SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit Ryanodine receptor (hence the name), are homologous to B30.2. SPRY domains have been identified in at least 11 protein families, covering a wide range of functions, including regulation of cytokine signaling (SOCS), RNA metabolism (DDX1 and hnRNP), immunity to retroviruses (TRIM5alpha), intracellular calcium release (ryanodine receptors or RyR) and regulatory and developmental processes (HERC1 and Ash2L). B30.2 also contains residues in the N-terminus that form a distinct PRY domain structure; i.e. B30.2 domain consists of PRY and SPRY subdomains. B30.2 domains comprise the C-terminus of three protein families: BTNs (receptor glycoproteins of immunoglobulin superfamily); several TRIM proteins (composed of RING/B-box/coiled-coil or RBCC core); Stonutoxin (secreted poisonous protein of the stonefish Synanceia horrida). TRIM/RBCC proteins are involved in a variety of processes, including apoptosis, cell cycle regulation, cell growth, senescence, viral response, meiosis, cell differentiation, and vesicular transport. Genes belonging to this family are implicated in several human diseases that vary from cancer to rare genetic syndromes. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site. While SPRY domains are evolutionarily ancient, B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. Mutations found in the SPRY-containing proteins have shown to cause Mediterranean fever and Opitz syndrome.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751  32 FKLEEKTAHSSLALFRGDTGVKYGLVGLEPTKVALNLERFRDWAVVLADTTVTSGRHYWEVTVKRSQQFRIGVADVDMSR 111
Cdd:cd12903    1 FKLDERTAHSSLDLFKKDTGVIYRMLGVDPTKVPQNPERFRDWAVVLGDTPVTSGRHYWEVTVKRSQEFRIGVADVDMSR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751 112 DSCVGADDRSWVFSYAQRKWHSMLANEKAPIKGIGQPEKVGLLLDYEAKKLSLVDVNRISVIHTLQTDFRGPVAPAFALW 191
Cdd:cd12903   81 DECIGTNESSWVFAYAQRKWYAMVANETVPVPLVGKPDRVGLLLDYEAGKLSLVDVEKNSVVHTMSAEFRGPVVPAFALW 160

                 ....*....
gi 564357751 192 DGELLTHSG 200
Cdd:cd12903  161 DGELLTHSG 169

PRY/SPRY domain containing protein 4 (SPRYD4); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain and is encoded by the SPRYD4 gene. SPRYD4 (SPRY containing domain 4) is ubiquitously expressed in many human tissues, most strongly in kidney, bladder, brain, thymus and stomach. Subcellular localization demonstrates that SPRYD4 protein is localized in the nucleus when overexpressed in COS-7 green monkey cell. It has remained uncharacterized thus far.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751  32 FKLEEKTAHSSLALFRGDTGVKYGLVGLEPTKVALNLERFRDWAVVLADTTVTSGRHYWEVTVKRSQQFRIGVADVDMSR 111
Cdd:cd12903    1 FKLDERTAHSSLDLFKKDTGVIYRMLGVDPTKVPQNPERFRDWAVVLGDTPVTSGRHYWEVTVKRSQEFRIGVADVDMSR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751 112 DSCVGADDRSWVFSYAQRKWHSMLANEKAPIKGIGQPEKVGLLLDYEAKKLSLVDVNRISVIHTLQTDFRGPVAPAFALW 191
Cdd:cd12903   81 DECIGTNESSWVFAYAQRKWYAMVANETVPVPLVGKPDRVGLLLDYEAGKLSLVDVEKNSVVHTMSAEFRGPVVPAFALW 160

                 ....*....
gi 564357751 192 DGELLTHSG 200
Cdd:cd12903  161 DGELLTHSG 169

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751   87 RHYWEVTV--KRSQQFRIGVA--DVDMSRDSCVGADDRSWVFS--YAQRKWHSMlaNEKAPIKGIGQPEKVGLLLDYEAK 160
Cdd:pfam00622   1 RHYFEVEIfgQDGGGWRVGWAtkSVPRKGERFLGDESGSWGYDgwTGKKYWAST--SPLTGLPLFEPGDVIGCFLDYEAG 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 564357751  161 KLSLVDVNRiSVIHTLQT-DFRGPVAPAFAL 190
Cdd:pfam00622  79 TISFTKNGK-SLGYAFRDvPFAGPLFPAVSL 108

PRY/SPRY domain containing protein 4 (SPRYD4); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain and is encoded by the SPRYD4 gene. SPRYD4 (SPRY containing domain 4) is ubiquitously expressed in many human tissues, most strongly in kidney, bladder, brain, thymus and stomach. Subcellular localization demonstrates that SPRYD4 protein is localized in the nucleus when overexpressed in COS-7 green monkey cell. It has remained uncharacterized thus far.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751  32 FKLEEKTAHSSLALFRGDTGVKYGLVGLEPTKVALNLERFRDWAVVLADTTVTSGRHYWEVTVKRSQQFRIGVADVDMSR 111
Cdd:cd12903    1 FKLDERTAHSSLDLFKKDTGVIYRMLGVDPTKVPQNPERFRDWAVVLGDTPVTSGRHYWEVTVKRSQEFRIGVADVDMSR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751 112 DSCVGADDRSWVFSYAQRKWHSMLANEKAPIKGIGQPEKVGLLLDYEAKKLSLVDVNRISVIHTLQTDFRGPVAPAFALW 191
Cdd:cd12903   81 DECIGTNESSWVFAYAQRKWYAMVANETVPVPLVGKPDRVGLLLDYEAGKLSLVDVEKNSVVHTMSAEFRGPVVPAFALW 160

