIFGNIQEIYDFHNnIFLKELEKY----EQLPEDVG 1359
Cdd:cd00160      3 EVIKELLQTERNYVRDLKLLVEVFLKPLDKELLPLSP---EEVELLFGNIEEIYEFHR-IFLKSLEERveewDKSGPRIG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296 1360 HCFVTWADKFQMYVTYCKNKPDSNQLILEHAG--TFFDEIQQRHGLAN---SISSYLIKPVQRVTKYQLLLKELLTCCEE 1434
Cdd:cd00160     79 DVFLKLAPFFKIYSEYCSNHPDALELLKKLKKfnKFFQEFLEKAESECgrlKLESLLLKPVQRLTKYPLLLKELLKHTPD 158

                          170       180
                   ....*....|....*....|...
gi 1958666296 1435 G---KGELKDGLEVMLSVPKKAN 1454
Cdd:cd00160    159 GhedREDLKKALEAIKEVASQVN 181
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 1285-1455 1.48e-41

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: 150.91  E-value: 1.48e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  1285 IMAELLQTEKAYVRDLHECLETYLWEMTSGVEEIPPgilNKEHIIFGNIQEIYDFHNnIFLKELEKY----EQLPEDVGH 1360
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELKLLSP---NELETLFGNIEEIYEFHR-DFLDELEERieewDDSVERIGD 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  1361 CFVTWADKFQMYVTYCKNKPDSNQLI--LEHAGTFFDEIQQRHGLAN----SISSYLIKPVQRVTKYQLLLKELLTCCEE 1434
Cdd:smart00325   77 VFLKLEEFFKIYSEYCSNHPDALELLkkLKKNPRFQKFLKEIESSPQcrrlTLESLLLKPVQRLTKYPLLLKELLKHTPE 156

                           170       180
                    ....*....|....*....|....
gi 1958666296  1435 G---KGELKDGLEVMLSVPKKAND 1455
Cdd:smart00325  157 DhedREDLKKALKAIKELANQVNE 180
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 1285-1454 7.11e-41

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: 148.99  E-value: 7.11e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296 1285 IMAELLQTEKAYVRDLHECLETYLWEMTSGVEEIPPGIlnkeHIIFGNIQEIYDFHNNIFLKELEKYEQLPEDVGHCFVT 1364
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEI----KTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIFLK 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296 1365 WADKFQMYVTYCKNKPDSNQLI------LEHAGTFFDEIQQR---HGLanSISSYLIKPVQRVTKYQLLLKELLTCCEEG 1435
Cdd:pfam00621   77 FAPGFKVYSTYCSNYPKALKLLkkllkkNPKFRAFLEELEANpecRGL--DLNSFLIKPVQRIPRYPLLLKELLKHTPPD 154

                          170       180
                   ....*....|....*....|..
gi 1958666296 1436 ---KGELKDGLEVMLSVPKKAN 1454
Cdd:pfam00621  155 hpdYEDLKKALEAIKEVAKQIN 176
PH2_Kalirin_Trio_p63RhoGEF cd13241
p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor ...
 1459-1594 3.60e-29

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: 114.28  E-value: 3.60e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296 1459 VSMLEGFDENLDVQGELILQDAFQVWDPKS-LIRKGRERHLFLFEISLVFSKEI--KDSSGHTKYVYKNKLLTSELGVTE 1535
Cdd:cd13241      1 VGRLQGFDGKITAQGKLLLQGTLLVSEPSAgLLQKGKERRVFLFEQIIIFSEILgkKTQFSNPGYIYKNHIKVNKMSLEE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296 1536 HVEGDPCKFALWSgRTPSSDNKT-VLKASNIETKQEWIKNIREVIQERIIHLKgALKEPI 1594
Cdd:cd13241     81 NVDGDPLRFALKS-RDPNNPSETfILQAASPEVRQEWVDTINQILDTQRDFLK-ALQSPI 138
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 39-177 2.30e-24

