RNA recognition motif (RRM) found in UHM domain of 45 kDa-splicing factor (SPF45) and similar proteins; This subgroup corresponds to the RRM of SPF45, also termed RNA-binding motif protein 17 (RBM17), an RNA-binding protein consisting of an unstructured N-terminal region, followed by a G-patch motif and a C-terminal U2AF (U2 auxiliary factor) homology motifs (UHM) that harbors a RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain) and an Arg-Xaa-Phe sequence motif. SPF45 regulates alternative splicing of the apoptosis regulatory gene FAS (also known as CD95). It induces exon 6 skipping in FAS pre-mRNA through the UHM domain that binds to tryptophan-containing linear peptide motifs (UHM ligand motifs, ULMs) present in the 3' splice site-recognizing factors U2AF65, SF1 and SF3b155.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166694   277 PTRVLLLRNMVGPGQVDDELEDEVGGECAKYGTVTRVLIFEITEPnfPVHEAVRIFVQFSRPEETTKALVDLDGRYFGGR 356
Cdd:cd12647   1 PSKVVLLRNMVGPGEVDEDLEPEVKEECEKYGKVTKVVIFEIPGA--PDDEAVRIFVEFERVESAIKAVVDLNGRFFGGR 78

                        90
                ....*....|....*..
gi 166694   357 TVRATFYDEEKFSKNEL 373
Cdd:cd12647  79 TVKASFYDLDRFRRLDL 95

ORF080 virion core protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166694     10 PPPTDDEKPSGNSSSVWSRSTKMAPPTLRKPPAfAPPQTILRPLNKPKPIVSAPYKPPPNSSQSVlIPANESAPSHQPAL 89
Cdd:PHA02682 117 PPATAPTCPPPAVCPAPARPAPACPPSTRQCPP-APPLPTPKPAPAAKPIFLHNQLPPPDYPAAS-CPTIETAPAASPVL 194

RNA recognition motif (RRM) found in UHM domain of 45 kDa-splicing factor (SPF45) and similar proteins; This subgroup corresponds to the RRM of SPF45, also termed RNA-binding motif protein 17 (RBM17), an RNA-binding protein consisting of an unstructured N-terminal region, followed by a G-patch motif and a C-terminal U2AF (U2 auxiliary factor) homology motifs (UHM) that harbors a RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain) and an Arg-Xaa-Phe sequence motif. SPF45 regulates alternative splicing of the apoptosis regulatory gene FAS (also known as CD95). It induces exon 6 skipping in FAS pre-mRNA through the UHM domain that binds to tryptophan-containing linear peptide motifs (UHM ligand motifs, ULMs) present in the 3' splice site-recognizing factors U2AF65, SF1 and SF3b155.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166694   277 PTRVLLLRNMVGPGQVDDELEDEVGGECAKYGTVTRVLIFEITEPnfPVHEAVRIFVQFSRPEETTKALVDLDGRYFGGR 356
Cdd:cd12647   1 PSKVVLLRNMVGPGEVDEDLEPEVKEECEKYGKVTKVVIFEIPGA--PDDEAVRIFVEFERVESAIKAVVDLNGRFFGGR 78

                        90
                ....*....|....*..
gi 166694   357 TVRATFYDEEKFSKNEL 373
Cdd:cd12647  79 TVKASFYDLDRFRRLDL 95

RNA recognition motif;

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166694      292 VDDELEDEVGGECAKYGTVTRVLIFEITEPNFPVHEAVRIFVQFSRPEETTKALVDLDGRYFGGRTVRAT 361
Cdd:smart00361   1 KDEDFERELKEEEEYFGEVGKINKIYIDDVGYENHKRGNVYITFERSEDAARAIVDLNGRYFDGRLVKAE 70

glycine rich nucleic binding domain; A predicted glycine rich nucleic binding domain found in the splicing factor 45, SON DNA binding protein and D-type Retrovirus- polyproteins.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 166694      209 GQMTPAQRMMPKMGWKQGQGLGKSEQGIPTPLMAKKTDRRAGVIVN 254
Cdd:smart00443   2 STSNIGAKLLRKMGWKEGQGLGKNEQGIVEPISAEIKKDRKGLGAV 47

RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic of an RNA binding protein. RRMs are found in a variety of RNA binding proteins, including various hnRNP proteins, proteins implicated in regulation of alternative splicing, and protein components of snRNPs. The motif also appears in a few single stranded DNA binding proteins. The RRM structure consists of four strands and two helices arranged in an alpha/beta sandwich, with a third helix present during RNA binding in some cases The C-terminal beta strand (4th strand) and final helix are hard to align and have been omitted in the SEED alignment The LA proteins have an N terminal rrm which is included in the seed. There is a second region towards the C terminus that has some features characteriztic of a rrm but does not appear to have the important structural core of a rrm. The LA proteins are one of the main autoantigens in Systemic lupus erythematosus (SLE), an autoimmune disease.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 166694     293 DDELEDEvggeCAKYGTVTRV-LIFEITEPNFPVheavrIFVQFSRPEETTKALVDLDGRYFGGRTVR 359
Cdd:pfam00076  12 EEDLKDL----FSKFGPIKSIrLVRDETGRSKGF-----AFVEFEDEEDAEKAIEALNGKELGGRELK 70

Pneumovirinae attachment membrane glycoprotein G;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166694      10 PPPTDDEKPSGNSSSVWSRST-KMAPPTLRKPPAFAPPQTILRPLNK-PKPIVSAPYKPPP---NSSQSVLIPANESAPS 84
Cdd:pfam05539 243 PSGSPQHPPSTTSQDQSTTGDgQEHTQRRKTPPATSNRRSPHSTATPpPTTKRQETGRPTPrptATTQSGSSPPHSSPPG 322

                          90       100
                  ....*....|....*....|..
gi 166694      85 HQPALVGVTSSVIEEYDPARPN 106
Cdd:pfam05539 323 VQANPTTQNLVDCKELDPPKPN 344

RNA recognition motif (RRM) found in UHM domain of 45 kDa-splicing factor (SPF45) and similar proteins; This subgroup corresponds to the RRM of SPF45, also termed RNA-binding motif protein 17 (RBM17), an RNA-binding protein consisting of an unstructured N-terminal region, followed by a G-patch motif and a C-terminal U2AF (U2 auxiliary factor) homology motifs (UHM) that harbors a RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain) and an Arg-Xaa-Phe sequence motif. SPF45 regulates alternative splicing of the apoptosis regulatory gene FAS (also known as CD95). It induces exon 6 skipping in FAS pre-mRNA through the UHM domain that binds to tryptophan-containing linear peptide motifs (UHM ligand motifs, ULMs) present in the 3' splice site-recognizing factors U2AF65, SF1 and SF3b155.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166694   277 PTRVLLLRNMVGPGQVDDELEDEVGGECAKYGTVTRVLIFEITEPnfPVHEAVRIFVQFSRPEETTKALVDLDGRYFGGR 356
Cdd:cd12647   1 PSKVVLLRNMVGPGEVDEDLEPEVKEECEKYGKVTKVVIFEIPGA--PDDEAVRIFVEFERVESAIKAVVDLNGRFFGGR 78

                        90
                ....*....|....*..
gi 166694   357 TVRATFYDEEKFSKNEL 373
Cdd:cd12647  79 TVKASFYDLDRFRRLDL 95

RNA recognition motif 3 (RRM3) found in UHM domain of poly(U)-binding-splicing factor PUF60 and similar proteins; This subgroup corresponds to the RRM3 of PUF60, also termed FUSE-binding protein-interacting repressor (FBP-interacting repressor or FIR), or Ro-binding protein 1 (RoBP1), or Siah-binding protein 1 (Siah-BP1), an essential splicing factor that functions as a poly-U RNA-binding protein required to reconstitute splicing in depleted nuclear extracts. Its function is enhanced through interaction with U2 auxiliary factor U2AF65. PUF60 also controls human c-myc gene expression by binding and inhibiting the transcription factor far upstream sequence element (FUSE)-binding-protein (FBP), an activator of c-myc promoters. PUF60 contains two central RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a C-terminal U2AF (U2 auxiliary factor) homology motifs (UHM) that harbors another RRM and binds to tryptophan-containing linear peptide motifs (UHM ligand motifs, ULMs) in several nuclear proteins. The research indicates that PUF60 binds FUSE as a dimer, and only the first two RRM domains participate in the single-stranded DNA recognition.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166694   278 TRVLLLRNMVGPGQVDDELEDEVGGECAKYGTVTRVLIF---EITEPNFPVheAVRIFVQFSRPEETTKALVDLDGRYFG 354
Cdd:cd12648   1 SRVMVLRNMVGPEDIDDDLEGEVTEECGKFGAVNRVIIYqekQGEEEDAEI--IVKIFVEFSMPSEAEKAIQALNGRWFG 78