                 ....*....
gi 564357751 192 DGELLTHSG 200
Cdd:cd12903  161 DGELLTHSG 169

PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76)-like; This domain is similar to the distinct PRY/SPRY subdomain found at the C-terminus of TRIM76, a Class I TRIM protein. TRIM76 (also known as cardiomyopathy-associated protein 5 or CMYA5 or myospryn or SPRYD2) is a muscle-specific member of the TRIM superfamily, but lacks the RING domain. It has been suggested that TRIM76 is involved in two distinct processes, protein kinase A signaling and vesicular trafficking.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751  32 FKLEEKTAHSSLALFRGDTGVKYGLVGLEPTKVALNLERFRDWAVVLADTTVTSGRHYWEVTVKRSQQFRIGVADVDMSR 111
Cdd:cd12899    2 FHLNEDTAHPLLSISEDGFTVVYGEEELPARDLSFSDNSFTRCVAVMGSLIPVRGKHYWEVEVDEQTEYRVGVAFEDTQR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751 112 DSCVGADDRSWVFSY---AQRKWHSMLANEKAP-IKGIGQPEKVGLLLDYEAKKLSLVDVNRISVIHTLQTDFRGPVAPA 187
Cdd:cd12899   82 NGYLGANNTSWCMRHiitPSRHKYEFLHNGWTPdIRITVPPKKIGILLDYDSGRLSFFNVDLAQHLYTFSCQFQHFVHPC 161

                        170
                 ....*....|....*
gi 564357751 188 FALWD-GELLTHSGL 201
Cdd:cd12899  162 FSLEKpGALKVHNGI 176

PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM14-like, TRIM16-like, TRIM25-like, TRIM47-like, TRIM65 and RNF135, and stonustoxin; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several Class I TRIM proteins, including TRIM14, TRIM16 and TRIM25, TRIM47 as well as RING finger protein RNF135 and stonustoxin, a secreted poisonous protein of the stonefish Synanceja horrida. TRIM16 (also known as estrogen-responsive B box protein or EBBP) has E3 ubiquitin ligase activity. It is a regulator of keratinocyte differentiation and a tumor suppressor in retinoid-sensitive neuroblastoma. TRIM25 (also called Efp) ubiquitinates the N terminus of the viral RNA receptor retinoic acid-inducible gene-I (RIG-I) in response to viral infection, leading to activation of the RIG-I signaling pathway, thus resulting in type I interferon production to limit viral replication. It has been shown that the influenza A virus targets TRIM25 and disables its antiviral function. TRIM47, also known as GOA (Gene overexpressed in astrocytoma protein) or RNF100 (RING finger protein 100), is highly expressed in kidney tubular cells, but low expressed in most tissue. It is overexpressed in astrocytoma tumor cells and plays an important role in the process of dedifferentiation that is associated with astrocytoma tumorigenesis. RNF135 ubiquitinates RIG-I (retinoic acid-inducible gene-I) to promote interferon-beta induction during the early phase of viral infection. Stonustoxin (STNX) is a hypotensive and lethal protein factor that also possesses other biological activities such as species-specific hemolysis (due to its ability to form pores in the cell membrane) and platelet aggregation, edema-induction, and endothelium-dependent vasorelaxation (mediated by the nitric oxide pathway and activation of potassium channels). The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751  34 LEEKTAHSSLALFRGDTGVKYGLVGLE-PtkvaLNLERFRDWAVvLADTTVTSGRHYWEVTVKRSQQFRIGVADVDMSR- 111
Cdd:cd12891    3 LDPNTAHNNLALSGDLKTVTCSSENQHyP----DSPERFTHSQV-LSTQSFSSGRHYWEVEVSESGGWSVGVAYPSIERk 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751 112 --DSCVGADDRSWVFSYAQRK---WHSmlaNEKAPIKGiGQPEKVGLLLDYEAKKLSLVDV-NRISVIHTLQTDFRGPVA 185
Cdd:cd12891   78 gdESRIGRNDKSWCLEWQDKSfsaWHN---NEETPLPS-VSSRRLGVYLDYEAGRLSFYELsDPIRHLHTFTATFTEPLH 153