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: 100.84  E-value: 2.30e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296    39 LKEKVAFVSGGR--DKRGGPILTFPARS--NHDRIRQEDLRKLVTYLASVPS---EDVCKRGFTVIIDMRGSK-----WD 106
Cdd:smart00516    2 LELLKAYIPGGRgyDKDGRPVLIERAGRfdLKSVTLEELLRYLVYVLEKILQeekKTGGIEGFTVIFDLKGLSmsnpdLS 81

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958666296   107 LIKPLLKTLQEAFPAEIHVALIIKPDNFWQ---KQKTNFGSSKFIFETSMVS---VEGLTKLVDPSQLTEEFDGSLD 177
Cdd:smart00516   82 VLRKILKILQDHYPERLGKVYIINPPWFFRvlwKIIKPFLDEKTREKIRFVGndsKEELLEYIDKEQLPEELGGTLD 158
PH_puratrophin-1 cd13242
Puratrophin-1 pleckstrin homology (PH) domain; Puratrophin-1 (also called Purkinje cell ...
 1454-1587 8.19e-23

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: 95.82  E-value: 8.19e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296 1454 NDAMHVSMLEGFDENLDVQGELILQDAFQVWDPksliRKGRERHLFLFEISLVFSKEIKDSSGHTKYVYKNKLLTSELGV 1533
Cdd:cd13242      8 NDLLAMDSIRGCDVNLKEQGQLLRQDEFLVWQG----RKKCLRHVFLFEDLILFSKPKKTPGGKDVYIYKHSIKTSDIGL 83

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958666296 1534 TEHVEGDPCKFALWSGRTPSSDNkTVLKASNIETKQEWIKNIREVIQERIIHLK 1587
Cdd:cd13242     84 TENVGDSGLKFEIWFRRRKARDT-YILQATSPEIKQAWTSDIAKLLWKQAIRNR 136
PH_Dbs cd01227
DBL's big sister protein pleckstrin homology (PH) domain; Dbs (also called MCF2-transforming ...
 1464-1579 4.81e-20

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: 87.64  E-value: 4.81e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296 1464 GFDENLDVQGELILQDAFQVW------DPKSLIR-KGRERHLFLFEISLVFSKEIKDSSGHTKYVYKNKLLTSELGVTEH 1536
Cdd:cd01227      4 GYDGNLGDLGKLLMQGSFNVWtehkkgHTKKLARfKPMQRHIFLYEKAVLFCKKRGENGEAPSYSYKNSLNTTAVGLTEN 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1958666296 1537 VEGDPCKFALW-SGRTpssdNKTVLKASNIETKQEWIKNIREVI 1579
Cdd:cd01227     84 VKGDTKKFEIWlNGRE----EVFIIQAPTPEIKAAWVKAIRQVL 123
PH_Obscurin cd13239
Obscurin pleckstrin homology (PH) domain; Obscurin (also called Obscurin-RhoGEF; ...
 1461-1582 1.73e-16

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


Pssm-ID: 270059  Cd Length: 125  Bit Score: 77.20  E-value: 1.73e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296 1461 MLEGFDENLDVQGELILQDAFQVWDPKSLIR---KGRERHLFLFEISLVFSKEIKDSSGHTK-YVYKNKLLTSELGVTEH 1536
Cdd:cd13239      1 LIENYPAPLQALGEPIRQGHFTVWEEAPEVKtssRGHHRHVFLFKNCVVICKPKRDSRTDTVtYVFKNKMKLSDIDVKDT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958666296 1537 VEGDPCKFALWSGRTpSSDNKTVLKASNIETKQEWIKNIREvIQER 1582
Cdd:cd13239     81 VEGDDRSFGLWHEHR-GSVRKYTLQARSAIIKSSWLKDLRD-LQQR 124
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 891-1129 3.28e-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: 76.33  E-value: 3.28e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  891 QLRHLQAEVKQVLGWIRNGESMLnASLVNASSLSEAEQLQREHEQFQlaieslfhaTSLQKTHQSALQVQQKAEALLQAG 970
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELL-SSTDYGDDLESVEALLKKHEALE---------AELAAHEERVEALNELGEQLIEEG 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  971 HYDADAIRECAEKVALHWQQLMLKMEDRLKLVNASVAFYKTSEQVCSVlesleqeyrrdEDWCGGRDKLGPAAEMDHVIP 1050
Cdd:cd00176     71 HPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL-----------EQWLEEKEAALASEDLGKDLE 139

