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Conserved domains on  [gi|24654948|ref|NP_728560|]
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trio, isoform C [Drosophila melanogaster]

Protein Classification

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; ...
 1462-1584 4.87e-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: 224.96  E-value: 4.87e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 1462 LLENCDVSVDKLGEVVLQDAFQAWDTKQIIRKGRERRVFLFELYLLFAKEVKESNV-VKYQFKSKLMTTDMGITEHIEGD 1540
Cdd:cd13240    1 LLEGCDEDLDSLGEVILQDSFQVWDPKQLIRKGRERHVFLFELCLVFSKEVKDSNGkSKYIYKSRLMTSEIGVTEHIEGD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 24654948 1541 ETKFAVWTGRSPmLSDCRIVLKATSLETKQIWVKKLREVMQETC 1584
Cdd:cd13240   81 PCKFALWTGRVP-TSDNKIVLKASSLEVKQTWVKKLREVIQERI 123
PH2_Kalirin_Trio_p63RhoGEF cd13241
p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor ...
 2130-2260 3.26e-62

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: 209.04  E-value: 3.26e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 2130 LQDFDGEITAQGSLLMQGPMNCVVDAA---QKHRELQVFLFQQIIIFADIEKTKNQYASPIFKYRSHIQLNHMQMKELGD 2206
Cdd:cd13241    4 LQGFDGKITAQGKLLLQGTLLVSEPSAgllQKGKERRVFLFEQIIIFSEILGKKTQFSNPGYIYKNHIKVNKMSLEENVD 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24654948 2207 ---CRFQIRSTDPKIPEMTIICQAASQENYAGWRDMLNKILQQQNDLIFMLSNPLST 2260
Cdd:cd13241   84 gdpLRFALKSRDPNNPSETFILQAASPEVRQEWVDTINQILDTQRDFLKALQSPIAY 140
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 1287-1455 2.65e-43

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


:

Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 156.31  E-value: 2.65e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948   1287 IMAELMQTERAYVNDLATCIKCFLEEFRAGKSVPSALIgqeDVIFGNIKEIHHFHQKIFLRELEKYETMPEDVGHCFVTW 1366
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEI---KTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIFLKF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948   1367 ASKFDMYVHYCKNKPTSNNLLVQ------HGGSFFEELQRRLEVD-HPLPAYLIKPVQRITKYQLLLKDLLSCCEESHGE 1439
Cdd:pfam00621   78 APGFKVYSTYCSNYPKALKLLKKllkknpKFRAFLEELEANPECRgLDLNSFLIKPVQRIPRYPLLLKELLKHTPPDHPD 157

                          170
                   ....*....|....*....
gi 24654948   1440 ---IKEGLEVMLNVPKKAN 1455
Cdd:pfam00621  158 yedLKKALEAIKEVAKQIN 176
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 1945-2121 2.62e-40

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


:

Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 147.83  E-value: 2.62e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948   1945 VFAELMSTEEAYVQDLHEIVNGYMTEINNtnsdiPMPEDLKggKMKLVFNNIKDIYEWHRDFFLRALRNCQKSPADLGPL 2024
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSK-----PLSESEE--EIKTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDI 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948   2025 IKRSATKFALYYTYCSNKPLSEYIVS-------AHYQYFDSIR-QKLGHRLDLSNLIIKPVQRITKYELLIKEIIKATEG 2096
Cdd:pfam00621   74 FLKFAPGFKVYSTYCSNYPKALKLLKkllkknpKFRAFLEELEaNPECRGLDLNSFLIKPVQRIPRYPLLLKELLKHTPP 153

                          170       180
                   ....*....|....*....|....*
gi 24654948   2097 AGlyKEVPMLQEAYQQMKVVVKTVN 2121
Cdd:pfam00621  154 DH--PDYEDLKKALEAIKEVAKQIN 176
SH3_Kalirin_1 cd11852
First Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or ...
 1643-1707 1.68e-25

First Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or TRAD, is a large neuronal dual Rho guanine nucleotide exchange factor (RhoGEF) that activates Rac1, RhoA, and RhoG using two RhoGEF domains. Kalirin exists in many isoforms generated by alternative splicing and the use of multiple promoters; the major isoforms are kalirin-7, -9, and -12, which differ at their C-terminal ends. Kalirin-12, the longest isoform, contains an N-terminal Sec14p domain, spectrin-like repeats, two RhoGEF domains, two SH3 domains, as well as Ig, FNIII, and kinase domains at the C-terminal end. Kalirin-7 contains only a single RhoGEF domain and does not contain an SH3 domain. Kalirin, through its many isoforms, interacts with many different proteins and is able to localize to different locations within the cell. It influences neurite initiation, axon growth, dendritic morphogenesis, vesicle trafficking, neuronal maintenance, and neurodegeneration. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


:

Pssm-ID: 212786  Cd Length: 62  Bit Score: 101.32  E-value: 1.68e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24654948 1643 EATWVVADYIATSgSNELSVSKGQQVEIVEPPTaGEPDFCLVRLNPQhDDAAVQEGLVPVSVLKP 1707
Cdd:cd11852    1 ELTVVIEDFEATS-SQELTVSKGQTVEVLERPS-SRPDWCLVRTLEQ-DNSPPQEGLVPSSILCI 62
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 13-152 2.14e-20

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: 90.05  E-value: 2.14e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948      13 LQERVVFLTGGR--DRRGGPLLCFPA--TPRRDRLKPEDLRRLLSYLISIPSDAAK---NLGFTVIIDMRG---NGNCST 82
Cdd:smart00516    2 LELLKAYIPGGRgyDKDGRPVLIERAgrFDLKSVTLEELLRYLVYVLEKILQEEKKtggIEGFTVIFDLKGlsmSNPDLS 81

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24654948      83 NVKTILKVLQEHFSANIHNVVIIKPDNFWQ---KQRASISSHKYKFETTTVS---IESLNKIVESHQLTGDFEGQQ 152
Cdd:smart00516   82 VLRKILKILQDHYPERLGKVYIINPPWFFRvlwKIIKPFLDEKTREKIRFVGndsKEELLEYIDKEQLPEELGGTL 157
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 782-997 1.05e-16

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 80.95  E-value: 1.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  782 RLRYFERDARLLSVQMEMWSEELQHADLSRDYQKAEQLIRMHN---ESVTEIQNATYEVVQQGQDLLQlfenagfismad 858
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEaleAELAAHEERVEALNELGEQLIE------------ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  859 ATHTAQARIEYLLDFLREREIDLEEMSEAKRAKLEQAVQLCQFQNDANQVISWIRNGEAMLvASFVTPNSLQEAEQLRKG 938
Cdd:cd00176   69 EGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAAL-ASEDLGKDLESVEELLKK 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  939 HEQFQIAIEKTHTSAVQVKYRADALINANHYDPL-SIDEISDDVTKKWQQLVTYAEERHK 997
Cdd:cd00176  148 HKELEEELEAHEPRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEERQK 207
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 897-1119 1.21e-15

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 77.87  E-value: 1.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  897 QLCQFQNDANQVISWIRNGEAMLvASFVTPNSLQEAEQLRKGHEQFQIAIEKTHTSAVQVKYRADALINANHYDPLSIDE 976
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELL-SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  977 ISDDVTKKWQQLVTYAEERHKLVTASIN---FYKTAEQVCSVLDSLEREYKREDDwcdgGGGSDKAQAivqLISKHQEQK 1053
Cdd:cd00176   80 RLEELNQRWEELRELAEERRQRLEEALDlqqFFRDADDLEQWLEEKEAALASEDL----GKDLESVEE---LLKKHKELE 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24654948 1054 EAFLKACTL---ARRTAETFLKYANRSQqcyqykgncEGHVKSKLDKLLTQENQVLDYWTLRKKSLDQC 1119
Cdd:cd00176  153 EELEAHEPRlksLNELAEELLEEGHPDA---------DEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC smart00150
Spectrin repeats;
1125-1226 7.29e-13

Spectrin repeats;


:

Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 66.58  E-value: 7.29e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    1125 FERSAKQAIEWIHNTgEAYLSSRSnlVGISKEETEGLLKEHNEFRSTAKETRERVKLLIQLADSLVEKGHAHASDIKQWV 1204
Cdd:smart00150    3 FLRDADELEAWLEEK-EQLLASED--LGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79

                            90       100
                    ....*....|....*....|..
gi 24654948    1205 ASVDQRYKDFSNRMDSYCEQLE 1226
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 563-778 5.55e-11

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 64.39  E-value: 5.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  563 LRLFQEDVKQVLDWLKNHGEVFlrKNTGIGRNFHKARVYQTSHDNFENVAQNTYSNAQKLLAAADELARSGEADPNEIYS 642
Cdd:cd00176    2 LQQFLRDADELEAWLSEKEELL--SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  643 VARELELQVGSFAERVEQRRRRLDMAVI---FYTHEKDVTAWIDKLRTDVSTDETRLSQENLEGIERILQQYQRD--QQE 717
Cdd:cd00176   80 RLEELNQRWEELRELAEERRQRLEEALDlqqFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEEleAHE 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24654948  718 SSVNVCLttiSQGEALLQEMRSleyadntGSIAALEATLEKLNKQKVELEELWSARKFRAD 778
Cdd:cd00176  160 PRLKSLN---ELAEELLEEGHP-------DADEEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 314-468 1.67e-10

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 62.85  E-value: 1.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  314 QWRLFEQDCEKMFDWILHNRDVFQMSyvEIGHNYSVAKSLQDEHQKFAVASMNVSVNIDRILAVAARLIESQHYAAQHIK 393
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSST--DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24654948  394 TLAQRLDRTWKDFAAGLDERTAVLQLSVLFHHKAEQyCNSVASWAAACQ---ASQPLPSDIQSLETAIRTHQSLYEAM 468
Cdd:cd00176   79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEaalASEDLGKDLESVEELLKKHKELEEEL 155
 
Name Accession Description Interval E-value
PH1_Kalirin_Trio_like cd13240
Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; ...
 1462-1584 4.87e-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: 224.96  E-value: 4.87e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 1462 LLENCDVSVDKLGEVVLQDAFQAWDTKQIIRKGRERRVFLFELYLLFAKEVKESNV-VKYQFKSKLMTTDMGITEHIEGD 1540
Cdd:cd13240    1 LLEGCDEDLDSLGEVILQDSFQVWDPKQLIRKGRERHVFLFELCLVFSKEVKDSNGkSKYIYKSRLMTSEIGVTEHIEGD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 24654948 1541 ETKFAVWTGRSPmLSDCRIVLKATSLETKQIWVKKLREVMQETC 1584
Cdd:cd13240   81 PCKFALWTGRVP-TSDNKIVLKASSLEVKQTWVKKLREVIQERI 123
PH2_Kalirin_Trio_p63RhoGEF cd13241
p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor ...
 2130-2260 3.26e-62

