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Conserved domains on  [gi|568995854|ref|XP_006522446|]
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kalirin isoform X36 [Mus musculus]

Protein Classification

RhoGEF family protein( domain architecture ID 11271280)

RhoGEF (rho guanine nucleotide exchange factor) family protein similar to RhoGEF and PH (pleckstrin homology) domain regions of Homo sapiens triple functional domain protein

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; ...
 1460-1582 4.31e-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: 224.57  E-value: 4.31e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854 1460 MLEGFDENLDVQGELILQDAFQVWDPKSLIRKGRERHLFLFEISLVFSKEIKDSSGHTKYVYKNKLLTSELGVTEHVEGD 1539
Cdd:cd13240     1 LLEGCDEDLDSLGEVILQDSFQVWDPKQLIRKGRERHVFLFELCLVFSKEVKDSNGKSKYIYKSRLMTSEIGVTEHIEGD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568995854 1540 PCKFALWSGRTPSSDNKTVLKASNIETKQEWIKNIREVIQERI 1582
Cdd:cd13240    81 PCKFALWTGRVPTSDNKIVLKASSLEVKQTWVKKLREVIQERI 123
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 1283-1453 7.34e-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: 157.84  E-value: 7.34e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854 1283 FIMAELLQTEKAYVRDLHECLETYLWEMTSGVEEIPPgilNKEHIIFGNIQEIYDFHNnIFLKELEKY----EQLPEDVG 1358
Cdd:cd00160     3 EVIKELLQTERNYVRDLKLLVEVFLKPLDKELLPLSP---EEVELLFGNIEEIYEFHR-IFLKSLEERveewDKSGPRIG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854 1359 HCFVTWADKFQMYVTYCKNKPDSNQLILEHAG--TFFDEIQQRHGLAN---SISSYLIKPVQRVTKYQLLLKELLTCCEE 1433
Cdd:cd00160    79 DVFLKLAPFFKIYSEYCSNHPDALELLKKLKKfnKFFQEFLEKAESECgrlKLESLLLKPVQRLTKYPLLLKELLKHTPD 158

                         170       180
                  ....*....|....*....|...
gi 568995854 1434 G---KGELKDGLEVMLSVPKKAN 1453
Cdd:cd00160   159 GhedREDLKKALEAIKEVASQVN 181
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 47-185 2.16e-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: 101.22  E-value: 2.16e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854     47 LKEKVAFVSGGR--DKRGGPILTFPARS--NHDRIRQEDLRKLVTYLASVPS---EDVCKRGFTVIIDMRGSK-----WD 114
Cdd:smart00516    2 LELLKAYIPGGRgyDKDGRPVLIERAGRfdLKSVTLEELLRYLVYVLEKILQeekKTGGIEGFTVIFDLKGLSmsnpdLS 81

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568995854    115 LIKPLLKTLQEAFPAEIHVALIIKPDNFWQ---KQKTNFGSSKFIFETSMVS---VEGLTKLVDPSQLTEEFDGSLD 185
Cdd:smart00516   82 VLRKILKILQDHYPERLGKVYIINPPWFFRvlwKIIKPFLDEKTREKIRFVGndsKEELLEYIDKEQLPEELGGTLD 158
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 899-1128 1.10e-17

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: 83.65  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  899 QLRHLQAEVKQVLGWIRNGESMLnASLVNASSLSEAEQLQREHEQFQLAIEKTHQSALQVQQKAEALLQAGHYDADAIRE 978
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELL-SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  979 CAEKVALHWQQLMLKMEDRLKLVNASVAFYKTSEQVCSVlesleqeyrrdEDWCGGRDKLGPAAEMDHVIPLLSKHLEQK 1058
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL-----------EQWLEEKEAALASEDLGKDLESVEELLKKH 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854 1059 EAFLKACTlarrNAEVFLKYIHRNNVSMpsVASHTRGPEQQVKAILSELLQRENRVLHFWTLKKRRLDQC 1128
Cdd:cd00176   149 KELEEELE----AHEPRLKSLNELAEEL--LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 545-727 4.12e-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: 75.95  E-value: 4.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  545 QLCVFQQDVQQVLDWIENHGEAFLSkhTGVGKSLHRARALQKRHDDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIY 624
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  625 KAARHLEVRIQDFVRRVEQRKLLLDMSV---SFHTHTKELWTWMEDLQKEVLEDVCADSVDAVQELIKQFQQQQtATLDA 701
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALdlqQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELE-EELEA 157

                         170       180
                  ....*....|....*....|....*.
gi 568995854  702 TLNVIKEGEDLIQQLRSAPPSLGEPT 727
Cdd:cd00176   158 HEPRLKSLNELAEELLEEGHPDADEE 183
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 791-1005 1.96e-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: 65.16  E-value: 1.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  791 AELDAWNEDLLRQMNDFNT-EDLTLAEQRLQRHTERKLAMnnmtfeviqqgQDLHQYIMEVQASGIELIcEKDLDLAAQV 869
Cdd:cd00176    10 DELEAWLSEKEELLSSTDYgDDLESVEALLKKHEALEAEL-----------AAHEERVEALNELGEQLI-EEGHPDAEEI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  870 QELLEFLHEKQHELELNAEQTHKRLEQCLQLRHLQAEVKQVLGWIRNGESMLnASLVNASSLSEAEQLQREHEQFQLAIE 949
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEELE 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568995854  950 KTHQSALQVQQKAEALLQAGHYDADA-IRECAEKVALHWQQLMLKMEDRLKLVNASV 1005
Cdd:cd00176   157 AHEPRLKSLNELAEELLEEGHPDADEeIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 319-544 2.26e-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: 65.16  E-value: 2.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  319 QLRLFEQDAEKMFDWISHnKELFLQShTEIGVSYQHALDLQTQHNHFAMNSMNAYVNINRIMSVASRLSEAGHYASQQIK 398
Cdd:cd00176     1 KLQQFLRDADELEAWLSE-KEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  399 QISTQLDQEWKSFAAALDERSTILAMSAVFHQKAEQFLSgVDAWC----KMCSEGGLPSEMQDLELAIHHHQSLYEQVTQ 474
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLeekeAALASEDLGKDLESVEELLKKHKELEEELEA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  475 AytevSQDGKALLDVLQRPLSPGNSESLTATAnyskavhqvlDVVHEVLHHQRRLESIWQHRKVRLHQRL 544
Cdd:cd00176   158 H----EPRLKSLNELAEELLEEGHPDADEEIE----------EKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 198-418 2.97e-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: 64.77  E-value: 2.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  198 LEEFFNSAVHLLSRLEDLQEMLARKEFPVDVEGSRRLIDEHTQLKK--KVLKAPVEELDREGQRLLQcircsdgfsgrnc 275
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAelAAHEERVEALNELGEQLIE------------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  276 ipgsaDFQSLVPKITSLLDKLHSTRQHLHQMWHVRKLKLDQCFQLRLFEQDAEKMFDWIShNKELFLQSHtEIGVSYQHA 355
Cdd:cd00176    69 -----EGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLE-EKEAALASE-DLGKDLESV 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568995854  356 LDLQTQHNHFaMNSMNAY-VNINRIMSVASRLSEAGHYASQ-QIKQISTQLDQEWKSFAAALDER 418
Cdd:cd00176   142 EELLKKHKEL-EEELEAHePRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEER 205
SPEC smart00150
Spectrin repeats;
1134-1234 2.05e-03