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958666296 1051 LLSKHLEQKEAFLKACTlarrNAEVFLKYIHRNNVSMpsVASHTRGPEQQVKAILSELLQRENRVLHFWTLKKRRLDQC 1129
Cdd:cd00176    140 SVEELLKKHKELEEELE----AHEPRLKSLNELAEEL--LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 44-175 4.67e-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: 74.29  E-value: 4.67e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296   44 AFVSGGRDKRGGPILTFPAR-SNHDRIRQEDLRKLVTYLASVPSEDVCKR--GFTVIIDMRGSKW------DLIKPLLKT 114
Cdd:cd00170     11 IGYLGGRDKEGRPVLVFRAGwDPPKLLDLEELLRYLVYLLEKALRELEEQveGFVVIIDLKGFSLsnlsdlSLLKKLLKI 90

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958666296  115 LQEAFPAEIHVALIIKPdNFWQKQKTNFGS--------SKFIFETSmvSVEGLTKLVDPSQLTEEFDGS 175
Cdd:cd00170     91 LQDHYPERLKKIYIVNA-PWIFSALWKIVKpflsektrKKIVFLGS--DLEELLEYIDPDQLPKELGGT 156
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 537-719 6.51e-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: 75.56  E-value: 6.51e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  537 QLCVFQQDVQQVLDWIENHGEAFLSkhTGVGKSLHRARALQKRHDDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIY 616
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  617 KAARHLEVRIQDFVRRVEQRKLLLDMSV---SFHTHTKELWTWMEDLQKEVLEDVCADSVDAVQELIKQFQQQQtATLDA 693
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALdlqQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELE-EELEA 157

                          170       180
                   ....*....|....*....|....*.
gi 1958666296  694 TLNVIKEGEDLIQQLRSAPPSLGEPT 719
Cdd:cd00176    158 HEPRLKSLNELAEELLEEGHPDADEE 183
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 311-536 3.66e-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: 64.39  E-value: 3.66e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  311 QLRLFEQDAEKMFDWISHnKELFLQShTEIGVSYQHALDLQTQHNHFAMNSMNAYVNINRIMSVASRLSEAGHYASQQIK 390
Cdd:cd00176      1 KLQQFLRDADELEAWLSE-KEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  391 QISTQLDQEWKSFAAALDERSTILAMSAVFHQKAEQFLSgVDAWC----KMCSEGGLPSEMQDLELAIHHHQSLYEQVTQ 466
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLeekeAALASEDLGKDLESVEELLKKHKELEEELEA 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  467 AytevSQDGKALLDVLQRPLSPGNSESLTATAnyskavhqvlDVVHEVLHHQRRLESIWQHRKVRLHQRL 536
Cdd:cd00176    158 H----EPRLKSLNELAEELLEEGHPDADEEIE----------EKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 190-410 4.63e-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: 64.39  E-value: 4.63e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  190 LEEFFNSAVHLLSRLEDLQEMLARKEFPVDVEGSRRLIDEHTQLKK--KVLKAPVEELDREGQRLLQcircsdgfsgrnc 267
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAelAAHEERVEALNELGEQLIE------------- 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  268 ipgsaDFQSLVPKITSLLDKLHSTRQHLHQMWHVRKLKLDQCFQLRLFEQDAEKMFDWIShNKELFLQSHtEIGVSYQHA 347
Cdd:cd00176     69 -----EGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLE-EKEAALASE-DLGKDLESV 141

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958666296  348 LDLQTQHNHFaMNSMNAY-VNINRIMSVASRLSEAGHYASQ-QIKQISTQLDQEWKSFAAALDER 410
Cdd:cd00176    142 EELLKKHKEL-EEELEAHePRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEER 205
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 54-181 6.81e-11