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: 209.04  E-value: 3.26e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 2130 LQDFDGEITAQGSLLMQGPMNCVVDAA---QKHRELQVFLFQQIIIFADIEKTKNQYASPIFKYRSHIQLNHMQMKELGD 2206
Cdd:cd13241    4 LQGFDGKITAQGKLLLQGTLLVSEPSAgllQKGKERRVFLFEQIIIFSEILGKKTQFSNPGYIYKNHIKVNKMSLEENVD 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24654948 2207 ---CRFQIRSTDPKIPEMTIICQAASQENYAGWRDMLNKILQQQNDLIFMLSNPLST 2260
Cdd:cd13241   84 gdpLRFALKSRDPNNPSETFILQAASPEVRQEWVDTINQILDTQRDFLKALQSPIAY 140
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 1287-1455 2.65e-43

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 156.31  E-value: 2.65e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948   1287 IMAELMQTERAYVNDLATCIKCFLEEFRAGKSVPSALIgqeDVIFGNIKEIHHFHQKIFLRELEKYETMPEDVGHCFVTW 1366
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEI---KTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIFLKF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948   1367 ASKFDMYVHYCKNKPTSNNLLVQ------HGGSFFEELQRRLEVD-HPLPAYLIKPVQRITKYQLLLKDLLSCCEESHGE 1439
Cdd:pfam00621   78 APGFKVYSTYCSNYPKALKLLKKllkknpKFRAFLEELEANPECRgLDLNSFLIKPVQRIPRYPLLLKELLKHTPPDHPD 157

                          170
                   ....*....|....*....
gi 24654948   1440 ---IKEGLEVMLNVPKKAN 1455
Cdd:pfam00621  158 yedLKKALEAIKEVAKQIN 176
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 1286-1455 9.52e-43

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 155.15  E-value: 9.52e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 1286 FIMAELMQTERAYVNDLATCIKCFLEEFRagKSVPSALIGQEDVIFGNIKEIHHFHqKIFLRELEKY----ETMPEDVGH 1361
Cdd:cd00160    3 EVIKELLQTERNYVRDLKLLVEVFLKPLD--KELLPLSPEEVELLFGNIEEIYEFH-RIFLKSLEERveewDKSGPRIGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 1362 CFVTWASKFDMYVHYCKNKPTSNNLLVQH--GGSFFEELQRRLE---VDHPLPAYLIKPVQRITKYQLLLKDLLSCCEES 1436
Cdd:cd00160   80 VFLKLAPFFKIYSEYCSNHPDALELLKKLkkFNKFFQEFLEKAEsecGRLKLESLLLKPVQRLTKYPLLLKELLKHTPDG 159

                        170       180
                 ....*....|....*....|..
gi 24654948 1437 HGE---IKEGLEVMLNVPKKAN 1455
Cdd:cd00160  160 HEDredLKKALEAIKEVASQVN 181
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 1945-2121 2.62e-40

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 147.83  E-value: 2.62e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948   1945 VFAELMSTEEAYVQDLHEIVNGYMTEINNtnsdiPMPEDLKggKMKLVFNNIKDIYEWHRDFFLRALRNCQKSPADLGPL 2024
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSK-----PLSESEE--EIKTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDI 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948   2025 IKRSATKFALYYTYCSNKPLSEYIVS-------AHYQYFDSIR-QKLGHRLDLSNLIIKPVQRITKYELLIKEIIKATEG 2096
Cdd:pfam00621   74 FLKFAPGFKVYSTYCSNYPKALKLLKkllkknpKFRAFLEELEaNPECRGLDLNSFLIKPVQRIPRYPLLLKELLKHTPP 153

                          170       180
                   ....*....|....*....|....*
gi 24654948   2097 AGlyKEVPMLQEAYQQMKVVVKTVN 2121
Cdd:pfam00621  154 DH--PDYEDLKKALEAIKEVAKQIN 176
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 1287-1456 8.49e-40

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 146.29  E-value: 8.49e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    1287 IMAELMQTERAYVNDLATCIKCFLEEFRAGKSVPSAliGQEDVIFGNIKEIHHFHQkIFLRELEKY----ETMPEDVGHC 1362
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELKLLSP--NELETLFGNIEEIYEFHR-DFLDELEERieewDDSVERIGDV 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    1363 FVTWASKFDMYVHYCKNKPTSNNLLVQHGGS-----FFEELQRRLEVD-HPLPAYLIKPVQRITKYQLLLKDLLSCCEES 1436
Cdd:smart00325   78 FLKLEEFFKIYSEYCSNHPDALELLKKLKKNprfqkFLKEIESSPQCRrLTLESLLLKPVQRLTKYPLLLKELLKHTPED 157

                           170       180
                    ....*....|....*....|...
gi 24654948    1437 HGE---IKEGLEVMLNVPKKAND 1456
Cdd:smart00325  158 HEDredLKKALKAIKELANQVNE 180
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 1942-2121 4.87e-35

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: 132.81  E-value: 4.87e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 1942 RQCVFAELMSTEEAYVQDLHEIVNGYMTEINNtnSDIPMPEDlkggKMKLVFNNIKDIYEWHRDFFLR---ALRNCQKSP 2018
Cdd:cd00160    1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDK--ELLPLSPE----EVELLFGNIEEIYEFHRIFLKSleeRVEEWDKSG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 2019 ADLGPLIKRSATKFALYYTYCSNKPLSEYIVSAHYQ---YFDSIRQKLG---HRLDLSNLIIKPVQRITKYELLIKEIIK 2092
Cdd:cd00160   75 PRIGDVFLKLAPFFKIYSEYCSNHPDALELLKKLKKfnkFFQEFLEKAEsecGRLKLESLLLKPVQRLTKYPLLLKELLK 154

                        170       180
                 ....*....|....*....|....*....
gi 24654948 2093 ATEGAglYKEVPMLQEAYQQMKVVVKTVN 2121
Cdd:cd00160  155 HTPDG--HEDREDLKKALEAIKEVASQVN 181
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 1945-2122 2.70e-30

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: 119.33  E-value: 2.70e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    1945 VFAELMSTEEAYVQDLHEIVNGYMTEINNTNSDIPMPEdlkggkMKLVFNNIKDIYEWHRDFFLR---ALRNCQKSPADL 2021
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELKLLSPNE------LETLFGNIEEIYEFHRDFLDEleeRIEEWDDSVERI 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    2022 GPLIKRSATKFALYYTYCSNKPLSEYIVS---------AHYQYFDSirQKLGHRLDLSNLIIKPVQRITKYELLIKEIIK 2092
Cdd:smart00325   75 GDVFLKLEEFFKIYSEYCSNHPDALELLKklkknprfqKFLKEIES--SPQCRRLTLESLLLKPVQRLTKYPLLLKELLK 152

                           170       180       190
                    ....*....|....*....|....*....|
gi 24654948    2093 ATEGAglYKEVPMLQEAYQQMKVVVKTVND 2122
Cdd:smart00325  153 HTPED--HEDREDLKKALKAIKELANQVNE 180
SH3_Kalirin_1 cd11852
First Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or ...
 1643-1707 1.68e-25

First Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or TRAD, is a large neuronal dual Rho guanine nucleotide exchange factor (RhoGEF) that activates Rac1, RhoA, and RhoG using two RhoGEF domains. Kalirin exists in many isoforms generated by alternative splicing and the use of multiple promoters; the major isoforms are kalirin-7, -9, and -12, which differ at their C-terminal ends. Kalirin-12, the longest isoform, contains an N-terminal Sec14p domain, spectrin-like repeats, two RhoGEF domains, two SH3 domains, as well as Ig, FNIII, and kinase domains at the C-terminal end. Kalirin-7 contains only a single RhoGEF domain and does not contain an SH3 domain. Kalirin, through its many isoforms, interacts with many different proteins and is able to localize to different locations within the cell. It influences neurite initiation, axon growth, dendritic morphogenesis, vesicle trafficking, neuronal maintenance, and neurodegeneration. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212786  Cd Length: 62  Bit Score: 101.32  E-value: 1.68e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24654948 1643 EATWVVADYIATSgSNELSVSKGQQVEIVEPPTaGEPDFCLVRLNPQhDDAAVQEGLVPVSVLKP 1707
Cdd:cd11852    1 ELTVVIEDFEATS-SQELTVSKGQTVEVLERPS-SRPDWCLVRTLEQ-DNSPPQEGLVPSSILCI 62
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 13-152 2.14e-20

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: 90.05  E-value: 2.14e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948      13 LQERVVFLTGGR--DRRGGPLLCFPA--TPRRDRLKPEDLRRLLSYLISIPSDAAK---NLGFTVIIDMRG---NGNCST 82
Cdd:smart00516    2 LELLKAYIPGGRgyDKDGRPVLIERAgrFDLKSVTLEELLRYLVYVLEKILQEEKKtggIEGFTVIFDLKGlsmSNPDLS 81

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24654948      83 NVKTILKVLQEHFSANIHNVVIIKPDNFWQ---KQRASISSHKYKFETTTVS---IESLNKIVESHQLTGDFEGQQ 152
Cdd:smart00516   82 VLRKILKILQDHYPERLGKVYIINPPWFFRvlwKIIKPFLDEKTREKIRFVGndsKEELLEYIDKEQLPEELGGTL 157
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 782-997 1.05e-16

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 80.95  E-value: 1.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  782 RLRYFERDARLLSVQMEMWSEELQHADLSRDYQKAEQLIRMHN---ESVTEIQNATYEVVQQGQDLLQlfenagfismad 858
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEaleAELAAHEERVEALNELGEQLIE------------ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  859 ATHTAQARIEYLLDFLREREIDLEEMSEAKRAKLEQAVQLCQFQNDANQVISWIRNGEAMLvASFVTPNSLQEAEQLRKG 938
Cdd:cd00176   69 EGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAAL-ASEDLGKDLESVEELLKK 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  939 HEQFQIAIEKTHTSAVQVKYRADALINANHYDPL-SIDEISDDVTKKWQQLVTYAEERHK 997
Cdd:cd00176  148 HKELEEELEAHEPRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEERQK 207
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 897-1119 1.21e-15