Spectrin repeats;


:

Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 39.24  E-value: 2.05e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854   1134 FERSAKQALDWIQETgEYYLSTHTSTGETTEETQeLLKEYGEFRVPAKQTKEKVKLLIQLADSFVEKGHIHATEIRKWVT 1213
Cdd:smart00150    3 FLRDADELEAWLEEK-EQLLASEDLGKDLESVEA-LLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 568995854   1214 TVDKHYRDFSLRMGKYRYSLE 1234
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
 
Name Accession Description Interval E-value
PH1_Kalirin_Trio_like cd13240
Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; ...
 1460-1582 4.31e-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: 224.57  E-value: 4.31e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854 1460 MLEGFDENLDVQGELILQDAFQVWDPKSLIRKGRERHLFLFEISLVFSKEIKDSSGHTKYVYKNKLLTSELGVTEHVEGD 1539
Cdd:cd13240     1 LLEGCDEDLDSLGEVILQDSFQVWDPKQLIRKGRERHVFLFELCLVFSKEVKDSNGKSKYIYKSRLMTSEIGVTEHIEGD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568995854 1540 PCKFALWSGRTPSSDNKTVLKASNIETKQEWIKNIREVIQERI 1582
Cdd:cd13240    81 PCKFALWTGRVPTSDNKIVLKASSLEVKQTWVKKLREVIQERI 123
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 1283-1453 7.34e-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: 157.84  E-value: 7.34e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854 1283 FIMAELLQTEKAYVRDLHECLETYLWEMTSGVEEIPPgilNKEHIIFGNIQEIYDFHNnIFLKELEKY----EQLPEDVG 1358
Cdd:cd00160     3 EVIKELLQTERNYVRDLKLLVEVFLKPLDKELLPLSP---EEVELLFGNIEEIYEFHR-IFLKSLEERveewDKSGPRIG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854 1359 HCFVTWADKFQMYVTYCKNKPDSNQLILEHAG--TFFDEIQQRHGLAN---SISSYLIKPVQRVTKYQLLLKELLTCCEE 1433
Cdd:cd00160    79 DVFLKLAPFFKIYSEYCSNHPDALELLKKLKKfnKFFQEFLEKAESECgrlKLESLLLKPVQRLTKYPLLLKELLKHTPD 158

                         170       180
                  ....*....|....*....|...
gi 568995854 1434 G---KGELKDGLEVMLSVPKKAN 1453
Cdd:cd00160   159 GhedREDLKKALEAIKEVASQVN 181
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 1284-1454 1.32e-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: 151.30  E-value: 1.32e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854   1284 IMAELLQTEKAYVRDLHECLETYLWEMTSGVEEIPPgilNKEHIIFGNIQEIYDFHNnIFLKELEKY----EQLPEDVGH 1359
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELKLLSP---NELETLFGNIEEIYEFHR-DFLDELEERieewDDSVERIGD 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854   1360 CFVTWADKFQMYVTYCKNKPDSNQLI--LEHAGTFFDEIQQRHGLAN----SISSYLIKPVQRVTKYQLLLKELLTCCEE 1433
Cdd:smart00325   77 VFLKLEEFFKIYSEYCSNHPDALELLkkLKKNPRFQKFLKEIESSPQcrrlTLESLLLKPVQRLTKYPLLLKELLKHTPE 156

                           170       180
                    ....*....|....*....|....
gi 568995854   1434 G---KGELKDGLEVMLSVPKKAND 1454
Cdd:smart00325  157 DhedREDLKKALKAIKELANQVNE 180
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 1284-1453 6.26e-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: 6.26e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  1284 IMAELLQTEKAYVRDLHECLETYLWEMTSGVEEIPPGIlnkeHIIFGNIQEIYDFHNNIFLKELEKYEQLPEDVGHCFVT 1363
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEI----KTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIFLK 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  1364 WADKFQMYVTYCKNKPDSNQLI------LEHAGTFFDEIQQR---HGLanSISSYLIKPVQRVTKYQLLLKELLTCCEEG 1434
Cdd:pfam00621   77 FAPGFKVYSTYCSNYPKALKLLkkllkkNPKFRAFLEELEANpecRGL--DLNSFLIKPVQRIPRYPLLLKELLKHTPPD 154

                          170       180
                   ....*....|....*....|..
gi 568995854  1435 ---KGELKDGLEVMLSVPKKAN 1453
Cdd:pfam00621  155 hpdYEDLKKALEAIKEVAKQIN 176
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 47-185 2.16e-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: 101.22  E-value: 2.16e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854     47 LKEKVAFVSGGR--DKRGGPILTFPARS--NHDRIRQEDLRKLVTYLASVPS---EDVCKRGFTVIIDMRGSK-----WD 114
Cdd:smart00516    2 LELLKAYIPGGRgyDKDGRPVLIERAGRfdLKSVTLEELLRYLVYVLEKILQeekKTGGIEGFTVIFDLKGLSmsnpdLS 81

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568995854    115 LIKPLLKTLQEAFPAEIHVALIIKPDNFWQ---KQKTNFGSSKFIFETSMVS---VEGLTKLVDPSQLTEEFDGSLD 185
Cdd:smart00516   82 VLRKILKILQDHYPERLGKVYIINPPWFFRvlwKIIKPFLDEKTREKIRFVGndsKEELLEYIDKEQLPEELGGTLD 158
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 899-1128 1.10e-17

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: 83.65  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  899 QLRHLQAEVKQVLGWIRNGESMLnASLVNASSLSEAEQLQREHEQFQLAIEKTHQSALQVQQKAEALLQAGHYDADAIRE 978
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELL-SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  979 CAEKVALHWQQLMLKMEDRLKLVNASVAFYKTSEQVCSVlesleqeyrrdEDWCGGRDKLGPAAEMDHVIPLLSKHLEQK 1058
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL-----------EQWLEEKEAALASEDLGKDLESVEELLKKH 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854 1059 EAFLKACTlarrNAEVFLKYIHRNNVSMpsVASHTRGPEQQVKAILSELLQRENRVLHFWTLKKRRLDQC 1128
Cdd:cd00176   149 KELEEELE----AHEPRLKSLNELAEEL--LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 545-727 4.12e-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: 75.95  E-value: 4.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  545 QLCVFQQDVQQVLDWIENHGEAFLSkhTGVGKSLHRARALQKRHDDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIY 624
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  625 KAARHLEVRIQDFVRRVEQRKLLLDMSV---SFHTHTKELWTWMEDLQKEVLEDVCADSVDAVQELIKQFQQQQtATLDA 701
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALdlqQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELE-EELEA 157

