Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here are composed of the immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG). MOG, a minor component of the myelin sheath, is an important CNS-specific autoantigen, linked to the pathogenesis of multiple sclerosis (MS) and experimental autoimmune encephalomyelitis (EAE). It is a transmembrane protein having an extracellular Ig domain. MOG is expressed in the CNS on the outermost lamellae of the myelin sheath, and on the surface of oligodendrocytes, and may participate in the completion, compaction, and/or maintenance of myelin. This group also includes butyrophilin (BTN). BTN is the most abundant protein in bovine milk-fat globule membrane (MFGM).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274180  30 FIVVGPTDPILATVGENTTLRCHLSPEKNAEDMEVRWFRSQFSPAVFVYKGGRERTEEQMEEYRGRTTFVSKDISRGSVA 109
Cdd:cd05713    1 FSVIGPTEPILALVGEDAELPCHLSPKMSAEHMEVRWFRSQFSPVVHLYRDGQDQEEEQMPEYRGRTELLKDAIAEGSVA 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 215274180 110 LVIHNITAQENGTYRCYFQEGRSYDEAILHLVVA 143
Cdd:cd05713   81 LRIHNVRPSDEGQYTCFFRSGSFYEEATLELKVA 114

Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here are composed of the immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG). MOG, a minor component of the myelin sheath, is an important CNS-specific autoantigen, linked to the pathogenesis of multiple sclerosis (MS) and experimental autoimmune encephalomyelitis (EAE). It is a transmembrane protein having an extracellular Ig domain. MOG is expressed in the CNS on the outermost lamellae of the myelin sheath, and on the surface of oligodendrocytes, and may participate in the completion, compaction, and/or maintenance of myelin. This group also includes butyrophilin (BTN). BTN is the most abundant protein in bovine milk-fat globule membrane (MFGM).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274180  30 FIVVGPTDPILATVGENTTLRCHLSPEKNAEDMEVRWFRSQFSPAVFVYKGGRERTEEQMEEYRGRTTFVSKDISRGSVA 109
Cdd:cd05713    1 FSVIGPTEPILALVGEDAELPCHLSPKMSAEHMEVRWFRSQFSPVVHLYRDGQDQEEEQMPEYRGRTELLKDAIAEGSVA 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 215274180 110 LVIHNITAQENGTYRCYFQEGRSYDEAILHLVVA 143
Cdd:cd05713   81 LRIHNVRPSDEGQYTCFFRSGSFYEEATLELKVA 114

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 215274180  385 KHYWEVEVENVI--EWTVGVCRDSVERKGEVLLIPQNGFWTLEMHKGQ-YRAVSSPDRILPLKESLCRVGVFLDYEAGDV 461
Cdd:pfam00622   1 RHYFEVEIFGQDggGWRVGWATKSVPRKGERFLGDESGSWGYDGWTGKkYWASTSPLTGLPLFEPGDVIGCFLDYEAGTI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 215274180  462 SFYNMrDRSHIYTCPRSAFSVPVRPFFRLG 491
Cdd:pfam00622  81 SFTKN-GKSLGYAFRDVPFAGPLFPAVSLG 109

Immunoglobulin V-Type;

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 215274180    48 TLRCHLSPEKNAeDMEVRWFR-SQFSPAVFVYKGGRERTEEQMEEYRGRTTFvSKDISRGSVALVIHNITAQENGTYRC 125
Cdd:smart00406   3 TLSCKFSGSTFS-SYYVSWVRqPPGKGLEWLGYIGSNGSSYYQESYKGRFTI-SKDTSKNDVSLTISNLRVEDTGTYYC 79

Synaptonemal complex central element protein 1; This family of proteins includes synaptonemal complex central element protein 1, a component of the synaptonemal complex involved in meiosis, and synaptonemal complex central element protein 1-like, which may be involved in meiosis.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215274180  262 IAVCIYWINKLQKEKKILS---GEKEFERETREIALKELEKERVQKEEELQVKeklQEELR 319
Cdd:pfam15233   7 IEDLINRINELQQAKKKSSeelGEAQALWEALQRELDSLNGEKVHLEEVLNKK---QEALR 64

PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM5, TRIM6, TRIM7, TRIM10, TRIM11, TRIM17, TRIM20, TRIM21, TRIM27, TRIM35, TRIM38, TRIM41, TRIM50, TRIM58, TRIM60, TRIM62, TRIM69, TRIM72, NF7 and bloodthirsty; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several Class IV TRIM proteins, including TRIM7, TRIM35, TRIM41, TRIM50, TRIM62, TRIM69, TRIM72, TRIM protein NF7 and bloodthirsty (bty). TRIM7 interacts with glycogenin and stimulates its self-glucosylating activity via its SPRY domain. TRIM35 may play a role as a tumor suppressor and is implicated in the cell death mechanism. TRIM41 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. 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. TRIM62 is involved in the morphogenesis of the mammary gland; loss of TRIM62 gene expression in breast is associated with increased risk of recurrence in early-onset breast cancer. 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. TRIM72 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. 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 215274180 329 DVVLDPDTAHPDLFLSEDRRSVRRCPFRhlgESVPDNPERFDSQPCVLGRESFASGKHYWEVEVENVIEWTVGVCRDSVE 408
Cdd:cd13733    1 DVTLDPDTAHPNLILSEDLKSVRYGDKR---QNLPDNPERFDTCVCVLGSEGFSSGRHYWEVEVGGKTDWDLGVARESVN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274180 409 RKGEVLLIPQNGFWTLEMHKG-QYRAVSSPDRILPLKESLCRVGVFLDYEAGDVSFYNMRDRSHIYTCpRSAFSVPVRPF 487
Cdd:cd13733   78 RKGKITLSPENGYWTVGLRNGnEYKALTSPSTPLSLREKPQKVGVFLDYEEGQVSFYNVDDGSHIYTF-TDCFTEKLYPY 156

                        170
                 ....*....|....*...
gi 215274180 488 FRLGCEDS-----PIFIC 500
Cdd:cd13733  157 FSPCLNDGgknsaPLIIC 174

PRY/SPRY domain in tripartite motif-binding protein 20 (TRIM20), also known as pyrin; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM20, which is also known as pyrin or marenostrin. Unlike TRIM domains that are composed of RING/B-box/coiled-coil core, the N-terminal RING domain in TRIM20 is exchanged by a PYRIN domain (PYD), a prime mediator of protein interactions necessary for apoptosis, inflammation and innate immune signaling pathway, and it also harbors a C-terminal B30.2 domain. Mutations in pyrin (TRIM20) are associated with familial Mediterranean fever (FMF), a recessively hereditary periodic fever syndrome, characterized by episodes of inflammation and fever. These mutations cluster in the C-terminal B30.2 domain and therefore it is assumed that pyrin plays a role in the innate immune system by possibly effecting caspase-1-dependent IL-1beta maturation.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274180 320 WRRTFLHAVDVVLDPDTAHPDLFLSEDRRSVRrcpFRHLGESVPDNPERFDSQPCVLGRESFASGKHYWEVEVENVIEWT 399
Cdd:cd15813    1 LRAAQAHAVNVTLDPETAHPNLIFSDDLKSVR---LGNKWDRLPDNPERFDSCIIVLGSPSFTSGRHYWEVEVGDKTGWI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274180 400 VGVCRDSVERKGEVLLIPQNGFWTLEMHKG-QYRAVSSPDRILPLKESLCRVGVFLDYEAGDVSFYNMRDRSHIYTCPRS 478
Cdd:cd15813   78 LGVCKASVSRKGSMTLSPENGYWVVMMTKRnEYQASTSPPTRLWLREPPRRVGIFLDYEAGDISFYNVTAKSHIYTFTSF 157

                        170       180
                 ....*....|....*....|....*..
gi 215274180 479 AFSVPVRPFFRLGCED-----SPIFIC 500
Cdd:cd15813  158 SSSGPLQPIFSPGTHDggknmDPLTIC 184

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 215274180 329 DVVLDPDTAHPDLFLSEDRRSVRRCPFRHlgeSVPDNPERFDSQPCVLGRESFASGKHYWEVEVENVIEWTVGVCRDSVE 408
Cdd:cd12888    1 NVTLDPDTAHPRLVLSEDRKSVRWGDTRQ---DLPDNPERFDTWPCVLGCEGFTSGRHYWEVEVGDGGGWAVGVARESVR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274180 409 RKGEVLLIPQNGFWTLEMHKGQYRAVSSPDRILPLKESLCRVGVFLDYEAGDVSFYNMRDRSHIYTCPRSAFSVP-VRPF 487
Cdd:cd12888   78 RKGEISFSPEEGIWAVGQWGGQYWALTSPETPLPLSEVPRRIRVYLDYEGGQVAFFDADNEAPIFTFPPASFAGErIFPW 157

                        170
                 ....*....|...
gi 215274180 488 FRLgCEDSPIFIC 500
Cdd:cd12888  158 FWV-GKGSQLKLC 169

