Calponin family repeat;

                          10        20
                  ....*....|....*....|....*
gi 1958752335 123 IGLQMGTNKCASQAGMTAYGTRRHL 147
Cdd:pfam00402   1 IGLQMGTNKGASQSGMTAFGAVRHI 25

Calponin family repeat;

                          10        20
                  ....*....|....*....|....*
gi 1958752335 202 ISLQMGTNKVASQKGMSVYGLGRQV 226
Cdd:pfam00402   1 IGLQMGTNKGASQSGMTAFGAVRHI 25

Calponin [Cytoskeleton];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752335  11 LKDGIILCELINKLQPGSVKkVNESSLNWPQLENIGNFIKAIQAYGMKPHDIFEANDLFENGNMTQVQTTLVALAGLAKT 90
Cdd:COG5199    40 LKDGVRLCRILNEASPLDIK-YKESKMPFVQMENISSFINGLKKLRVPEYELFQTNDLFEAKDLRQVVICLYSLSRYAQK 118

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958752335  91 KGFHTTIDIGVKYAEKQTRRFDEGK-LKAGQSVIGLQMGTNKCASQAG-MTAYGTRRHL 147
Cdd:COG5199   119 ERMFSGPFLGPHLATKKPRVFSSQEvLDRSKGAIHLQYGYSDLSEQSTeKGASNVRRDL 177

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752335    5 TNFQLGLKDGIILCELINKLQPGSV--KKVNESSLNWPQLENIGNFIKAIQAYGMKPhDIFEANDLFENGNMT-QVQTTL 81
Cdd:smart00033  20 TNFSSDLKDGVALCALLNSLSPGLVdkKKVAASLSRFKKIENINLALSFAEKLGGKV-VLFEPEDLVEGPKLIlGVIWTL 98

                   ...
gi 1958752335   82 VAL 84
Cdd:smart00033  99 ISL 101

Calponin family repeat;

                          10        20
                  ....*....|....*....|....*
gi 1958752335 163 ISLQMGTNKGASQAGMSAPGTRRDI 187
Cdd:pfam00402   1 IGLQMGTNKGASQSGMTAFGAVRHI 25

calponin homology (CH) domain found in the calponin family; Calponin is an actin filament-associated regulatory protein expressed in smooth muscle and many types of non-muscle cells. There are three calponin isoforms, calponin-1, -2, -3. All of them are actin-binding proteins with functions in inhibiting actin-activated myosin ATPase and stabilizing the actin cytoskeleton. Calponin-1 is specifically expressed in smooth muscle cells and plays a role in fine-tuning smooth muscle contractility. Calponin-2 is expressed in both smooth muscle and non-muscle cells and regulates multiple actin cytoskeleton-based functions. Calponin-3 is expressed in the brain and participates in actin cytoskeleton-based activities in embryonic development and myogenesis. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752335   1 MGIGTNFQLGLKDGIILCELINKLQPGSVKKVNESSLNWPQLENIGNFIKAIQAYGMKPHDIFEANDLFENGNMTQVQTT 80
Cdd:cd21211    18 LSIGPNFQKGLKDGIILCELINKLQPGSVKKINESMQNWHQLENIGNFIKAIVSYGMKPHDIFEANDLFENGNMTQVQVT 97

                          90
                  ....*....|.
gi 1958752335  81 LVALAGLAKTK 91
Cdd:cd21211    98 LLALAGKAKTK 108

calponin homology (CH) domain found in calponin-1 and similar proteins; Calponin-1 (CNN1), also called basic calponin, or smooth muscle calponin H1, is a thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C, and tropomyosin. Calponin-1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752335   3 IGTNFQLGLKDGIILCELINKLQPGSVKKVNESSLNWPQLENIGNFIKAIQAYGMKPHDIFEANDLFENGNMTQVQTTLV 82
Cdd:cd21282    20 IGDNFMDGLKDGVILCELINKLQPGSVRKINESTQNWHKLENIGNFIKAIMHYGVKPHDIFEANDLFENTNHTQVQSTLI 99

                  ....*....
gi 1958752335  83 ALAGLAKTK 91
Cdd:cd21282   100 ALASMAKTK 108

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752335   5 TNFQLGLKDGIILCELINKLQPGSVKKVNESSLN-WPQLENIGNFIKAIQAYGMKPHDIFEANDLFENGNMTQVQTTLVA 83
Cdd:cd00014    21 TDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSpFKKRENINLFLNACKKLGLPELDLFEPEDLYEKGNLKKVLGTLWA 100