                         170       180
                  ....*....|....*....|....*.
gi 568995854  702 TLNVIKEGEDLIQQLRSAPPSLGEPT 727
Cdd:cd00176   158 HEPRLKSLNELAEELLEEGHPDADEE 183
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 52-183 4.28e-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: 4.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854   52 AFVSGGRDKRGGPILTFPAR-SNHDRIRQEDLRKLVTYLASVPSEDVCKR--GFTVIIDMRGSKW------DLIKPLLKT 122
Cdd:cd00170    11 IGYLGGRDKEGRPVLVFRAGwDPPKLLDLEELLRYLVYLLEKALRELEEQveGFVVIIDLKGFSLsnlsdlSLLKKLLKI 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568995854  123 LQEAFPAEIHVALIIKPdNFWQKQKTNFGS--------SKFIFETSmvSVEGLTKLVDPSQLTEEFDGS 183
Cdd:cd00170    91 LQDHYPERLKKIYIVNA-PWIFSALWKIVKpflsektrKKIVFLGS--DLEELLEYIDPDQLPKELGGT 156
SPEC smart00150
Spectrin repeats;
901-999 7.95e-12

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 63.12  E-value: 7.95e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854    901 RHLQAEVKQVLGWIRNGESMLnASLVNASSLSEAEQLQREHEQFQLAIEKTHQSALQVQQKAEALLQAGHYDADAIRECA 980
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLL-ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79

                            90
                    ....*....|....*....
gi 568995854    981 EKVALHWQQLMLKMEDRLK 999
Cdd:smart00150   80 EELNERWEELKELAEERRQ 98
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 791-1005 1.96e-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: 65.16  E-value: 1.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  791 AELDAWNEDLLRQMNDFNT-EDLTLAEQRLQRHTERKLAMnnmtfeviqqgQDLHQYIMEVQASGIELIcEKDLDLAAQV 869
Cdd:cd00176    10 DELEAWLSEKEELLSSTDYgDDLESVEALLKKHEALEAEL-----------AAHEERVEALNELGEQLI-EEGHPDAEEI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  870 QELLEFLHEKQHELELNAEQTHKRLEQCLQLRHLQAEVKQVLGWIRNGESMLnASLVNASSLSEAEQLQREHEQFQLAIE 949
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEELE 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568995854  950 KTHQSALQVQQKAEALLQAGHYDADA-IRECAEKVALHWQQLMLKMEDRLKLVNASV 1005
Cdd:cd00176   157 AHEPRLKSLNELAEELLEEGHPDADEeIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 319-544 2.26e-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: 65.16  E-value: 2.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  319 QLRLFEQDAEKMFDWISHnKELFLQShTEIGVSYQHALDLQTQHNHFAMNSMNAYVNINRIMSVASRLSEAGHYASQQIK 398
Cdd:cd00176     1 KLQQFLRDADELEAWLSE-KEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  399 QISTQLDQEWKSFAAALDERSTILAMSAVFHQKAEQFLSgVDAWC----KMCSEGGLPSEMQDLELAIHHHQSLYEQVTQ 474
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLeekeAALASEDLGKDLESVEELLKKHKELEEELEA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  475 AytevSQDGKALLDVLQRPLSPGNSESLTATAnyskavhqvlDVVHEVLHHQRRLESIWQHRKVRLHQRL 544
Cdd:cd00176   158 H----EPRLKSLNELAEELLEEGHPDADEEIE----------EKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 198-418 2.97e-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: 64.77  E-value: 2.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  198 LEEFFNSAVHLLSRLEDLQEMLARKEFPVDVEGSRRLIDEHTQLKK--KVLKAPVEELDREGQRLLQcircsdgfsgrnc 275
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAelAAHEERVEALNELGEQLIE------------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  276 ipgsaDFQSLVPKITSLLDKLHSTRQHLHQMWHVRKLKLDQCFQLRLFEQDAEKMFDWIShNKELFLQSHtEIGVSYQHA 355
Cdd:cd00176    69 -----EGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLE-EKEAALASE-DLGKDLESV 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568995854  356 LDLQTQHNHFaMNSMNAY-VNINRIMSVASRLSEAGHYASQ-QIKQISTQLDQEWKSFAAALDER 418
Cdd:cd00176   142 EELLKKHKEL-EEELEAHePRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEER 205
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 62-189 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 568995854    62 GGPILTFPARS-NHDRIRQEDLRKLVTYLASVPSEDVCKRGFTVIIDMRGS------KWDLIKPLLKTLQEAFPAEIHVA 134
Cdd:pfam13716    1 GRPVLVFISKLlPSRPASLDDLDRLLFYLLKTLSEKLKGKPFVVVVDHTGVtsenfpSLSFLKKAYDLLPRAFKKNLKAV 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854   135 LIIKPDNFWQKQ----KTNFGSSKFIFETSMVS-VEGLTKLVDPSQLTEEFDGSLDYNHE 189
Cdd:pfam13716   81 YVVHPSTFLRTFlktlGSLLGSKKLRKKVHYVSsLSELWEGIDREQLPTELPGVLSYDEE 140
SPEC smart00150
Spectrin repeats;
549-649 2.40e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 58.88  E-value: 2.40e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854    549 FQQDVQQVLDWIENHgEAFLSkHTGVGKSLHRARALQKRHDDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIYKAAR 628
Cdd:smart00150    3 FLRDADELEAWLEEK-EQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 568995854    629 HLEVRIQDFVRRVEQRKLLLD 649
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
323-422 3.41e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 52.72  E-value: 3.41e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854    323 FEQDAEKMFDWIShNKELFLQShTEIGVSYQHALDLQTQHNHFAMNSMNAYVNINRIMSVASRLSEAGHYASQQIKQIST 402
Cdd:smart00150    3 FLRDADELEAWLE-EKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|
gi 568995854    403 QLDQEWKSFAAALDERSTIL 422
Cdd:smart00150   81 ELNERWEELKELAEERRQKL 100
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 1225-1445 2.91e-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: 55.67  E-value: 2.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854 1225 RMGKYRYSLEKaLGVNTEDNKDLELDiipASLSDREVKLRDANHEINEEKRKSARKKEFIMAELLQTEKAYVRDLhECLE 1304
Cdd:COG5422   433 RLEQQARLHLK-LMGGLKRNSSLALD---KFDEEKNLWTLSVPKEVWESLPKQEIKRQEAIYEVIYTERDFVKDL-EYLR 507

