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Conserved domains on  [gi|19923536|ref|NP_061008|]
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erythroid membrane-associated protein precursor [Homo sapiens]

Protein Classification

Ig and SPRY_PRY_TRIM20 domain-containing protein( domain architecture ID 10958096)

Ig and SPRY_PRY_TRIM20 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SPRY_PRY_TRIM20 cd15813
PRY/SPRY domain in tripartite motif-binding protein 20 (TRIM20), also known as pyrin; This ...
230-412 2.94e-129

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.


:

Pssm-ID: 293985  Cd Length: 184  Bit Score: 372.17  E-value: 2.94e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 230 WRRARLHFVAVTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGV 309
Cdd:cd15813   1 LRAAQAHAVNVTLDPETAHPNLIFSDDLKSVRLGNKWDRLPDNPERFDSCIIVLGSPSFTSGRHYWEVEVGDKTGWILGV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 310 CSESVSRKGKVTASPANGHWLLRQSRGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTFTHNFS- 388
Cdd:cd15813  81 CKASVSRKGSMTLSPENGYWVVMMTKRNEYQASTSPPTRLWLREPPRRVGIFLDYEAGDISFYNVTAKSHIYTFTSFSSs 160
                       170       180
                ....*....|....*....|....
gi 19923536 389 GPLRPFFEPCLHDGGKNTAPLVIC 412
Cdd:cd15813 161 GPLQPIFSPGTHDGGKNMDPLTIC 184
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
39-144 1.14e-33

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd05713:

Pssm-ID: 472250  Cd Length: 114  Bit Score: 122.69  E-value: 1.14e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536  39 VALLGGTAELLCPLSlwpgtvPK------EVRWLRSPFpqrSQAVHIFRDGKDQDEDLMPEYKGRTVLVRDA-QEGSVTL 111
Cdd:cd05713  11 LALVGEDAELPCHLS------PKmsaehmEVRWFRSQF---SPVVHLYRDGQDQEEEQMPEYRGRTELLKDAiAEGSVAL 81
                        90       100       110
                ....*....|....*....|....*....|...
gi 19923536 112 QILDVRLEDQGSYRCLIQVGNLSKEDTVILQVA 144
Cdd:cd05713  82 RIHNVRPSDEGQYTCFFRSGSFYEEATLELKVA 114
 
Name Accession Description Interval E-value
SPRY_PRY_TRIM20 cd15813
PRY/SPRY domain in tripartite motif-binding protein 20 (TRIM20), also known as pyrin; This ...
230-412 2.94e-129

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.


Pssm-ID: 293985  Cd Length: 184  Bit Score: 372.17  E-value: 2.94e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 230 WRRARLHFVAVTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGV 309
Cdd:cd15813   1 LRAAQAHAVNVTLDPETAHPNLIFSDDLKSVRLGNKWDRLPDNPERFDSCIIVLGSPSFTSGRHYWEVEVGDKTGWILGV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 310 CSESVSRKGKVTASPANGHWLLRQSRGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTFTHNFS- 388
Cdd:cd15813  81 CKASVSRKGSMTLSPENGYWVVMMTKRNEYQASTSPPTRLWLREPPRRVGIFLDYEAGDISFYNVTAKSHIYTFTSFSSs 160
                       170       180
                ....*....|....*....|....
gi 19923536 389 GPLRPFFEPCLHDGGKNTAPLVIC 412
Cdd:cd15813 161 GPLQPIFSPGTHDGGKNMDPLTIC 184
IgV_MOG_like cd05713
Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here ...
39-144 1.14e-33

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).


Pssm-ID: 409378  Cd Length: 114  Bit Score: 122.69  E-value: 1.14e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536  39 VALLGGTAELLCPLSlwpgtvPK------EVRWLRSPFpqrSQAVHIFRDGKDQDEDLMPEYKGRTVLVRDA-QEGSVTL 111
Cdd:cd05713  11 LALVGEDAELPCHLS------PKmsaehmEVRWFRSQF---SPVVHLYRDGQDQEEEQMPEYRGRTELLKDAiAEGSVAL 81
                        90       100       110
                ....*....|....*....|....*....|...
gi 19923536 112 QILDVRLEDQGSYRCLIQVGNLSKEDTVILQVA 144
Cdd:cd05713  82 RIHNVRPSDEGQYTCFFRSGSFYEEATLELKVA 114
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
291-414 1.24e-29

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


Pssm-ID: 214669  Cd Length: 122  Bit Score: 112.00  E-value: 1.24e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536    291 GCHYWEVYVGDKTKWILGVCSESVSRKGKVTASPANGHWLLRQSRGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVIS 370
Cdd:smart00449   2 GRHYFEVEIGDGGHWRVGVATKSVPRGYFALLGEDKGSWGYDGDGGKKYHNSTGPEYGLPLQEPGDVIGCFLDLEAGTIS 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 19923536    371 FYNVTNKSHIFTFTH-NFSGPLRPFFepCLhdGGKNTAPLVICSE 414
Cdd:smart00449  82 FYKNGKYLHGLAFFDvKFSGPLYPAF--SL--GSGNSVRLNFGPL 122
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
293-395 5.58e-29

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.