                        90
                ....*....|....*....
gi 166694   355 GRTVRATFYDEEKFSKNEL 373
Cdd:cd12648  79 GRKVVAELYDQTRFDNSDL 97

RNA recognition motif;

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166694      292 VDDELEDEVGGECAKYGTVTRVLIFEITEPNFPVHEAVRIFVQFSRPEETTKALVDLDGRYFGGRTVRAT 361
Cdd:smart00361   1 KDEDFERELKEEEEYFGEVGKINKIYIDDVGYENHKRGNVYITFERSEDAARAIVDLNGRYFDGRLVKAE 70

RNA recognition motif 3 (RRM3) found in vertebrate RNA-binding protein 39 (RBM39) and similar proteins; This subfamily corresponds to the RRM3 of RBM39, also termed hepatocellular carcinoma protein 1, or RNA-binding region-containing protein 2, or splicing factor HCC1, ia nuclear autoantigen that contains an N-terminal arginine/serine rich (RS) motif and three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). An octapeptide sequence called the RS-ERK motif is repeated six times in the RS region of RBM39. Based on the specific domain composition, RBM39 has been classified into a family of non-snRNP (small nuclear ribonucleoprotein) splicing factors that are usually not complexed to snRNAs.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166694   278 TRVLLLRNMVGPGQ-----VDDELEDEVGGECAKYGTVTRVLIFEitepnfpVHEAVRIFVQFSRPEETTKALVDLDGRY 352
Cdd:cd12285   1 SRCVILKNMFDPAEetednWDDEIKEDVIEECSKYGPVLHIYVDK-------NSPQGNVYVKFKTIEAAQKCVQAMNGRW 73

                        90
                ....*....|..
gi 166694   353 FGGRTVRATFYD 364
Cdd:cd12285  74 FDGRQITAAYVP 85

glycine rich nucleic binding domain; A predicted glycine rich nucleic binding domain found in the splicing factor 45, SON DNA binding protein and D-type Retrovirus- polyproteins.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 166694      209 GQMTPAQRMMPKMGWKQGQGLGKSEQGIPTPLMAKKTDRRAGVIVN 254
Cdd:smart00443   2 STSNIGAKLLRKMGWKEGQGLGKNEQGIVEPISAEIKKDRKGLGAV 47

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166694     269 KSVNINGEPTRVLLLRNMVGPGQ--VDDELED---EVGGECAKYGTVTRVlifEITEPNfPVHEAV----RIFVQFSRPE 339
Cdd:TIGR01642 400 SILQIGGKPTKVVQLTNLVTGDDlmDDEEYEEiyeDVKTEFSKYGPLINI---VIPRPN-GDRNSTpgvgKVFLEYADVR 475

                          90       100       110
                  ....*....|....*....|....*....|...
gi 166694     340 ETTKALVDLDGRYFGGRTVRATFYDEEKFSKNE 372
Cdd:TIGR01642 476 SAEKAMEGMNGRKFNDRVVVAAFYGEDCYKAGD 508

RNA recognition motif (RRM) found in U2AF homology motif kinase 1 (UHMK1) and similar proteins; This subgroup corresponds to the RRM of UHMK1. UHMK1, also termed kinase interacting with stathmin (KIS) or P-CIP2, is a serine/threonine protein kinase functionally related to RNA metabolism and neurite outgrowth. It contains an N-terminal kinase domain and a C-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), with high homology to the corresponding motif of the mammalian U2 small nuclear ribonucleoprotein auxiliary factor U2AF 65 kDa subunit (U2AF65 or U2AF2). UHMK1 targets two key regulators of cell proliferation and migration, the cyclin-dependent kinase (CDK) inhibitor p27Kip1 and the microtubule-destabilizing protein stathmin. It plays a critical role during vascular wound repair by preventing excessive vascular smooth muscle cell (VSMC) migration into the vascular lesion. Moreover, UHMK1 may control cell migration and neurite outgrowth by interacting with and phosphorylating the splicing factor SF1, thereby probably contributing to the control of protein expression. Furthermore, UHMK1 may be functionally related to microtubule dynamics and axon development. It localizes to RNA granules, interacts with three proteins found in RNA granules (KIF3A, NonO, and eEF1A), and further enhances the local translation. UHMK1 is highly expressed in regions of the brain implicated in schizophrenia and may play a role in susceptibility to schizophrenia.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166694   277 PTRVLLLRNMVGPG--QVDDELED---EVGGECAKYGTVTRVLIfeitepnfPVHEAVR--IFVQFSRPEETTKALVDLD 349
Cdd:cd12465   2 PTPVLRLLNVIDDSylQSEEEYEDiveDVREECQKYGPVVSLLI--------PKENPGKgqVFVEYANAGDSKAAQKMLT 73