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854 1305 TYlWEMTSGVEEIPPGILNKEHI--IFGNIQEIYDFhNNIFLKELEK---YEQLPEDVGHCFVTWADKFQMYVTYCKNKP 1379
Cdd:COG5422   508 DT-WIKPLEESNIIPENARRNFIkhVFANINEIYAV-NSKLLKALTNrqcLSPIVNGIADIFLDYVPKFEPFIKYGASQP 585

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568995854 1380 DSNQLILEHAGT------FFDEIQ-----QRHGlansISSYLIKPVQRVTKYQLLLKELLTCCEEGKGELKDGLEVM 1445
Cdd:COG5422   586 YAKYEFEREKSVnpnfarFDHEVErldesRKLE----LDGYLTKPTTRLARYPLLLEEVLKFTDPDNPDTEDIPKVI 658
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 898-990 1.44e-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: 48.47  E-value: 1.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854   898 LQLRHLQAEVKQVLGWIRNGESMLnASLVNASSLSEAEQLQREHEQFQLAIEkTHQSALQ-VQQKAEALLQAGHYDADAI 976
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALL-SSEDYGKDLESVQALLKKHKALEAELA-AHQDRVEaLNELAEKLIDEGHYASEEI 78

                           90
                   ....*....|....
gi 568995854   977 RECAEKVALHWQQL 990
Cdd:pfam00435   79 QERLEELNERWEQL 92
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 319-418 3.62e-06

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 47.31  E-value: 3.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854   319 QLRLFEQDAEKMFDWIShNKELFLQShTEIGVSYQHALDLQTQHNHFaMNSMNAY-VNINRIMSVASRLSEAGHYASQQI 397
Cdd:pfam00435    2 LLQQFFRDADDLESWIE-EKEALLSS-EDYGKDLESVQALLKKHKAL-EAELAAHqDRVEALNELAEKLIDEGHYASEEI 78

                           90       100
                   ....*....|....*....|.
gi 568995854   398 KQISTQLDQEWKSFAAALDER 418
Cdd:pfam00435   79 QERLEELNERWEQLLELAAER 99
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 1486-1579 5.19e-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: 5.19e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854   1486 KSLIRKGRERHLFLFEISLVFSKeikDSSGHTKYVYKNKLLTSELGVTEHVEGD----PCKFALWSGrtpssDNKT-VLK 1560
Cdd:smart00233   12 GGGKKSWKKRYFVLFNSTLLYYK---SKKDKKSYKPKGSIDLSGCTVREAPDPDsskkPHCFEIKTS-----DRKTlLLQ 83

                            90
                    ....*....|....*....
gi 568995854   1561 ASNIETKQEWIKNIREVIQ 1579
Cdd:smart00233   84 AESEEEREKWVEALRKAIA 102
SPEC smart00150
Spectrin repeats;
199-315 6.25e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 46.55  E-value: 6.25e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854    199 EEFFNSAVHLLSRLEDLQEMLARKEFPVDVEGSRRLIDEHTQLKKKV--LKAPVEELDREGQRLLQcircsdgfsgrnci 276
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELeaHEERVEALNELGEQLIE-------------- 66

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 568995854    277 pgSADFQSlvPKITSLLDKLHSTRQHLHQMWHVRKLKLD 315
Cdd:smart00150   67 --EGHPDA--EEIEERLEELNERWEELKELAEERRQKLE 101
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 1493-1578 2.38e-05

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 44.86  E-value: 2.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  1493 RERHLFLFEISLVFSKeikDSSGHTKYVYKNKLLTSELGVTEHVEGD----PCKFALWSGrTPSSDNKTVLKASNIETKQ 1568
Cdd:pfam00169   19 KKRYFVLFDGSLLYYK---DDKSGKSKEPKGSISLSGCEVVEVVASDspkrKFCFELRTG-ERTGKRTYLLQAESEEERK 94

                           90
                   ....*....|
gi 568995854  1569 EWIKNIREVI 1578
Cdd:pfam00169   95 DWIKAIQSAI 104
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 549-648 1.72e-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: 42.31  E-value: 1.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854   549 FQQDVQQVLDWIENHgEAFLSKhTGVGKSLHRARALQKRHDDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIYKAAR 628
Cdd:pfam00435    6 FFRDADDLESWIEEK-EALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83

                           90       100
                   ....*....|....*....|
gi 568995854   629 HLEVRIQDFVRRVEQRKLLL 648
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKL 103
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 198-316 1.32e-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: 39.99  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854   198 LEEFFNSAVHLLSRLEDLQEMLARKEFPVDVEGSRRLIDEHTQLKK--KVLKAPVEELDREGQRLLQcircsdgfsgrnc 275
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAelAAHQDRVEALNELAEKLID------------- 69

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 568995854   276 ipgSADFQSlvPKITSLLDKLHSTRQHLHQMWHVRKLKLDQ 316
Cdd:pfam00435   70 ---EGHYAS--EEIQERLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
1134-1234 2.05e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 39.24  E-value: 2.05e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854   1134 FERSAKQALDWIQETgEYYLSTHTSTGETTEETQeLLKEYGEFRVPAKQTKEKVKLLIQLADSFVEKGHIHATEIRKWVT 1213
Cdd:smart00150    3 FLRDADELEAWLEEK-EQLLASEDLGKDLESVEA-LLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 568995854   1214 TVDKHYRDFSLRMGKYRYSLE 1234
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 768-968 7.64e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 7.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  768 ERKIKLdIFLQLRIFEQYTIEVTAELDAWNEDLLRQMNDFNTEDLTLAEQRLQRHTERKlamnnmtfEVIQQGQDLHQYI 847
Cdd:COG1196   224 ELEAEL-LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL--------ELEEAQAEEYELL 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  848 MEVQA--SGIELICEK-------DLDLAAQVQElLEFLHEKQHELELNAEQTHKRLEQclQLRHLQAEVKQVLgwirngE 918
Cdd:COG1196   295 AELARleQDIARLEERrreleerLEELEEELAE-LEEELEELEEELEELEEELEEAEE--ELEEAEAELAEAE------E 365

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 568995854  919 SMLNASLVNASSLSEAEQLQREHEQFQLAIEKTHQSALQVQQKAEALLQA 968
Cdd:COG1196   366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
 