Pssm-ID: 459877  Cd Length: 121  Bit Score: 110.51  E-value: 5.58e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536   293 HYWEVYVG--DKTKWILGVCSESVSRKGKVTASPANGHWLLRQSRGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVIS 370
Cdd:pfam00622   2 HYFEVEIFgqDGGGWRVGWATKSVPRKGERFLGDESGSWGYDGWTGKKYWASTSPLTGLPLFEPGDVIGCFLDYEAGTIS 81
                          90       100
                  ....*....|....*....|....*.
gi 19923536   371 FYNVtNKSHIFTFTH-NFSGPLRPFF 395
Cdd:pfam00622  82 FTKN-GKSLGYAFRDvPFAGPLFPAV 106
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
42-128 3.60e-10

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 57.08  E-value: 3.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536    42 LGGTAELLCPLSLWPGTVPKEVRWLRSPFPQRSQAVHIFRDGKDQdedlMPEYKGRTVLVRDAQEGSVTLQILDVRLEDQ 121
Cdd:pfam07686  10 LGGSVTLPCTYSSSMSEASTSVYWYRQPPGKGPTFLIAYYSNGSE----EGVKKGRFSGRGDPSNGDGSLTIQNLTLSDS 85

                  ....*..
gi 19923536   122 GSYRCLI 128
Cdd:pfam07686  86 GTYTCAV 92
IGv smart00406
Immunoglobulin V-Type;
45-128 1.21e-08

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 52.00  E-value: 1.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536     45 TAELLCplSLWPGTVPK-EVRWLRSPfpQRSQAVHIFRDGKDQDEDLMPEYKGRTVLVRDAQEGSVTLQILDVRLEDQGS 123
Cdd:smart00406   1 SVTLSC--KFSGSTFSSyYVSWVRQP--PGKGLEWLGYIGSNGSSYYQESYKGRFTISKDTSKNDVSLTISNLRVEDTGT 76

                   ....*
gi 19923536    124 YRCLI 128
Cdd:smart00406  77 YYCAV 81
 
Name Accession Description Interval E-value
SPRY_PRY_TRIM20 cd15813
PRY/SPRY domain in tripartite motif-binding protein 20 (TRIM20), also known as pyrin; This ...
230-412 2.94e-129

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.


Pssm-ID: 293985  Cd Length: 184  Bit Score: 372.17  E-value: 2.94e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 230 WRRARLHFVAVTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGV 309
Cdd:cd15813   1 LRAAQAHAVNVTLDPETAHPNLIFSDDLKSVRLGNKWDRLPDNPERFDSCIIVLGSPSFTSGRHYWEVEVGDKTGWILGV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 310 CSESVSRKGKVTASPANGHWLLRQSRGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTFTHNFS- 388
Cdd:cd15813  81 CKASVSRKGSMTLSPENGYWVVMMTKRNEYQASTSPPTRLWLREPPRRVGIFLDYEAGDISFYNVTAKSHIYTFTSFSSs 160
                       170       180
                ....*....|....*....|....
gi 19923536 389 GPLRPFFEPCLHDGGKNTAPLVIC 412
Cdd:cd15813 161 GPLQPIFSPGTHDGGKNMDPLTIC 184
SPRY_PRY_C-I_1 cd13733
PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM5, TRIM6, TRIM7, ...
240-412 3.86e-112

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.


Pssm-ID: 293968 [Multi-domain]  Cd Length: 174  Bit Score: 327.90  E-value: 3.86e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 240 VTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRKGK 319
Cdd:cd13733   2 VTLDPDTAHPNLILSEDLKSVRYGDKRQNLPDNPERFDTCVCVLGSEGFSSGRHYWEVEVGGKTDWDLGVARESVNRKGK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 320 VTASPANGHWLLRQSRGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTFTHNFSGPLRPFFEPCL 399
Cdd:cd13733  82 ITLSPENGYWTVGLRNGNEYKALTSPSTPLSLREKPQKVGVFLDYEEGQVSFYNVDDGSHIYTFTDCFTEKLYPYFSPCL 161
                       170
                ....*....|...
gi 19923536 400 HDGGKNTAPLVIC 412
Cdd:cd13733 162 NDGGKNSAPLIIC 174
SPRY_PRY_TRIM39 cd13745
PRY/SPRY domain in tripartite motif-binding protein 39 (TRIM39) and TRIM39-like; This domain, ...
238-413 3.03e-111

PRY/SPRY domain in tripartite motif-binding protein 39 (TRIM39) and TRIM39-like; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of pyrin, several tripartite motif-containing proteins (TRIMs), including E3 ubiquitin-protein ligase (TRIM21), RET finger protein (RFP)/tripartite motif protein 27 (TRIM27), as well as butyrophilin (Btns) and butyrophilin-like (Btnl) family members, with the exception of Btnl2. Btn and Btnl family members are novel regulators of immune responses, with many of the genes located within the MHC. They are implicated in T-cell inhibition and modulation of epithelial cell-T cell interactions. TRIM21 (also known as RO52, SSA1 or RNF81) is a major autoantigen in autoimmune diseases such as rheumatoid arthritis, systemic lupus erythematosus, and Sjorgen's syndrome. TRIM27 (also known as Ret finger protein, RFP or RNF76) negatively regulates CD4 T-cells by ubiquitinating and inhibiting the class II phosphatidylinositol 3 kinase C2beta (PI3K-C2beta), a kinase critical for KCa3.1 channel activation. The PRY/SPRY domain of Pyrin, which is mutated in familial Mediterranean fever patients, interacts with inflammasome components and inhibits proIL-1beta processing.


Pssm-ID: 293979 [Multi-domain]  Cd Length: 177  Bit Score: 326.12  E-value: 3.03e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 238 VAVTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRK 317
Cdd:cd13745   3 VDVTLDPDTAHPNLVLSEDRKSVRHGDTRQDLPDNPERFDTYPCVLGAEGFTGGRHYWEVEVGDKTEWTLGVCRESVSRK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 318 GKVTASPANGHWLLRQsRGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTFTHNFSGPLRPFFEP 397
Cdd:cd13745  83 GEVTLSPENGYWTVWL-RDGKYEALTSPPTPLPVSVRPSRVGIFLDYEAGEVSFYNVTDRSHLFTFTDTFSGTLRPYFYP 161
                       170
                ....*....|....*.
gi 19923536 398 CLHDGGKNTAPLVICS 413
Cdd:cd13745 162 GLNAGGKNAAPLIICP 177
SPRY_PRY_BTN1_2 cd15819
butyrophilin subfamily member A1 and A2 (BTN1A and BTN2A); This domain, consisting of the ...
238-412 5.82e-89

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.