                        90
                ....*....|....
gi 166694   350 GRYFGGRTVRATFY 363
Cdd:cd12465  74 GRMFDGKFVVATFY 87

RNA recognition motif (RRM) found in Eukaryotic CCR4-NOT transcription complex subunit 4 (NOT4) and similar proteins; This subfamily corresponds to the RRM of NOT4, also termed CCR4-associated factor 4, or E3 ubiquitin-protein ligase CNOT4, or potential transcriptional repressor NOT4Hp, a component of the CCR4-NOT complex, a global negative regulator of RNA polymerase II transcription. NOT4 functions as an ubiquitin-protein ligase (E3). It contains an N-terminal C4C4 type RING finger motif, followed by a RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). The RING fingers may interact with a subset of ubiquitin-conjugating enzymes (E2s), including UbcH5B, and mediate protein-protein interactions. T

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 166694   306 KYGTVTRVLIFEITEPNFPVHEAVRIFVQFSRPEETTKALVDLDGRYFGGRTVRATF 362
Cdd:cd12438  31 QYGKIKKIVINRSTSYAGSQGPSASAYVTYSRKEDALRAIQAVDGFVLDGRTLKASF 87

RNA recognition motif;

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 166694      297 EDEVGGECAKYGTVTRVLIFEITEPNFPVHEAvriFVQFSRPEETTKALVDLDGRYFGGRTVR 359
Cdd:smart00360  13 EEELRELFSKFGKVESVRLVRDKETGKSKGFA---FVEFESEEDAEKALEALNGKELDGRPLK 72

RNA recognition motif 4 (RRM4) found in type I polyadenylate-binding proteins; This subfamily corresponds to the RRM4 of type I poly(A)-binding proteins (PABPs), highly conserved proteins that bind to the poly(A) tail present at the 3' ends of most eukaryotic mRNAs. They have been implicated in theThe CD corresponds to the RRM. regulation of poly(A) tail length during the polyadenylation reaction, translation initiation, mRNA stabilization by influencing the rate of deadenylation and inhibition of mRNA decapping. The family represents type I polyadenylate-binding proteins (PABPs), including polyadenylate-binding protein 1 (PABP-1 or PABPC1), polyadenylate-binding protein 3 (PABP-3 or PABPC3), polyadenylate-binding protein 4 (PABP-4 or APP-1 or iPABP), polyadenylate-binding protein 5 (PABP-5 or PABPC5), polyadenylate-binding protein 1-like (PABP-1-like or PABPC1L), polyadenylate-binding protein 1-like 2 (PABPC1L2 or RBM32), polyadenylate-binding protein 4-like (PABP-4-like or PABPC4L), yeast polyadenylate-binding protein, cytoplasmic and nuclear (PABP or ACBP-67), and similar proteins. PABP-1 is an ubiquitously expressed multifunctional protein that may play a role in 3' end formation of mRNA, translation initiation, mRNA stabilization, protection of poly(A) from nuclease activity, mRNA deadenylation, inhibition of mRNA decapping, and mRNP maturation. Although PABP-1 is thought to be a cytoplasmic protein, it is also found in the nucleus. PABP-1 may be involved in nucleocytoplasmic trafficking and utilization of mRNP particles. PABP-1 contains four copies of RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), a less well conserved linker region, and a proline-rich C-terminal conserved domain (CTD). PABP-3 is a testis-specific poly(A)-binding protein specifically expressed in round spermatids. It is mainly found in mammalian and may play an important role in the testis-specific regulation of mRNA homeostasis. PABP-3 shows significant sequence similarity to PABP-1. However, it binds to poly(A) with a lower affinity than PABP-1. Moreover, PABP-1 possesses an A-rich sequence in its 5'-UTR and allows binding of PABP and blockage of translation of its own mRNA. In contrast, PABP-3 lacks the A-rich sequence in its 5'-UTR. PABP-4 is an inducible poly(A)-binding protein (iPABP) that is primarily localized to the cytoplasm. It shows significant sequence similarity to PABP-1 as well. The RNA binding properties of PABP-1 and PABP-4 appear to be identical. PABP-5 is encoded by PABPC5 gene within the X-specific subinterval, and expressed in fetal brain and in a range of adult tissues in mammalian, such as ovary and testis. It may play an important role in germ cell development. Moreover, unlike other PABPs, PABP-5 contains only four RRMs, but lacks both the linker region and the CTD. PABP-1-like and PABP-1-like 2 are the orthologs of PABP-1. PABP-4-like is the ortholog of PABP-5. Their cellular functions remain unclear. The family also includes the yeast PABP, a conserved poly(A) binding protein containing poly(A) tails that can be attached to the 3'-ends of mRNAs. The yeast PABP and its homologs may play important roles in the initiation of translation and in mRNA decay. Like vertebrate PABP-1, the yeast PABP contains four RRMs, a linker region, and a proline-rich CTD as well. The first two RRMs are mainly responsible for specific binding to poly(A). The proline-rich region may be involved in protein-protein interactions.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 166694   293 DDELEDEVggecAKYGTVTRVLIfeITEPN-----FPvheavriFVQFSRPEETTKALVDLDGRYFGGR 356
Cdd:cd12381  15 DEKLREEF----SPFGTITSAKV--MTDEGgrskgFG-------FVCFSSPEEATKAVTEMNGRIIGGK 70