Name Accession Description Interval E-value
PH1_Kalirin_Trio_like cd13240
Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; ...
 1460-1582 4.31e-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: 224.57  E-value: 4.31e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854 1460 MLEGFDENLDVQGELILQDAFQVWDPKSLIRKGRERHLFLFEISLVFSKEIKDSSGHTKYVYKNKLLTSELGVTEHVEGD 1539
Cdd:cd13240     1 LLEGCDEDLDSLGEVILQDSFQVWDPKQLIRKGRERHVFLFELCLVFSKEVKDSNGKSKYIYKSRLMTSEIGVTEHIEGD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568995854 1540 PCKFALWSGRTPSSDNKTVLKASNIETKQEWIKNIREVIQERI 1582
Cdd:cd13240    81 PCKFALWTGRVPTSDNKIVLKASSLEVKQTWVKKLREVIQERI 123
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 1283-1453 7.34e-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: 157.84  E-value: 7.34e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854 1283 FIMAELLQTEKAYVRDLHECLETYLWEMTSGVEEIPPgilNKEHIIFGNIQEIYDFHNnIFLKELEKY----EQLPEDVG 1358
Cdd:cd00160     3 EVIKELLQTERNYVRDLKLLVEVFLKPLDKELLPLSP---EEVELLFGNIEEIYEFHR-IFLKSLEERveewDKSGPRIG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854 1359 HCFVTWADKFQMYVTYCKNKPDSNQLILEHAG--TFFDEIQQRHGLAN---SISSYLIKPVQRVTKYQLLLKELLTCCEE 1433
Cdd:cd00160    79 DVFLKLAPFFKIYSEYCSNHPDALELLKKLKKfnKFFQEFLEKAESECgrlKLESLLLKPVQRLTKYPLLLKELLKHTPD 158

                         170       180
                  ....*....|....*....|...
gi 568995854 1434 G---KGELKDGLEVMLSVPKKAN 1453
Cdd:cd00160   159 GhedREDLKKALEAIKEVASQVN 181
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 1284-1454 1.32e-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: 151.30  E-value: 1.32e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854   1284 IMAELLQTEKAYVRDLHECLETYLWEMTSGVEEIPPgilNKEHIIFGNIQEIYDFHNnIFLKELEKY----EQLPEDVGH 1359
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELKLLSP---NELETLFGNIEEIYEFHR-DFLDELEERieewDDSVERIGD 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854   1360 CFVTWADKFQMYVTYCKNKPDSNQLI--LEHAGTFFDEIQQRHGLAN----SISSYLIKPVQRVTKYQLLLKELLTCCEE 1433
Cdd:smart00325   77 VFLKLEEFFKIYSEYCSNHPDALELLkkLKKNPRFQKFLKEIESSPQcrrlTLESLLLKPVQRLTKYPLLLKELLKHTPE 156

                           170       180
                    ....*....|....*....|....
gi 568995854   1434 G---KGELKDGLEVMLSVPKKAND 1454
Cdd:smart00325  157 DhedREDLKKALKAIKELANQVNE 180
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 1284-1453 6.26e-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: 6.26e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  1284 IMAELLQTEKAYVRDLHECLETYLWEMTSGVEEIPPGIlnkeHIIFGNIQEIYDFHNNIFLKELEKYEQLPEDVGHCFVT 1363
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEI----KTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIFLK 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  1364 WADKFQMYVTYCKNKPDSNQLI------LEHAGTFFDEIQQR---HGLanSISSYLIKPVQRVTKYQLLLKELLTCCEEG 1434
Cdd:pfam00621   77 FAPGFKVYSTYCSNYPKALKLLkkllkkNPKFRAFLEELEANpecRGL--DLNSFLIKPVQRIPRYPLLLKELLKHTPPD 154

                          170       180
                   ....*....|....*....|..
gi 568995854  1435 ---KGELKDGLEVMLSVPKKAN 1453
Cdd:pfam00621  155 hpdYEDLKKALEAIKEVAKQIN 176
PH2_Kalirin_Trio_p63RhoGEF cd13241
p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor ...
 1458-1593 2.82e-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: 2.82e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854 1458 VSMLEGFDENLDVQGELILQDAFQVWDPKS-LIRKGRERHLFLFEISLVFSKEI--KDSSGHTKYVYKNKLLTSELGVTE 1534
Cdd:cd13241     1 VGRLQGFDGKITAQGKLLLQGTLLVSEPSAgLLQKGKERRVFLFEQIIIFSEILgkKTQFSNPGYIYKNHIKVNKMSLEE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854 1535 HVEGDPCKFALWSgRTPSSDNKT-VLKASNIETKQEWIKNIREVIQERIIHLKgALKEPI 1593
Cdd:cd13241    81 NVDGDPLRFALKS-RDPNNPSETfILQAASPEVRQEWVDTINQILDTQRDFLK-ALQSPI 138
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 47-185 2.16e-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: 101.22  E-value: 2.16e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854     47 LKEKVAFVSGGR--DKRGGPILTFPARS--NHDRIRQEDLRKLVTYLASVPS---EDVCKRGFTVIIDMRGSK-----WD 114
Cdd:smart00516    2 LELLKAYIPGGRgyDKDGRPVLIERAGRfdLKSVTLEELLRYLVYVLEKILQeekKTGGIEGFTVIFDLKGLSmsnpdLS 81

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568995854    115 LIKPLLKTLQEAFPAEIHVALIIKPDNFWQ---KQKTNFGSSKFIFETSMVS---VEGLTKLVDPSQLTEEFDGSLD 185
Cdd:smart00516   82 VLRKILKILQDHYPERLGKVYIINPPWFFRvlwKIIKPFLDEKTREKIRFVGndsKEELLEYIDKEQLPEELGGTLD 158
PH_puratrophin-1 cd13242
Puratrophin-1 pleckstrin homology (PH) domain; Puratrophin-1 (also called Purkinje cell ...
 1453-1586 6.55e-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: 96.21  E-value: 6.55e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854 1453 NDAMHVSMLEGFDENLDVQGELILQDAFQVWDPksliRKGRERHLFLFEISLVFSKEIKDSSGHTKYVYKNKLLTSELGV 1532
Cdd:cd13242     8 NDLLAMDSIRGCDVNLKEQGQLLRQDEFLVWQG----RKKCLRHVFLFEDLILFSKPKKTPGGKDVYIYKHSIKTSDIGL 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568995854 1533 TEHVEGDPCKFALWSGRTPSSDNkTVLKASNIETKQEWIKNIREVIQERIIHLK 1586
Cdd:cd13242    84 TENVGDSGLKFEIWFRRRKARDT-YILQATSPEIKQAWTSDIAKLLWKQAIRNR 136
PH_Dbs cd01227
DBL's big sister protein pleckstrin homology (PH) domain; Dbs (also called MCF2-transforming ...
 1463-1578 3.59e-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: 88.02  E-value: 3.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854 1463 GFDENLDVQGELILQDAFQVW------DPKSLIR-KGRERHLFLFEISLVFSKEIKDSSGHTKYVYKNKLLTSELGVTEH 1535
Cdd:cd01227     4 GYDGNLGDLGKLLMQGSFNVWtehkkgHTKKLARfKPMQRHIFLYEKAVLFCKKRGENGEAPSYSYKNSLNTTAVGLTEN 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568995854 1536 VEGDPCKFALW-SGRTpssdNKTVLKASNIETKQEWIKNIREVI 1578
Cdd:cd01227    84 VKGDTKKFEIWlNGRE----EVFIIQAPTPEIKAAWVKAIRQVL 123
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 899-1128 1.10e-17