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 77.87  E-value: 1.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  897 QLCQFQNDANQVISWIRNGEAMLvASFVTPNSLQEAEQLRKGHEQFQIAIEKTHTSAVQVKYRADALINANHYDPLSIDE 976
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELL-SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  977 ISDDVTKKWQQLVTYAEERHKLVTASIN---FYKTAEQVCSVLDSLEREYKREDDwcdgGGGSDKAQAivqLISKHQEQK 1053
Cdd:cd00176   80 RLEELNQRWEELRELAEERRQRLEEALDlqqFFRDADDLEQWLEEKEAALASEDL----GKDLESVEE---LLKKHKELE 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24654948 1054 EAFLKACTL---ARRTAETFLKYANRSQqcyqykgncEGHVKSKLDKLLTQENQVLDYWTLRKKSLDQC 1119
Cdd:cd00176  153 EELEAHEPRlksLNELAEELLEEGHPDA---------DEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC smart00150
Spectrin repeats;
1125-1226 7.29e-13

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 66.58  E-value: 7.29e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    1125 FERSAKQAIEWIHNTgEAYLSSRSnlVGISKEETEGLLKEHNEFRSTAKETRERVKLLIQLADSLVEKGHAHASDIKQWV 1204
Cdd:smart00150    3 FLRDADELEAWLEEK-EQLLASED--LGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79

                            90       100
                    ....*....|....*....|..
gi 24654948    1205 ASVDQRYKDFSNRMDSYCEQLE 1226
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 18-150 1.95e-11

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: 64.28  E-value: 1.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948   18 VFLTGGRDRRGGPLLCFPA-TPRRDRLKPEDLRRLLSYLI--SIPSDAAKNLGFTVIIDMRG----NGNCSTNVKTILKV 90
Cdd:cd00170   11 IGYLGGRDKEGRPVLVFRAgWDPPKLLDLEELLRYLVYLLekALRELEEQVEGFVVIIDLKGfslsNLSDLSLLKKLLKI 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24654948   91 LQEHFSANIHNVVIIKPdNFWQKQ-----RASISSH-KYKFETTTVSIESLNKIVESHQLTGDFEG 150
Cdd:cd00170   91 LQDHYPERLKKIYIVNA-PWIFSAlwkivKPFLSEKtRKKIVFLGSDLEELLEYIDPDQLPKELGG 155
SPEC smart00150
Spectrin repeats;
900-997 2.97e-11

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 61.96  E-value: 2.97e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948     900 QFQNDANQVISWIRNGEAMLvASFVTPNSLQEAEQLRKGHEQFQIAIEKTHTSAVQVKYRADALINANHYDPLSIDEISD 979
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLL-ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90
                    ....*....|....*...
gi 24654948     980 DVTKKWQQLVTYAEERHK 997
Cdd:smart00150   81 ELNERWEELKELAEERRQ 98
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 563-778 5.55e-11

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 64.39  E-value: 5.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  563 LRLFQEDVKQVLDWLKNHGEVFlrKNTGIGRNFHKARVYQTSHDNFENVAQNTYSNAQKLLAAADELARSGEADPNEIYS 642
Cdd:cd00176    2 LQQFLRDADELEAWLSEKEELL--SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  643 VARELELQVGSFAERVEQRRRRLDMAVI---FYTHEKDVTAWIDKLRTDVSTDETRLSQENLEGIERILQQYQRD--QQE 717
Cdd:cd00176   80 RLEELNQRWEELRELAEERRQRLEEALDlqqFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEEleAHE 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24654948  718 SSVNVCLttiSQGEALLQEMRSleyadntGSIAALEATLEKLNKQKVELEELWSARKFRAD 778
Cdd:cd00176  160 PRLKSLN---ELAEELLEEGHP-------DADEEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 314-468 1.67e-10

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 62.85  E-value: 1.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  314 QWRLFEQDCEKMFDWILHNRDVFQMSyvEIGHNYSVAKSLQDEHQKFAVASMNVSVNIDRILAVAARLIESQHYAAQHIK 393
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSST--DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24654948  394 TLAQRLDRTWKDFAAGLDERTAVLQLSVLFHHKAEQyCNSVASWAAACQ---ASQPLPSDIQSLETAIRTHQSLYEAM 468
Cdd:cd00176   79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEaalASEDLGKDLESVEELLKKHKELEEEL 155
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 1121-1229 1.67e-10

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 62.85  E-value: 1.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 1121 QFVLFERSAKQAIEWIHNTgEAYLSSRSnlVGISKEETEGLLKEHNEFRSTAKETRERVKLLIQLADSLVEKGHAHASDI 1200
Cdd:cd00176    1 KLQQFLRDADELEAWLSEK-EELLSSTD--YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI 77

                         90       100
                 ....*....|....*....|....*....
gi 24654948 1201 KQWVASVDQRYKDFSNRMDSYCEQLEKSL 1229
Cdd:cd00176   78 QERLEELNQRWEELRELAEERRQRLEEAL 106
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 900-997 3.16e-10

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: 59.25  E-value: 3.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    900 QFQNDANQVISWIRNGEAMLvASFVTPNSLQEAEQLRKGHEQFQIAIEKTHTSAVQVKYRADALINANHYDPLSIDEISD 979
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALL-SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83

                           90
                   ....*....|....*...
gi 24654948    980 DVTKKWQQLVTYAEERHK 997
Cdd:pfam00435   84 ELNERWEQLLELAAERKQ 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 1120-1226 1.25e-08

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: 54.63  E-value: 1.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948   1120 QQFVLFERSAKQAIEWIHNTgEAYLSSRSnlVGISKEETEGLLKEHNEFRSTAKETRERVKLLIQLADSLVEKGHAHASD 1199
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEK-EALLSSED--YGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE 77

                           90       100
                   ....*....|....*....|....*..
gi 24654948   1200 IKQWVASVDQRYKDFSNRMDSYCEQLE 1226
Cdd:pfam00435   78 IQERLEELNERWEQLLELAAERKQKLE 104
SPEC smart00150
Spectrin repeats;
318-418 5.58e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 52.72  E-value: 5.58e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948     318 FEQDCEKMFDWILHNRDvfQMSYVEIGHNYSVAKSLQDEHQKFAVASMNVSVNIDRILAVAARLIESQHYAAQHIKTLAQ 397
Cdd:smart00150    3 FLRDADELEAWLEEKEQ--LLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 24654948     398 RLDRTWKDFAAGLDERTAVLQ 418
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 28-156 7.02e-08

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: 53.49  E-value: 7.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948     28 GGPLLCFPATPRRDRLKP-EDLRRLLSYLISIPSDAAKNLGFTVIIDMRGNGncSTN------VKTILKVLQEHFSANIH 100
Cdd:pfam13716    1 GRPVLVFISKLLPSRPASlDDLDRLLFYLLKTLSEKLKGKPFVVVVDHTGVT--SENfpslsfLKKAYDLLPRAFKKNLK 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24654948    101 NVVIIKPDNFWqkqRASISSHKY-----KFETTTVSIESLNKI---VESHQLTGDFEGQQLYDH 156
Cdd:pfam13716   79 AVYVVHPSTFL---RTFLKTLGSllgskKLRKKVHYVSSLSELwegIDREQLPTELPGVLSYDE 139
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 1941-2111 8.88e-08

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


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 57.98  E-value: 8.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 1941 KRQCVFAELMSTEEAYVQDLHEIVNGYMTEINNTNSdipMPEDLKGGKMKLVFNNIKDIYEWHRDFfLRALRNCQK-SPA 2019
Cdd:COG5422  484 KRQEAIYEVIYTERDFVKDLEYLRDTWIKPLEESNI---IPENARRNFIKHVFANINEIYAVNSKL-LKALTNRQClSPI 559

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 2020 --DLGPLIKRSATKFALYYTYCSNKPLSEYIV----SAHYQYF----DSIRQKLGHRLDLSNLIIKPVQRITKYELLIKE 2089
Cdd:COG5422  560 vnGIADIFLDYVPKFEPFIKYGASQPYAKYEFerekSVNPNFArfdhEVERLDESRKLELDGYLTKPTTRLARYPLLLEE 639

                        170       180
                 ....*....|....*....|...
gi 24654948 2090 IIKAT-EGAGLYKEVPMLQEAYQ 2111
Cdd:COG5422  640 VLKFTdPDNPDTEDIPKVIDMLR 662
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 1487-1581 2.48e-05

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: 45.23  E-value: 2.48e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    1487 TKQIIRKGRERRVFLFELYLLFAKEVKESNVVKYQFKSKLMTTDMGITEHIEGDETK--FAVWTGrspmlSDCRIVLKAT 1564
Cdd:smart00233   11 SGGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYKPKGSIDLSGCTVREAPDPDSSKKPhcFEIKTS-----DRKTLLLQAE 85

                            90
                    ....*....|....*..
gi 24654948    1565 SLETKQIWVKKLREVMQ 1581
Cdd:smart00233   86 SEEEREKWVEALRKAIA 102
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 314-418 2.83e-05

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 45.00  E-value: 2.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    314 QWRLFEQDCEKMFDWIlhNRDVFQMSYVEIGHNYSVAKSLQDEHQKFaVASMNV-SVNIDRILAVAARLIESQHYAAQHI 392
Cdd:pfam00435    2 LLQQFFRDADDLESWI--EEKEALLSSEDYGKDLESVQALLKKHKAL-EAELAAhQDRVEALNELAEKLIDEGHYASEEI 78

                           90       100
                   ....*....|....*....|....*.
gi 24654948    393 KTLAQRLDRTWKDFAAGLDERTAVLQ 418
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLE 104
SPEC smart00150
Spectrin repeats;
566-666 2.49e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 42.32  E-value: 2.49e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948     566 FQEDVKQVLDWLKNHgEVFLRkNTGIGRNFHKARVYQTSHDNFENVAQNTYSNAQKLLAAADELARSGEADPNEIYSVAR 645
Cdd:smart00150    3 FLRDADELEAWLEEK-EQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 24654948     646 ELELQVGSFAERVEQRRRRLD 666
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 622-908 2.61e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 2.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    622 LLAAADELARSGEADPNEIYSVARELE---LQVGSFAERVEQRRRRLDmavifythekDVTAWIDKLRTD----VSTD-- 692
Cdd:TIGR02169  228 LLKEKEALERQKEAIERQLASLEEELEkltEEISELEKRLEEIEQLLE----------ELNKKIKDLGEEeqlrVKEKig 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    693 ETRLSQENLEGIERILQQYQRDQQESSVNvcltTISQGEALLQEMRSLEyadntGSIAALEATLEKLNkqkvelEELWSA 772
Cdd:TIGR02169  298 ELEAEIASLERSIAEKERELEDAEERLAK----LEAEIDKLLAEIEELE-----REIEEERKRRDKLT------EEYAEL 362