Pssm-ID: 293991 [Multi-domain]  Cd Length: 172  Bit Score: 268.71  E-value: 5.82e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 238 VAVTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRK 317
Cdd:cd15819   2 VNVTLDPDTAHPALILSEDGRSVTWGETRQDLPENPERFDSLPCVLGQEGFTSGRHYWEVEVGDRTSWDLGVCRDNVMRK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 318 GKVTASPANGHWLLRQSrGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTFTHN-FSGPLRPFFE 396
Cdd:cd15819  82 GRVTLSPENGFWAIRLY-GNEYWALTSPETPLTLKEPPRRVGIFLDYEAGDVSFYNMTDGSHIYTFPQTaFSGPLRPFFR 160
                       170
                ....*....|....*.
gi 19923536 397 PCLHDGGkntaPLVIC 412
Cdd:cd15819 161 LWSSDSG----PLTIC 172
SPRY_PRY_TRIM69 cd15818
PRY/SPRY domain in tripartite motif-binding protein 69 (TRIM69), also known as RING finger ...
240-411 1.10e-76

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.


Pssm-ID: 293990 [Multi-domain]  Cd Length: 187  Bit Score: 238.16  E-value: 1.10e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 240 VTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRKGK 319
Cdd:cd15818  15 ITLDPKTAHPNLILSEDLTCVWHGDTKQMLPDNPERFDSSVAVLGSEGFTSGKHYWEVEVAKKTKWTLGVVRESINRKGN 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 320 VTASPANGHWLLRQSRGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTFTHNFSGPLRPFFEPCL 399
Cdd:cd15818  95 CPLSPEDGFWLLRLRNQNELKALDVPSFSLTLTSNLNKVGIYLDYEGGQVSFYNANTMSHIYTFSDTFTEKIYPYFCPCL 174
                       170
                ....*....|..
gi 19923536 400 HDGGKNTAPLVI 411
Cdd:cd15818 175 NDSGENKEPLKI 186
SPRY_PRY_TRIM75 cd15829
PRY/SPRY domain of tripartite motif-binding protein 75 (TRIM75); This domain, consisting of ...
238-412 3.10e-71

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.


Pssm-ID: 294001  Cd Length: 187  Bit Score: 224.09  E-value: 3.10e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 238 VAVTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRK 317
Cdd:cd15829  19 VDVTLDPETAHPNLLVSEDKKCVTFTKKKQRVPDSPKRFTVNPVVLGFPGFHSGRHFWEVEVGDKPEWAVGVCKDSLSTK 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 318 GKVTASPANGHWLLRQsRGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTFTHNFSGPLRPFFep 397
Cdd:cd15829  99 ARRPPSGQQGCWRIQL-QGGDYDAPGAVPPPLLLEVKPRGIGVFLDYELGEISFYNMPEKSHIHTFTDTFSGPLRPYF-- 175
                       170
                ....*....|....*
gi 19923536 398 CLhdgGKNTAPLVIC 412
Cdd:cd15829 176 YV---GPDSKPLRIC 187
SPRY_PRY_BTN3 cd15820
PRY/SPRY domain of butyrophilin 3 (BTN3), includes BTN3A1, BTN3A2, BTN3A3 as well as BTN-like ...
240-412 3.34e-70

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.


Pssm-ID: 293992 [Multi-domain]  Cd Length: 176  Bit Score: 220.76  E-value: 3.34e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 240 VTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRKGK 319
Cdd:cd15820   6 VILDPDTANPILLISEDQRSLQWADEPQNLPDNPKRFDWHYCVLGCKSFTSGRHFWEVEVGDRKEWYVGVCRENVERKLW 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 320 VTASPANGHWLLRQSRGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTFTH-NFSGPLRPFFEPC 398
Cdd:cd15820  86 VKMAPENGFWTIGLSDGNDYQALTDPRTKLTIANPPQRVGVFLDYETGEVSFYNAMDGSHIYTFPHtSFSGPLYPVFRLL 165
                       170
                ....*....|....
gi 19923536 399 LHDggknTAPLVIC 412
Cdd:cd15820 166 SWD----PTALTIC 175
SPRY_PRY_TRIM58 cd15816
PRY/SPRY domain in tripartite motif-binding protein 58 (TRIM58), also known as BIA2; This ...
240-411 1.41e-69

PRY/SPRY domain in tripartite motif-binding protein 58 (TRIM58), also known as BIA2; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM58, also known as BIA2. TRIM58 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins.It is implicated by genome-wide association studies (GWAS) to regulate erythrocyte traits, including cell size and number. Trim58 facilitates erythroblast enucleation by inducing proteolytic degradation of the microtubule motor dynein.


Pssm-ID: 293988 [Multi-domain]  Cd Length: 168  Bit Score: 218.89  E-value: 1.41e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 240 VTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRKGK 319
Cdd:cd15816   2 VKLDPATAHPSLLLTADLRSVQDGELWRDVPGNPERFDTWPCVLGLQSFSSGRHYWEVAVGEKAEWGLGVCQDSAPRKGE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 320 VTASPANGHWLLRQSRGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTFTHNFSGPLRPFFEPCl 399
Cdd:cd15816  82 TTPSPENGVWAVWLLKGNEYMVLASPSVPLLQLRRPRRVGVFLDYEAGEISFYNVTAGSHIYTFRQLFSGILRPYFFVC- 160
                       170
                ....*....|..
gi 19923536 400 hdggkNTAPLVI 411
Cdd:cd15816 161 -----DTTPLTL 167
SPRY_PRY_A33L cd12905
zinc-binding protein A33-like; This domain, consisting of the distinct N-terminal PRY ...
239-412 4.70e-69

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.


Pssm-ID: 293962 [Multi-domain]  Cd Length: 178  Bit Score: 218.05  E-value: 4.70e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 239 AVTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRKG 318
Cdd:cd12905   5 PLTFDPETAHPSLILSRDLTAVTESDEMQPYPRSPKRFLQCVNVLASQGFQSGRHYWEVWVGSKTKWDLGVASESVDRQA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 319 KVTASPANGHWLLRQSRGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTFTHNFSGPLRPFFEPC 398
Cdd:cd12905  85 RVKLCPENGYWTLRLRNGDEYWAGTQPWTRLRVTSRPQRIGVFLDCEERKVSFYNADDMSLLYSFHQGPRGKVFPFFSTC 164
                       170
                ....*....|....
gi 19923536 399 LHDGGKNTAPLVIC 412
Cdd:cd12905 165 FSDDGQNAEPMRLL 178
SPRY_PRY_TRIM21 cd12900
PRY/SPRY domain in tripartite motif-binding protein 21 (TRIM21) also known as 52kD ...
236-412 7.27e-69

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.


