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 27451495 208 FWVDITLHHNEANSHIFRCGDLRSICIGCDRQNP-PHITATPTSFLAWGAQTFTSGKYYWEVHVGDSWNWAFGVCNKywk 286
Cdd:cd15821   2 FQVDMTLDVDTANNYLIISEDLRSVRCGCFRQNRkELAERFDDALCVLGSPRFTSGRHYWEVDVGTSTEWDLGVCRE--- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27451495 287 GKNQNGNIY--GEEGLFSLGCVKNDIQCSlfTTSPITLQYVPRPTNHVELFLDCEARTVSFVDVSQSSPIYTIPNCSFSP 364
Cdd:cd15821  79 SVNRQGPIElsPEHGFWTVSLRDGSVFFA--STVPLTVLWVNPRLHRVGIFLDMEMGTISFYDVSDGSHIFTFTKISAEE 156

                ....*...
gi 27451495 365 PLRPiFFC 372
Cdd:cd15821 157 PLRP-FFA 163

Ret finger protein-like (RFPL), includes RFP1, 2, 3, 4; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of RFPL protein family, which includes RFPL1, RFPL2, RFPL3 and RFPL4. In humans, RFPL transcripts can be detected at the onset of neurogenesis in differentiating human embryonic stem cells, and in the developing human neocortex. The human RFPL1, 2, 3 genes have a role in neocortex development. RFPL1 is a primate-specific target gene of Pax6, a key transcription factor for pancreas, eye and neocortex development; human RFPL1 decreases cell number through its RFPL-defining motif (RDM) and SPRY domains. The RFPL4 (also known as RFPL4A) gene encodes a putative E3 ubiquitin-protein ligase expressed in adult germ cells and interacts with oocyte proteins of the ubiquitin-proteasome degradation pathway.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27451495 208 FWVDITLHHNEANSHIFRCGDLRSICIGCDRQNP-PHITATPTSFLAWGAQTFTSGKYYWEVHVGDSWNWAFGVCNKywk 286
Cdd:cd15821   2 FQVDMTLDVDTANNYLIISEDLRSVRCGCFRQNRkELAERFDDALCVLGSPRFTSGRHYWEVDVGTSTEWDLGVCRE--- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27451495 287 GKNQNGNIY--GEEGLFSLGCVKNDIQCSlfTTSPITLQYVPRPTNHVELFLDCEARTVSFVDVSQSSPIYTIPNCSFSP 364
Cdd:cd15821  79 SVNRQGPIElsPEHGFWTVSLRDGSVFFA--STVPLTVLWVNPRLHRVGIFLDMEMGTISFYDVSDGSHIFTFTKISAEE 156

                ....*...
gi 27451495 365 PLRPiFFC 372
Cdd:cd15821 157 PLRP-FFA 163

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27451495    261 SGKYYWEVHVGDSWNWAFGVCNKYWKGKNQNGNIYgEEGLFSL-GCVKNDIQCSLFTTSPITLQYVPRptnHVELFLDCE 339
Cdd:smart00449   1 SGRHYFEVEIGDGGHWRVGVATKSVPRGYFALLGE-DKGSWGYdGDGGKKYHNSTGPEYGLPLQEPGD---VIGCFLDLE 76

                           90       100       110
                   ....*....|....*....|....*....|...
gi 27451495    340 ARTVSFVDVSQSSPIYTIPNCSFSPPLRPIFFC 372
Cdd:smart00449  77 AGTISFYKNGKYLHGLAFFDVKFSGPLYPAFSL 109

zinc finger of C3HC4-type, RING; This is a family of primate-specific Ret finger protein-like (RFPL) zinc-fingers of the C3HC4 type. Ret finger protein-like proteins are primate-specific target genes of Pax6, a key transcription factor for pancreas, eye and neocortex development. This domain is likely to be DNA-binding. This zinc-finger domain together with the RDM domain, pfam11002, forms a large zinc-finger structure of the RING/U-Box superfamily. RING-containing proteins are known to exert an E3 ubiquitin protein ligase activity with the zinc-finger structure being mandatory for binding to the E2 ubiquitin-conjugating enzyme.