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    773 RKFRADLILRLRYFERDARllsvqmeMWSEELqhadlsRDYQKA-EQLIRMHNESVTEIQNATYEVVQQGQDLLQLfENA 851
Cdd:TIGR02169  363 KEELEDLRAELEEVDKEFA-------ETRDEL------KDYREKlEKLKREINELKRELDRLQEELQRLSEELADL-NAA 428

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 24654948    852 gfISMADATHTA-QARIEYLLDFLREREIDLEEMSeAKRAKLEQavQLCQFQNDANQV 908
Cdd:TIGR02169  429 --IAGIEAKINElEEEKEDKALEIKKQEWKLEQLA-ADLSKYEQ--ELYDLKEEYDRV 481
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 645-898 1.81e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  645 RELELQVGSFAERVEQRRRRLDMAvifythekdvTAWIDKLRTDVSTDETRLSQENLEgIERILQQYQRDQQEssvnvcL 724
Cdd:COG1196  235 RELEAELEELEAELEELEAELEEL----------EAELAELEAELEELRLELEELELE-LEEAQAEEYELLAE------L 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  725 TTISQGEALLQEMRsleyADNTGSIAALEATLEKLNKQKVELEELwsarkfRADLILRLRyfERDARLLSVQMEMWSEEL 804
Cdd:COG1196  298 ARLEQDIARLEERR----RELEERLEELEEELAELEEELEELEEE------LEELEEELE--EAEEELEEAEAELAEAEE 365

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  805 QHADLSRDYQKAEQLIRMHNESVTEIQNATYEVVQQGQDLLQLFENAgFISMADATHTAQARIEYLLDFLREREIDLEEM 884
Cdd:COG1196  366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL-LERLERLEEELEELEEALAELEEEEEEEEEAL 444

                        250
                 ....*....|....
gi 24654948  885 SEAKRAKLEQAVQL 898
Cdd:COG1196  445 EEAAEEEAELEEEE 458
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 690-917 3.42e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 3.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  690 STDETRLSQENLEGIERILQQYQRDQQEssvnvcltTISQGEALLQEMRSLEYA---------DNTGSIAALEATLEKLN 760
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELAA--------LKKEEKALLKQLAALERRiaalarrirALEQELAALEAELAELE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  761 KQKVELEELWSARkfRADLILRLRYFERDARLLSVQMEMWSEELqhADLSRDYQKAEQLIRMHNESVTEIQNATYEVVQQ 840
Cdd:COG4942   90 KEIAELRAELEAQ--KEELAELLRALYRLGRQPPLALLLSPEDF--LDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24654948  841 GQDLLQLFEnagfiSMADATHTAQARIEYLLDFLREREIDLEEMSEAKRAKLEQAVQLCQFQNDANQVISWIRNGEA 917
Cdd:COG4942  166 RAELEAERA-----ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 1256-1430 3.50e-03

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


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 42.57  E-value: 3.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 1256 DPTLEAKLNSSNKENKEINEEKRKSARRKEFIMAELMQTERAYVNDLATCIKCFLEEFRAGKSVPSAlIGQEDV--IFGN 1333
Cdd:COG5422  457 DKFDEEKNLWTLSVPKEVWESLPKQEIKRQEAIYEVIYTERDFVKDLEYLRDTWIKPLEESNIIPEN-ARRNFIkhVFAN 535

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 1334 IKEIHHFHQKIF--LRELEKYETMPEDVGHCFVTWASKFDMYVHYCKNKPTSNNLLVQHGGS------FFEELQR-RLEV 1404
Cdd:COG5422  536 INEIYAVNSKLLkaLTNRQCLSPIVNGIADIFLDYVPKFEPFIKYGASQPYAKYEFEREKSVnpnfarFDHEVERlDESR 615

                        170       180
                 ....*....|....*....|....*.
gi 24654948 1405 DHPLPAYLIKPVQRITKYQLLLKDLL 1430
Cdd:COG5422  616 KLELDGYLTKPTTRLARYPLLLEEVL 641
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 729-1025 5.53e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 5.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    729 QGEALLQEMRSL--EYADNTGSIAALEATLEKLNKQKVELEELWSarkfradlILRLRYFERDARLLSVQmemwsEELQh 806
Cdd:TIGR02168  226 ELALLVLRLEELreELEELQEELKEAEEELEELTAELQELEEKLE--------ELRLEVSELEEEIEELQ-----KELY- 291

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    807 aDLSRDYQKAEQLIRMHNES----VTEIQNATYEVVQQGQDLLQLFENAGfiSMADATHTAQARIEYLLDFLREREIDLE 882
Cdd:TIGR02168  292 -ALANEISRLEQQKQILRERlanlERQLEELEAQLEELESKLDELAEELA--ELEEKLEELKEELESLEAELEELEAELE 368

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    883 EMSEAKRaklEQAVQLCQFQNDANQViswirngeamlvasfvtpnsLQEAEQLRKghEQFQIAIEKTHTSAVQVKYRADA 962
Cdd:TIGR02168  369 ELESRLE---ELEEQLETLRSKVAQL--------------------ELQIASLNN--EIERLEARLERLEDRRERLQQEI 423

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24654948    963 LINANHYDPLSIDEISDDVTKKWQQLVTYAEERHKLVTASINFYKTAEQVCSVLDSLEREYKR 1025
Cdd:TIGR02168  424 EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
PH_10 pfam15411
Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.
 2140-2182 9.27e-03

Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.


Pssm-ID: 464707  Cd Length: 120  Bit Score: 38.34  E-value: 9.27e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 24654948   2140 QGSLLMQGPMNcVVDAAQKHRELQVFLFQQIIIFADIEKTKNQ 2182
Cdd:pfam15411    2 FGELLLHDKLT-VGKDSDSEREYHVYLFEKILLCCKEISPKKK 43
 
Name Accession Description Interval E-value
PH1_Kalirin_Trio_like cd13240
Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; ...
 1462-1584 4.87e-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: 224.96  E-value: 4.87e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 1462 LLENCDVSVDKLGEVVLQDAFQAWDTKQIIRKGRERRVFLFELYLLFAKEVKESNV-VKYQFKSKLMTTDMGITEHIEGD 1540
Cdd:cd13240    1 LLEGCDEDLDSLGEVILQDSFQVWDPKQLIRKGRERHVFLFELCLVFSKEVKDSNGkSKYIYKSRLMTSEIGVTEHIEGD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 24654948 1541 ETKFAVWTGRSPmLSDCRIVLKATSLETKQIWVKKLREVMQETC 1584
Cdd:cd13240   81 PCKFALWTGRVP-TSDNKIVLKASSLEVKQTWVKKLREVIQERI 123
PH2_Kalirin_Trio_p63RhoGEF cd13241
p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor ...
 2130-2260 3.26e-62

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: 209.04  E-value: 3.26e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 2130 LQDFDGEITAQGSLLMQGPMNCVVDAA---QKHRELQVFLFQQIIIFADIEKTKNQYASPIFKYRSHIQLNHMQMKELGD 2206
Cdd:cd13241    4 LQGFDGKITAQGKLLLQGTLLVSEPSAgllQKGKERRVFLFEQIIIFSEILGKKTQFSNPGYIYKNHIKVNKMSLEENVD 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24654948 2207 ---CRFQIRSTDPKIPEMTIICQAASQENYAGWRDMLNKILQQQNDLIFMLSNPLST 2260
Cdd:cd13241   84 gdpLRFALKSRDPNNPSETFILQAASPEVRQEWVDTINQILDTQRDFLKALQSPIAY 140
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 1287-1455 2.65e-43

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 156.31  E-value: 2.65e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948   1287 IMAELMQTERAYVNDLATCIKCFLEEFRAGKSVPSALIgqeDVIFGNIKEIHHFHQKIFLRELEKYETMPEDVGHCFVTW 1366
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEI---KTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIFLKF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948   1367 ASKFDMYVHYCKNKPTSNNLLVQ------HGGSFFEELQRRLEVD-HPLPAYLIKPVQRITKYQLLLKDLLSCCEESHGE 1439
Cdd:pfam00621   78 APGFKVYSTYCSNYPKALKLLKKllkknpKFRAFLEELEANPECRgLDLNSFLIKPVQRIPRYPLLLKELLKHTPPDHPD 157

                          170
                   ....*....|....*....
gi 24654948   1440 ---IKEGLEVMLNVPKKAN 1455
Cdd:pfam00621  158 yedLKKALEAIKEVAKQIN 176
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 1286-1455 9.52e-43

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 155.15  E-value: 9.52e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 1286 FIMAELMQTERAYVNDLATCIKCFLEEFRagKSVPSALIGQEDVIFGNIKEIHHFHqKIFLRELEKY----ETMPEDVGH 1361
Cdd:cd00160    3 EVIKELLQTERNYVRDLKLLVEVFLKPLD--KELLPLSPEEVELLFGNIEEIYEFH-RIFLKSLEERveewDKSGPRIGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 1362 CFVTWASKFDMYVHYCKNKPTSNNLLVQH--GGSFFEELQRRLE---VDHPLPAYLIKPVQRITKYQLLLKDLLSCCEES 1436
Cdd:cd00160   80 VFLKLAPFFKIYSEYCSNHPDALELLKKLkkFNKFFQEFLEKAEsecGRLKLESLLLKPVQRLTKYPLLLKELLKHTPDG 159

                        170       180
                 ....*....|....*....|..
gi 24654948 1437 HGE---IKEGLEVMLNVPKKAN 1455
Cdd:cd00160  160 HEDredLKKALEAIKEVASQVN 181
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 1945-2121 2.62e-40