                        170
                 ....*....|..
gi 564357751 186 PAFALWDGELLT 197
Cdd:cd12891  154 PAFWVLEGGWIR 165

PRY/SPRY domain of tripartite motif-binding protein 1 (TRIM1) or MID2; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM1 (also known as MID2 or midline 2). MID2 and its close homolog, TRIM18 (also known as MID1), both contain a B30.2-like domain at their C-terminus and a single fibronectin type III (FN3) motif between it and their N-terminal RBCC domain. MID2 and MID1 coiled-coil motifs mediate both homo- and heterodimerization, a prerequisite for association of the rapamycin-sensitive PP2A regulatory subunit Alpha 4 with microtubules. Mutations in MID1 have shown to cause Opitz syndrome, a disorder causing congenital anomalies such as cleft lip and palate as well as heart defects.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751  32 FKLEEKTAHSSLALFRGDTGVKYGLVGLEPTKVAlnlERFRDWAVVLADTTV--TSGRHYWEVTVKRSQQFRIGVADVDM 109
Cdd:cd13739    1 FKLDPKMAHKKLKISNDGLQMEKDESSLKKSHTP---ERFSGTGCYGAAGNIfiDSGCHYWEVVVGSSTWYAIGIAYKSA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751 110 SRDSCVGADDRSWVFSYAQRKWHSMLANEKAPIKGIGQPEKVGLLLDYEAKKLSLVDVNRISVIHTLQTDFRGPVAPAFA 189
Cdd:cd13739   78 PKNEWIGKNSSSWVFSRCNNNFVVRHNNKEMLVDVPPQLKRLGVLLDYDNNMLSFYDPANSLHLHTFEVSFILPVCPTFT 157

                        170
                 ....*....|..
gi 564357751 190 LWDGELLTHSGL 201
Cdd:cd13739  158 IWNKSLMILSGL 169

PRY/SPRY domain in tripartite motif-binding protein 50 (TRIM50); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM50. TRIM50, an E3 ubiquitin ligase, is deleted in Williams-Beuren (WBS) syndrome, a multi-system neurodevelopmental disorder caused by the deletion of contiguous genes at chromosome region 7q11.23. It is specifically expressed in gastric parietal cells and may play an essential role in tubulovesicular dynamics. It also interacts with and increases the level of p62, a multifunctional adaptor protein that is implicated in various cellular processes such as the autophagy clearance of polyubiquitinated protein aggregates.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751  31 SFKLEEKTAHSSLALFRGDTGVKYGLvglEPTKVALNLERFRDWAVVLADTTVTSGRHYWEVTVKRSQQFRIGVADVDMS 110
Cdd:cd13743   13 LLKLDPLTAHPMLELSKGNTVVECGL---LAQRLPSNPERFDYSNCVLASRGFSSGKHYWEVVVGSKSKWRLGLIKGTTS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751 111 RDSCVGADDRS--WVFSYAQRKWHSMLANEKAPIKGIGQPEKVGLLLDYEAKKLSLVDVNR---ISVIHTLQTDFRGPVA 185
Cdd:cd13743   90 RKGKLNKSPENgvWLIGLKEGRVYEAFANPRVPLPLSTRPQRIGVFLDYEKGELTFYNADSpdeLVPIYTFQAEFQGKLY 169

                 ...
gi 564357751 186 PAF 188
Cdd:cd13743  170 PLL 172

Fibronectin type III and SPRY containing 1 (FSD1) domain includes PRY at the N-terminus; This domain is part of the fibronectin type III and SPRY domain containing 1 (FSD1) and FSD1-like (FSD1L) proteins. These are centrosome-associated proteins that are characterized by an N-terminal coiled-coil region downstream of B-box (BBC) domain, a central fibronectin type III (FN3) domain, and C-terminal repeats in PRY/SPRY domain. The FSD1 protein associates with a subset of microtubules and may be involved in the stability and organization of microtubules during cytokinesis.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751  77 VLADTTVTSGRHYWEVTV-KRSQQFRIGVADVDMSRDSCVGADDRSWVFSYAQRKWHSMLA--NEKAPIKGIGQPEKVGL 153
Cdd:cd12901   76 VLGDTLIDGGQHYWEVRAqKDSKAFSVGVAYRSLGKFDQLGKTNASWCLHVNNWLQNSFAAkhNNKAKTLDVPVPDRIGV 155

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564357751 154 LLDYEAKKLSLVDVNRISVIHTLQTDFRGPVAPAFALWDGELLTHSGLEVP 204
Cdd:cd12901  156 YCDFDEGQLSFYNARTKQLLHTFKMKFTQPVLPAFMVWCGGLSVSTGLQVP 206

PRY/SPRY domain in tripartite motif-binding protein 69 (TRIM69), also known as RING finger protein 36 (RNF36); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM69, which is also known as RING finger protein 36 (RNF36) or testis-specific ring finger (Trif). TRIM69 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. It is a novel testis E3 ubiquitin ligase that may function to ubiquitinate its particular substrates during spermatogenesis. In humans, TRIM69 localizes in the cytoplasm and nucleus, and requires an intact RING finger domain to function. The mouse ortholog of this gene is specifically expressed in germ cells at the round spermatid stages during spermatogenesis and, when overexpressed, induces apoptosis. TRIM69 has been shown to be a novel regulator of mitotic spindle assembly in tumor cells; it associates with spindle poles and promotes centrosomal clustering, and is therefore essential for formation of a bipolar spindle.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751  29 GISF-KLEEKTAHSSLALFRGDTGVKYGlvglePTKVAL--NLERFRDWAVVLADTTVTSGRHYWEVTVKRSQQFRIGVA 105
Cdd:cd15818   11 GLSLiTLDPKTAHPNLILSEDLTCVWHG-----DTKQMLpdNPERFDSSVAVLGSEGFTSGKHYWEVEVAKKTKWTLGVV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751 106 DVDMSRDSCVgaddrswVFSYAQRKWHSMLANE---KA---PIKGI---GQPEKVGLLLDYEAKKLSLVDVNRISVIHTL 176
Cdd:cd15818   86 RESINRKGNC-------PLSPEDGFWLLRLRNQnelKAldvPSFSLtltSNLNKVGIYLDYEGGQVSFYNANTMSHIYTF 158