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 215274180 328 VDVVLDPDTAHPDLFLSEDRRSVRrcpFRHLGESVPDNPERFDSQPCVLGRESFASGKHYWEVEVENVIEWTVGVCRDSV 407
Cdd:cd15829   19 VDVTLDPETAHPNLLVSEDKKCVT---FTKKKQRVPDSPKRFTVNPVVLGFPGFHSGRHFWEVEVGDKPEWAVGVCKDSL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274180 408 ERKGEVLLIPQNGFWTLEMHKGQYRAVSSPDRILPLKESLCRVGVFLDYEAGDVSFYNMRDRSHIYTCpRSAFSVPVRPF 487
Cdd:cd15829   96 STKARRPPSGQQGCWRIQLQGGDYDAPGAVPPPLLLEVKPRGIGVFLDYELGEISFYNMPEKSHIHTF-TDTFSGPLRPY 174

                        170
                 ....*....|...
gi 215274180 488 FRLGCEDSPIFIC 500
Cdd:cd15829  175 FYVGPDSKPLRIC 187

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 215274180 326 HAVDVVLDPDTAHPDLFLSEDRRSVRRcpfRHLGESVPDNPERFDSQPCVLGRESFASGKHYWEVEVENVIEWTVGVCRD 405
Cdd:cd15815   11 HQVSVTLDPDTAHPELTLSKDQRQVTY---GRCQENLDASPKRFTVLPCVLGCEGFTSGRHYFEVDVGEGTGWDVGVCLE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274180 406 SVERKGEVLLIPQNGFWTLEMHKGQ-YRAVSSPDRILPLKESLCRVGVFLDYEAGDVSFYNMRDRSHIYTCPRSAFSVPV 484
Cdd:cd15815   88 NVQRGFGMKQEPEFGFWTIRLCEEDgYVALTSPPTPLPLREKPLVVGVFLDYEAGLVSFYNMTTGSHIFTFPKASFSDTL 167

                        170
                 ....*....|....*
gi 215274180 485 RPFFRLgCEDSPIFI 499
Cdd:cd15815  168 RPYFQV-YQYSPLFL 181

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 215274180 327 AVDVVLDPDTAHPDLFLSEDRRSVRrcpFRHLGESVPDNPERFDSQPCVLGRESFASGKHYWEVEVENVIEWTVGVCRDS 406
Cdd:cd15814    1 SVDVTLDPDTAYPSLILSDNLRQVR---YSYLQQDLPDNPERFNLFPCVLGSPCFIAGRHYWEVEVGDKAKWTIGVCEDS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274180 407 VERKGEVLLIPQNGFWTLEMHKG-QYRAVSSPDRILPLKESLCRVGVFLDYEAGDVSFYNMRDRSHIYTCPRSAFSVPVR 485
Cdd:cd15814   78 VCRKGGVTSAPQNGFWAVSLWYGkEYWALTSPMTALPLRTPLQRVGIFLDYDAGEVSFYNVTERCHTFTFSHATFCGPVR 157

                        170       180
                 ....*....|....*....|
gi 215274180 486 PFFRL----GCEDSPIFICP 501
Cdd:cd15814  158 PYFSLsysgGKSAAPLIICP 177

PRY/SPRY domain in tripartite motif-containing protein 35 (TRIM35); This PRY/SPRY domain is found at the C-terminus of the overall domain architecture of tripartite motif 35, TRIM35 (also known as hemopoietic lineage switch protein), which includes a RING finger domain (RING) and a B-box motif (BBOX). TRIM35 may play a role as a tumor suppressor and is implicated in the cell death mechanism.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274180 330 VVLDPDTAHPDLFLSEDRRSVRRCPFRhlgESVPDNPERFDSQPCVLGRESFASGKHYWEVEVENVIEWTVGVCRDSVER 409
Cdd:cd12893    2 VTLDPNTAHPWLSLSEDLTSVRYSSEK---QQLPDNPERFDPYPCVLGSEGFTSGKHSWDVEVGDNTSWMLGVAKESVQR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274180 410 KGEVLLIPQNGFWTLEMHKGQYRAVSSPDRI--LPLKESLCRVGVFLDYEAGDVSFYNMRDRSHIYTCpRSAFSVPVRPF 487
Cdd:cd12893   79 KGKFTLSPESGFWTIGFSEGKYSARTSPEPRtpLRVKQKPQRIRVQLDWDRGKVSFSDPDTNTHIHTF-THTFTERVFPY 157