                          10        20        30
                  ....*....|....*....|....*....|.
gi 27451495    15 CPICMNYFIDPVTIDCGHSFCRPCFYLNWQD 45
Cdd:pfam15227   1 CPICLDYLEKPVSIECGHSFCLSCINSLQKE 31

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)

                           10        20
                   ....*....|....*....|....*
gi 27451495     15 CPICMNYFI-DPVTIDCGHSFCRPC 38
Cdd:smart00184   1 CPICLEEYLkDPVILPCGHTFCRSC 25

E3 ubiquitin-protein ligase RMA2; Provisional

                         10        20
                 ....*....|....*....|....*....
gi 27451495   12 ELTCPICMNYFIDPVTIDCGHSFCRPCFY 40
Cdd:PLN03208  18 DFDCNICLDQVRDPVVTLCGHLFCWPCIH 46

Ret finger protein-like (RFPL), includes RFP1, 2, 3, 4; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of RFPL protein family, which includes RFPL1, RFPL2, RFPL3 and RFPL4. In humans, RFPL transcripts can be detected at the onset of neurogenesis in differentiating human embryonic stem cells, and in the developing human neocortex. The human RFPL1, 2, 3 genes have a role in neocortex development. RFPL1 is a primate-specific target gene of Pax6, a key transcription factor for pancreas, eye and neocortex development; human RFPL1 decreases cell number through its RFPL-defining motif (RDM) and SPRY domains. The RFPL4 (also known as RFPL4A) gene encodes a putative E3 ubiquitin-protein ligase expressed in adult germ cells and interacts with oocyte proteins of the ubiquitin-proteasome degradation pathway.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27451495 208 FWVDITLHHNEANSHIFRCGDLRSICIGCDRQNP-PHITATPTSFLAWGAQTFTSGKYYWEVHVGDSWNWAFGVCNKywk 286
Cdd:cd15821   2 FQVDMTLDVDTANNYLIISEDLRSVRCGCFRQNRkELAERFDDALCVLGSPRFTSGRHYWEVDVGTSTEWDLGVCRE--- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27451495 287 GKNQNGNIY--GEEGLFSLGCVKNDIQCSlfTTSPITLQYVPRPTNHVELFLDCEARTVSFVDVSQSSPIYTIPNCSFSP 364
Cdd:cd15821  79 SVNRQGPIElsPEHGFWTVSLRDGSVFFA--STVPLTVLWVNPRLHRVGIFLDMEMGTISFYDVSDGSHIFTFTKISAEE 156

                ....*...
gi 27451495 365 PLRPiFFC 372
Cdd:cd15821 157 PLRP-FFA 163

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 27451495 210 VDITLHHNEANSHIFRCGDLRSICIGCDRQNPPhitATPTSFLAW----GAQTFTSGKYYWEVHVGDSWNWAFGVC--NK 283
Cdd:cd15819   2 VNVTLDPDTAHPALILSEDGRSVTWGETRQDLP---ENPERFDSLpcvlGQEGFTSGRHYWEVEVGDRTSWDLGVCrdNV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27451495 284 YWKGKNQngnIYGEEGLFSLGCVKNDIQCslfTTSPITLQYVPRPTNHVELFLDCEARTVSFVDVSQSSPIYTIPNCSFS 363
Cdd:cd15819  79 MRKGRVT---LSPENGFWAIRLYGNEYWA---LTSPETPLTLKEPPRRVGIFLDYEAGDVSFYNMTDGSHIYTFPQTAFS 152

                ....*..
gi 27451495 364 PPLRPIF 370
Cdd:cd15819 153 GPLRPFF 159

B-box-type 2 zinc finger found in tripartite motif-containing proteins TRIM43, TRIM48, TRIM49, TRIM51, TRIM64, TRIM77 and similar proteins; The family includes a group of closely related uncharacterized tripartite motif-containing proteins, TRIM43, TRIM43B, TRIM48/RNF101, TRIM49/RNF18, TRIM49B, TRIM49C/TRIM49L2, TRIM49D/TRIM49L, TRIM51/SPRYD5, TRIM64, TRIM64B, TRIM64C, and TRIM77, whose biological functions remain unclear. TRIM49, also known as testis-specific RING-finger protein, has moderate similarity with SS-A/Ro52 antigen, suggesting it may be one of target proteins of autoantibodies in the sera of patients with these autoimmune disorders. All family members (except for TRIM51) belong to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. TRIM51 belongs to unclassified TRIM (tripartite motif) family of proteins that do not have RING fingers. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 27451495  87 SSEEQMCGIHRETKKMFCEVDRSLLCLLCSSSQEHRYHRHCPAEWAAEEHWEK 139
Cdd:cd19783   1 SSEEQICGTHRETKKLFCEADKSLLCLLCSSSQEHRAHRHYPIEWAAEEHREK 53