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: 61.96  E-value: 6.81e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296   54 GGPILTFPARS-NHDRIRQEDLRKLVTYLASVPSEDVCKRGFTVIIDMRGS------KWDLIKPLLKTLQEAFPAEIHVA 126
Cdd:pfam13716    1 GRPVLVFISKLlPSRPASLDDLDRLLFYLLKTLSEKLKGKPFVVVVDHTGVtsenfpSLSFLKKAYDLLPRAFKKNLKAV 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  127 LIIKPDNFWQKQ----KTNFGSSKFIFETSMVS-VEGLTKLVDPSQLTEEFDGSLDYNHE 181
Cdd:pfam13716   81 YVVHPSTFLRTFlktlGSLLGSKKLRKKVHYVSsLSELWEGIDREQLPTELPGVLSYDEE 140
SPEC smart00150
Spectrin repeats;
541-641 3.44e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 58.50  E-value: 3.44e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296   541 FQQDVQQVLDWIENHgEAFLSkHTGVGKSLHRARALQKRHDDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIYKAAR 620
Cdd:smart00150    3 FLRDADELEAWLEEK-EQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 1958666296   621 HLEVRIQDFVRRVEQRKLLLD 641
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
PH_PLEKHG1_G2_G3 cd13243
Pleckstrin homology domain-containing family G members 1, 2, and 3 pleckstrin homology (PH) ...
 1438-1581 6.99e-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: 58.90  E-value: 6.99e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296 1438 ELKDGLEVMLSVPKKAND-------AMHV----SMLEGFDE-NLDVQGELILQDAFQVWdpksliRKGRERHLFLFEISL 1505
Cdd:cd13243      3 VVEEALDTMTQVAWHINDmkrkhehAVRVqeiqSLLDGWEGpELTTYGDLVLEGTFRMA------GAKNERLLFLFDKML 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958666296 1506 VFSKEIKDSSghtkYVYKNKLLTSELGVTEHVEGDPCKFALWSGRTPssDNKTVLKASNIETKQEWIKNIREVIQE 1581
Cdd:cd13243     77 LITKKREDGI----LQYKTHIMCSNLMLSESIPKEPLSFQVLPFDNP--KLQYTLQAKNQEQKRLWTQEIKRLILE 146
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 783-1006 7.53e-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: 60.54  E-value: 7.53e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  783 AELDAWNEDLLRQMNDFNT-EDLTLAEQRLQRHTERKLAMnnmtfeviqqgQDLHQYIMEVQASGIELIcEKDVDLAAQV 861
Cdd:cd00176     10 DELEAWLSEKEELLSSTDYgDDLESVEALLKKHEALEAEL-----------AAHEERVEALNELGEQLI-EEGHPDAEEI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  862 QELLEFLHEKQHELELNAEQTHKRLEQCLQLRHLQAEVKQVLGWIRNGESMLnASLVNASSLSEAEQLQREHEQFQLAIE 941
Cdd:cd00176     78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEELE 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958666296  942 SlfHATSLQkthqsalQVQQKAEALLQAGHYDADA-IRECAEKVALHWQQLMLKMEDRLKLVNASV 1006
Cdd:cd00176    157 A--HEPRLK-------SLNELAEELLEEGHPDADEeIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC smart00150
Spectrin repeats;
893-1000 2.19e-09

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 56.18  E-value: 2.19e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296   893 RHLQAEVKQVLGWIRNGESMLnASLVNASSLSEAEQLQREHEQFQlaieslfhaTSLQKTHQSALQVQQKAEALLQAGHY 972
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLL-ASEDLGKDLESVEALLKKHEAFE---------AELEAHEERVEALNELGEQLIEEGHP 70

                            90       100
                    ....*....|....*....|....*...
gi 1958666296   973 DADAIRECAEKVALHWQQLMLKMEDRLK 1000
Cdd:smart00150   71 DAEEIEERLEELNERWEELKELAEERRQ 98
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 420-641 1.03e-08