                        170
                 ....*....|....
gi 215274180 488 FRLGCEDSPIFICP 501
Cdd:cd12893  158 FYTGCKSEPLRILP 171

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 215274180 330 VVLDPDTAHPDLFLSEDRRSVRRCPFRHLgesVPDNPERFDSQPCVLGRESFASGKHYWEVEVENVIEWTVGVCRDSVER 409
Cdd:cd15818   15 ITLDPKTAHPNLILSEDLTCVWHGDTKQM---LPDNPERFDSSVAVLGSEGFTSGKHYWEVEVAKKTKWTLGVVRESINR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274180 410 KGEVLLIPQNGFWTLEM-HKGQYRAVSSPDRILPLKESLCRVGVFLDYEAGDVSFYNMRDRSHIYTCpRSAFSVPVRPFF 488
Cdd:cd15818   92 KGNCPLSPEDGFWLLRLrNQNELKALDVPSFSLTLTSNLNKVGIYLDYEGGQVSFYNANTMSHIYTF-SDTFTEKIYPYF 170

                        170       180
                 ....*....|....*....|..
gi 215274180 489 rlgcedspifiCPAL--TGANG 508
Cdd:cd15818  171 -----------CPCLndSGENK 181

PRY/SPRY domain of tripartite motif-binding protein 60 (TRIM60) also known as RING finger protein 33 (RNF33); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM60, which is also known as RING finger protein 33 (RNF33) or 129 (RNF129). TRIM60 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274180 328 VDVVLDPDTAHPDLFLSEDRRSVRrcpFRHLGESVPDNPERFDSQPCVLGRESFASGKHYWEVEVENVIEWTVGVCRDSV 407
Cdd:cd15828   10 VDVTLDPETAHPQLTVSEDRKSVL---YGEMKQNVCYNPRRFYLCPAVLGSEGFHSGRQYWEVEVGDKPEWTLGVCQDCL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274180 408 ERKGEVLLIPQNGFWTLEMHKGQYRAVSSPDRI--LPlKESLCRVGVFLDYEAGDVSFYNMRDRSHIYTCpRSAFSVPVR 485
Cdd:cd15828   87 PRNWSNQPSVQDGLWAIGRYSESNYVALGPKKIqlLP-KVRPSKIGIFLDYELGEVSFYNMNDRSLLYTF-SDSFTGTLW 164

                        170
                 ....*....|....*.
gi 215274180 486 PFFRLGCEDSPIFICP 501
Cdd:cd15828  165 PYFYTGTDSEPLKICT 180

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 215274180 330 VVLDPDTAHPDLFLSEDRRSVRRCPFRhlgESVPDNPERFDSQPCVLGRESFASGKHYWEVEVENVIEWTVGVCRDSVER 409
Cdd:cd12905    6 LTFDPETAHPSLILSRDLTAVTESDEM---QPYPRSPKRFLQCVNVLASQGFQSGRHYWEVWVGSKTKWDLGVASESVDR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274180 410 KGEVLLIPQNGFWTLEMHKG-QYRAVSSPDRILPLKESLCRVGVFLDYEAGDVSFYNMRDRSHIYTcprsaFSVPVR--- 485
Cdd:cd12905   83 QARVKLCPENGYWTLRLRNGdEYWAGTQPWTRLRVTSRPQRIGVFLDCEERKVSFYNADDMSLLYS-----FHQGPRgkv 157

                        170       180
                 ....*....|....*....|.
gi 215274180 486 -PFFRLGCEDS-----PIFIC 500
Cdd:cd12905  158 fPFFSTCFSDDgqnaePMRLL 178

PRY/SPRY domain in tripartite motif-binding protein 15 (TRIM15); 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 15 (TRIM15), also referred to as RING finger protein 93 (RNF93) or Zinc finger protein B7 or 178 (ZNFB7 or ZNF178). TRIM15 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. The PRY and SPRY/B30.2 domains can function as immune defense components and in pathogen sensing. TRIM15 has been shown to regulate inflammatory and innate immune signaling, in addition to displaying antiviral activities. Down-regulation of TRIM15, as well as TRIM11, enhances virus release, suggesting that these proteins contribute to the endogenous restriction of retroviruses in cells. TRIM15 is also a regulatory component of focal adhesion turnover and cell migration.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274180 330 VVLDPDTAHPDLFLSEDRRSVRrcpFRHLGESVPDNPERFDSQPCVLGRESFASGKHYWEVEVE--NVIEWTVGVCRDSV 407
Cdd:cd15826    2 VTLDPQTASGSLVLSEDRKSVR---YTRQKQNLPDSPLRFDGLPAVLGSPGFSSGRHRWQVEVQlgDGGGCTVGVAGESV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274180 408 ERKGEVLLIPQNGFWTLEMHKGQYRAVSSPDRILPLKESLCRVGVFLDYEAGDVSFYNMRDRSHIYTCPRSaFSVPVRPF 487
Cdd:cd15826   79 RRKGEMGLSAEDGVWAVILSHQQCWASTSPGTDLPLSEIPRRVGVALDYEAGTVTLTNAETQEPIFTFTAS-FSGKVFPF 157