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 27451495 211 DITLHHNEANSHIFRCGDLRSICIGCDRQNPPHitaTPTSF----LAWGAQTFTSGKYYWEVHVGDSWNWAFGVC----N 282
Cdd:cd15811   1 DVTLDPDTANPELVLSEDRRSVRRGDLRQALPD---SPERFdpgpCVLGRERFTSGRHYWEVEVGDRTSWALGVCkenvN 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27451495 283 KYWKGKNQNGNiyGEEGLFSLGcvkndiqcSLFTTSPITLQYVPRPTNHVELFLDCEARTVSFVDVSQSSPIYTIPNCSF 362
Cdd:cd15811  78 RKEKGELSAGN--GFWILVFLG--------NYYSSERRTFAPLRDPPRRVGIFLDYEAGHLSFYSATDGSLLFIFPETPF 147

                ....*...
gi 27451495 363 SPPLRPIF 370
Cdd:cd15811 148 SGTLRPLF 155

PRY/SPRY domain of tripartite motif-binding protein 38 (TRIM38), also known as Ring finger protein 15 (RNF15); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM38, which is also known as RING finger protein 15 (RNF15) or RORET. TRIM38 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. TRIM38 has been shown to act as a suppressor in TOLL-like receptor (TLR)-mediated interferon (IFN)-beta induction by promoting degradation of TRAF6 and NAP1 through the ubiquitin-proteasome system. Another study has shown that TRIM38 may act as a novel negative regulator for TLR3-mediated IFN-beta signaling by targeting TRIF for degradation. TRIM38 has been identified as a critical negative regulator in TNFalpha- and IL-1beta-triggered activation of NF-kappaB and MAP Kinases (MAPKs); it causes degradation of two essential cellular components, TGFbeta-associated kinase 1 (TAK1)-associating chaperones 2 and 3 (TAB2/3). The degradation is promoted through a lysosomal-dependent pathway, which requires the C-terminal PRY-SPRY of TRIM38. Enterovirus 71 infection induces degradation of TRIM38, suggesting that TRIM38 may play a role in viral infections.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27451495 201 LRDRLNQFWVDITLHHNEANSHIFRCGDLRSICIGCDRQNpphITATPTSFLAW----GAQTFTSGKYYWEVHVGDSWNW 276
Cdd:cd15815   4 VKKMLRRHQVSVTLDPDTAHPELTLSKDQRQVTYGRCQEN---LDASPKRFTVLpcvlGCEGFTSGRHYFEVDVGEGTGW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27451495 277 AFGVCNK---------------YWKGKnqngnIYGEEGLFSLgcvkndiqcslftTSPIT-LQYVPRPTnHVELFLDCEA 340
Cdd:cd15815  81 DVGVCLEnvqrgfgmkqepefgFWTIR-----LCEEDGYVAL-------------TSPPTpLPLREKPL-VVGVFLDYEA 141

                       170       180       190
                ....*....|....*....|....*....|
gi 27451495 341 RTVSFVDVSQSSPIYTIPNCSFSPPLRPIF 370
Cdd:cd15815 142 GLVSFYNMTTGSHIFTFPKASFSDTLRPYF 171

PRY/SPRY domain of tripartite motif-binding protein 5, 6, 22 and 34 (TRIM5, TRIM6, TRIM22 and TRIM34); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of very close paralogs, TRIM5, TRIM6, TRIM22 and TRIM34. These domains are composed of RING/B-box/coiled-coil core and are also known as RBCC proteins. They form a locus of four closely related TRIM genes within an olfactory receptor-rich region on chromosome 11 of the human genome. Genetic analysis of this locus indicates that these four genes have evolved by gene duplication from a common ancestral gene. All genes in the TRIM6/TRIM34/TRIM5/TRIM22 locus are type I interferon inducible, with TRIM5 and TRIM22 possessing antiviral properties. TRIM5 promotes innate immune signaling by activating the TAK1 kinase complex by cooperating with the heterodimeric E2, UBC13/UEV1A. It also stimulates NFkB and AP-1 signaling, and the transcription of inflammatory cytokines and chemokines, amplifying these activities upon retroviral infection. Interaction of its PRY-SPRY or cyclophilin domains with the retroviral capsid lattice stimulates the formation of a complementary lattice by TRIM5, with greatly increased TRIM5 E3 activity, and host cell signal transduction. TRIM6 is selectively expressed in embryonic stem (ES) cells and interacts with the proto-oncogene product Myc, maintaining the pluripotency of the ES cells. TRIM6, together with E2 Ubiquitin conjugase (UbE2K) and K48-linked poly-Ub chains, is critical for the IkappaB kinase epsilon (IKKepsilon) branch of type I interferon (IFN-I) signaling pathway and subsequent establishment of a protective antiviral response. TRIM22 plays an integral role in the host innate immune response to viruses; it has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. Altered TRIM22 expression has also been associated with multiple sclerosis, cancer, and autoimmune disease. While the PRY-SPRY domain of TRIM5a provides specificity and the capsid recognition motif to retroviral restriction, TRIM34 binds HIV-1 capsid but does not restrict HIV-1 infection.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27451495 211 DITLHHNEANSHIFRCGDLRSICIGCDRQNPPHITATPTSFLAWGAQTFTSGKYYWEVHVGDSWNWAFGVCNK------- 283
Cdd:cd15810   1 DVTLNPVNISLNIVISEDQRQVRIVPPQTSGQALTNNNYDFGVLGSQYFSSGKHYWEVDVSKKSAWILGVCSHkrsdamt 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27451495 284 -----YWKGKNQNGNIYGEEGLFSLGcVKNDIQCSLFTTS-----PITLQYVPRPTNHVELFLDCEARTVSFVDVS-QSS 352
Cdd:cd15810  81 ksnanQINHQNVYSRYQPQYGYWVIG-LQNESEYNAFEDSssfnpHVLTLSVTVPPHRVGVFLDYEAGTVSFFNVTnHGS 159