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 147.83  E-value: 2.62e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948   1945 VFAELMSTEEAYVQDLHEIVNGYMTEINNtnsdiPMPEDLKggKMKLVFNNIKDIYEWHRDFFLRALRNCQKSPADLGPL 2024
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSK-----PLSESEE--EIKTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDI 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948   2025 IKRSATKFALYYTYCSNKPLSEYIVS-------AHYQYFDSIR-QKLGHRLDLSNLIIKPVQRITKYELLIKEIIKATEG 2096
Cdd:pfam00621   74 FLKFAPGFKVYSTYCSNYPKALKLLKkllkknpKFRAFLEELEaNPECRGLDLNSFLIKPVQRIPRYPLLLKELLKHTPP 153

                          170       180
                   ....*....|....*....|....*
gi 24654948   2097 AGlyKEVPMLQEAYQQMKVVVKTVN 2121
Cdd:pfam00621  154 DH--PDYEDLKKALEAIKEVAKQIN 176
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 1287-1456 8.49e-40

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 146.29  E-value: 8.49e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    1287 IMAELMQTERAYVNDLATCIKCFLEEFRAGKSVPSAliGQEDVIFGNIKEIHHFHQkIFLRELEKY----ETMPEDVGHC 1362
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELKLLSP--NELETLFGNIEEIYEFHR-DFLDELEERieewDDSVERIGDV 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    1363 FVTWASKFDMYVHYCKNKPTSNNLLVQHGGS-----FFEELQRRLEVD-HPLPAYLIKPVQRITKYQLLLKDLLSCCEES 1436
Cdd:smart00325   78 FLKLEEFFKIYSEYCSNHPDALELLKKLKKNprfqkFLKEIESSPQCRrLTLESLLLKPVQRLTKYPLLLKELLKHTPED 157

                           170       180
                    ....*....|....*....|...
gi 24654948    1437 HGE---IKEGLEVMLNVPKKAND 1456
Cdd:smart00325  158 HEDredLKKALKAIKELANQVNE 180
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 1942-2121 4.87e-35

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: 132.81  E-value: 4.87e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 1942 RQCVFAELMSTEEAYVQDLHEIVNGYMTEINNtnSDIPMPEDlkggKMKLVFNNIKDIYEWHRDFFLR---ALRNCQKSP 2018
Cdd:cd00160    1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDK--ELLPLSPE----EVELLFGNIEEIYEFHRIFLKSleeRVEEWDKSG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 2019 ADLGPLIKRSATKFALYYTYCSNKPLSEYIVSAHYQ---YFDSIRQKLG---HRLDLSNLIIKPVQRITKYELLIKEIIK 2092
Cdd:cd00160   75 PRIGDVFLKLAPFFKIYSEYCSNHPDALELLKKLKKfnkFFQEFLEKAEsecGRLKLESLLLKPVQRLTKYPLLLKELLK 154

                        170       180
                 ....*....|....*....|....*....
gi 24654948 2093 ATEGAglYKEVPMLQEAYQQMKVVVKTVN 2121
Cdd:cd00160  155 HTPDG--HEDREDLKKALEAIKEVASQVN 181
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 1945-2122 2.70e-30

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: 119.33  E-value: 2.70e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    1945 VFAELMSTEEAYVQDLHEIVNGYMTEINNTNSDIPMPEdlkggkMKLVFNNIKDIYEWHRDFFLR---ALRNCQKSPADL 2021
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELKLLSPNE------LETLFGNIEEIYEFHRDFLDEleeRIEEWDDSVERI 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    2022 GPLIKRSATKFALYYTYCSNKPLSEYIVS---------AHYQYFDSirQKLGHRLDLSNLIIKPVQRITKYELLIKEIIK 2092
Cdd:smart00325   75 GDVFLKLEEFFKIYSEYCSNHPDALELLKklkknprfqKFLKEIES--SPQCRRLTLESLLLKPVQRLTKYPLLLKELLK 152

                           170       180       190
                    ....*....|....*....|....*....|
gi 24654948    2093 ATEGAglYKEVPMLQEAYQQMKVVVKTVND 2122
Cdd:smart00325  153 HTPED--HEDREDLKKALKAIKELANQVNE 180
SH3_Kalirin_1 cd11852
First Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or ...
 1643-1707 1.68e-25

First Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or TRAD, is a large neuronal dual Rho guanine nucleotide exchange factor (RhoGEF) that activates Rac1, RhoA, and RhoG using two RhoGEF domains. Kalirin exists in many isoforms generated by alternative splicing and the use of multiple promoters; the major isoforms are kalirin-7, -9, and -12, which differ at their C-terminal ends. Kalirin-12, the longest isoform, contains an N-terminal Sec14p domain, spectrin-like repeats, two RhoGEF domains, two SH3 domains, as well as Ig, FNIII, and kinase domains at the C-terminal end. Kalirin-7 contains only a single RhoGEF domain and does not contain an SH3 domain. Kalirin, through its many isoforms, interacts with many different proteins and is able to localize to different locations within the cell. It influences neurite initiation, axon growth, dendritic morphogenesis, vesicle trafficking, neuronal maintenance, and neurodegeneration. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212786  Cd Length: 62  Bit Score: 101.32  E-value: 1.68e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24654948 1643 EATWVVADYIATSgSNELSVSKGQQVEIVEPPTaGEPDFCLVRLNPQhDDAAVQEGLVPVSVLKP 1707
Cdd:cd11852    1 ELTVVIEDFEATS-SQELTVSKGQTVEVLERPS-SRPDWCLVRTLEQ-DNSPPQEGLVPSSILCI 62
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 13-152 2.14e-20

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: 90.05  E-value: 2.14e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948      13 LQERVVFLTGGR--DRRGGPLLCFPA--TPRRDRLKPEDLRRLLSYLISIPSDAAK---NLGFTVIIDMRG---NGNCST 82
Cdd:smart00516    2 LELLKAYIPGGRgyDKDGRPVLIERAgrFDLKSVTLEELLRYLVYVLEKILQEEKKtggIEGFTVIFDLKGlsmSNPDLS 81

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24654948      83 NVKTILKVLQEHFSANIHNVVIIKPDNFWQ---KQRASISSHKYKFETTTVS---IESLNKIVESHQLTGDFEGQQ 152
Cdd:smart00516   82 VLRKILKILQDHYPERLGKVYIINPPWFFRvlwKIIKPFLDEKTREKIRFVGndsKEELLEYIDKEQLPEELGGTL 157
PH2_Kalirin_Trio_p63RhoGEF cd13241
p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor ...
 1463-1581 7.42e-17

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: 79.23  E-value: 7.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 1463 LENCDVSVDKLGEVVLQDAFQAWDTK-QIIRKGRERRVFLFELYLLFAKEV---KESNVVKYQFKSKLMTTDMGITEHIE 1538
Cdd:cd13241    4 LQGFDGKITAQGKLLLQGTLLVSEPSaGLLQKGKERRVFLFEQIIIFSEILgkkTQFSNPGYIYKNHIKVNKMSLEENVD 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 24654948 1539 GDETKFAVWTgRSPMLSDCRIVLKATSLETKQIWVKKLREVMQ 1581
Cdd:cd13241   84 GDPLRFALKS-RDPNNPSETFILQAASPEVRQEWVDTINQILD 125
PH_puratrophin-1 cd13242
Puratrophin-1 pleckstrin homology (PH) domain; Puratrophin-1 (also called Purkinje cell ...
 1455-1573 7.52e-17

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: 79.26  E-value: 7.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 1455 NDAMHLSLLENCDVSVDKLGEVVLQDAFQAWdtkqIIRKGRERRVFLFELYLLFAKEVK-ESNVVKYQFKSKLMTTDMGI 1533
Cdd:cd13242    8 NDLLAMDSIRGCDVNLKEQGQLLRQDEFLVW----QGRKKCLRHVFLFEDLILFSKPKKtPGGKDVYIYKHSIKTSDIGL 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 24654948 1534 TEHIEGDETKFAVWTgRSPMLSDCrIVLKATSLETKQIWV 1573
Cdd:cd13242   84 TENVGDSGLKFEIWF-RRRKARDT-YILQATSPEIKQAWT 121
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 782-997 1.05e-16

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 80.95  E-value: 1.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  782 RLRYFERDARLLSVQMEMWSEELQHADLSRDYQKAEQLIRMHN---ESVTEIQNATYEVVQQGQDLLQlfenagfismad 858
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEaleAELAAHEERVEALNELGEQLIE------------ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  859 ATHTAQARIEYLLDFLREREIDLEEMSEAKRAKLEQAVQLCQFQNDANQVISWIRNGEAMLvASFVTPNSLQEAEQLRKG 938
Cdd:cd00176   69 EGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAAL-ASEDLGKDLESVEELLKK 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  939 HEQFQIAIEKTHTSAVQVKYRADALINANHYDPL-SIDEISDDVTKKWQQLVTYAEERHK 997
Cdd:cd00176  148 HKELEEELEAHEPRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEERQK 207
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 897-1119 1.21e-15

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 77.87  E-value: 1.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  897 QLCQFQNDANQVISWIRNGEAMLvASFVTPNSLQEAEQLRKGHEQFQIAIEKTHTSAVQVKYRADALINANHYDPLSIDE 976
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELL-SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  977 ISDDVTKKWQQLVTYAEERHKLVTASIN---FYKTAEQVCSVLDSLEREYKREDDwcdgGGGSDKAQAivqLISKHQEQK 1053
Cdd:cd00176   80 RLEELNQRWEELRELAEERRQRLEEALDlqqFFRDADDLEQWLEEKEAALASEDL----GKDLESVEE---LLKKHKELE 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24654948 1054 EAFLKACTL---ARRTAETFLKYANRSQqcyqykgncEGHVKSKLDKLLTQENQVLDYWTLRKKSLDQC 1119
Cdd:cd00176  153 EELEAHEPRlksLNELAEELLEEGHPDA---------DEEIEEKLEELNERWEELLELAEERQKKLEEA 212
PH_Obscurin cd13239
Obscurin pleckstrin homology (PH) domain; Obscurin (also called Obscurin-RhoGEF; ...
 1462-1581 2.63e-15