Pssm-ID: 293957  Cd Length: 180  Bit Score: 217.44  E-value: 7.27e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 236 HFVAVTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVS 315
Cdd:cd12900   1 HMVHITLDPDTANPWLILSKDRRQVRLGDTHQNVPENEERFDNYPMVLGAQRFNSGKHYWEVDVTGKEAWDLGVCRDSVR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 316 RKGKVTASPANGHWLLRQSRGnEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTN-KSHIFTFTH-NFSGPLRP 393
Cdd:cd12900  81 RKGQFLLSPENGFWTIWLWNK-KYEAGTSPQTTLHLQVPPCQVGIFLDYEAGVVSFYNITDhGSLIYTFSEcAFTGPLRP 159
                       170
                ....*....|....*....
gi 19923536 394 FFEPCLHDGGKNTAPLVIC 412
Cdd:cd12900 160 FFNPGFNDSGGNAAPLTLC 178
SPRY_PRY_TRIM7_like cd12888
PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7)-like, including TRIM7, TRIM10, ...
240-395 8.66e-69

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.


Pssm-ID: 293946 [Multi-domain]  Cd Length: 169  Bit Score: 217.04  E-value: 8.66e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 240 VTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRKGK 319
Cdd:cd12888   2 VTLDPDTAHPRLVLSEDRKSVRWGDTRQDLPDNPERFDTWPCVLGCEGFTSGRHYWEVEVGDGGGWAVGVARESVRRKGE 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19923536 320 VTASPANGHWLLRQsRGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTFTHNF--SGPLRPFF 395
Cdd:cd12888  82 ISFSPEEGIWAVGQ-WGGQYWALTSPETPLPLSEVPRRIRVYLDYEGGQVAFFDADNEAPIFTFPPASfaGERIFPWF 158
SPRY_PRY_RFPL cd15821
Ret finger protein-like (RFPL), includes RFP1, 2, 3, 4; This domain, consisting of the ...
238-412 4.98e-67

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.


Pssm-ID: 293993 [Multi-domain]  Cd Length: 178  Bit Score: 212.56  E-value: 4.98e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 238 VAVTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRK 317
Cdd:cd15821   4 VDMTLDVDTANNYLIISEDLRSVRCGCFRQNRKELAERFDDALCVLGSPRFTSGRHYWEVDVGTSTEWDLGVCRESVNRQ 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 318 GKVTASPANGHWLLRQSRGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTFTHNF-SGPLRPFFE 396
Cdd:cd15821  84 GPIELSPEHGFWTVSLRDGSVFFASTVPLTVLWVNPRLHRVGIFLDMEMGTISFYDVSDGSHIFTFTKISaEEPLRPFFA 163
                       170
                ....*....|....*.
gi 19923536 397 PCLHDGGkNTAPLVIC 412
Cdd:cd15821 164 PANPYGD-DQGVLSIC 178
SPRY_PRY_TRIM35 cd12893
PRY/SPRY domain in tripartite motif-containing protein 35 (TRIM35); This PRY/SPRY domain is ...
240-412 5.90e-67

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.


Pssm-ID: 293950 [Multi-domain]  Cd Length: 171  Bit Score: 212.11  E-value: 5.90e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 240 VTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRKGK 319
Cdd:cd12893   2 VTLDPNTAHPWLSLSEDLTSVRYSSEKQQLPDNPERFDPYPCVLGSEGFTSGKHSWDVEVGDNTSWMLGVAKESVQRKGK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 320 VTASPANGHWLLRQSRGnEYEALTS--PQTSFRLKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTFTHNFSGPLRPFFEP 397
Cdd:cd12893  82 FTLSPESGFWTIGFSEG-KYSARTSpePRTPLRVKQKPQRIRVQLDWDRGKVSFSDPDTNTHIHTFTHTFTERVFPYFYT 160
                       170
                ....*....|....*
gi 19923536 398 clhdgGKNTAPLVIC 412
Cdd:cd12893 161 -----GCKSEPLRIL 170
SPRY_PRY_TRIM38 cd15815
PRY/SPRY domain of tripartite motif-binding protein 38 (TRIM38), also known as Ring finger ...
234-400 1.88e-65

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.


Pssm-ID: 293987 [Multi-domain]  Cd Length: 182  Bit Score: 208.74  E-value: 1.88e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 234 RLHFVAVTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSES 313
Cdd:cd15815   9 RRHQVSVTLDPDTAHPELTLSKDQRQVTYGRCQENLDASPKRFTVLPCVLGCEGFTSGRHYFEVDVGEGTGWDVGVCLEN 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 314 VSRKGKVTASPANGHWLLRQSRGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTFTHN-FSGPLR 392
Cdd:cd15815  89 VQRGFGMKQEPEFGFWTIRLCEEDGYVALTSPPTPLPLREKPLVVGVFLDYEAGLVSFYNMTTGSHIFTFPKAsFSDTLR 168

                ....*...
gi 19923536 393 PFFEPCLH 400
Cdd:cd15815 169 PYFQVYQY 176
SPRY_PRY_TRIM27 cd15814
PRY/SPRY domain in tripartite motif-containing protein 27 (TRIM27), also known as RING finger ...
238-412 2.09e-65

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.