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 57.46  E-value: 1.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  420 FHQKAEQFLSGVDAWCKMCSEGGLPSEMQDLELAIHHHQSLYEQVTQAYTEVSQ---DGKALLDvlqrpLSPGNSESLTA 496
Cdd:cd00176      5 FLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEAlneLGEQLIE-----EGHPDAEEIQE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  497 TanyskavhqvldvVHEVLHHQRRLESIWQHRKVRLHQRLQLCVFQQDVQQVLDWIENHGEAFLSkhTGVGKSLHRARAL 576
Cdd:cd00176     80 R-------------LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALAS--EDLGKDLESVEEL 144

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958666296  577 QKRHDDFEEVAQNTYTNADKLLEAAEQLAQTGECD-PEEIYKAARHLEVRIQDFVRRVEQRKLLLD 641
Cdd:cd00176    145 LKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDaDEEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC smart00150
Spectrin repeats;
315-414 4.53e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 52.33  E-value: 4.53e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296   315 FEQDAEKMFDWIShNKELFLQShTEIGVSYQHALDLQTQHNHFAMNSMNAYVNINRIMSVASRLSEAGHYASQQIKQIST 394
Cdd:smart00150    3 FLRDADELEAWLE-EKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|
gi 1958666296   395 QLDQEWKSFAAALDERSTIL 414
Cdd:smart00150   81 ELNERWEELKELAEERRQKL 100
CRAL_TRIO pfam00650
CRAL/TRIO domain;
44-174 8.21e-08

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 53.03  E-value: 8.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296   44 AFVSGGRDKRGGPILTF-PARSNHDRIRQEDLRKLVTYL---ASVPSEDVCKRGFTVIIDMRGSK--------WDLIKPL 111
Cdd:pfam00650    3 KVYLHGRDKEGRPVLYLrLGRHDPKKSSEEELVRFLVLVlerALLLMPEGQVEGLTVIIDLKGLSlsnmdwwsISLLKKI 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958666296  112 LKTLQEAFPAEIHVALIIKP----DNFWQ------KQKTNfgsSKFIFeTSMVSVEGLTKLVDPSQLTEEFDG 174
Cdd:pfam00650   83 IKILQDNYPERLGKILIVNApwifNTIWKlikpflDPKTR---EKIVF-LKNSNEEELEKYIPPEQLPKEYGG 151
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 1226-1446 2.42e-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: 56.05  E-value: 2.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296 1226 RMGKYRYTLEKaLGVNTEDNKDLELDiipASLSDREVKLRDANHEVNEEKRKSARKKEFIMAELLQTEKAYVRDLhECLE 1305
Cdd:COG5422    433 RLEQQARLHLK-LMGGLKRNSSLALD---KFDEEKNLWTLSVPKEVWESLPKQEIKRQEAIYEVIYTERDFVKDL-EYLR 507

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296 1306 TYlWEMTSGVEEIPPGILNKEHI--IFGNIQEIYDFhNNIFLKELEK---YEQLPEDVGHCFVTWADKFQMYVTYCKNKP 1380
Cdd:COG5422    508 DT-WIKPLEESNIIPENARRNFIkhVFANINEIYAV-NSKLLKALTNrqcLSPIVNGIADIFLDYVPKFEPFIKYGASQP 585

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958666296 1381 DSNQLILEHAGT------FFDEIQ-----QRHGlansISSYLIKPVQRVTKYQLLLKELLTCCEEGKGELKDGLEVM 1446
Cdd:COG5422    586 YAKYEFEREKSVnpnfarFDHEVErldesRKLE----LDGYLTKPTTRLARYPLLLEEVLKFTDPDNPDTEDIPKVI 658
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 311-410 4.61e-06

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 46.93  E-value: 4.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  311 QLRLFEQDAEKMFDWIShNKELFLQShTEIGVSYQHALDLQTQHNHFaMNSMNAY-VNINRIMSVASRLSEAGHYASQQI 389
Cdd:pfam00435    2 LLQQFFRDADDLESWIE-EKEALLSS-EDYGKDLESVQALLKKHKAL-EAELAAHqDRVEALNELAEKLIDEGHYASEEI 78

                           90       100
                   ....*....|....*....|.
gi 1958666296  390 KQISTQLDQEWKSFAAALDER 410
Cdd:pfam00435   79 QERLEELNERWEQLLELAAER 99
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 1487-1580 5.72e-06