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: 74.50  E-value: 2.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 1462 LLENCDVSVDKLGEVVLQDAFQAWDTKQIIR---KGRERRVFLFELYLLFAKEVKESNV--VKYQFKSKLMTTDMGITEH 1536
Cdd:cd13239    1 LIENYPAPLQALGEPIRQGHFTVWEEAPEVKtssRGHHRHVFLFKNCVVICKPKRDSRTdtVTYVFKNKMKLSDIDVKDT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 24654948 1537 IEGDETKFAVWTGRSPMLSdcRIVLKATSLETKQIWVKKLREVMQ 1581
Cdd:cd13239   81 VEGDDRSFGLWHEHRGSVR--KYTLQARSAIIKSSWLKDLRDLQQ 123
PH_Dbs cd01227
DBL's big sister protein pleckstrin homology (PH) domain; Dbs (also called MCF2-transforming ...
 1467-1580 3.83e-14

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: 71.07  E-value: 3.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 1467 DVSVDKLGEVVLQDAFQAW------DTKQIIR-KGRERRVFLFELYLLFAKEVKE-SNVVKYQFKSKLMTTDMGITEHIE 1538
Cdd:cd01227    6 DGNLGDLGKLLMQGSFNVWtehkkgHTKKLARfKPMQRHIFLYEKAVLFCKKRGEnGEAPSYSYKNSLNTTAVGLTENVK 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 24654948 1539 GDETKFAVW-TGRSPMLsdcriVLKATSLETKQIWVKKLREVM 1580
Cdd:cd01227   86 GDTKKFEIWlNGREEVF-----IIQAPTPEIKAAWVKAIRQVL 123
SPEC smart00150
Spectrin repeats;
1125-1226 7.29e-13

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 66.58  E-value: 7.29e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    1125 FERSAKQAIEWIHNTgEAYLSSRSnlVGISKEETEGLLKEHNEFRSTAKETRERVKLLIQLADSLVEKGHAHASDIKQWV 1204
Cdd:smart00150    3 FLRDADELEAWLEEK-EQLLASED--LGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79

                            90       100
                    ....*....|....*....|..
gi 24654948    1205 ASVDQRYKDFSNRMDSYCEQLE 1226
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 18-150 1.95e-11

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: 64.28  E-value: 1.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948   18 VFLTGGRDRRGGPLLCFPA-TPRRDRLKPEDLRRLLSYLI--SIPSDAAKNLGFTVIIDMRG----NGNCSTNVKTILKV 90
Cdd:cd00170   11 IGYLGGRDKEGRPVLVFRAgWDPPKLLDLEELLRYLVYLLekALRELEEQVEGFVVIIDLKGfslsNLSDLSLLKKLLKI 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24654948   91 LQEHFSANIHNVVIIKPdNFWQKQ-----RASISSH-KYKFETTTVSIESLNKIVESHQLTGDFEG 150
Cdd:cd00170   91 LQDHYPERLKKIYIVNA-PWIFSAlwkivKPFLSEKtRKKIVFLGSDLEELLEYIDPDQLPKELGG 155
SPEC smart00150
Spectrin repeats;
900-997 2.97e-11

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 61.96  E-value: 2.97e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948     900 QFQNDANQVISWIRNGEAMLvASFVTPNSLQEAEQLRKGHEQFQIAIEKTHTSAVQVKYRADALINANHYDPLSIDEISD 979
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLL-ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90
                    ....*....|....*...
gi 24654948     980 DVTKKWQQLVTYAEERHK 997
Cdd:smart00150   81 ELNERWEELKELAEERRQ 98
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 563-778 5.55e-11

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 64.39  E-value: 5.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  563 LRLFQEDVKQVLDWLKNHGEVFlrKNTGIGRNFHKARVYQTSHDNFENVAQNTYSNAQKLLAAADELARSGEADPNEIYS 642
Cdd:cd00176    2 LQQFLRDADELEAWLSEKEELL--SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  643 VARELELQVGSFAERVEQRRRRLDMAVI---FYTHEKDVTAWIDKLRTDVSTDETRLSQENLEGIERILQQYQRD--QQE 717
Cdd:cd00176   80 RLEELNQRWEELRELAEERRQRLEEALDlqqFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEEleAHE 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24654948  718 SSVNVCLttiSQGEALLQEMRSleyadntGSIAALEATLEKLNKQKVELEELWSARKFRAD 778
Cdd:cd00176  160 PRLKSLN---ELAEELLEEGHP-------DADEEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 314-468 1.67e-10

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 62.85  E-value: 1.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  314 QWRLFEQDCEKMFDWILHNRDVFQMSyvEIGHNYSVAKSLQDEHQKFAVASMNVSVNIDRILAVAARLIESQHYAAQHIK 393
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSST--DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24654948  394 TLAQRLDRTWKDFAAGLDERTAVLQLSVLFHHKAEQyCNSVASWAAACQ---ASQPLPSDIQSLETAIRTHQSLYEAM 468
Cdd:cd00176   79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEaalASEDLGKDLESVEELLKKHKELEEEL 155
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 1121-1229 1.67e-10

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 62.85  E-value: 1.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 1121 QFVLFERSAKQAIEWIHNTgEAYLSSRSnlVGISKEETEGLLKEHNEFRSTAKETRERVKLLIQLADSLVEKGHAHASDI 1200
Cdd:cd00176    1 KLQQFLRDADELEAWLSEK-EELLSSTD--YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI 77

                         90       100
                 ....*....|....*....|....*....
gi 24654948 1201 KQWVASVDQRYKDFSNRMDSYCEQLEKSL 1229
Cdd:cd00176   78 QERLEELNQRWEELRELAEERRQRLEEAL 106
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 900-997 3.16e-10

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: 59.25  E-value: 3.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    900 QFQNDANQVISWIRNGEAMLvASFVTPNSLQEAEQLRKGHEQFQIAIEKTHTSAVQVKYRADALINANHYDPLSIDEISD 979
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALL-SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83

                           90
                   ....*....|....*...
gi 24654948    980 DVTKKWQQLVTYAEERHK 997
Cdd:pfam00435   84 ELNERWEQLLELAAERKQ 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 1005-1229 5.53e-10

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 61.31  E-value: 5.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 1005 FYKTAEQVCSVLDSLEREYKREDDwcdggggSDKAQAIVQLISKHQeqkeAFLKACTLARRTAETFLKYANR-SQQCYQY 1083
Cdd:cd00176    5 FLRDADELEAWLSEKEELLSSTDY-------GDDLESVEALLKKHE----ALEAELAAHEERVEALNELGEQlIEEGHPD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 1084 KGNceghVKSKLDKLLTQENQVLDYWTLRKKSLDQCQQFVLFERSAKQAIEWIHNTgEAYLSSRSnlVGISKEETEGLLK 1163
Cdd:cd00176   74 AEE----IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEK-EAALASED--LGKDLESVEELLK 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24654948 1164 EHNEFRSTAKETRERVKLLIQLADSLVEKGHAHASD-IKQWVASVDQRYKDFSNRMDSYCEQLEKSL 1229
Cdd:cd00176  147 KHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEeIEEKLEELNERWEELLELAEERQKKLEEAL 213
PH_PLEKHG1_G2_G3 cd13243
Pleckstrin homology domain-containing family G members 1, 2, and 3 pleckstrin homology (PH) ...
 1439-1582 1.34e-09

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


Pssm-ID: 270063 [Multi-domain]  Cd Length: 147  Bit Score: 58.52  E-value: 1.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 1439 EIKEGLEVMLNVPKKAND-------AMHL----SLLEN-CDVSVDKLGEVVLQDAFQawdtkqIIRKGRERRVFLFELYL 1506
Cdd:cd13243    3 VVEEALDTMTQVAWHINDmkrkhehAVRVqeiqSLLDGwEGPELTTYGDLVLEGTFR------MAGAKNERLLFLFDKML 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24654948 1507 LFAKEVKEsnvVKYQFKSKLMTTDMGITEHIEGDETKFAVWTGRSPMLsdcRIVLKATSLETKQIWVKKLREVMQE 1582
Cdd:cd13243   77 LITKKRED---GILQYKTHIMCSNLMLSESIPKEPLSFQVLPFDNPKL---QYTLQAKNQEQKRLWTQEIKRLILE 146
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 676-896 2.71e-09

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 59.38  E-value: 2.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  676 KDVTAWIDKLRTDVSTDETRLSQENLEGIERILQQYQRDQQESSVNVcLTTISQGEALLQEmrsleyadNTGSIAALEAT 755
Cdd:cd00176   10 DELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERV-EALNELGEQLIEE--------GHPDAEEIQER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  756 LEKLNKQKVELEELWSARKFRADLILRLRYFERDARLLSVQMEMWSEELQHADLSRDYQKAEQLIRMHNESVTEIQNATY 835
Cdd:cd00176   81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEP 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24654948  836 EV---VQQGQDLLQlfenagfismaDATHTAQARIEYLLDFLREREIDLEEMSEAKRAKLEQAV 896
Cdd:cd00176  161 RLkslNELAEELLE-----------EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 1120-1226 1.25e-08

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: 54.63  E-value: 1.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948   1120 QQFVLFERSAKQAIEWIHNTgEAYLSSRSnlVGISKEETEGLLKEHNEFRSTAKETRERVKLLIQLADSLVEKGHAHASD 1199
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEK-EALLSSED--YGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE 77

                           90       100
                   ....*....|....*....|....*..
gi 24654948   1200 IKQWVASVDQRYKDFSNRMDSYCEQLE 1226
Cdd:pfam00435   78 IQERLEELNERWEQLLELAAERKQKLE 104
SPEC smart00150
Spectrin repeats;
318-418 5.58e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 52.72  E-value: 5.58e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948     318 FEQDCEKMFDWILHNRDvfQMSYVEIGHNYSVAKSLQDEHQKFAVASMNVSVNIDRILAVAARLIESQHYAAQHIKTLAQ 397
Cdd:smart00150    3 FLRDADELEAWLEEKEQ--LLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 24654948     398 RLDRTWKDFAAGLDERTAVLQ 418
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 28-156 7.02e-08

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: 53.49  E-value: 7.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948     28 GGPLLCFPATPRRDRLKP-EDLRRLLSYLISIPSDAAKNLGFTVIIDMRGNGncSTN------VKTILKVLQEHFSANIH 100
Cdd:pfam13716    1 GRPVLVFISKLLPSRPASlDDLDRLLFYLLKTLSEKLKGKPFVVVVDHTGVT--SENfpslsfLKKAYDLLPRAFKKNLK 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24654948    101 NVVIIKPDNFWqkqRASISSHKY-----KFETTTVSIESLNKI---VESHQLTGDFEGQQLYDH 156
Cdd:pfam13716   79 AVYVVHPSTFL---RTFLKTLGSllgskKLRKKVHYVSSLSELwegIDREQLPTELPGVLSYDE 139
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 1941-2111 8.88e-08