Pssm-ID: 293986 [Multi-domain]  Cd Length: 177  Bit Score: 208.77  E-value: 2.09e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 238 VAVTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRK 317
Cdd:cd15814   2 VDVTLDPDTAYPSLILSDNLRQVRYSYLQQDLPDNPERFNLFPCVLGSPCFIAGRHYWEVEVGDKAKWTIGVCEDSVCRK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 318 GKVTASPANGHWLLRQSRGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTFTH-NFSGPLRPFFE 396
Cdd:cd15814  82 GGVTSAPQNGFWAVSLWYGKEYWALTSPMTALPLRTPLQRVGIFLDYDAGEVSFYNVTERCHTFTFSHaTFCGPVRPYFS 161
                       170
                ....*....|....*.
gi 19923536 397 pCLHDGGKNTAPLVIC 412
Cdd:cd15814 162 -LSYSGGKSAAPLIIC 176
SPRY_PRY_TRIM11 cd15811
PRY/SPRY domain of tripartite motif-binding protein 11 (TRIM11), also known as RING finger ...
240-412 7.12e-60

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.


Pssm-ID: 293983 [Multi-domain]  Cd Length: 169  Bit Score: 194.02  E-value: 7.12e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 240 VTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRKGK 319
Cdd:cd15811   2 VTLDPDTANPELVLSEDRRSVRRGDLRQALPDSPERFDPGPCVLGRERFTSGRHYWEVEVGDRTSWALGVCKENVNRKEK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 320 VTASPANGHWLLrQSRGNEYealTSPQTSFR-LKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTFTHN-FSGPLRPFFEP 397
Cdd:cd15811  82 GELSAGNGFWIL-VFLGNYY---SSERRTFApLRDPPRRVGIFLDYEAGHLSFYSATDGSLLFIFPETpFSGTLRPLFSP 157
                       170
                ....*....|....*
gi 19923536 398 ClhdgGKNTAPLVIC 412
Cdd:cd15811 158 L----SSSPTPMTIC 168
SPRY_PRY_TRIM60 cd15828
PRY/SPRY domain of tripartite motif-binding protein 60 (TRIM60) also known as RING finger ...
238-413 1.59e-54

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.


Pssm-ID: 294000 [Multi-domain]  Cd Length: 180  Bit Score: 180.18  E-value: 1.59e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 238 VAVTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRK 317
Cdd:cd15828  10 VDVTLDPETAHPQLTVSEDRKSVLYGEMKQNVCYNPRRFYLCPAVLGSEGFHSGRQYWEVEVGDKPEWTLGVCQDCLPRN 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 318 GKVTASPANGHWLLRQSRGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTFTHNFSGPLRPFFep 397
Cdd:cd15828  90 WSNQPSVQDGLWAIGRYSESNYVALGPKKIQLLPKVRPSKIGIFLDYELGEVSFYNMNDRSLLYTFSDSFTGTLWPYF-- 167
                       170
                ....*....|....*.
gi 19923536 398 clhDGGKNTAPLVICS 413
Cdd:cd15828 168 ---YTGTDSEPLKICT 180
SPRY_PRY_TRIM72 cd13742
PRY/SPRY domain in tripartite motif-binding protein 72 (TRIM72); This domain, consisting of ...
240-412 2.21e-54

PRY/SPRY domain in tripartite motif-binding protein 72 (TRIM72); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM72. Muscle-specific TRIM72 (also known as Mitsugumin 53 or 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. TRIM72 interacts with dysferlin, a sarcolemmal protein whose deficiency causes Miyoshi myopathy (MM) and limb girdle muscular dystrophy type 2B (LGMD2B); this coordination plays an important role in the repair of sarcolemma damage.


Pssm-ID: 293976 [Multi-domain]  Cd Length: 192  Bit Score: 180.44  E-value: 2.21e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 240 VTLDPDTAHPKLILSEDQRCVRLGDRRQPV-PDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRKG 318
Cdd:cd13742  14 LTFDPDTAHPYLVVSSDGKRVECADQKQAVsSDDPNRFDKANCVVSHQSFSEGEHYWEVIVGDKPRWALGVISAEAGRKG 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 319 KVTASPANGHWLLRQSRGNEYEALTSPQT--SFRLKEPPRCVGIFLDYEAGVISFYNVT---NKSHIFTFTHNFSGPLRP 393
Cdd:cd13742  94 RLHALPSNGFWLLGCKEGKVYEAHVEHKEprALRVEGRPTRIGVYLSFSDGVLSFYDASdedNLVQLFAFHERFPGPLYP 173
                       170
                ....*....|....*....
gi 19923536 394 FFEPCLHDGGKNTAPLVIC 412
Cdd:cd13742 174 FFDVCWHDKGKNSQPLKIF 192
SPRY_PRY_TRIM62 cd13744
PRY/SPRY domain in tripartite motif-binding protein 62 (TRIM62); This domain, consisting of ...
239-411 3.52e-53

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.


Pssm-ID: 293978  Cd Length: 188  Bit Score: 177.12  E-value: 3.52e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 239 AVTLDPDTAHPKLILSEDQRCVRLGD-RRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRK 317
Cdd:cd13744  13 ALTLDPVTAHQRLILSDDCTIVAYGNlHPQPLQDSPKRFDVEVSVLGSEGFSGGVHYWEVVVSEKTQWMIGLAHEAVSRK 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 318 GKVTASPANGHWLLRQSRGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTFTHNFSGPLRPFFEP 397
Cdd:cd13744  93 GSIQIQPGRGFYCIVMHDGNQYSACTEPWTRLNVKSKLEKVGVYLDYDKGLLIFYNADDMSWLYTFREKFPGKLCSYFSP 172
                       170
                ....*....|....*
gi 19923536 398 CL-HDGGKNTAPLVI 411
Cdd:cd13744 173 GQsHANGKNVQPLRI 187
SPRY_PRY_TRIM50_72 cd12897
PRY/SPRY domain in tripartite motif-binding (TRIM) proteins TRIM50 and TRIM72; This domain, ...
240-411 2.78e-52

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.