                       170
                ....*....|....*...
gi 27451495 353 PIYTIPNCSFSPPLRPIF 370
Cdd:cd15810 160 LIYKFSKCCFSTTVCPYF 177

PRY/SPRY domain in tripartite motif-containing protein 22 (TRIM22), also known as RING finger protein 94 (RNF94) or Stimulated trans-acting factor of 50 kDa (STAF50); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM22, also known as RING finger protein 94 (RNF94) or STAF50 (Stimulated trans-acting factor of 50 kDa). TRIM6 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. TRIM22 is an interferon-induced protein, predominantly expressed in peripheral blood leukocytes, in lymphoid tissue such as spleen and thymus, and in the ovary.TRIM22 plays an integral role in the host innate immune response to viruses; it has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. TRIM22 inhibits influenza A virus (IAV) infection by targeting the viral nucleoprotein for degradation; it represents a novel restriction factor up-regulated upon IAV infection that curtails its replicative capacity in epithelial cells. Altered TRIM22 expression has also been associated with multiple sclerosis, cancer, and autoimmune disease. A large number of high-risk non-synonymous (ns)SNPs have been identified in the highly polymorphic TRIM22 gene, most of which are located in the SPRY domain and could possibly alter critical regions of the SPRY structural and functional residues, including several sites that undergo post-translational modification. TRIM22 is a direct p53 target gene and inhibits the clonogenic growth of leukemic cells. Its expression in Wilms tumors is negatively associated with disease relapse. It is greatly under-expressed in breast cancer cells as compared to non-malignant cell lines; p53 dysfunction may be one of the mechanisms for its down-regulation.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27451495 208 FWVDITLHHNEANSHIFRCGDLRSICIGCD----RQNPPHITAtptsFLAWGAQTFTSGKYYWEVHVGDSWNWAFGVCNK 283
Cdd:cd15824   1 YWVDVMLNPVNAVSNVVVSADQRQVTVVHIcmfrNSNPCDFSA----FDVLGCQYFSSGKYYWEVDVSGKIAWILGVYSK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27451495 284 Y--WKGKNQNG----------NIYG----EEGLFSLGcVKNDIQCSLF----TTSPITLQ-YVPRPTNHVELFLDCEART 342
Cdd:cd15824  77 RnnLNKRKSSGfafdpnvnhpNVYSryrpQNGYWVIG-LQNESEYNAFedssSSDPKVLTlSMAVPPHRVGVFLDYEAGT 155

                       170       180
                ....*....|....*....|....*....
gi 27451495 343 VSFVDVS-QSSPIYTIPNCSFSPPLRPIF 370
Cdd:cd15824 156 VSFFNVTnHGSLIYKFSKCCFSQPVYPYF 184

RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM7, TRIM11 and TRIM27, and similar proteins; TRIM7, TRIM11 and TRIM27, closely related tripartite motif-containing proteins, belong to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. TRIM7, also known as glycogenin-interacting protein (GNIP) or RING finger protein 90 (RNF90), is an E3 ubiquitin-protein ligase that mediates c-Jun/AP-1 activation by Ras signalling. Its phosphorylation and activation by MSK1 in response to direct activation by the Ras-Raf-MEK-ERK pathway can stimulate TRIM7 E3 ubiquitin ligase activity in mediating Lys63-linked ubiquitination of the AP-1 coactivator RACO-1, leading to RACO-1 protein stabilization. Moreover, TRIM7 binds and activates glycogenin, the self-glucosylating initiator of glycogen biosynthesis. TRIM11, also known as protein BIA1, or RING finger protein 92 (RNF92), is an E3 ubiquitin-protein ligase involved in the development of the central nervous system. It is overexpressed in high-grade gliomas and promotes proliferation, invasion, migration and glial tumor growth. TRIM11 acts as a potential therapeutic target for congenital central hypoventilation syndrome (CCHS) by mediating the degradation of CCHS-associated polyalanine-expanded Phox2b. TRIM11 modulates the function of neurogenic transcription factor Pax6 through the ubiquitin-proteosome system, and thus plays an essential role for Pax6-dependent neurogenesis. It also binds to and destabilizes a key component of the activator-mediated cofactor complex (ARC105), humanin, a neuroprotective peptide against Alzheimer's disease-relevant insults, and further regulates ARC105 function in transforming growth factor beta (TGFbeta) signaling. Moreover, TRIM11 negatively regulates retinoic acid-inducible gene-I (RIG-I)-mediated interferon-beta (IFNbeta) production and antiviral activity by targeting TANK-binding kinase-1 (TBK1). It may contribute to the endogenous restriction of retroviruses in cells. It enhances N-tropic murine leukemia virus (N-MLV) entry by interfering with Ref1 restriction. It also suppresses the early steps of human immunodeficiency virus HIV-1 transduction, resulting in decreased reverse transcripts. TRIM27, also known as RING finger protein 76 (RNF76), RET finger protein (RFP), or zinc finger protein RFP, is a nuclear E3 ubiquitin-protein ligase that is highly expressed in testis and in various tumor cell lines. Expression of TRIM27 is associated with prognosis of colon and endometrial cancers. TRIM27 was first identified as a fusion partner of the RET receptor tyrosine kinase. It functions as a transcriptional repressor and associates with several proteins involved in transcriptional activity, such as enhancer of polycomb 1 (Epc1), a member of the Polycomb group proteins, and Mi-2beta, a main component of the nucleosome remodeling and deacetylase (NuRD) complex, and the cell cycle regulator retinoblastoma protein (RB1). It also interacts with HDAC1, leading to downregulation of thioredoxin binding protein 2 (TBP-2), which inhibits the function of thioredoxin. Moreover, TRIM27 mediates Pax7-induced ubiquitination of MyoD in skeletal muscle atrophy. In addition, it inhibits muscle differentiation by modulating serum response factor (SRF) and Epc1. TRIM27 promotes a non-canonical polyubiquitination of PTEN, a lipid phosphatase that catalyzes PtdIns(3,4,5)P3 (PIP3) to PtdIns(4,5)P2 (PIP2). It is an IKKepsilon-interacting protein that regulates IkappaB kinase (IKK) function and negatively regulates signaling involved in the antiviral response and inflammation. TRIM27 also forms a protein complex with MBD4 or MBD2 or MBD3, and thus plays an important role in the enhancement of transcriptional repression through MBD proteins in tumorigenesis, spermatogenesis, and embryogenesis. It is a component of an estrogen receptor 1 (ESR1) regulatory complex that is involved in estrogen receptor-mediated transcription in MCF-7 cells.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 27451495   9 FQRELTCPICMNYFIDPVTIDCGHSFCRPCFYLNWQDIPILTQCFECIKTIQQRNLKTN 67
Cdd:cd16594   2 LQEELTCPICLDYFTDPVTLDCGHSFCRACIARCWEEPETSASCPQCRETCPQRNLRPN 60