                        170
                 ....*....|..
gi 564357751 177 QTDFRGPVAPAF 188
Cdd:cd15818  159 SDTFTEKIYPYF 170

Stonustoxin subunit alpha or SNTX subunit alpha; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of Stonustoxin alpha proteins. Stonustoxin (SNTX) is a multifunctional lethal protein isolated from venom elaborated by the stonefish. It comprises two subunits, termed alpha and beta. SNTX elicits an array of biological responses, particularly a potent hypotension and respiratory difficulties.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751  38 TAHSSLALFRGDTGVKYGLvglEPTKVALNLERFRDWAVVLADTTVTsGRHYWEVTVkRSQQFRIGVADVDMSR-----D 112
Cdd:cd16040   17 TAHRNLSLSEGNRKVTRVK---EEQPYPDHPERFDYWPQVLCREGLS-GRCYWEVEW-SGGGVDIAVAYKGISRkgdgdD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751 113 SCVGADDRSWVFSYAQRK---WHsmlANEKAPIKGIGQPE-KVGLLLDYEAKKLSLVDVNRI-SVIHTLQTDFRGPVAPA 187
Cdd:cd16040   92 SRFGYNDKSWSLECSPSGysfWH---NNKKTEISVPSSSSsRVGVYLDHSAGTLSFYSVSDTmTLLHTVQTTFTEPLYPG 168

                 ....*..
gi 564357751 188 FALWDGE 194
Cdd:cd16040  169 FGVGYGS 175

butyrophilin subfamily member A1 and A2 (BTN1A and BTN2A); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of butyrophilin family 1A and 2A (BTN1A and BTN2A). BTNs belong to receptor glycoproteins of immunoglobulin (Ig) superfamily, characterized by the presence of extracellular Ig-like domains (IgV and/or IgC). BTN1A plays a role in the secretion, formation and stabilization of milk fat globules. The B30.2 domain of BTN1A1 binds the enzyme xanthine oxidoreductase (XOR) in order to participate in milk fat globule secretion; this interaction may lead to the production of reactive oxygen species, which have immunomodulatory and antimicrobial functions. Duplication events have led to three paralogs of BTN2A in primates: BTN2A1, BTN2A2, and BTN2A3. In humans, only BTN2A1 has been functionally characterized; it has been detected on epithelial cells and leukocytes, and identified as a novel ligand of dendritic cell-specific ICAM-3 grabbing nonintegrin (DCSIGN), a C-type lectin receptor that acts as an internalization receptor for HIV-1, HCV, and other pathogens. BTN2A2 mRNA has been shown to be expressed in circulating human immune cells.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751  34 LEEKTAHSSLALFRGDTGVKyglVGLEPTKVALNLERFRDWAVVLADTTVTSGRHYWEVTVKRSQQFRIGVADVDMSRDS 113
Cdd:cd15819    6 LDPDTAHPALILSEDGRSVT---WGETRQDLPENPERFDSLPCVLGQEGFTSGRHYWEVEVGDRTSWDLGVCRDNVMRKG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751 114 --CVGADDRSWVF-SYAQRKWhsMLANEKAPIKGIGQPEKVGLLLDYEAKKLSLVDVNRISVIHTL-QTDFRGPVAPAFA 189
Cdd:cd15819   83 rvTLSPENGFWAIrLYGNEYW--ALTSPETPLTLKEPPRRVGIFLDYEAGDVSFYNMTDGSHIYTFpQTAFSGPLRPFFR 160

                 ..
gi 564357751 190 LW 191
Cdd:cd15819  161 LW 162

PRY/SPRY domain of butyrophilin 3 (BTN3), includes BTN3A1, BTN3A2, BTN3A3 as well as BTN-like 3 (BTNL3); BTN3A also known as CD277; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of butyrophilin family 3A (BTN3A); duplication events have led to three paralogs in primates: BTN3A1, BTN3A2, and BTN3A3. BTNs belong to receptor glycoproteins of immunoglobulin (Ig) superfamily, characterized by the presence of extracellular Ig-like domains (IgV and/or IgC). BTN3 transcripts are ubiquitously present in all immune cells (T cells, B cells, NK cells, monocytes, dendritic cells, and hematopoietic precursors) with different expression levels; BTN3A1 and BTN3A2 are expressed mainly by CD4+ and CD8+ T cells, BTN3A2 is the major form expressed in NK cells, and BTN3A3 is poorly expressed in these immune cells. The PRY/SPRY domain of the BTN3A1 isoform mediates phosphoantigen (pAg)-induced activation by binding directly to the pAg.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751  60 EPTKVALNLERFRDWAVVLADTTVTSGRHYWEVTVKRSQQFRIGVADVDMSRDSCVGADDRS--WVFSYAQRKWHSMLAN 137
Cdd:cd15820   31 EPQNLPDNPKRFDWHYCVLGCKSFTSGRHFWEVEVGDRKEWYVGVCRENVERKLWVKMAPENgfWTIGLSDGNDYQALTD 110