Pssm-ID: 293954  Cd Length: 191  Bit Score: 175.11  E-value: 2.78e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 240 VTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRKGK 319
Cdd:cd12897  14 LTFDPATAHPLLVVSSGGTVVECGLQKQRRASQPERFDKSTCVVASQGFSEGEHYWEVVVGDKPRWALGVIKGTASRKGK 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 320 VTASPANGHWLLRQSRGNEYEALTSPQT--SFRLKEPPRCVGIFLDYEAGVISFYNVTNKSH---IFTFTHNFSGPLRPF 394
Cdd:cd12897  94 LHASPSHGVWLIGLKEGKVYEAHGEPKEprPLRVAGRPHRIGVYLSFEDGVLSFFDASDPDDlrtLYTFQERFQGKLYPF 173
                       170
                ....*....|....*..
gi 19923536 395 FEPCLHDGGKNTAPLVI 411
Cdd:cd12897 174 FDVCWHDKGKNSQPLVL 190
SPRY_PRY_TRIM60_75 cd15817
PRY/SPRY domain of tripartite motif-binding protein 60 and 75 (TRIM60 and TRIM75); This domain, ...
240-412 2.50e-51

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.


Pssm-ID: 293989 [Multi-domain]  Cd Length: 168  Bit Score: 171.58  E-value: 2.50e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 240 VTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRKGK 319
Cdd:cd15817   2 LILDPETAHPNLIVSEDRKAVRYRRMKPNCPYDPRRFTVYPAVLGSEGFDSGRHFWEVEVGGKGEWILGVCKDSLPRNAQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 320 VTASPANGHWLLRQSRgNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTFTHNFSGPLRPFFEPcl 399
Cdd:cd15817  82 DPPSPLGGCWQIGRYM-SGYVASGPKTTQLLPVVKPSRIGIFLDYELGEVSFYNMNDRSHLYTFTDTFTGKLIPYFYV-- 158
                       170
                ....*....|...
gi 19923536 400 hdgGKNTAPLVIC 412
Cdd:cd15817 159 ---GPDSEPLTIC 168
SPRY_PRY_TRIM50 cd13743
PRY/SPRY domain in tripartite motif-binding protein 50 (TRIM50); This domain, consisting of ...
242-411 2.08e-49

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.


Pssm-ID: 293977  Cd Length: 189  Bit Score: 167.29  E-value: 2.08e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 242 LDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRKGKVT 321
Cdd:cd13743  16 LDPLTAHPMLELSKGNTVVECGLLAQRLPSNPERFDYSNCVLASRGFSSGKHYWEVVVGSKSKWRLGLIKGTTSRKGKLN 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 322 ASPANGHWLLRQSRGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTNKSH---IFTFTHNFSGPLRPFFEPC 398
Cdd:cd13743  96 KSPENGVWLIGLKEGRVYEAFANPRVPLPLSTRPQRIGVFLDYEKGELTFYNADSPDElvpIYTFQAEFQGKLYPLLDVC 175
                       170
                ....*....|...
gi 19923536 399 LHDGGKNTAPLVI 411
Cdd:cd13743 176 WHERGANKLPIIL 188
SPRY_PRY cd12874
PRY/SPRY domain, also known as B30.2; This domain contains residues in the N-terminus that ...
240-412 8.00e-49

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.


Pssm-ID: 293934 [Multi-domain]  Cd Length: 168  Bit Score: 164.79  E-value: 8.00e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 240 VTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRKGK 319
Cdd:cd12874   1 LTFDPDTAHLNLILSDDLRSVRVGDISQHPPEPPPRFFECWQVLGSQSFSSGRHYWEVDVQDDSSWYVGVTYKSLPRKGK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 320 V-TASPANGHWLLrQSRGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTN-KSHIFTFTHNFSGPLRPFFEP 397
Cdd:cd12874  81 MsNLGRNNGSWCL-EWRENEFSAWHNNPETRLPVTPPRRLGVFLDCDGGSLSFYGVTDgVQLLYTFKAKFTEPLYPAFWL 159
                       170
                ....*....|....*
gi 19923536 398 ClhdggkNTAPLVIC 412
Cdd:cd12874 160 G------EGSTLSIC 168
SPRY_PRY_TRIM15 cd15826
PRY/SPRY domain in tripartite motif-binding protein 15 (TRIM15); This domain, consisting of ...
240-395 2.16e-46

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.


Pssm-ID: 293998 [Multi-domain]  Cd Length: 170  Bit Score: 158.88  E-value: 2.16e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 240 VTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYV--GDKTKWILGVCSESVSRK 317
Cdd:cd15826   2 VTLDPQTASGSLVLSEDRKSVRYTRQKQNLPDSPLRFDGLPAVLGSPGFSSGRHRWQVEVqlGDGGGCTVGVAGESVRRK 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19923536 318 GKVTASPANGHWLLRQSRGNEYeALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTFTHNFSGPLRPFF 395
Cdd:cd15826  82 GEMGLSAEDGVWAVILSHQQCW-ASTSPGTDLPLSEIPRRVGVALDYEAGTVTLTNAETQEPIFTFTASFSGKVFPFF 158
SPRY_PRY_TRIM41 cd13741
PRY/SPRY domain in tripartite motif-binding protein 41 (TRIM41); This domain, consisting of ...
240-395 3.02e-45

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.


Pssm-ID: 240499 [Multi-domain]  Cd Length: 199  Bit Score: 156.85  E-value: 3.02e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 240 VTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRKGK 319
Cdd:cd13741   2 LTLDPDTAHPALLLSPDRRGVRLAERRQEVPEHPKRFSADCCVLGAQGFRSGRHYWEVEVGGRRGWAVGAARESTHHKEK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 320 V----------TASPANGHWLLRQ-----------------SRGNEYEALTS-PQTSFRLKEPPRCVGIFLDYEAGVISF 371
Cdd:cd13741  82 VgsggssvssgDASSSRHHHRRRRlhlpqqpllqrevwcvgTNGKRYQAQSStEQTLLSPSEKPRRFGVYLDYEAGRLGF 161
                       170       180
                ....*....|....*....|....*
gi 19923536 372 YNVTNKSHIFTFTHNFSGP-LRPFF 395
Cdd:cd13741 162 YNAETLAHVHTFSAAFLGErVFPFF 186
SPRY_PRY_TRIM7 cd13740
PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7); This domain, consisting of the ...
239-398 8.24e-43

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.