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


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 46.77  E-value: 5.72e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  1487 KSLIRKGRERHLFLFEISLVFSKeikDSSGHTKYVYKNKLLTSELGVTEHVEGD----PCKFALWSGrtpssDNKT-VLK 1561
Cdd:smart00233   12 GGGKKSWKKRYFVLFNSTLLYYK---SKKDKKSYKPKGSIDLSGCTVREAPDPDsskkPHCFEIKTS-----DRKTlLLQ 83

                            90
                    ....*....|....*....
gi 1958666296  1562 ASNIETKQEWIKNIREVIQ 1580
Cdd:smart00233   84 AESEEEREKWVEALRKAIA 102
PH_unc89 cd13325
unc89 pleckstrin homology (PH) domain; unc89 is a myofibrillar protein. unc89-B the largest ...
 1473-1581 7.12e-06

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: 46.58  E-value: 7.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296 1473 GELILQDAFQVWDPKSlirKGRERHLFLFEISLVFSKEIKDSSGHTKYVYKNKLLTSELGVTEHvEGDPCKFALWSGRTP 1552
Cdd:cd13325      7 GRLLRHDWFTVTDGEG---KAKERYLFLFKSRILITKVRRISEDRSVFILKDIIRLPEVNVKQH-PDDERTFELQPKLPA 82

                           90       100
                   ....*....|....*....|....*....
gi 1958666296 1553 SSDNKTVLKASNIETKQEWIKNIREVIQE 1581
Cdd:cd13325     83 FGILPIDFKAHKDEIKDYWLNEIEEYAND 111
SPEC smart00150
Spectrin repeats;
191-307 8.70e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 46.17  E-value: 8.70e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296   191 EEFFNSAVHLLSRLEDLQEMLARKEFPVDVEGSRRLIDEHTQLKKKV--LKAPVEELDREGQRLLQcircsdgfsgrnci 268
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELeaHEERVEALNELGEQLIE-------------- 66

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 1958666296   269 pgSADFQSlvPKITSLLDKLHSTRQHLHQMWHVRKLKLD 307
Cdd:smart00150   67 --EGHPDA--EEIEERLEELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 890-991 1.51e-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: 45.39  E-value: 1.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  890 LQLRHLQAEVKQVLGWIRNGESMLnASLVNASSLSEAEQLQREHEQFQLAIESlfHATSLQkthqsalQVQQKAEALLQA 969
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALL-SSEDYGKDLESVQALLKKHKALEAELAA--HQDRVE-------ALNELAEKLIDE 70

                           90       100
                   ....*....|....*....|..
gi 1958666296  970 GHYDADAIRECAEKVALHWQQL 991
Cdd:pfam00435   71 GHYASEEIQERLEELNERWEQL 92
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 1486-1575 1.79e-05

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: 44.84  E-value: 1.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296 1486 PKSLIRKGRERHLFLFEISLVFSKEIKDSsghtKYVYKNKL-LTSELGVTEHVEGD-PCKFALWsgrtpSSDNKT-VLKA 1562
Cdd:cd00821      9 GGGGLKSWKKRWFVLFEGVLLYYKSKKDS----SYKPKGSIpLSGILEVEEVSPKErPHCFELV-----TPDGRTyYLQA 79

                           90
                   ....*....|...
gi 1958666296 1563 SNIETKQEWIKNI 1575
Cdd:cd00821     80 DSEEERQEWLKAL 92
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 1494-1579 2.67e-05

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 44.86  E-value: 2.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296 1494 RERHLFLFEISLVFSKeikDSSGHTKYVYKNKLLTSELGVTEHVEGD----PCKFALWSGrTPSSDNKTVLKASNIETKQ 1569
Cdd:pfam00169   19 KKRYFVLFDGSLLYYK---DDKSGKSKEPKGSISLSGCEVVEVVASDspkrKFCFELRTG-ERTGKRTYLLQAESEEERK 94

                           90
                   ....*....|
gi 1958666296 1570 EWIKNIREVI 1579
Cdd:pfam00169   95 DWIKAIQSAI 104
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 541-640 2.23e-04