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


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 57.98  E-value: 8.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 1941 KRQCVFAELMSTEEAYVQDLHEIVNGYMTEINNTNSdipMPEDLKGGKMKLVFNNIKDIYEWHRDFfLRALRNCQK-SPA 2019
Cdd:COG5422  484 KRQEAIYEVIYTERDFVKDLEYLRDTWIKPLEESNI---IPENARRNFIKHVFANINEIYAVNSKL-LKALTNRQClSPI 559

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 2020 --DLGPLIKRSATKFALYYTYCSNKPLSEYIV----SAHYQYF----DSIRQKLGHRLDLSNLIIKPVQRITKYELLIKE 2089
Cdd:COG5422  560 vnGIADIFLDYVPKFEPFIKYGASQPYAKYEFerekSVNPNFArfdhEVERLDESRKLELDGYLTKPTTRLARYPLLLEE 639

                        170       180
                 ....*....|....*....|...
gi 24654948 2090 IIKAT-EGAGLYKEVPMLQEAYQ 2111
Cdd:COG5422  640 VLKFTdPDNPDTEDIPKVIDMLR 662
PH_puratrophin-1 cd13242
Puratrophin-1 pleckstrin homology (PH) domain; Puratrophin-1 (also called Purkinje cell ...
 2129-2247 8.95e-07

Puratrophin-1 pleckstrin homology (PH) domain; Puratrophin-1 (also called Purkinje cell atrophy-associated protein 1 or PLEKHG4/Pleckstrin homology domain-containing family G member 4) contains a spectrin repeat, a RhoGEF (DH) domain, and a PH domain. It is thought to function in intracellular signaling and cytoskeleton dynamics at the Golgi. Puratrophin-1 is expressed in kidney, Leydig cells in the testis, epithelial cells in the prostate gland and Langerhans islet in the pancreas. A single nucleotide substitution in the puratrophin-1 gene were once thought to result in autosomal dominant cerebellar ataxia (ADCA), but now it has been demonstrated that this ataxia is a result of defects in the BEAN gene. Puratrophin contains a domain architecture similar to that of Dbl family members Dbs and Trio. Dbs is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a RhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Trio is a multidomain signaling protein that contains two RhoGEF(DH)-PH domains in tandem. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270062  Cd Length: 136  Bit Score: 50.37  E-value: 8.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 2129 SLQDFDGEITAQGSLLMQGPMncVVDAAQKHRELQVFLFQQIIIFADIEKTKNqyASPIFKYRSHIQLNHMQMKE-LGD- 2206
Cdd:cd13242   15 SIRGCDVNLKEQGQLLRQDEF--LVWQGRKKCLRHVFLFEDLILFSKPKKTPG--GKDVYIYKHSIKTSDIGLTEnVGDs 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 24654948 2207 -CRFQIRSTDPKIPEmTIICQAASQENYAGWRDMLNKILQQQ 2247
Cdd:cd13242   91 gLKFEIWFRRRKARD-TYILQATSPEIKQAWTSDIAKLLWKQ 131
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 167-418 3.99e-06

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: 50.14  E-value: 3.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  167 EDFFWQAGDMADRIDDLQEDLNRNDFAEDVPLARHAIDHHNEMRKKITKL--PIEDLDMQGKKLLAKinamappggqapt 244
Cdd:cd00176    3 QQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHeeRVEALNELGEQLIEE------------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  245 nsggpdmdsgpssagqqsqpsqqsrsvggNPDMSAAVNKALRQIELIHtgqEKLLMLWQHKKVKLDQCFQWRLFEQDCEK 324
Cdd:cd00176   70 -----------------------------GHPDAEEIQERLEELNQRW---EELRELAEERRQRLEEALDLQQFFRDADD 117

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  325 MFDWIlhNRDVFQMSYVEIGHNYSVAKSLQDEHQKFAVASMNVSVNIDRILAVAARLIESQHYAAQ-HIKTLAQRLDRTW 403
Cdd:cd00176  118 LEQWL--EEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADeEIEEKLEELNERW 195

                        250
                 ....*....|....*
gi 24654948  404 KDFAAGLDERTAVLQ 418
Cdd:cd00176  196 EELLELAEERQKKLE 210
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 1487-1581 2.48e-05

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: 45.23  E-value: 2.48e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    1487 TKQIIRKGRERRVFLFELYLLFAKEVKESNVVKYQFKSKLMTTDMGITEHIEGDETK--FAVWTGrspmlSDCRIVLKAT 1564
Cdd:smart00233   11 SGGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYKPKGSIDLSGCTVREAPDPDSSKKPhcFEIKTS-----DRKTLLLQAE 85

                            90
                    ....*....|....*..
gi 24654948    1565 SLETKQIWVKKLREVMQ 1581
Cdd:smart00233   86 SEEEREKWVEALRKAIA 102
PH1_Kalirin_Trio_like cd13240
Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; ...
 2130-2246 2.59e-05

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: 45.84  E-value: 2.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 2130 LQDFDGEITAQGSLLMQGPMNcVVDAAQ---KHRELQVFLFQQIIIFAdiEKTKNQYASPIFKYRSHIQLNHMQMKEL-- 2204
Cdd:cd13240    2 LEGCDEDLDSLGEVILQDSFQ-VWDPKQlirKGRERHVFLFELCLVFS--KEVKDSNGKSKYIYKSRLMTSEIGVTEHie 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 24654948 2205 GD-CRFQIRSTDPKIPEMTIICQAASQENYAGWRDMLNKILQQ 2246
Cdd:cd13240   79 GDpCKFALWTGRVPTSDNKIVLKASSLEVKQTWVKKLREVIQE 121
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 314-418 2.83e-05

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 45.00  E-value: 2.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    314 QWRLFEQDCEKMFDWIlhNRDVFQMSYVEIGHNYSVAKSLQDEHQKFaVASMNV-SVNIDRILAVAARLIESQHYAAQHI 392
Cdd:pfam00435    2 LLQQFFRDADDLESWI--EEKEALLSSEDYGKDLESVQALLKKHKAL-EAELAAhQDRVEALNELAEKLIDEGHYASEEI 78

                           90       100
                   ....*....|....*....|....*.
gi 24654948    393 KTLAQRLDRTWKDFAAGLDERTAVLQ 418
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLE 104
SPEC smart00150
Spectrin repeats;
566-666 2.49e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 42.32  E-value: 2.49e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948     566 FQEDVKQVLDWLKNHgEVFLRkNTGIGRNFHKARVYQTSHDNFENVAQNTYSNAQKLLAAADELARSGEADPNEIYSVAR 645
Cdd:smart00150    3 FLRDADELEAWLEEK-EQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                            90       100
                    ....*....|....*....|.
gi 24654948     646 ELELQVGSFAERVEQRRRRLD 666
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 622-908 2.61e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 2.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    622 LLAAADELARSGEADPNEIYSVARELE---LQVGSFAERVEQRRRRLDmavifythekDVTAWIDKLRTD----VSTD-- 692
Cdd:TIGR02169  228 LLKEKEALERQKEAIERQLASLEEELEkltEEISELEKRLEEIEQLLE----------ELNKKIKDLGEEeqlrVKEKig 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    693 ETRLSQENLEGIERILQQYQRDQQESSVNvcltTISQGEALLQEMRSLEyadntGSIAALEATLEKLNkqkvelEELWSA 772
Cdd:TIGR02169  298 ELEAEIASLERSIAEKERELEDAEERLAK----LEAEIDKLLAEIEELE-----REIEEERKRRDKLT------EEYAEL 362

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    773 RKFRADLILRLRYFERDARllsvqmeMWSEELqhadlsRDYQKA-EQLIRMHNESVTEIQNATYEVVQQGQDLLQLfENA 851
Cdd:TIGR02169  363 KEELEDLRAELEEVDKEFA-------ETRDEL------KDYREKlEKLKREINELKRELDRLQEELQRLSEELADL-NAA 428

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 24654948    852 gfISMADATHTA-QARIEYLLDFLREREIDLEEMSeAKRAKLEQavQLCQFQNDANQV 908
Cdd:TIGR02169  429 --IAGIEAKINElEEEKEDKALEIKKQEWKLEQLA-ADLSKYEQ--ELYDLKEEYDRV 481
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 568-840 6.33e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 6.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    568 EDVKQVLDWLKNHGEVFLRKNTGIGRNFHKARVYQTSHDNFENVAQNTYSNAQKLLAAADELARSGEADPNEIYSVAREL 647
Cdd:TIGR02168  701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    648 ELQVGSFAERVEQRRRRLdmavifythekdvtawiDKLRTDVSTDETRLSQENLEgieriLQQYQRDQQESSVNVCLTTI 727
Cdd:TIGR02168  781 EAEIEELEAQIEQLKEEL-----------------KALREALDELRAELTLLNEE-----AANLRERLESLERRIAATER 838

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    728 SQGEALLQ-EMRSLEYADNTGSIAALEATLEKLNKQKVELEELwSARKFRADLILRLRYFERDARLLSV-----QMEMWS 801
Cdd:TIGR02168  839 RLEDLEEQiEELSEDIESLAAEIEELEELIEELESELEALLNE-RASLEEALALLRSELEELSEELRELeskrsELRREL 917

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 24654948    802 EELQH--ADLSRDYQKAEQLIRMHNESVTEIQNATYEVVQQ 840
Cdd:TIGR02168  918 EELREklAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEA 958
SH3_p47phox_like cd11856
Src homology 3 domains of the p47phox subunit of NADPH oxidase and similar domains; This ...
 1647-1707 1.18e-03

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


Pssm-ID: 212790 [Multi-domain]  Cd Length: 53  Bit Score: 38.77  E-value: 1.18e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24654948 1647 VVADYIAtSGSNELSVSKGQQVEIVEpptAGEPDFCLVRLNPqhddaavQEGLVPVSVLKP 1707
Cdd:cd11856    4 AIADYEA-QGDDEISLQEGEVVEVLE---KNDSGWWYVRKGD-------KEGWVPASYLEP 53
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 645-898 1.81e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  645 RELELQVGSFAERVEQRRRRLDMAvifythekdvTAWIDKLRTDVSTDETRLSQENLEgIERILQQYQRDQQEssvnvcL 724
Cdd:COG1196  235 RELEAELEELEAELEELEAELEEL----------EAELAELEAELEELRLELEELELE-LEEAQAEEYELLAE------L 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  725 TTISQGEALLQEMRsleyADNTGSIAALEATLEKLNKQKVELEELwsarkfRADLILRLRyfERDARLLSVQMEMWSEEL 804
Cdd:COG1196  298 ARLEQDIARLEERR----RELEERLEELEEELAELEEELEELEEE------LEELEEELE--EAEEELEEAEAELAEAEE 365