RNA recognition motif (RRM) found in U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 1 (U2AFBPL) and similar proteins; This subgroup corresponds to the RRM of U2AFBPL, a human homolog of the imprinted mouse gene U2afbp-rs, which encodes a U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 1 (U2AFBPL), also termed CCCH type zinc finger, RNA-binding motif and serine/arginine rich protein 1 (U2AF1RS1), or U2 small nuclear RNA auxiliary factor 1-like 1 (U2AF1L1). Although the biological role of U2AFBPL remains unclear, it shows high sequence homology to splicing factor U2AF 35 kDa subunit (U2AF35 or U2AF1) that directly binds to the 3' splice site of the conserved AG dinucleotide and performs multiple functions in the splicing process in a substrate-specific manner. Like U2AF35, U2AFBPL contains two N-terminal zinc fingers, a central RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal arginine/serine (SR)-rich domain.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 166694   294 DELEDEVGGECAKYGTVTRVLIFEITEPnfpvHEAVRIFVQFSRPEETTKALVDLDGRYFGGRTVRATF 362
Cdd:cd12540  39 LEFYEDVLPEFKKFGKVVQFKVCCNSEP----HLRGNVYVQYQSEEEALKAFTSFNGRWYAGKQLQCEF 103

RNA recognition motif (RRM) found in U2 small nuclear ribonucleoprotein auxiliary factor U2AF 35 kDa subunit (U2AF35) and similar proteins; This subfamily corresponds to the RRM in U2 small nuclear ribonucleoprotein (snRNP) auxiliary factor (U2AF) which has been implicated in the recruitment of U2 snRNP to pre-mRNAs. It is a highly conserved heterodimer composed of large and small subunits; this family includes the small subunit of U2AF (U2AF35 or U2AF1) and U2AF 35 kDa subunit B (U2AF35B or C3H60). U2AF35 directly binds to the 3' splice site of the conserved AG dinucleotide and performs multiple functions in the splicing process in a substrate-specific manner. It promotes U2 snRNP binding to the branch-point sequences of introns through association with the large subunit of U2AF (U2AF65 or U2AF2). Although the biological role of U2AF35B remains unclear, it shows high sequence homolgy to U2AF35, which contains two N-terminal zinc fingers, a central RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal arginine/serine (SR) -rich segment interrupted by glycines. In contrast to U2AF35, U2AF35B has a plant-specific conserved C-terminal region containing SERE motif(s), which may have an important function specific to higher plants.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 166694   294 DELEDEVGGECAKYGTVTRVLIFEitepNFPVHEAVRIFVQFSRPEETTKALVDLDGRYFGGRTVRATF 362
Cdd:cd12287  35 DEFYEDVFLELSRFGEIEDLVVCS----NLNDHLLGNVYVKFESEEDAEAALQALNGRYYAGRPLYPEL 99