                  ..
gi 1958752335  84 LA 85
Cdd:cd00014   101 LA 102

calponin homology (CH) domain found in the transgelin family; The transgelin (TAGLN) family includes transgelin, transgelin-2 and transgelin-3. Transgelin, also called 22 kDa actin-binding protein, protein WS3-10, or smooth muscle protein 22-alpha (SM22-alpha), acts as an actin cross-linking/gelling protein that may be involved in calcium interactions and in regulating contractile properties of the cell. Transgelin-2, also called epididymis tissue protein Li 7e, or SM22-alpha homolog, acts as an actin-binding protein that induces actin gelation and regulates actin cytoskeleton. It may participate in the development and progression of multiple cancers. Transgelin-3, also called neuronal protein 22 (NP22), or neuronal protein NP25, may have a role in alcohol-related adaptations and may mediate regulatory signal transduction pathways in neurons. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752335   5 TNFQLGLKDGIILCELINKLQP---GSVKKVNESSLNWPQLENIGNFIKAIQAYGMKPHDIFEANDLFENGNMTQVQTTL 81
Cdd:cd21209    28 LGFQKWLKDGTVLCKLINSLYPegsKPVKKIQSSKMAFKQMEQISQFLKAAEDYGVRTTDIFQTVDLWEGKDMAAVQRTL 107

                          90
                  ....*....|
gi 1958752335  82 VALAGLAKTK 91
Cdd:cd21209   108 MALGSLAVTK 117

calponin homology (CH) domain found in transgelin-3; Transgelin-3, also called neuronal protein 22 (NP22), or neuronal protein NP25, may have a role in alcohol-related adaptations and may mediate regulatory signal transduction pathways in neurons. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752335   6 NFQLGLKDGIILCELINKLQPGS---VKKVNESSLNWPQLENIGNFIKAIQAYGMKPHDIFEANDLFENGNMTQVQTTLV 82
Cdd:cd21281    29 NFQKWLMDGTILCRLINSLYPPGkepIKKISETKMAFKQMEKISQFLQAAEAYGVITTDIFQTVDLWEGKDMAAVQRTLM 108

                  ....*....
gi 1958752335  83 ALAGLAKTK 91
Cdd:cd21281   109 ALGSVAVTK 117

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752335   5 TNFQLGLKDGIILCELINKLQPGSVKKVNESSLNWPQLENIGNFIK-AIQAYGMKPHDIfEANDLFENGNMtQVQTTLVA 83
Cdd:pfam00307  25 TNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDvAEKKLGVPKVLI-EPEDLVEGDNK-SVLTYLAS 102

                  ....*..
gi 1958752335  84 LAGLAKT 90
Cdd:pfam00307 103 LFRRFQA 109

calponin homology (CH) domain found in transgelin; Transgelin, also called 22 kDa actin-binding protein, protein WS3-10, or smooth muscle protein 22-alpha (SM22-alpha), acts as an actin cross-linking/gelling protein that may be involved in calcium interactions and in regulating contractile properties of the cell. It may also contribute to replicative senescence. Transgelin contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752335   7 FQLGLKDGIILCELINKLQPGSVKKV----NESSLNWPQLENIGNFIKAIQAYGMKPHDIFEANDLFENGNMTQVQTTLV 82
Cdd:cd21279    30 FQVWLKNGVVLSKLVNSLYPDGSKPVkipdNPPSMVFKQMEQVAQFLKAAEDYGVVKTDMFQTVDLYEGKDMAAVQRTLV 109

                  ....*....
gi 1958752335  83 ALAGLAKTK 91
Cdd:cd21279   110 ALGSLAVTK 118

calponin homology (CH) domain found in the Pak Interactive eXchange factor family; Pak Interactive eXchange factor (PIX) proteins are Rho guanine nucleotide exchange factors (GEFs), which activate small GTPases by exchanging bound GDP for free GTP. They act as GEFs for both Cdc42 and Rac1, and have been implicated in cell motility, adhesion, neurite outgrowth, and cell polarity. Vertebrates contain two proteins from the PIX family, alpha-PIX and beta-PIX. Alpha-PIX, also called Rho guanine nucleotide exchange factor 6 (ARHGEF6), is localized in dendritic spines where it regulates spine morphogenesis. It controls dendritic length and spine density in the hippocampus. Mutations in the ARHGEF6 gene cause X-linked intellectual disability in humans. Beta-PIX, also called Rho guanine nucleotide exchange factor 7 (ARHGEF7), plays important roles in regulating neuroendocrine exocytosis, focal adhesion maturation, cell migration, synaptic vesicle localization, and insulin secretion. Both alpha-PIX and beta-PIX contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958752335  11 LKDGIILCELINKLQPGSVKKVNESSLNWPQ-LENIGNFIKAIQAYGMKPHDIFEANDLFENGNMTQVQTTLVAL 84
Cdd:cd21202    34 LKNGVVLCRLVNRLKPGTVEKIYDEPTTEEEcLYNFESFLKACQELGILAEEIFDPNDLYSGGNFQKVLSTLERL 108