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564357751 138 EKAPIKGIGQPEKVGLLLDYEAKKLSLVDVNRISVIHT-LQTDFRGPVAPAFAL--WDGELLT 197
Cdd:cd15820  111 PRTKLTIANPPQRVGVFLDYETGEVSFYNAMDGSHIYTfPHTSFSGPLYPVFRLlsWDPTALT 173

PRY/SPRY domain in tripartite motif-binding (TRIM) proteins TRIM50 and TRIM72; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several TRIM proteins, including TRIM72 and TRIM50. TRIM72 (also known as MG53) has been shown to perform a critical function in membrane repair following acute muscle injury by nucleating the assembly of the repair machinery at injury sites. It is expressed specifically in skeletal muscle and heart, and tethered to the plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine. TRIM50, an E3 ubiquitin ligase, is deleted in Williams-Beuren (WBS) syndrome, a multi-system neurodevelopmental disorder caused by the deletion of contiguous genes at chromosome region 7q11.23.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751  31 SFKLEEKTAHSSLALFRGDTGVKyglVGLEPTKVALNLERFRDWAVVLADTTVTSGRHYWEVTVKRSQQFRIGVADVDMS 110
Cdd:cd12897   13 SLTFDPATAHPLLVVSSGGTVVE---CGLQKQRRASQPERFDKSTCVVASQGFSEGEHYWEVVVGDKPRWALGVIKGTAS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751 111 RDSCVGADDRS--WVFSYAQRKWHSMLANEKAP--IKGIGQPEKVGLLLDYEAKKLSLVDVNR---ISVIHTLQTDFRGP 183
Cdd:cd12897   90 RKGKLHASPSHgvWLIGLKEGKVYEAHGEPKEPrpLRVAGRPHRIGVYLSFEDGVLSFFDASDpddLRTLYTFQERFQGK 169

                 ....*
gi 564357751 184 VAPAF 188
Cdd:cd12897  170 LYPFF 174

PRY/SPRY domain in tripartite motif-containing proteins, TRIM9 and TRIM67; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM9 proteins. TRIM9 protein is expressed mainly in the cerebral cortex, and functions as an E3 ubiquitin ligase. It has been shown that TRIM9 is localized to the neurons in the normal human brain and its immunoreactivity in affected brain areas in Parkinson's disease and dementia with Lewy bodies is severely decreased, possibly playing an important role in the regulation of neuronal function and participating in pathological process of Lewy body disease through its ligase. TRIM67 negatively regulates Ras activity via degradation of 80K-H, leading to neural differentiation, including neuritogenesis.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751  76 VVLADTTVTSGRHYWEVTVKR---SQQFRIGVADVDMSRDSCVGADDRSWVFsY--AQRKWHsMLANEKA--PIKGIGQP 148
Cdd:cd12889   39 VVLGSVGFSRGVHYWEVTIDRydgHPDPAFGVARIDVNKDKMLGKDDKGWSM-YidNNRSWF-LHNNEHSnrTEGGITVG 116

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564357751 149 EKVGLLLDYEAKKLSLvdvnrisvihTLQTDFRGPVA---------PAFALWDGELLT-HSGLEVP 204
Cdd:cd12889  117 SVVGVLLDLDRHTLSF----------YVNDEPQGPIAfrnlpgvfyPAVSLNRNVQVTlHTGLEPP 172

PRY/SPRY domain in tripartite motif-containing protein 16 (TRIM16); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM16 and TRIM-like proteins. TRIM16 (also known as estrogen-responsive B box protein or EBBP) does not possess a RING domain like the other TRIM proteins, but contains two B-box domains and can heterodimerize with other TRIM proteins such as TRIM24, Promyelocytic leukemia (PML) protein and Midline-1 (MID1 or TRIM18). It is a regulator of keratinocyte differentiation and a tumor suppressor in retinoid-sensitive neuroblastoma. It has been shown that loss of TRIM16 expression plays an important role in the development of cutaneous squamous cell carcinoma (SCC) and is a determinant of retinoid sensitivity. TRIM16 also has E3 ubiquitin ligase activity.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751  69 ERFRDWAVVLADTTVTSGRHYWEVTVKRSQQFrIGVADVDMSR-----DSCVGADDRSWVFSYAQRK---WHSmlaNEKA 140
Cdd:cd12890   46 ERFEHWRQVLSQQSLYLGRYYFEVEISGEGTY-VGLTYKSIDRkgsesNSCISGNNFSWCLQWNGKEfsaWHS---DVET 121