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: 41.92  E-value: 2.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  541 FQQDVQQVLDWIENHgEAFLSKhTGVGKSLHRARALQKRHDDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIYKAAR 620
Cdd:pfam00435    6 FFRDADDLESWIEEK-EALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83

                           90       100
                   ....*....|....*....|
gi 1958666296  621 HLEVRIQDFVRRVEQRKLLL 640
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKL 103
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 190-308 1.62e-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: 39.61  E-value: 1.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  190 LEEFFNSAVHLLSRLEDLQEMLARKEFPVDVEGSRRLIDEHTQLKK--KVLKAPVEELDREGQRLLQcircsdgfsgrnc 267
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAelAAHQDRVEALNELAEKLID------------- 69

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1958666296  268 ipgSADFQSlvPKITSLLDKLHSTRQHLHQMWHVRKLKLDQ 308
Cdd:pfam00435   70 ---EGHYAS--EEIQERLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
1135-1235 2.72e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 38.85  E-value: 2.72e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  1135 FERSAKQALDWIQETgEYYLSTHTSTGETTEETQeLLKEYGEFRVPAKQTKEKVKLLIQLADSFVEKGHIHATEIRKWVT 1214
Cdd:smart00150    3 FLRDADELEAWLEEK-EQLLASEDLGKDLESVEA-LLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 1958666296  1215 TVDKHYRDFSLRMGKYRYTLE 1235
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
PH_Collybistin_ASEF cd01224
Collybistin/APC-stimulated guanine nucleotide exchange factor pleckstrin homology (PH) domain; ...
 1490-1582 4.58e-03

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: 39.17  E-value: 4.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296 1490 IRKGR--ERHLFLFEISLVFSKeiKDSSGHTKYVYKNKLLTSELGV------TEHVEGDPCKFALWSGRTpsSDNKT-VL 1560
Cdd:cd01224     38 ISAGRaqERTFFLFDHQLVYCK--KDLLRRKNYIYKGRIDTDNMEIedlpdgKDDESGVTVKNAWKIYNA--SKNKWyVL 113

                           90       100
                   ....*....|....*....|..
gi 1958666296 1561 KASNIETKQEWIKNIREviqER 1582
Cdd:cd01224    114 CAKSAEEKQRWLEAFAE---ER 132
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 1099-1238 6.28e-03

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 40.12  E-value: 6.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296 1099 QQVKAILSELLQRENRVLHFWTLKKRRLDQCQQYVVFERSAKQALDWIQETGEYYLSthTSTGETTEETQELLKEYGEFR 1178
Cdd:cd00176     75 EEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALAS--EDLGKDLESVEELLKKHKELE 152

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958666296 1179 VPAKQTKEKVKLLIQLADSFVEKGHIHAT-EIRKWVTTVDKHYRDFSLRMGKYRYTLEKAL 1238
Cdd:cd00176    153 EELEAHEPRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 745-991 9.51e-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: 40.81  E-value: 9.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  745 QQLDDAQVQMEELFHERKIKLDIFLQLRIFEQYTIEVTAELDAWNEDLLRQMNDFNTEDLTLAEQRLQRHTERKLAmNNM 824
Cdd:TIGR02168  698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA-EEE 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  825 TFEVIQQGQDLHQYIMEVQASgIELICEKDVDLAAQVQELLEFLHEKQHELElNAEQTHKRLEQCLQLRHLQAEVKQvlg 904
Cdd:TIGR02168  777 LAEAEAEIEELEAQIEQLKEE-LKALREALDELRAELTLLNEEAANLRERLE-SLERRIAATERRLEDLEEQIEELS--- 851

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666296  905 wirngESMLNASLVNASSLSEAEQLQREHEQFQLAIESLFHATSLQKTHQSALQVQ-QKAEALLQAGHYDADAIRECAEK 983
Cdd:TIGR02168  852 -----EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEElRELESKRSELRRELEELREKLAQ 926


                   ....*...
gi 1958666296  984 VALHWQQL 991
Cdd:TIGR02168  927 LELRLEGL 934
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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