calponin homology (CH) domain found in VAV proteins; VAV proteins function both as cytoplasmic guanine nucleotide exchange factors (GEFs) for Rho GTPases and as scaffold proteins, and they play important roles in cell signaling by coupling cell surface receptors to various effector functions. They play key roles in processes that require cytoskeletal reorganization including immune synapse formation, phagocytosis, cell spreading, and platelet aggregation, among others. Vertebrates have three VAV proteins (VAV1, VAV2, and VAV3). VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. This model corresponds to the CH domain, an actin-binding domain which is present as a single copy in VAV proteins.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958752335  11 LKDGIILCELINKLQPGSVKKVNESslNWPQ------LENIGNFIKAIQA-YGMKPHDIFEANDLFENGNMTQVQTTL 81
Cdd:cd21201    36 LRDGVLLCQLLNRLSPGSVDDREIN--LRPQmsqflcLKNIRTFLQACRTvFGLRSADLFEPEDLYDVTNFGKVIRTL 111

calponin homology (CH) domain found in the IQ motif containing GTPase activating protein family; Members of the IQ motif containing GTPase activating protein (IQGAP) family are associated with the Ras GTP-binding protein and act as essential regulators of cytoskeletal function. There are three known IQGAP family members: IQGAP1, IQGAP2, and IQGAP3. They are multi-domain molecules having a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeats, a single WW domain, four IQ motifs that mediate interactions with calmodulin, and a RasGAP related domain that binds active Rho family GTPases. IQGAP1 negatively regulates Ras family GTPases by stimulating their intrinsic GTPase activity. It lacks GAP activity. Both IQGAP1 and IQGAP2 specifically bind to Cdc42 and Rac1, but not to RhoA. Despite similarities to part of the sequence of RasGAP, neither IQGAP1 nor IQGAP2 interacts with Ras. IQGAP3 regulates the organization of the cytoskeleton under the regulation of Rac1 and Cdc42 in neuronal cells. The depletion of IQGAP3 is shown to impair neurite or axon outgrowth in neuronal cells with disorganized cytoskeleton.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752335   1 MGIGTNFQLGLKDGIILCELINKLQPGSV--KKVNESSLNWPQLENIGNFIKAIQAYGMKPHDIFEANDLFENGNMTQVQ 78
Cdd:cd21206    25 LPPTTEFEEELRNGVVLAKLANKFAPKLVplKKIYDVGLQFRHTDNINHFLRALKKIGLPKIFHFETTDLYEKKNIPKVI 104

                          90
                  ....*....|....
gi 1958752335  79 TTLVALAGLAKTKG 92
Cdd:cd21206   105 YCLHALSLLLFKLG 118

calponin homology (CH) domain found in LIM and calponin homology domains-containing protein 1; LIM and calponin homology domains-containing protein 1 (LIMCH1) acts as an actin stress fiber-associated protein that activates the non-muscle myosin IIa complex by promoting the phosphorylation of its regulatory subunit MRLC/MYL9. It positively regulates actin stress fiber assembly and stabilizes focal adhesions, and therefore negatively regulates cell spreading and cell migration. LIMCH1 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958752335   6 NFQLGLKDGIILCELINKLQPGSVKKVNESSLNWPQLENIGNFIKAIQAYGMKPHDIFEANDLFENGNMTQVQTT 80
Cdd:cd21278    21 DFRSGLENGILLCELLNAIKPGLVKKINRLPTPIAGLDNITLFLRGCKELGLKESQLFDPGDLQDTSNRVTIKSS 95

Calponin family repeat;

                          10        20
                  ....*....|....*....|....*
gi 1958752335 123 IGLQMGTNKCASQAGMTAYGTRRHL 147
Cdd:pfam00402   1 IGLQMGTNKGASQSGMTAFGAVRHI 25

calponin homology (CH) domain found in VAV3 protein and similar proteins; VAV3 is ubiquitously expressed and functions as a phosphorylation-dependent guanine nucleotide exchange factor (GEF) for RhoA, RhoG, and Rac1. Its function has been implicated in the hematopoietic, bone, cerebellar, and cardiovascular systems. VAV3 is essential in axon guidance in neurons that control blood pressure and respiration. It is overexpressed in prostate cancer cells and it plays a role in regulating androgen receptor transcriptional activity. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The model corresponds to CH domain, an actin-binding domain which is present as a single copy in VAV3 protein.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752335  11 LKDGIILCELINKLQPGSVkKVNESSLNwPQ------LENIGNFIKA-IQAYGMKPHDIFEANDLFENGNMTQVQTTLVA 83
Cdd:cd21264    36 LRDGVLLCQLLNNLRPHSI-NLKEINLR-PQmsqflcLKNIRTFLSAcCETFGMRKSELFEAFDLFDVRDFGKVIETLSK 113