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564357751 141 PIKGiGQPEKVGLLLDYEAKKLSL--VDVNRISVIHTLQTDFRGPVAPAFAL 190
Cdd:cd12890  122 PLKK-GPFTRLGIYLDYPGGTLSFygVEDDGMTLLHKFQCKFTEPLYPAFWL 172

PRY/SPRY domain in tripartite motif-binding protein 41 (TRIM41); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of tripartite motif-containing protein 41 (TRIM41). TRIM41 (also known as RING finger-interacting protein with C kinase or RINCK) is localized to speckles in the cytoplasm and nucleus, and functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751  34 LEEKTAHSSLALFRGDTGVKyglVGLEPTKVALNLERFRDWAVVLADTTVTSGRHYWEVTVKRSQQFRIGVA-------D 106
Cdd:cd13741    4 LDPDTAHPALLLSPDRRGVR---LAERRQEVPEHPKRFSADCCVLGAQGFRSGRHYWEVEVGGRRGWAVGAAresthhkE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751 107 VDMSRDSCVGADDRS-----------------------WVFSYAQRKWHSMLANEKAPIKGIGQPEKVGLLLDYEAKKLS 163
Cdd:cd13741   81 KVGSGGSSVSSGDASssrhhhrrrrlhlpqqpllqrevWCVGTNGKRYQAQSSTEQTLLSPSEKPRRFGVYLDYEAGRLG 160

                        170       180
                 ....*....|....*....|....*.
gi 564357751 164 LVDVNRISVIHTLQTDFRGP-VAPAF 188
Cdd:cd13741  161 FYNAETLAHVHTFSAAFLGErVFPFF 186

PRY/SPRY domain of tripartite motif-binding protein 11 (TRIM11), also known as RING finger protein 92 (RNF92); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM11, also known as RING finger protein 92 (RNF92) or BIA1. TRIM11 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. It localizes to the nucleus and the cytoplasm; it is overexpressed in high-grade gliomas and promotes proliferation, invasion, migration and glial tumor growth. TRIM11 increases expression of dopamine beta-hydroxylase gene by interacting with the homeodomain transcription factor, PHOX2B, via the B30.2/SPRY domain, thus playing a potential role in the specification of noradrenergic (NA) neuron phenotype. It has also been shown that TRIM11 plays a critical role in the clearance of mutant PHOX2B, which causes congenital central hypoventilation syndrome, via the proteasome. TRIM11 binds a key component of the activator-mediated cofactor complex (ARC105), and destabilizes it, through the ubiquitin-proteasome system; ARC105 mediates chromatin-directed transcription activation and is a key regulatory factor for transforming growth factor beta (TGFbeta) signaling.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751  69 ERFRDWAVVLADTTVTSGRHYWEVTVKRSQQFRIGVADVDMSRDSC--VGADDRSWVFSYAQRKWHSMLANeKAPIKgiG 146
Cdd:cd15811   36 ERFDPGPCVLGRERFTSGRHYWEVEVGDRTSWALGVCKENVNRKEKgeLSAGNGFWILVFLGNYYSSERRT-FAPLR--D 112

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 564357751 147 QPEKVGLLLDYEAKKLSLVDVNRISVIHTL-QTDFRGPVAPAFA 189
Cdd:cd15811  113 PPRRVGIFLDYEAGHLSFYSATDGSLLFIFpETPFSGTLRPLFS 156

PRY/SPRY domain in tripartite motif-containing protein 27 (TRIM27), also known as RING finger protein 76 (RNF76); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM27, also known as RING finger protein 76 (RNF76) or RET finger protein (RFP). TRIM27 domain is composed of RING/B-box/coiled-coil core and also known as RBCC proteins. It is highly expressed in the spleen, thymus and in cells of the hematopoietic compartment. TRIM27 exhibits either nuclear or cytosolic localization depending on the cell type. TRIM27 negatively regulates nucleotide-binding oligomerization domain containing 2 (NOD2)-mediated signaling by proteasomal degradation of NOD2, suggesting that TRIM27 could be a new target for therapeutic intervention in NOD2-associated diseases such as Crohn's. High expression of TRIM27 is observed in several human cancers, including breast and endometrial cancer, where elevated TRIM27 expression predicts poor prognosis. Also, TRIM27 forms an oncogenic fusion protein with Ret proto-oncogene. It is involved in different stages of spermatogenesis and its significant expression in male germ cells and seminomas, suggests that TRIM27 may be associated with the regulation of testicular germ cell proliferation and histological-type of germ cell tumors. TRIM27 could also be a predictive marker for chemoresistance in ovarian cancer patients. In the neurotoxin model of Parkinson's disease (PD), deficiency of TRIM27 decreases apoptosis and protects dopaminergic neurons, making TRIM27 an effective potential target during the treatment of PD.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751  30 ISFKLEEKTAHSSLALFRGDTGVKYGLVGLEptkVALNLERFRDWAVVLADTTVTSGRHYWEVTVKRSQQFRIGVADVDM 109
Cdd:cd15814    2 VDVTLDPDTAYPSLILSDNLRQVRYSYLQQD---LPDNPERFNLFPCVLGSPCFIAGRHYWEVEVGDKAKWTIGVCEDSV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751 110 SRDSCVGADDRS--WVFS--YAQRKWHSMLANEKAPIKGIGQpeKVGLLLDYEAKKLSLVDVN-RISVIHTLQTDFRGPV 184
Cdd:cd15814   79 CRKGGVTSAPQNgfWAVSlwYGKEYWALTSPMTALPLRTPLQ--RVGIFLDYDAGEVSFYNVTeRCHTFTFSHATFCGPV 156