Pssm-ID: 293975 [Multi-domain]  Cd Length: 169  Bit Score: 149.34  E-value: 8.24e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 239 AVTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRKG 318
Cdd:cd13740   1 ELTLDPDSANPRLILSLDLKSVRLGERAQDLPNHPCRFDTNTRVLASCGFSSGRHHWEVEVGSKDGWAFGVARESVRRKG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 319 KVTASPANGHWLLRQSrGNEYEALTSPQTSfrlkepPRCVG------IFLDYEAGVISFYNVTNKSHIFTFTHNFSGPLR 392
Cdd:cd13740  81 LTPFTPEEGVWALQLN-GGQYWAVTSPERT------PLSCGhlsrvrVALDLEVGAVSFYAAEDMRHIYTFRVNFQERVF 153

                ....*.
gi 19923536 393 PFFEPC 398
Cdd:cd13740 154 PLFSVC 159
SPRY_PRY_TRIM17 cd15812
PRY/SPRY domain of tripartite motif-binding protein 17 (TRIM17), also known as testis RING ...
239-411 2.96e-40

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.


Pssm-ID: 293984 [Multi-domain]  Cd Length: 176  Bit Score: 142.72  E-value: 2.96e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 239 AVTLDPDTAHPKLILSED-QRCVrLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEV---YVGDkTKWILGVCSESV 314
Cdd:cd15812   1 DVVPDPSTAYPYLLLYESrQRRY-LSTPPDGTPCSKDRFLAYPCAVGQETFSSGRHYWEVgmnLTGD-ALWALGVCRDNV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 315 SRKGKVTASPANGHWLLRQSRGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTFTH-NFSGPLRP 393
Cdd:cd15812  79 SRKDRVPKSPENGFWVVQLSKGKKYLSAMSALTPVTLTEPPSHMGIFLDFEAGEVSFYSVNDGSHLHTYSQaAFPGPLQP 158
                       170
                ....*....|....*...
gi 19923536 394 FFepCLhdGGKNTAPLVI 411
Cdd:cd15812 159 FF--CL--GAPKSGQMVI 172
SPRY_PRY_TRIM5_6_22_34 cd15810
PRY/SPRY domain of tripartite motif-binding protein 5, 6, 22 and 34 (TRIM5, TRIM6, TRIM22 and ...
240-412 1.15e-38

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.


Pssm-ID: 293982 [Multi-domain]  Cd Length: 189  Bit Score: 138.77  E-value: 1.15e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 240 VTLDPDTAHPKLILSEDQRCVRLgDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVS--RK 317
Cdd:cd15810   2 VTLNPVNISLNIVISEDQRQVRI-VPPQTSGQALTNNNYDFGVLGSQYFSSGKHYWEVDVSKKSAWILGVCSHKRSdaMT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 318 GKVTAS-----------PANGHWLLRQSRGNEYEALTSPQTS------FRLKEPPRCVGIFLDYEAGVISFYNVTNK-SH 379
Cdd:cd15810  81 KSNANQinhqnvysryqPQYGYWVIGLQNESEYNAFEDSSSFnphvltLSVTVPPHRVGVFLDYEAGTVSFFNVTNHgSL 160
                       170       180       190
                ....*....|....*....|....*....|....
gi 19923536 380 IFTFTH-NFSGPLRPFFEPClhdggKNTAPLVIC 412
Cdd:cd15810 161 IYKFSKcCFSTTVCPYFNPW-----NCPVPMTLC 189
SPRY_PRY_TRIM6 cd15823
PRY/SPRY domain in tripartite motif-binding protein 6 (TRIM6), also known as RING finger ...
236-398 5.17e-38

PRY/SPRY domain in tripartite motif-binding protein 6 (TRIM6), also known as RING finger protein 89 (RNF89); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM6, also known as RING finger protein 89 (RNF89). TRIM6 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. It 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.


Pssm-ID: 293995  Cd Length: 188  Bit Score: 136.92  E-value: 5.17e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 236 HFVAVTLDPDTAHPKLILSEDQRCVRLGDRRQPVPdNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESV- 314
Cdd:cd15823   1 YWVDVTLNPHTANLNLVLSKNRRQVRFVGAKLSGP-SYLEEHYDCSVLGSQHFSSGKHYWEVDVTKKTAWILGVCSHSLg 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 315 ----------SRKGKVTASPANGHWLLRQSRGNEYEALTSPQTSFRLKE--PPRCVGIFLDYEAGVISFYNVTNKSH-IF 381
Cdd:cd15823  80 ptfsfnqyaqNHNAYSRYQPQSGYWVIGLQHNHEYRAYEDSSTSLLLSMtvPPRRVGVFLDYEAGTVSFYNVTNHGFpIY 159
                       170
                ....*....|....*...
gi 19923536 382 TFT-HNFSGPLRPFFEPC 398
Cdd:cd15823 160 TFSkYYFPTTLCPYFNPC 177
SPRY_PRY_TRIM10 cd15827
PRY/SPRY domain of tripartite motif-binding protein 10 (TRIM10) also known as hematopoietic ...
240-395 1.74e-37

PRY/SPRY domain of tripartite motif-binding protein 10 (TRIM10) also known as hematopoietic RING finger 1 (HERF1); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM10, also known as RING finger protein 9 (RNF9) or hematopoietic RING finger 1 (HERF1). TRIM10 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. TRIM10/HERF1 is predominantly expressed during definitive erythropoiesis and in embryonic liver, and minimally expressed in adult liver, kidney, and colon. It is critical for erythroid cell differentiation and its down-regulation leads to cell death; inhibition of TRIM10 expression blocks terminal erythroid differentiation, while its over-expression in erythroid cells induces beta-major globin expression and erythroid differentiation.