PRY/SPRY domain, also known as B30.2; This domain contains residues in the N-terminus that form a distinct PRY domain structure such that the 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 core); Stonutoxin (secreted poisonous protein of the stonefish Synanceia horrida). 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. Among the TRIM proteins, also known as the N-terminal RING finger/B-box/coiled coil (RBCC) family, only Classes I and II contain the B30.2 domain that has evolved under positive selection. Class I TRIM proteins include multiple members involved in antiviral immunity at various levels of interferon signaling cascade. Among the 75 human TRIMs, roughly half enhance immune response, which they do at multiple levels in signaling pathways. 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 27451495 212 ITLHHNEANSHIFRCGDLRSICIGCDRQNPPHitaTPTSFLAW----GAQTFTSGKYYWEVHVGDSWNWAFGVCNKYWKG 287
Cdd:cd12874   1 LTFDPDTAHLNLILSDDLRSVRVGDISQHPPE---PPPRFFECwqvlGSQSFSSGRHYWEVDVQDDSSWYVGVTYKSLPR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27451495 288 KNQNGNIYGEEGLFSLGCVKNDIQCSlFTTSPITLQyvPRPTNHVELFLDCEARTVSFVDVSQS-SPIYTIpNCSFSPPL 366
Cdd:cd12874  78 KGKMSNLGRNNGSWCLEWRENEFSAW-HNNPETRLP--VTPPRRLGVFLDCDGGSLSFYGVTDGvQLLYTF-KAKFTEPL 153

                ....*
gi 27451495 367 RPIFF 371
Cdd:cd12874 154 YPAFW 158

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 27451495 207 QFWVDITLHHNEANSHIFRCGDLRSICIGCDRQNPPHitaTPTSFLA----WGAQTFTSGKYYWEVHVGDSWNWAFGVC- 281
Cdd:cd15829  16 KFRVDVTLDPETAHPNLLVSEDKKCVTFTKKKQRVPD---SPKRFTVnpvvLGFPGFHSGRHFWEVEVGDKPEWAVGVCk 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27451495 282 --------------NKYWKGKNQNGNiYGEEGlfslgcvkndiqcslftTSPITLQYVPRPTNhVELFLDCEARTVSFVD 347
Cdd:cd15829  93 dslstkarrppsgqQGCWRIQLQGGD-YDAPG-----------------AVPPPLLLEVKPRG-IGVFLDYELGEISFYN 153

                       170       180
                ....*....|....*....|....*.
gi 27451495 348 VSQSSPIYTIPNcSFSPPLRPiFFCI 373
Cdd:cd15829 154 MPEKSHIHTFTD-TFSGPLRP-YFYV 177

PRY/SPRY domain in tripartite motif-binding protein 5 (TRIM5), also known as RING finger protein 88 (RNF88); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM5 which is also known as RING finger protein 88 (RNF88) or TRIM5alpha (TRIM5a), an antiretroviral restriction factor and a retrovirus capsid sensor in immune signaling. TRIM5 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. It blocks retrovirus infection soon after the virion core enters the cell cytoplasm by recognizing the capsid protein lattice that encases the viral genomic RNA; the SPRY domain provides the capsid recognition motif that dictates specificity to retroviral restriction. TRIM5a, an E3 ubiquitin ligase, promotes innate immune signaling by activating the TAK1 kinase complex by cooperating with the heterodimeric E2, UBC13/UEV1A. It also stimulates NFkB and AP-1 signaling, and the transcription of inflammatory cytokines and chemokines, and amplifies these activities upon retroviral infection. Interaction of its PRY-SPRY or cyclophilin domains with the retroviral capsid lattice stimulates the formation of a complementary lattice by TRIM5, with greatly increased TRIM5 E3 activity, and host cell signal transduction.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27451495 199 TGLRDrLNQFWVDITLHHNEaNSHIFRCGDLRSI------CIGCDRQNPPHitatpTSFLawGAQTFTSGKYYWEVHVGD 272
Cdd:cd15822   2 NELTD-VQRYWVHVTLDPSN-NKNIVISEDRRQVryvrkqQRYNSNGNNED-----YGVL--GSPSITSGKHYWEVDVSK 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27451495 273 SWNWAFGVCNKywKGKNQNGNIYGEEGLFSLGCV--------------KNDIQ------CSLFTTSPITLqYVPRPTNHV 332
Cdd:cd15822  73 KRAWILGVCGG--KYPNSTLKDFNKQGKNNQKQCsnyqpkygywviglQNKSEynafedSSSSDPLILTL-SLTVPPCRV 149

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 27451495 333 ELFLDCEARTVSFVDVSQS-SPIYTIPNCSFSPPLRPIF 370
Cdd:cd15822 150 GVFLDYEAGTVSFFNVTNHgFLIYKFSSCSFSQEVFPYF 188