                 ....*.
gi 564357751 185 APAFAL 190
Cdd:cd15814  157 RPYFSL 162

PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7)-like, including TRIM7, TRIM10, TRIM15, TRIM26, TRIM39, TRIM41; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several tripartite motif-containing (TRIM) proteins, including TRIM7 (also referred to as glycogenin-interacting protein, RING finger protein 90 or RNF90), TRIM10, TRIM15, TRIM26, TRIM39 and TRIM41. TRIM7 or GNIP interacts with glycogenin and stimulates its self-glucosylating activity via its SPRY domain. TRIM10 (also known as hematopoietic RING finger 1 (HERF1) or TRIM10/HERF1) plays a key role in definitive erythroid development; downregulation of the Spi-1/PU.1 oncogene induces the expression of TRIM10/HERF1, a key factor required for terminal erythroid cell differentiation and survival. Antiviral activity of TRIM15 is dependent on the ability of its B-box to interact with the MLV Gag precursor protein; downregulation of TRIM15, along with TRIM11, enhances virus release suggesting that these proteins contribute to the endogenous restriction of retroviruses in cells. Tripartite motif-containing 26 (TRIM26) function is as yet unknown; however, since it is localized in the human histocompatibility complex (MHC) class I region, TRIM26 may play a role in immune response although studies show no association between TRIM26 polymorphisms and the risk of aspirin-exacerbated respiratory disease. TRIM39 is a MOAP-1 (Modulator of Apoptosis)-binding protein that stabilizes MOAP-1 through inhibition of its poly-ubiquitination process. TRIM41 (also known as RING finger-interacting protein with C kinase or RINCK) functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751  38 TAHSSLALFRGDTGVKYGLVglePTKVALNLERFRDWAVVLADTTVTSGRHYWEVTVKRSQQFRIGVADVDMSR--DSCV 115
Cdd:cd12888    8 TAHPRLVLSEDRKSVRWGDT---RQDLPDNPERFDTWPCVLGCEGFTSGRHYWEVEVGDGGGWAVGVARESVRRkgEISF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751 116 GADDRSWvfsyAQRKWH---SMLANEKAPIKGIGQPEKVGLLLDYEAKKLSLVDVNRISVIHTLQTDF--RGPVAPAFAL 190
Cdd:cd12888   85 SPEEGIW----AVGQWGgqyWALTSPETPLPLSEVPRRIRVYLDYEGGQVAFFDADNEAPIFTFPPASfaGERIFPWFWV 160

                 ....*..
gi 564357751 191 WDGELLT 197
Cdd:cd12888  161 GKGSQLK 167

PRY/SPRY domain of tripartite motif-binding protein 75 (TRIM75); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM75, also known as Gm794. TRIM75 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. TRIM75 has a single site of positive selection in its RING domain associated with E3 ubiquitin ligase activity. It has not been detectably expressed experimentally due to their constant turnover by the proteasome, and therefore not been characterized.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751  34 LEEKTAHSSLALFRGDTGVKYglvglepTK----VALNLERFRDWAVVLADTTVTSGRHYWEVTVKRSQQFRIGVADVDM 109
Cdd:cd15829   23 LDPETAHPNLLVSEDKKCVTF-------TKkkqrVPDSPKRFTVNPVVLGFPGFHSGRHFWEVEVGDKPEWAVGVCKDSL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751 110 SRdscvGADDRSwvfSYAQRKWHSMLANE--------KAPIKGIGQPEKVGLLLDYEAKKLSLVDVNRISVIHTLQTDFR 181
Cdd:cd15829   96 ST----KARRPP---SGQQGCWRIQLQGGdydapgavPPPLLLEVKPRGIGVFLDYELGEISFYNMPEKSHIHTFTDTFS 168

