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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512388686 530 REQEARGRDLLAVEAVRGCEIDLKEQGQLLHRDPFTVICGRKKCLRHVFLFEHLLLFSKLKGPEGGSEMFVYKQAFKTAD 609
Cdd:cd13242    1 RFQLRHGNDLLAMDSIRGCDVNLKEQGQLLRQDEFLVWQGRKKCLRHVFLFEDLILFSKPKKTPGGKDVYIYKHSIKTSD 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 512388686 610 MGLTENIGDSGLCFELWFRRRRAREAYTLQATSPEIKLKWTSSIAQLLWRQAAHNK 665
Cdd:cd13242   81 IGLTENVGDSGLKFEIWFRRRKARDTYILQATSPEIKQAWTSDIAKLLWKQAIRNR 136

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512388686  72 LRRLQQVLQWLSGpgEEQLASFAMPGDTLSALQETELRFRAFSAEVQER------LAQAREALALEENATSQKV---LDI 142
Cdd:cd00176    6 LRDADELEAWLSE--KEELLSSTDYGDDLESVEALLKKHEALEAELAAHeerveaLNELGEQLIEEGHPDAEEIqerLEE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512388686 143 FEQRLEQVESG-------LHRALRLQRFFQQAHE---WVDEGFARLAGAGPGR--EAVLAAL----ALRRAPEPSAGTFQ 206
Cdd:cd00176   84 LNQRWEELRELaeerrqrLEEALDLQQFFRDADDleqWLEEKEAALASEDLGKdlESVEELLkkhkELEEELEAHEPRLK 163

                        170       180       190
                 ....*....|....*....|....*....|....
gi 512388686 207 EMRALALDLGSPAALREWGRCQARCQELERRIQQ 240
Cdd:cd00176  164 SLNELAEELLEEGHPDADEEIEEKLEELNERWEE 197

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512388686 530 REQEARGRDLLAVEAVRGCEIDLKEQGQLLHRDPFTVICGRKKCLRHVFLFEHLLLFSKLKGPEGGSEMFVYKQAFKTAD 609
Cdd:cd13242    1 RFQLRHGNDLLAMDSIRGCDVNLKEQGQLLRQDEFLVWQGRKKCLRHVFLFEDLILFSKPKKTPGGKDVYIYKHSIKTSD 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 512388686 610 MGLTENIGDSGLCFELWFRRRRAREAYTLQATSPEIKLKWTSSIAQLLWRQAAHNK 665
Cdd:cd13242   81 IGLTENVGDSGLKFEIWFRRRKARDTYILQATSPEIKQAWTSDIAKLLWKQAIRNR 136

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512388686 372 QQRLVSELIACEQDYVATL-------SEPVPPPGPELTPELRgtwAAALSARERLRSFHRTHFLRELQGCA---THPLRI 441
Cdd:cd00160    1 RQEVIKELLQTERNYVRDLkllvevfLKPLDKELLPLSPEEV---ELLFGNIEEIYEFHRIFLKSLEERVEewdKSGPRI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512388686 442 GACFLRHGDQFSLYAQYVKHRHK----LENGLAALSPLSKGSMEAGPY-----LPRALQQPLEQLTRYGRLLEELLREAg 512
Cdd:cd00160   78 GDVFLKLAPFFKIYSEYCSNHPDalelLKKLKKFNKFFQEFLEKAESEcgrlkLESLLLKPVQRLTKYPLLLKELLKHT- 156

                        170
                 ....*....|....*....
gi 512388686 513 PELSSECRALGAAVQLLRE 531
Cdd:cd00160  157 PDGHEDREDLKKALEAIKE 175

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512388686   555 QGQLLHRDPFTvicGRKKCLRHVFLFEHLLLFSKLKGPEGGSEmfvYKQAFKTADMGLTENIGDSGL----CFELWFRRR 630
Cdd:smart00233   4 EGWLYKKSGGG---KKSWKKRYFVLFNSTLLYYKSKKDKKSYK---PKGSIDLSGCTVREAPDPDSSkkphCFEIKTSDR 77

                           90       100
                   ....*....|....*....|....*..
gi 512388686   631 RAreaYTLQATSPEIKLKWTSSIAQLL 657
Cdd:smart00233  78 KT---LLLQAESEEEREKWVEALRKAI 101

PH domain; PH stands for pleckstrin homology.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512388686  555 QGQLLHRDPFTVIcGRKKclRHVFLFEHLLLFSKLKGPEGGSEMfVYKQAFKTADMGLTENIGDSG--LCFELWFRRRRA 632
Cdd:pfam00169   4 EGWLLKKGGGKKK-SWKK--RYFVLFDGSLLYYKDDKSGKSKEP-KGSISLSGCEVVEVVASDSPKrkFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|.
gi 512388686  633 REAYTLQATSPEIKLKWTSSI 653
Cdd:pfam00169  80 KRTYLLQAESEEERKDWIKAI 100

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512388686 530 REQEARGRDLLAVEAVRGCEIDLKEQGQLLHRDPFTVICGRKKCLRHVFLFEHLLLFSKLKGPEGGSEMFVYKQAFKTAD 609
Cdd:cd13242    1 RFQLRHGNDLLAMDSIRGCDVNLKEQGQLLRQDEFLVWQGRKKCLRHVFLFEDLILFSKPKKTPGGKDVYIYKHSIKTSD 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 512388686 610 MGLTENIGDSGLCFELWFRRRRAREAYTLQATSPEIKLKWTSSIAQLLWRQAAHNK 665
Cdd:cd13242   81 IGLTENVGDSGLKFEIWFRRRKARDTYILQATSPEIKQAWTSDIAKLLWKQAIRNR 136