PRY/SPRY domain in tripartite motif-containing protein 34 (TRIM34), also known as RING finger protein 21 (RNF21) or interferon-responsive finger protein (IFP1); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM34, also known as RING finger protein 21 (RNF21) or interferon-responsive finger protein (IFP1). TRIM34 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. The TRIM21 cDNA possesses at least three kinds of isoforms, due to alternative splicing, of which only the long and medium forms contain the SPRY domain. It is an interferon-induced protein, predominantly expressed in the testis, kidney, and ovary. The SPRY domain provides the capsid recognition motif that dictates specificity to retroviral restriction. While the PRY-SPRY domain provides specificity and the capsid recognition motif to retroviral restriction, TRIM34 binds HIV-1 capsid but does not restrict HIV-1 infection.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27451495 255 GAQTFTSGKYYWEVHVGDSWNWAFGV-CNKYW-------KGKNQNgNIYG----EEGLFSLGcVKNDIQCSLF----TTS 318
Cdd:cd15825  41 GSQYFSSGKHYWEVDVSKKTAWILGVyCRKRSrtfkyvrQGKNHP-NVYSryrpQYGYWVIG-LQNKSEYYAFedssTSD 118

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 27451495 319 PITLQ-YVPRPTNHVELFLDCEARTVSFVDV-SQSSPIYTIPNCSFSPPLRPIF 370
Cdd:cd15825 119 PKVLTlSVATPPHRVGVFLDYEAGTVSFFNVtNHGSLIYKFSKCCFSQPVYPYF 172

RING finger, HC subclass, found in tripartite motif-containing protein TRIM4 and similar proteins; TRIM4 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. TRIM4, also known as RING finger protein 87 (RNF87), is a cytoplasmic E3 ubiquitin-protein ligase that has recently evolved and is present only in higher mammals. It transiently interacts with mitochondria, induces mitochondrial aggregation and sensitizes the cells to hydrogen peroxide (H2O2) induced death. Its interaction with peroxiredoxin 1 (PRX1) is critical for the regulation of H2O2 induced cell death. Moreover, TRIM4 functions as a positive regulator of RIG-I-mediated type I interferon induction. It regulates the K63-linked ubiquitination of RIG-1 and assembly of antiviral signaling complex at the mitochondria.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 27451495  10 QRELTCPICMNYFIDPVTIDCGHSFCRPCFYLNWQDIPILTQCFEC 55
Cdd:cd16590   4 QEELTCPICLDYFQDPVSIECGHNFCRGCLHRNWAPGGGPFPCPEC 49

PRY/SPRY domain of tripartite motif-binding protein 17 (TRIM17), also known as testis RING finger protein (terf); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM17, also known as RING finger protein 16 (RNF16) or testis RING finger protein (terf). TRIM17 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein, expressed almost exclusively in the testis. It exhibits E3 ligase activity, causing protein degradation of ZW10 interacting protein (ZWINT), a known component of the kinetochore complex required for the mitotic spindle checkpoint, and negatively regulates proliferation of breast cancer cells. TRIM17 undergoes ubiquitination in COS7 fibroblast-like cells but is inhibited and stabilized by TRIM44.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27451495 241 PPHitATPTS---FLAW----GAQTFTSGKYYWEVHV---GDSWnWAFGVC--NKYWKGKNQNGNiygEEGLFSLGCVKN 308
Cdd:cd15812  27 PPD--GTPCSkdrFLAYpcavGQETFSSGRHYWEVGMnltGDAL-WALGVCrdNVSRKDRVPKSP---ENGFWVVQLSKG 100

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27451495 309 DIQCSLFTTS-PITLQYvprPTNHVELFLDCEARTVSFVDVSQSSPIYTIPNCSFSPPLRPiFFCI 373
Cdd:cd15812 101 KKYLSAMSALtPVTLTE---PPSHMGIFLDFEAGEVSFYSVNDGSHLHTYSQAAFPGPLQP-FFCL 162