                 ....*..
gi 564357751 182 GPVAPAF 188
Cdd:cd15829  169 GPLRPYF 175

PRY/SPRY domain of tripartite motif-binding protein 60 and 75 (TRIM60 and TRIM75); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM60 and TRIM75, both composed of RING/B-box/coiled-coil core and also known as RBCC proteins. TRIM60 domain is also known as RING finger protein 33 (RNF33) or 129 (RNF129). Based on its expression profile, RNF33 likely plays an important role in the spermatogenesis process, the development of the pre-implantation embryo, and in testicular functions; Rnf33 is temporally transcribed in the unfertilized egg and the pre-implantation embryo, and is permanently silenced before the blastocyst stage. Mice experiments have shown that RNF33 associates with the cytoplasmic motor proteins, kinesin-2 family members 3A (KIF3A) and 3B (KIF3B), suggesting possible contribution to cargo movement along the microtubule in the expressed sites. TRIM75, also known as Gm794, has a single site of positive selection in its RING domain associated with E3 ubiquitin ligase activity. It has not been detectably expressed experimentally due to their constant turnover by the proteasome, and therefore not been characterized.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751  34 LEEKTAHSSLALFRGDTGVKYGLVGlepTKVALNLERFRDWAVVLADTTVTSGRHYWEVTVKRSQQFRIGVADVDMSRDS 113
Cdd:cd15817    4 LDPETAHPNLIVSEDRKAVRYRRMK---PNCPYDPRRFTVYPAVLGSEGFDSGRHFWEVEVGGKGEWILGVCKDSLPRNA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564357751 114 CV--GADDRSWVFSYAQRKWHSMlANEKAPIKGIGQPEKVGLLLDYEAKKLSLVDVNRISVIHTLQTDFRGPVAPAF 188
Cdd:cd15817   81 QDppSPLGGCWQIGRYMSGYVAS-GPKTTQLLPVVKPSRIGIFLDYELGEVSFYNMNDRSHLYTFTDTFTGKLIPYF 156

zinc-binding protein A33-like; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM69 and TRIM proteins NF7 and bloodthirsty (bty). TRIM69 is a novel testis E3 ubiquitin ligase that may function to ubiquitinate its particular substrates during spermatogenesis. In humans, TRIM69 localizes in the cytoplasm and nucleus, and requires an intact RING finger domain to function. TRIM protein NF7, which also contains a chromodomain (CHD) at the N-terminus and an RFP (Ret finger protein)-like domain at the C-terminus, is required for its association with transcriptional units of RNA polymerase II which is mediated by a trimeric B box. In Xenopus oocyte, xNF7 has been identified as a nuclear microtubule-associated protein (MAP) whose microtubule-bundling activity, but not E3-ligase activity, contributes to microtubule organization and spindle integrity. Bloodthirsty (bty) is a novel gene identified in zebrafish and has been shown to likely play a role in in regulation of the terminal steps of erythropoiesis.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751  34 LEEKTAHSSLALFRGDTGVkygLVGLEPTKVALNLERFRDWAVVLADTTVTSGRHYWEVTVKRSQQFRIGVADVDMSRDS 113
Cdd:cd12905    8 FDPETAHPSLILSRDLTAV---TESDEMQPYPRSPKRFLQCVNVLASQGFQSGRHYWEVWVGSKTKWDLGVASESVDRQA 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564357751 114 CVG--ADDRSWVFSYAQRKWHSMLANEKAPIKGIGQPEKVGLLLDYEAKKLSLVDVNRISVIHTLQTDFRGPVAPAFA 189
Cdd:cd12905   85 RVKlcPENGYWTLRLRNGDEYWAGTQPWTRLRVTSRPQRIGVFLDCEERKVSFYNADDMSLLYSFHQGPRGKVFPFFS 162

PRY/SPRY domain in tripartite motif-binding protein 21 (TRIM21) also known as 52kD Ribonucleoprotein Autoantigen (Ro52); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM21, which is also known as Sjogren Syndrome Antigen A (SSA), SSA1, 52kD Ribonucleoprotein Autoantigen (Ro52, Ro/SSA, SS-A/Ro) or RING finger protein 81 (RNF81). TRIM21 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. As an E3 ligase, TRIM21 mediates target specificity in ubiquitination; it regulates type 1 interferon and proinflammatory cytokines via ubiquitination of interferon regulatory factors (IRFs). It is up-regulated at the site of autoimmune inflammation, such as cutaneous lupus lesions, indicating a central role in the tissue destructive inflammatory process. It interacts with auto-antigens in patients with Sjogren syndrome and systemic lupus erythematosus, a chronic systemic autoimmune disease characterized by the presence of autoantibodies against the protein component of the human intracellular ribonucleoprotein-RNA complexes and more specifically TRIM21, Ro60/TROVE2 and La/SSB proteins. It binds the Fc part of IgG molecules via its PRY-SPRY domain with unexpectedly high affinity.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751  29 GISFKLEEKTAHSSLALFRGDTGVKyglVGLEPTKVALNLERFRDWAVVLADTTVTSGRHYWEVTVKRSQQFRIGVADVD 108
Cdd:cd12900    2 MVHITLDPDTANPWLILSKDRRQVR---LGDTHQNVPENEERFDNYPMVLGAQRFNSGKHYWEVDVTGKEAWDLGVCRDS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564357751 109 MSRDSCVGADDRS--WVFSYAQRKWHSMLANEKaPIKGIGQPEKVGLLLDYEAKKLSLVDVNRI-SVIHTL-QTDFRGPV 184
Cdd:cd12900   79 VRRKGQFLLSPENgfWTIWLWNKKYEAGTSPQT-TLHLQVPPCQVGIFLDYEAGVVSFYNITDHgSLIYTFsECAFTGPL 157

                 ....
gi 564357751 185 APAF 188
Cdd:cd12900  158 RPFF 161