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: 83.65  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  899 QLRHLQAEVKQVLGWIRNGESMLnASLVNASSLSEAEQLQREHEQFQLAIEKTHQSALQVQQKAEALLQAGHYDADAIRE 978
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELL-SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  979 CAEKVALHWQQLMLKMEDRLKLVNASVAFYKTSEQVCSVlesleqeyrrdEDWCGGRDKLGPAAEMDHVIPLLSKHLEQK 1058
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL-----------EQWLEEKEAALASEDLGKDLESVEELLKKH 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854 1059 EAFLKACTlarrNAEVFLKYIHRNNVSMpsVASHTRGPEQQVKAILSELLQRENRVLHFWTLKKRRLDQC 1128
Cdd:cd00176   149 KELEEELE----AHEPRLKSLNELAEEL--LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
PH_Obscurin cd13239
Obscurin pleckstrin homology (PH) domain; Obscurin (also called Obscurin-RhoGEF; ...
 1460-1581 1.37e-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: 77.58  E-value: 1.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854 1460 MLEGFDENLDVQGELILQDAFQVWDPKSLIR---KGRERHLFLFEISLVFSKEIKDSSGHTK-YVYKNKLLTSELGVTEH 1535
Cdd:cd13239     1 LIENYPAPLQALGEPIRQGHFTVWEEAPEVKtssRGHHRHVFLFKNCVVICKPKRDSRTDTVtYVFKNKMKLSDIDVKDT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568995854 1536 VEGDPCKFALWSGRTpSSDNKTVLKASNIETKQEWIKNIREvIQER 1581
Cdd:cd13239    81 VEGDDRSFGLWHEHR-GSVRKYTLQARSAIIKSSWLKDLRD-LQQR 124
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 545-727 4.12e-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: 75.95  E-value: 4.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  545 QLCVFQQDVQQVLDWIENHGEAFLSkhTGVGKSLHRARALQKRHDDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIY 624
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  625 KAARHLEVRIQDFVRRVEQRKLLLDMSV---SFHTHTKELWTWMEDLQKEVLEDVCADSVDAVQELIKQFQQQQtATLDA 701
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALdlqQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELE-EELEA 157

                         170       180
                  ....*....|....*....|....*.
gi 568995854  702 TLNVIKEGEDLIQQLRSAPPSLGEPT 727
Cdd:cd00176   158 HEPRLKSLNELAEELLEEGHPDADEE 183
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 52-183 4.28e-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: 4.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854   52 AFVSGGRDKRGGPILTFPAR-SNHDRIRQEDLRKLVTYLASVPSEDVCKR--GFTVIIDMRGSKW------DLIKPLLKT 122
Cdd:cd00170    11 IGYLGGRDKEGRPVLVFRAGwDPPKLLDLEELLRYLVYLLEKALRELEEQveGFVVIIDLKGFSLsnlsdlSLLKKLLKI 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568995854  123 LQEAFPAEIHVALIIKPdNFWQKQKTNFGS--------SKFIFETSmvSVEGLTKLVDPSQLTEEFDGS 183
Cdd:cd00170    91 LQDHYPERLKKIYIVNA-PWIFSALWKIVKpflsektrKKIVFLGS--DLEELLEYIDPDQLPKELGGT 156
SPEC smart00150
Spectrin repeats;
901-999 7.95e-12

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 63.12  E-value: 7.95e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854    901 RHLQAEVKQVLGWIRNGESMLnASLVNASSLSEAEQLQREHEQFQLAIEKTHQSALQVQQKAEALLQAGHYDADAIRECA 980
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLL-ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79

                            90
                    ....*....|....*....
gi 568995854    981 EKVALHWQQLMLKMEDRLK 999
Cdd:smart00150   80 EELNERWEELKELAEERRQ 98
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 791-1005 1.96e-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: 65.16  E-value: 1.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  791 AELDAWNEDLLRQMNDFNT-EDLTLAEQRLQRHTERKLAMnnmtfeviqqgQDLHQYIMEVQASGIELIcEKDLDLAAQV 869
Cdd:cd00176    10 DELEAWLSEKEELLSSTDYgDDLESVEALLKKHEALEAEL-----------AAHEERVEALNELGEQLI-EEGHPDAEEI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  870 QELLEFLHEKQHELELNAEQTHKRLEQCLQLRHLQAEVKQVLGWIRNGESMLnASLVNASSLSEAEQLQREHEQFQLAIE 949
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEELE 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568995854  950 KTHQSALQVQQKAEALLQAGHYDADA-IRECAEKVALHWQQLMLKMEDRLKLVNASV 1005
Cdd:cd00176   157 AHEPRLKSLNELAEELLEEGHPDADEeIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 319-544 2.26e-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: 65.16  E-value: 2.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  319 QLRLFEQDAEKMFDWISHnKELFLQShTEIGVSYQHALDLQTQHNHFAMNSMNAYVNINRIMSVASRLSEAGHYASQQIK 398
Cdd:cd00176     1 KLQQFLRDADELEAWLSE-KEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  399 QISTQLDQEWKSFAAALDERSTILAMSAVFHQKAEQFLSgVDAWC----KMCSEGGLPSEMQDLELAIHHHQSLYEQVTQ 474
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLeekeAALASEDLGKDLESVEELLKKHKELEEELEA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  475 AytevSQDGKALLDVLQRPLSPGNSESLTATAnyskavhqvlDVVHEVLHHQRRLESIWQHRKVRLHQRL 544
Cdd:cd00176   158 H----EPRLKSLNELAEELLEEGHPDADEEIE----------EKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 198-418 2.97e-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: 64.77  E-value: 2.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  198 LEEFFNSAVHLLSRLEDLQEMLARKEFPVDVEGSRRLIDEHTQLKK--KVLKAPVEELDREGQRLLQcircsdgfsgrnc 275
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAelAAHEERVEALNELGEQLIE------------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  276 ipgsaDFQSLVPKITSLLDKLHSTRQHLHQMWHVRKLKLDQCFQLRLFEQDAEKMFDWIShNKELFLQSHtEIGVSYQHA 355
Cdd:cd00176    69 -----EGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLE-EKEAALASE-DLGKDLESV 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568995854  356 LDLQTQHNHFaMNSMNAY-VNINRIMSVASRLSEAGHYASQ-QIKQISTQLDQEWKSFAAALDER 418
Cdd:cd00176   142 EELLKKHKEL-EEELEAHePRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEER 205
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 62-189 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 568995854    62 GGPILTFPARS-NHDRIRQEDLRKLVTYLASVPSEDVCKRGFTVIIDMRGS------KWDLIKPLLKTLQEAFPAEIHVA 134
Cdd:pfam13716    1 GRPVLVFISKLlPSRPASLDDLDRLLFYLLKTLSEKLKGKPFVVVVDHTGVtsenfpSLSFLKKAYDLLPRAFKKNLKAV 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854   135 LIIKPDNFWQKQ----KTNFGSSKFIFETSMVS-VEGLTKLVDPSQLTEEFDGSLDYNHE 189
Cdd:pfam13716   81 YVVHPSTFLRTFlktlGSLLGSKKLRKKVHYVSsLSELWEGIDREQLPTELPGVLSYDEE 140
SPEC smart00150
Spectrin repeats;
549-649 2.40e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 58.88  E-value: 2.40e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854    549 FQQDVQQVLDWIENHgEAFLSkHTGVGKSLHRARALQKRHDDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIYKAAR 628
Cdd:smart00150    3 FLRDADELEAWLEEK-EQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 568995854    629 HLEVRIQDFVRRVEQRKLLLD 649
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
PH_PLEKHG1_G2_G3 cd13243
Pleckstrin homology domain-containing family G members 1, 2, and 3 pleckstrin homology (PH) ...
 1437-1580 6.05e-10