RING finger, HC subclass, found in tripartite motif-containing protein TRIM25 and similar proteins; TRIM25, also known as estrogen-responsive finger protein (EFP), RING finger protein 147 (RNF147), or RING-type E3 ubiquitin transferase, is an E3 ubiquitin/ISG15 ligase that is induced by estrogen and is therefore particularly abundant in placenta and uterus. TRIM25 regulates various cellular processes through E3 ubiquitin ligase activity, transferring ubiquitin and ISG15 to target proteins. It mediates K63-linked polyubiquitination of retinoic acid inducible gene I (RIG-I) that is crucial for downstream antiviral interferon signaling. It is also required for melanoma differentiation-associated gene 5 (MDA5) and mitochondrial antiviral signaling (MAVS, also known as IPS-1, VISA, Cardiff) mediated activation of nuclear factor-kappaB (NF-kappaB) and interferon production. Upon UV irradiation, TRIM25 interacts with mono-ubiquitinated PCNA and promotes its ISG15 modification (ISGylation), suggesting a crucial role in termination of error-prone translesion DNA synthesis. TRIM25 also functions as a novel regulator of p53 and Mdm2. It enhances p53 and Mdm2 abundance by inhibiting their ubiquitination and degradation in 26S proteasomes. Meanwhile, it inhibits p53's transcriptional activity and dampens the response to DNA damage, and is essential for medaka development and this dependence is rescued by silencing of p53. Moreover, TRIM25 is involved in the host cellular innate immune response against retroviral infection. It interferes with the late stage of feline leukemia virus (FeLV) replication. Furthermore, TRIM25 acts as an oncogene in gastric cancer. Its blockade by RNA interference inhibits migration and invasion of gastric cancer cells through transforming growth factor-beta (TGF-beta) signaling, suggesting it presents a novel target for the detection and treatment of gastric cancer. In addition, TRIM25 acts as an RNA-specific activator for Lin28a/TuT4-mediated uridylation. TRIM25 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27451495  12 ELTCPICMNYFIDPVTIDCGHSFCRPCFYLNWQD-IPILTQCFECIKTIQQR-NLKTNIRLKKMA 74
Cdd:cd16597   5 ELTCSICLELFKDPVTLPCGHNFCGVCIEKTWDSqHGSEYSCPQCRATFPRRpELHKNTVLRNIV 69

RING finger, HC subclass, found in RING finger protein 39 (RNF39) and similar proteins; RNF39, also called protein HZFw, may play a role in prolonged long term-potentiation (LTP) maintenance. It is involved in the etiology of Behcet's disease (BD). It may also be involved in HIV-1 replication. RNF39 acts as an E3 ubiquitin ligase that inhibits retinoic acid-inducible gene-I (RIG-I)-like receptor (RLR) pathways by mediating K48-linked ubiquitination and proteasomal degradation of DDX3X (DEAD-box RNA helicase 3, X-linked). RNF39 contains a typical C3HC4-type RING-HC finger.

                        10        20        30
                ....*....|....*....|....*....|....
gi 27451495  10 QRELTCPICMNYFIDPVTIDCGHSFCRPCFYLNW 43
Cdd:cd16592   2 QEETTCPICLGYFKDPVILDCEHSFCRACIARHW 35

RING finger, HC subclass, found in tripartite motif-containing protein 77 (TRIM77) and similar proteins; TRIM77 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including two consecutive zinc-binding domains, a C3HC4-type RING-HC finger and Bbox2, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 27451495  10 QRELTCPICMNYFIDPVTIDCGHSFCRPCFYLNWQDIPILTQCFECIKTIQQR 62
Cdd:cd16543   1 EDQLTCSICLDLLKDPVTIPCGHSFCMNCITLLWDRKQGVPSCPQCRESFPPR 53

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 27451495 255 GAQTFTSGKYYWEVHVGDSWNWAFGV-------------C--NKYWKGKNQNGNiygeeglfslgcvkndiQCSLFTTSP 319
Cdd:cd12905  50 ASQGFQSGRHYWEVWVGSKTKWDLGVasesvdrqarvklCpeNGYWTLRLRNGD-----------------EYWAGTQPW 112

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 27451495 320 ITLQYVPRPtNHVELFLDCEARTVSFVDVSQSSPIYtipncSFSPPLRPIFF 371
Cdd:cd12905 113 TRLRVTSRP-QRIGVFLDCEERKVSFYNADDMSLLY-----SFHQGPRGKVF 158

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 27451495 211 DITLHHNEANSHIFRCGDLRSICIGCDRQNPPHITATPTSFLA-WGAQTFTSGKYYWEVHVGDSWNWAFGVCNKY----W 285
Cdd:cd15817   1 DLILDPETAHPNLIVSEDRKAVRYRRMKPNCPYDPRRFTVYPAvLGSEGFDSGRHFWEVEVGGKGEWILGVCKDSlprnA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27451495 286 KGKNQNGNIYGEEGLFSLGCVKndiqCSLFTTsPITLQYVPRptnHVELFLDCEARTVSFVDVSQSSPIYTIPNCsFSPP 365
Cdd:cd15817  81 QDPPSPLGGCWQIGRYMSGYVA----SGPKTT-QLLPVVKPS---RIGIFLDYELGEVSFYNMNDRSHLYTFTDT-FTGK 151

                ....*.
gi 27451495 366 LRPIFF 371
Cdd:cd15817 152 LIPYFY 157