                  ..
gi 1958752335  84 LA 85
Cdd:cd21264   114 LS 115

Calponin family repeat;

                          10        20
                  ....*....|....*....|....*
gi 1958752335 163 ISLQMGTNKGASQAGMSAPGTRRDI 187
Cdd:pfam00402   1 IGLQMGTNKGASQSGMTAFGAVRHI 25

first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958752335  11 LKDGIILCELINKLQPGSvkkVNESSLN-------WPQLENIGNFIKAIQAYGMK-----PHDIFEAN 66
Cdd:cd21217    37 LRDGVLLCKLINKIVPGT---IDERKLNkkkpkniFEATENLNLALNAAKKIGCKvvnigPQDILDGN 101

calponin homology (CH) domain found in leucine-rich repeat and calponin homology domain-containing protein 3; Leucine-rich repeat and calponin homology domain-containing protein 3 (LRCH3) is part of the DISP (DOCK7-Induced Septin disPlacement) complex. It may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. LRCH3 contains a single copy of the CH domain at the C-terminus. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752335  11 LKDGIILCELINKLQPGSVKKVNESSLNWPQL------ENIGNFIKAIQAYGMKPHDIFEANDLFENGNMTQVQTTLVAL 84
Cdd:cd21272    26 LTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLtmakcrRNVENFLEACRRIGVPQEQLCLPLHILEEKGLSQVAVTVQAL 105

                  ....
gi 1958752335  85 AGLA 88
Cdd:cd21272   106 LELA 109

calponin homology (CH) domain found in leucine-rich repeat and calponin homology domain-containing protein 2; Leucine-rich repeat and calponin homology domain-containing protein 2 (LRCH2) may play a role in the organization of the cytoskeleton. It contains a single copy of the CH domain at the C-terminus. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752335  11 LKDGIILCELINKLQPGSVKKVNESSLNWPQL------ENIGNFIKAIQAYGMK------PHDIFEandlfENGnMTQVQ 78
Cdd:cd21271    30 LMDGVVLCHLANHIRPRSVGSIHVPSPAVPKLsmakcrRNVENFLDACRKLGVPedklclPHHILE-----EKG-LVKVS 103

                  ....*.
gi 1958752335  79 TTLVAL 84
Cdd:cd21271   104 VTVQAL 109

calponin homology (CH) domain found in VAV2 protein and similar proteins; VAV2 is widely expressed and functions as a guanine nucleotide exchange factor (GEF) for RhoA, RhoB and RhoG and also activates Rac1 and Cdc42. It is implicated in many cellular and physiological functions including blood pressure control, eye development, neurite outgrowth and branching, EGFR endocytosis and degradation, and cell cluster morphology, among others. It has been reported to associate with Nek3. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The model corresponds to CH domain, an actin-binding domain which is present as a single copy in VAV2 protein.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752335  10 GLKDGIILCELINKLQPGSV--KKVNESslnwPQ------LENIGNFIKAIQ-AYGMKPHDIFEANDLFENGNMTQVQTT 80
Cdd:cd21263    35 ALRDGVLLCQLLHNLSPGSIdlKDINFR----PQmsqflcLKNIRTFLKVCHdKFGLRNSELFDPFDLFDVRDFGKVISA 110

                  ....*
gi 1958752335  81 LVALA 85
Cdd:cd21263   111 LSRLS 115

calponin homology (CH) domain found in leucine-rich repeat and calponin homology domain-containing protein 1; Leucine-rich repeat and calponin homology domain-containing protein 1 (LRCH1), also called calponin homology domain-containing protein 1, or neuronal protein 81 (NP81), acts as a negative regulator of GTPase CDC42 by sequestering CDC42-guanine exchange factor DOCK8. LRCH1 contains a single copy of the CH domain at the C-terminus. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752335  11 LKDGIILCELINKLQPGSVKKVNESSLNWPQL------ENIGNFIKAIQAYGMKPHDIFEANDLFENgNMTQVQTTLVAL 84
Cdd:cd21270    29 LMDGVVLCHLVNHVRPRSVASIHVPSPAVPKLsmakcrRNVENFLEACRKIGVPEADLCSPYDILQL-NLRGIRKTVETL 107

                  ...
gi 1958752335  85 AGL 87
Cdd:cd21270   108 LAL 110