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


Pssm-ID: 270063 [Multi-domain]  Cd Length: 147  Bit Score: 59.29  E-value: 6.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854 1437 ELKDGLEVMLSVPKKAND-------AMHV----SMLEGFDE-NLDVQGELILQDAFQVWdpksliRKGRERHLFLFEISL 1504
Cdd:cd13243     3 VVEEALDTMTQVAWHINDmkrkhehAVRVqeiqSLLDGWEGpELTTYGDLVLEGTFRMA------GAKNERLLFLFDKML 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568995854 1505 VFSKEIKDSSghtkYVYKNKLLTSELGVTEHVEGDPCKFALWSGRTPssDNKTVLKASNIETKQEWIKNIREVIQE 1580
Cdd:cd13243    77 LITKKREDGI----LQYKTHIMCSNLMLSESIPKEPLSFQVLPFDNP--KLQYTLQAKNQEQKRLWTQEIKRLILE 146
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 428-649 6.78e-09

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 57.84  E-value: 6.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  428 FHQKAEQFLSGVDAWCKMCSEGGLPSEMQDLELAIHHHQSLYEQVTQAYTEVSQ---DGKALLDvlqrpLSPGNSESLTA 504
Cdd:cd00176     5 FLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEAlneLGEQLIE-----EGHPDAEEIQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  505 TanyskavhqvldvVHEVLHHQRRLESIWQHRKVRLHQRLQLCVFQQDVQQVLDWIENHGEAFLSkhTGVGKSLHRARAL 584
Cdd:cd00176    80 R-------------LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALAS--EDLGKDLESVEEL 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568995854  585 QKRHDDFEEVAQNTYTNADKLLEAAEQLAQTGECD-PEEIYKAARHLEVRIQDFVRRVEQRKLLLD 649
Cdd:cd00176   145 LKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDaDEEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC smart00150
Spectrin repeats;
323-422 3.41e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 52.72  E-value: 3.41e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854    323 FEQDAEKMFDWIShNKELFLQShTEIGVSYQHALDLQTQHNHFAMNSMNAYVNINRIMSVASRLSEAGHYASQQIKQIST 402
Cdd:smart00150    3 FLRDADELEAWLE-EKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|
gi 568995854    403 QLDQEWKSFAAALDERSTIL 422
Cdd:smart00150   81 ELNERWEELKELAEERRQKL 100
CRAL_TRIO pfam00650
CRAL/TRIO domain;
52-182 7.97e-08

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 53.41  E-value: 7.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854    52 AFVSGGRDKRGGPILTF-PARSNHDRIRQEDLRKLVTYL---ASVPSEDVCKRGFTVIIDMRGSK--------WDLIKPL 119
Cdd:pfam00650    3 KVYLHGRDKEGRPVLYLrLGRHDPKKSSEEELVRFLVLVlerALLLMPEGQVEGLTVIIDLKGLSlsnmdwwsISLLKKI 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568995854   120 LKTLQEAFPAEIHVALIIKP----DNFWQ------KQKTNfgsSKFIFeTSMVSVEGLTKLVDPSQLTEEFDG 182
Cdd:pfam00650   83 IKILQDNYPERLGKILIVNApwifNTIWKlikpflDPKTR---EKIVF-LKNSNEEELEKYIPPEQLPKEYGG 151
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 1225-1445 2.91e-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: 55.67  E-value: 2.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854 1225 RMGKYRYSLEKaLGVNTEDNKDLELDiipASLSDREVKLRDANHEINEEKRKSARKKEFIMAELLQTEKAYVRDLhECLE 1304
Cdd:COG5422   433 RLEQQARLHLK-LMGGLKRNSSLALD---KFDEEKNLWTLSVPKEVWESLPKQEIKRQEAIYEVIYTERDFVKDL-EYLR 507

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854 1305 TYlWEMTSGVEEIPPGILNKEHI--IFGNIQEIYDFhNNIFLKELEK---YEQLPEDVGHCFVTWADKFQMYVTYCKNKP 1379
Cdd:COG5422   508 DT-WIKPLEESNIIPENARRNFIkhVFANINEIYAV-NSKLLKALTNrqcLSPIVNGIADIFLDYVPKFEPFIKYGASQP 585

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568995854 1380 DSNQLILEHAGT------FFDEIQ-----QRHGlansISSYLIKPVQRVTKYQLLLKELLTCCEEGKGELKDGLEVM 1445
Cdd:COG5422   586 YAKYEFEREKSVnpnfarFDHEVErldesRKLE----LDGYLTKPTTRLARYPLLLEEVLKFTDPDNPDTEDIPKVI 658
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 898-990 1.44e-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: 48.47  E-value: 1.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854   898 LQLRHLQAEVKQVLGWIRNGESMLnASLVNASSLSEAEQLQREHEQFQLAIEkTHQSALQ-VQQKAEALLQAGHYDADAI 976
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALL-SSEDYGKDLESVQALLKKHKALEAELA-AHQDRVEaLNELAEKLIDEGHYASEEI 78

                           90
                   ....*....|....
gi 568995854   977 RECAEKVALHWQQL 990
Cdd:pfam00435   79 QERLEELNERWEQL 92
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 319-418 3.62e-06

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 47.31  E-value: 3.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854   319 QLRLFEQDAEKMFDWIShNKELFLQShTEIGVSYQHALDLQTQHNHFaMNSMNAY-VNINRIMSVASRLSEAGHYASQQI 397
Cdd:pfam00435    2 LLQQFFRDADDLESWIE-EKEALLSS-EDYGKDLESVQALLKKHKAL-EAELAAHqDRVEALNELAEKLIDEGHYASEEI 78