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  805 QHADLSRDYQKAEQLIRMHNESVTEIQNATYEVVQQGQDLLQLFENAgFISMADATHTAQARIEYLLDFLREREIDLEEM 884
Cdd:COG1196  366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL-LERLERLEEELEELEEALAELEEEEEEEEEAL 444

                        250
                 ....*....|....
gi 24654948  885 SEAKRAKLEQAVQL 898
Cdd:COG1196  445 EEAAEEEAELEEEE 458
PH_unc89 cd13325
unc89 pleckstrin homology (PH) domain; unc89 is a myofibrillar protein. unc89-B the largest ...
 1472-1578 3.12e-03

unc89 pleckstrin homology (PH) domain; unc89 is a myofibrillar protein. unc89-B the largest isoform is composed of 53 immunoglobulin (Ig) domains, 2 Fn3 domains, a triplet of SH3, DH and PH domains at its N-terminus, and 2 protein kinase domains (PK1 and PK2) at its C-terminus. unc-89 mutants display disorganization of muscle A-bands, and usually lack M-lines. The COOH-terminal region of obscurin, the human homolog of unc89, interacts via two specific Ig-like domains with the NH(2)-terminal Z-disk region of titin, a protein that connects the Z line to the M line in the sarcomere and contributes to the contraction of striated muscle. obscurin is also thought to be involved in Ca2+/calmodulin via its IQ domains, as well as G protein-coupled signal transduction in the sarcomere via its RhoGEF/DH domain. The DH-PH region of OBSCN and unc89, the C. elegans homolog, has exchange activity for RhoA and Rho-1 respectively, but not for the small GTPases homologous to Cdc42 or Rac. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270134  Cd Length: 114  Bit Score: 39.64  E-value: 3.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 1472 KLGEVVLQDAFQAWDTKQiirKGRERRVFLFELYLLFAKeVKESNVVK--YQFKSKLMTTDMGITEHiEGDETKFaVWTG 1549
Cdd:cd13325    5 KLGRLLRHDWFTVTDGEG---KAKERYLFLFKSRILITK-VRRISEDRsvFILKDIIRLPEVNVKQH-PDDERTF-ELQP 78

                         90       100
                 ....*....|....*....|....*....
gi 24654948 1550 RSPMLSDCRIVLKATSLETKQIWVKKLRE 1578
Cdd:cd13325   79 KLPAFGILPIDFKAHKDEIKDYWLNEIEE 107
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 690-917 3.42e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 3.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  690 STDETRLSQENLEGIERILQQYQRDQQEssvnvcltTISQGEALLQEMRSLEYA---------DNTGSIAALEATLEKLN 760
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELAA--------LKKEEKALLKQLAALERRiaalarrirALEQELAALEAELAELE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948  761 KQKVELEELWSARkfRADLILRLRYFERDARLLSVQMEMWSEELqhADLSRDYQKAEQLIRMHNESVTEIQNATYEVVQQ 840
Cdd:COG4942   90 KEIAELRAELEAQ--KEELAELLRALYRLGRQPPLALLLSPEDF--LDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24654948  841 GQDLLQLFEnagfiSMADATHTAQARIEYLLDFLREREIDLEEMSEAKRAKLEQAVQLCQFQNDANQVISWIRNGEA 917
Cdd:COG4942  166 RAELEAERA-----ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 1256-1430 3.50e-03

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


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 42.57  E-value: 3.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 1256 DPTLEAKLNSSNKENKEINEEKRKSARRKEFIMAELMQTERAYVNDLATCIKCFLEEFRAGKSVPSAlIGQEDV--IFGN 1333
Cdd:COG5422  457 DKFDEEKNLWTLSVPKEVWESLPKQEIKRQEAIYEVIYTERDFVKDLEYLRDTWIKPLEESNIIPEN-ARRNFIkhVFAN 535

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 1334 IKEIHHFHQKIF--LRELEKYETMPEDVGHCFVTWASKFDMYVHYCKNKPTSNNLLVQHGGS------FFEELQR-RLEV 1404
Cdd:COG5422  536 INEIYAVNSKLLkaLTNRQCLSPIVNGIADIFLDYVPKFEPFIKYGASQPYAKYEFEREKSVnpnfarFDHEVERlDESR 615

                        170       180
                 ....*....|....*....|....*.
gi 24654948 1405 DHPLPAYLIKPVQRITKYQLLLKDLL 1430
Cdd:COG5422  616 KLELDGYLTKPTTRLARYPLLLEEVL 641
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 1487-1576 4.14e-03

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: 38.68  E-value: 4.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 1487 TKQIIRKGRERRVFLFELYLLFAKEVKESnvvKYQFKSKL-MTTDMGITEHIEGD-ETKFAVWTgrspmLSDCRIVLKAT 1564
Cdd:cd00821    9 GGGGLKSWKKRWFVLFEGVLLYYKSKKDS---SYKPKGSIpLSGILEVEEVSPKErPHCFELVT-----PDGRTYYLQAD 80

                         90
                 ....*....|..
gi 24654948 1565 SLETKQIWVKKL 1576
Cdd:cd00821   81 SEEERQEWLKAL 92
PH_Dbs cd01227
DBL's big sister protein pleckstrin homology (PH) domain; Dbs (also called MCF2-transforming ...
 2129-2247 5.30e-03

DBL's big sister protein pleckstrin homology (PH) domain; Dbs (also called MCF2-transforming sequence-like protein 2) is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a rhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269934 [Multi-domain]  Cd Length: 126  Bit Score: 39.10  E-value: 5.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948 2129 SLQDFDGEITAQGSLLMQGPMNCVVDAAQKHR---------ELQVFLFQQIIIFAdiEKTKNQYASPIFKYRSHIQLNHM 2199
Cdd:cd01227    1 AITGYDGNLGDLGKLLMQGSFNVWTEHKKGHTkklarfkpmQRHIFLYEKAVLFC--KKRGENGEAPSYSYKNSLNTTAV 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 24654948 2200 QMKE--LGDC-RFQIRSTDpkiPEMTIICQAASQENYAGWRDMLNKILQQQ 2247
Cdd:cd01227   79 GLTEnvKGDTkKFEIWLNG---REEVFIIQAPTPEIKAAWVKAIRQVLLSQ 126
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 729-1025 5.53e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 5.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    729 QGEALLQEMRSL--EYADNTGSIAALEATLEKLNKQKVELEELWSarkfradlILRLRYFERDARLLSVQmemwsEELQh 806
Cdd:TIGR02168  226 ELALLVLRLEELreELEELQEELKEAEEELEELTAELQELEEKLE--------ELRLEVSELEEEIEELQ-----KELY- 291

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    807 aDLSRDYQKAEQLIRMHNES----VTEIQNATYEVVQQGQDLLQLFENAGfiSMADATHTAQARIEYLLDFLREREIDLE 882
Cdd:TIGR02168  292 -ALANEISRLEQQKQILRERlanlERQLEELEAQLEELESKLDELAEELA--ELEEKLEELKEELESLEAELEELEAELE 368

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    883 EMSEAKRaklEQAVQLCQFQNDANQViswirngeamlvasfvtpnsLQEAEQLRKghEQFQIAIEKTHTSAVQVKYRADA 962
Cdd:TIGR02168  369 ELESRLE---ELEEQLETLRSKVAQL--------------------ELQIASLNN--EIERLEARLERLEDRRERLQQEI 423

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24654948    963 LINANHYDPLSIDEISDDVTKKWQQLVTYAEERHKLVTASINFYKTAEQVCSVLDSLEREYKR 1025
Cdd:TIGR02168  424 EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 682-934 6.17e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 6.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    682 IDKLRTDVSTDETRLSQENLEGIErilQQYQRDQQESSVNVCLTTISQGEALLQEmRSLEYADNTGSIAALEATLEKLNK 761
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEE---LSRQISALRKDLARLEAEVEQLEERIAQ-LSKELTELEAEIEELEERLEEAEE 775

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    762 QKVELEELW-----SARKFRADL--------ILRLRYFERDARLLSVQMEMWSEELQHADLSRDYQKAEQLIRMHNESVT 828
Cdd:TIGR02168  776 ELAEAEAEIeeleaQIEQLKEELkalrealdELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948    829 EIQNATYEVVQQGQDLLQLFENAGFISMADATHTAQARIEYL-----LDFLREREIDLEEMSEAKRAKLEQAV-QLCQFQ 902
Cdd:TIGR02168  856 SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEelseeLRELESKRSELRRELEELREKLAQLElRLEGLE 935

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 24654948    903 NDANQVIS-----WIRNGEAMLVASFVTPNSLQEAEQ 934
Cdd:TIGR02168  936 VRIDNLQErlseeYSLTLEEAEALENKIEDDEEEARR 972
CRAL_TRIO pfam00650
CRAL/TRIO domain;
23-107 6.34e-03

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 39.55  E-value: 6.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654948     23 GRDRRGGPLLCFpaTPRRDRLKPEDLRRLLSYLISI------PSDAAKNLGFTVIIDMRG------NGNCSTNVKTILKV 90
Cdd:pfam00650    8 GRDKEGRPVLYL--RLGRHDPKKSSEEELVRFLVLVlerallLMPEGQVEGLTVIIDLKGlslsnmDWWSISLLKKIIKI 85

                           90
                   ....*....|....*..
gi 24654948     91 LQEHFSANIHNVVIIKP 107
Cdd:pfam00650   86 LQDNYPERLGKILIVNA 102
PH_10 pfam15411
Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.
 2140-2182 9.27e-03

Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.


Pssm-ID: 464707  Cd Length: 120  Bit Score: 38.34  E-value: 9.27e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 24654948   2140 QGSLLMQGPMNcVVDAAQKHRELQVFLFQQIIIFADIEKTKNQ 2182
Cdd:pfam15411    2 FGELLLHDKLT-VGKDSDSEREYHVYLFEKILLCCKEISPKKK 43
 
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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