                 ...
gi 215274180 488 FRL 490
Cdd:cd15826  158 FAV 160

PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7); 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 7 (TRIM7), also referred to as glycogenin-interacting protein (GNIP) or RING finger protein 90 (RNF90). TRIM7 or GNIP interacts with glycogenin and stimulates its self-glucosylating activity via its SPRY domain. The GNIP gene encodes at least four distinct isoforms of GNIP, of which three (GNIP1, GNIP2, and GNIP3) have the B30.2 domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274180 329 DVVLDPDTAHPDLFLSEDRRSVRrcpfrhLGE---SVPDNPERFDSQPCVLGRESFASGKHYWEVEVENVIEWTVGVCRD 405
Cdd:cd13740    1 ELTLDPDSANPRLILSLDLKSVR------LGEraqDLPNHPCRFDTNTRVLASCGFSSGRHHWEVEVGSKDGWAFGVARE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274180 406 SVERKGEVLLIPQNGFWTLEMHKGQYRAVSSPDRIlPLK-ESLCRVGVFLDYEAGDVSFYNMRDRSHIYTCpRSAFSVPV 484
Cdd:cd13740   75 SVRRKGLTPFTPEEGVWALQLNGGQYWAVTSPERT-PLScGHLSRVRVALDLEVGAVSFYAAEDMRHIYTF-RVNFQERV 152

                        170
                 ....*....|....*..
gi 215274180 485 RPFFRLGCEDSPIFICP 501
Cdd:cd13740  153 FPLFSVCSTGTYLRIWP 169

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 215274180   383 SGKHYWEVEVENVIEWTVGVCRDSVERKGEVLLIPQNGFWTLEMHKGQ-YRAVSSPDRILPLKESLCRVGVFLDYEAGDV 461
Cdd:smart00449   1 SGRHYFEVEIGDGGHWRVGVATKSVPRGYFALLGEDKGSWGYDGDGGKkYHNSTGPEYGLPLQEPGDVIGCFLDLEAGTI 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 215274180   462 SFYNMRDRSHIYTCPRSAFSVPVRPFFRLGCEDS-PIFICP 501
Cdd:smart00449  81 SFYKNGKYLHGLAFFDVKFSGPLYPAFSLGSGNSvRLNFGP 121

PRY/SPRY domain in tripartite motif-binding protein 62 (TRIM62); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM62. It is also called DEAR1 ductal epithelium (associated RING chromosome 1) and is involved in the morphogenesis of the mammary gland; loss of TRIM62 gene expression in breast is associated with increased risk of recurrence in early-onset breast cancer and thus, making TRIM62 a predictive biomarker. Non-small cell lung cancer lesions show a step-wise loss of TRIM62 levels during disease progression, indicating that it may play a role in the evolution of lung cancer. Decreased levels of TRIM62 also represent an independent adverse prognostic factor in AML.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274180 330 VVLDPDTAHPDLFLSEDrrsvrrCPFRHLGESVP----DNPERFDSQPCVLGRESFASGKHYWEVEVENVIEWTVGVCRD 405
Cdd:cd13744   14 LTLDPVTAHQRLILSDD------CTIVAYGNLHPqplqDSPKRFDVEVSVLGSEGFSGGVHYWEVVVSEKTQWMIGLAHE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274180 406 SVERKGEVLLIPQNGFWTLEMHKG-QYRAVSSPDRILPLKESLCRVGVFLDYEAGDVSFYNMRDRSHIYTCpRSAFSVPV 484
Cdd:cd13744   88 AVSRKGSIQIQPGRGFYCIVMHDGnQYSACTEPWTRLNVKSKLEKVGVYLDYDKGLLIFYNADDMSWLYTF-REKFPGKL 166

                 ....*..
gi 215274180 485 RPFFRLG 491
Cdd:cd13744  167 CSYFSPG 173

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.