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512388686 555 QGQLLHRDPFTVI----CGRKKCL-RHVFLFEHLLLFSKL--KGPEGGSEMFVYKQAFKTADMGLTENIGDSGLCFELWF 627
Cdd:cd13241   14 QGKLLLQGTLLVSepsaGLLQKGKeRRVFLFEQIIIFSEIlgKKTQFSNPGYIYKNHIKVNKMSLEENVDGDPLRFALKS 93

                         90       100       110
                 ....*....|....*....|....*....|....
gi 512388686 628 R-RRRAREAYTLQATSPEIKLKWTSSIAQLLWRQ 660
Cdd:cd13241   94 RdPNNPSETFILQAASPEVRQEWVDTINQILDTQ 127

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512388686  376 VSELIACEQDYVATLS-------EPVPPPGPELTPELR---GTWaaalsarERLRSFHRTHFLRELQGCATHPLRIGACF 445
Cdd:pfam00621   2 IKELLQTERSYVRDLEilvevflPPNSKPLSESEEEIKtifSNI-------EEIYELHRQLLLEELLKEWISIQRIGDIF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512388686  446 LRHGDQFSLYAQYVKHRhklENGLAALSPLSKGSMEAGPYLPRALQQPLEQ--------------LTRYGRLLEELLReA 511
Cdd:pfam00621  75 LKFAPGFKVYSTYCSNY---PKALKLLKKLLKKNPKFRAFLEELEANPECRgldlnsflikpvqrIPRYPLLLKELLK-H 150

                         170       180
                  ....*....|....*....|
gi 512388686  512 GPELSSECRALGAAVQLLRE 531
Cdd:pfam00621 151 TPPDHPDYEDLKKALEAIKE 170

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512388686 548 CEIDLKEQGQLLHRDPFTVICgrKKCLRHVFLFEHLLLFSKLKGPEGgsemFVYKQAFKTADMGLTENIGDSGLCFE-LW 626
Cdd:cd13243   42 EGPELTTYGDLVLEGTFRMAG--AKNERLLFLFDKMLLITKKREDGI----LQYKTHIMCSNLMLSESIPKEPLSFQvLP 115

                         90       100       110
                 ....*....|....*....|....*....|.
gi 512388686 627 FRRRRAReaYTLQATSPEIKLKWTSSIAQLL 657
Cdd:cd13243  116 FDNPKLQ--YTLQAKNQEQKRLWTQEIKRLI 144

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512388686   375 LVSELIACEQDYVATL-------SEPVPPPGPELTPELRGTWAAALsarERLRSFHRThFLRELQGC----ATHPLRIGA 443
Cdd:smart00325   1 VLKELLQTERNYVRDLkllvevfLKPLKKELKLLSPNELETLFGNI---EEIYEFHRD-FLDELEERieewDDSVERIGD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512388686   444 CFLRHGDQFSLYAQYVKHR---HKLENGLAALSPLSKGSMEAGP-------YLPRALQQPLEQLTRYGRLLEELLREagP 513
Cdd:smart00325  77 VFLKLEEFFKIYSEYCSNHpdaLELLKKLKKNPRFQKFLKEIESspqcrrlTLESLLLKPVQRLTKYPLLLKELLKH--T 154

                          170
                   ....*....|....*....
gi 512388686   514 ELSSECR-ALGAAVQLLRE 531
Cdd:smart00325 155 PEDHEDReDLKKALKAIKE 173

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512388686 556 GQLLHRDPFTVICGRKKC-LRHVFLFEHLLLFSKLKGPEGGSEMFVYKQAFKTADMGLtENIGDSGLCFELWFRRRRAR- 633
Cdd:cd13325    7 GRLLRHDWFTVTDGEGKAkERYLFLFKSRILITKVRRISEDRSVFILKDIIRLPEVNV-KQHPDDERTFELQPKLPAFGi 85

                         90       100
                 ....*....|....*....|..
gi 512388686 634 EAYTLQATSPEIKLKWTSSIAQ 655
Cdd:cd13325   86 LPIDFKAHKDEIKDYWLNEIEE 107

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512388686  72 LRRLQQVLQWLSGpgEEQLASFAMPGDTLSALQETELRFRAFSAEVQER------LAQAREALALEENATSQKV---LDI 142
Cdd:cd00176    6 LRDADELEAWLSE--KEELLSSTDYGDDLESVEALLKKHEALEAELAAHeerveaLNELGEQLIEEGHPDAEEIqerLEE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512388686 143 FEQRLEQVESG-------LHRALRLQRFFQQAHE---WVDEGFARLAGAGPGR--EAVLAAL----ALRRAPEPSAGTFQ 206
Cdd:cd00176   84 LNQRWEELRELaeerrqrLEEALDLQQFFRDADDleqWLEEKEAALASEDLGKdlESVEELLkkhkELEEELEAHEPRLK 163

                        170       180       190
                 ....*....|....*....|....*....|....
gi 512388686 207 EMRALALDLGSPAALREWGRCQARCQELERRIQQ 240
Cdd:cd00176  164 SLNELAEELLEEGHPDADEEIEEKLEELNERWEE 197