                           90       100
                   ....*....|....*....|.
gi 568995854   398 KQISTQLDQEWKSFAAALDER 418
Cdd:pfam00435   79 QERLEELNERWEQLLELAAER 99
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 1486-1579 5.19e-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: 5.19e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854   1486 KSLIRKGRERHLFLFEISLVFSKeikDSSGHTKYVYKNKLLTSELGVTEHVEGD----PCKFALWSGrtpssDNKT-VLK 1560
Cdd:smart00233   12 GGGKKSWKKRYFVLFNSTLLYYK---SKKDKKSYKPKGSIDLSGCTVREAPDPDsskkPHCFEIKTS-----DRKTlLLQ 83

                            90
                    ....*....|....*....
gi 568995854   1561 ASNIETKQEWIKNIREVIQ 1579
Cdd:smart00233   84 AESEEEREKWVEALRKAIA 102
SPEC smart00150
Spectrin repeats;
199-315 6.25e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 46.55  E-value: 6.25e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854    199 EEFFNSAVHLLSRLEDLQEMLARKEFPVDVEGSRRLIDEHTQLKKKV--LKAPVEELDREGQRLLQcircsdgfsgrnci 276
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELeaHEERVEALNELGEQLIE-------------- 66

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 568995854    277 pgSADFQSlvPKITSLLDKLHSTRQHLHQMWHVRKLKLD 315
Cdd:smart00150   67 --EGHPDA--EEIEERLEELNERWEELKELAEERRQKLE 101
PH_unc89 cd13325
unc89 pleckstrin homology (PH) domain; unc89 is a myofibrillar protein. unc89-B the largest ...
 1472-1580 6.39e-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: 46.96  E-value: 6.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854 1472 GELILQDAFQVWDPKSlirKGRERHLFLFEISLVFSKEIKDSSGHTKYVYKNKLLTSELGVTEHvEGDPCKFALWSGRTP 1551
Cdd:cd13325     7 GRLLRHDWFTVTDGEG---KAKERYLFLFKSRILITKVRRISEDRSVFILKDIIRLPEVNVKQH-PDDERTFELQPKLPA 82

                          90       100
                  ....*....|....*....|....*....
gi 568995854 1552 SSDNKTVLKASNIETKQEWIKNIREVIQE 1580
Cdd:cd13325    83 FGILPIDFKAHKDEIKDYWLNEIEEYAND 111
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 1485-1574 1.52e-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: 45.23  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854 1485 PKSLIRKGRERHLFLFEISLVFSKEIKDSsghtKYVYKNKL-LTSELGVTEHVEGD-PCKFALWsgrtpSSDNKT-VLKA 1561
Cdd:cd00821     9 GGGGLKSWKKRWFVLFEGVLLYYKSKKDS----SYKPKGSIpLSGILEVEEVSPKErPHCFELV-----TPDGRTyYLQA 79

                          90
                  ....*....|...
gi 568995854 1562 SNIETKQEWIKNI 1574
Cdd:cd00821    80 DSEEERQEWLKAL 92
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 1493-1578 2.38e-05

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 44.86  E-value: 2.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  1493 RERHLFLFEISLVFSKeikDSSGHTKYVYKNKLLTSELGVTEHVEGD----PCKFALWSGrTPSSDNKTVLKASNIETKQ 1568
Cdd:pfam00169   19 KKRYFVLFDGSLLYYK---DDKSGKSKEPKGSISLSGCEVVEVVASDspkrKFCFELRTG-ERTGKRTYLLQAESEEERK 94

                           90
                   ....*....|
gi 568995854  1569 EWIKNIREVI 1578
Cdd:pfam00169   95 DWIKAIQSAI 104
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 549-648 1.72e-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: 42.31  E-value: 1.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854   549 FQQDVQQVLDWIENHgEAFLSKhTGVGKSLHRARALQKRHDDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIYKAAR 628
Cdd:pfam00435    6 FFRDADDLESWIEEK-EALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83

                           90       100
                   ....*....|....*....|
gi 568995854   629 HLEVRIQDFVRRVEQRKLLL 648
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKL 103
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 198-316 1.32e-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: 39.99  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854   198 LEEFFNSAVHLLSRLEDLQEMLARKEFPVDVEGSRRLIDEHTQLKK--KVLKAPVEELDREGQRLLQcircsdgfsgrnc 275
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAelAAHQDRVEALNELAEKLID------------- 69

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 568995854   276 ipgSADFQSlvPKITSLLDKLHSTRQHLHQMWHVRKLKLDQ 316
Cdd:pfam00435   70 ---EGHYAS--EEIQERLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
1134-1234 2.05e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 39.24  E-value: 2.05e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854   1134 FERSAKQALDWIQETgEYYLSTHTSTGETTEETQeLLKEYGEFRVPAKQTKEKVKLLIQLADSFVEKGHIHATEIRKWVT 1213
Cdd:smart00150    3 FLRDADELEAWLEEK-EQLLASEDLGKDLESVEA-LLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 568995854   1214 TVDKHYRDFSLRMGKYRYSLE 1234
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
PH_Collybistin_ASEF cd01224
Collybistin/APC-stimulated guanine nucleotide exchange factor pleckstrin homology (PH) domain; ...
 1489-1581 3.82e-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: 39.55  E-value: 3.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854 1489 IRKGR--ERHLFLFEISLVFSKeiKDSSGHTKYVYKNKLLTSELGV------TEHVEGDPCKFALWSGRTpsSDNKT-VL 1559
Cdd:cd01224    38 ISAGRaqERTFFLFDHQLVYCK--KDLLRRKNYIYKGRIDTDNMEIedlpdgKDDESGVTVKNAWKIYNA--SKNKWyVL 113

                          90       100
                  ....*....|....*....|..
gi 568995854 1560 KASNIETKQEWIKNIREviqER 1581
Cdd:cd01224   114 CAKSAEEKQRWLEAFAE---ER 132
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 768-968 7.64e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 7.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  768 ERKIKLdIFLQLRIFEQYTIEVTAELDAWNEDLLRQMNDFNTEDLTLAEQRLQRHTERKlamnnmtfEVIQQGQDLHQYI 847
Cdd:COG1196   224 ELEAEL-LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL--------ELEEAQAEEYELL 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995854  848 MEVQA--SGIELICEK-------DLDLAAQVQElLEFLHEKQHELELNAEQTHKRLEQclQLRHLQAEVKQVLgwirngE 918
Cdd:COG1196   295 AELARleQDIARLEERrreleerLEELEEELAE-LEEELEELEEELEELEEELEEAEE--ELEEAEAELAEAE------E 365

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 568995854  919 SMLNASLVNASSLSEAEQLQREHEQFQLAIEKTHQSALQVQQKAEALLQA 968
Cdd:COG1196   366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
 
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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