Pssm-ID: 293999 [Multi-domain]  Cd Length: 172  Bit Score: 134.96  E-value: 1.74e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 240 VTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYV-----GDKTkwiLGVCSESV 314
Cdd:cd15827   4 ISLDPQTSHPKLLLSEDHQRARFSYKWQNSPDNPQRFDRATCVLAHDGFTGGRHTWVVSVdlahgGSCT---VGVVSEDV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 315 SRKGKVTASPANGHWLLRQSRGNeYEALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTFTHNFSGPLRPF 394
Cdd:cd15827  81 RRKGELRLRPEEGVWAVRLAWGF-VSALGSFPTRLALEEQPRQVRVSLDYEVGWVTFVNAVTQEPIYTFTASFTQKVFPF 159

                .
gi 19923536 395 F 395
Cdd:cd15827 160 F 160
SPRY_PRY_TRIM5 cd15822
PRY/SPRY domain in tripartite motif-binding protein 5 (TRIM5), also known as RING finger ...
231-412 6.36e-35

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.


Pssm-ID: 293994  Cd Length: 200  Bit Score: 129.27  E-value: 6.36e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 231 RRARLHFVAVTLDPDTAHPKLIlSEDQRCVRLGDRRQPVPDNPQRFDFvvSILGSEYFTTGCHYWEVYVGDKTKWILGVC 310
Cdd:cd15822   5 TDVQRYWVHVTLDPSNNKNIVI-SEDRRQVRYVRKQQRYNSNGNNEDY--GVLGSPSITSGKHYWEVDVSKKRAWILGVC 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 311 SES------VSRKGKVTAS--------PANGHWLLRQSRGNEYEAL---TSPQTSF---RLKEPPRCVGIFLDYEAGVIS 370
Cdd:cd15822  82 GGKypnstlKDFNKQGKNNqkqcsnyqPKYGYWVIGLQNKSEYNAFedsSSSDPLIltlSLTVPPCRVGVFLDYEAGTVS 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 19923536 371 FYNVTNksH---IFTF-THNFSGPLRPFFEPClhdggKNTAPLVIC 412
Cdd:cd15822 162 FFNVTN--HgflIYKFsSCSFSQEVFPYFNPM-----KCPVPMTLC 200
SPRY_PRY_C-I_2 cd12891
PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM14-like, ...
240-395 1.04e-34

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.


Pssm-ID: 293949 [Multi-domain]  Cd Length: 167  Bit Score: 127.36  E-value: 1.04e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 240 VTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVvSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRKGK 319
Cdd:cd12891   1 LTLDPNTAHNNLALSGDLKTVTCSSENQHYPDSPERFTHS-QVLSTQSFSSGRHYWEVEVSESGGWSVGVAYPSIERKGD 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19923536 320 VTASPANGH-WLLRQSrGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTNK-SHIFTFTHNFSGPLRPFF 395
Cdd:cd12891  80 ESRIGRNDKsWCLEWQ-DKSFSAWHNNEETPLPSVSSRRLGVYLDYEAGRLSFYELSDPiRHLHTFTATFTEPLHPAF 156
IgV_MOG_like cd05713
Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here ...
39-144 1.14e-33

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).


Pssm-ID: 409378  Cd Length: 114  Bit Score: 122.69  E-value: 1.14e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536  39 VALLGGTAELLCPLSlwpgtvPK------EVRWLRSPFpqrSQAVHIFRDGKDQDEDLMPEYKGRTVLVRDA-QEGSVTL 111
Cdd:cd05713  11 LALVGEDAELPCHLS------PKmsaehmEVRWFRSQF---SPVVHLYRDGQDQEEEQMPEYRGRTELLKDAiAEGSVAL 81
                        90       100       110
                ....*....|....*....|....*....|...
gi 19923536 112 QILDVRLEDQGSYRCLIQVGNLSKEDTVILQVA 144
Cdd:cd05713  82 RIHNVRPSDEGQYTCFFRSGSFYEEATLELKVA 114
SPRY_PRY_TRIM34 cd15825
PRY/SPRY domain in tripartite motif-containing protein 34 (TRIM34), also known as RING finger ...
238-412 1.24e-33

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.


Pssm-ID: 293997  Cd Length: 185  Bit Score: 125.34  E-value: 1.24e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 238 VAVTLDPDTAHPKLILSEDQRCVRlgdrrqPVPDNPQRFDfVVSILGSEYFTTGCHYWEVYVGDKTKWILGV------CS 311
Cdd:cd15825   2 VDFTLNPVNLNLNLVLSEDQRQVT------SVPIWPFKCY-NYGILGSQYFSSGKHYWEVDVSKKTAWILGVycrkrsRT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 312 ESVSRKGKVTAS------PANGHWLLRQSRGNEYEALTSPQTS------FRLKEPPRCVGIFLDYEAGVISFYNVTNK-S 378
Cdd:cd15825  75 FKYVRQGKNHPNvysryrPQYGYWVIGLQNKSEYYAFEDSSTSdpkvltLSVATPPHRVGVFLDYEAGTVSFFNVTNHgS 154
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 19923536 379 HIFTFTH-NFSGPLRPFFEP--ClhdggknTAPLVIC 412
Cdd:cd15825 155 LIYKFSKcCFSQPVYPYFNPwnC-------PAPMTLC 184
SPRY_PRY_C-II cd13734
PRY/SPRY domain in tripartite motif-containing proteins 1, 9, 18, 36, 46, 67,76 (TRIM1, TRIM9, ...
241-395 2.86e-33

PRY/SPRY domain in tripartite motif-containing proteins 1, 9, 18, 36, 46, 67,76 (TRIM1, TRIM9, TRIM18, TRIM36, TRIM46, TRIM67, TRIM76); 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 TRIM1, TRIM9, TRIM18, TRIM36, TRIM46, TRIM67 and TRIM76. TRIM1 (also known as 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. Their 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 TRIM18 have shown to cause Opitz syndrome, a disorder causing congenital anomalies such as cleft lip and palate as well as heart defects. TRIM9 is expressed mainly in the cerebral cortex, and functions as an E3 ubiquitin ligase. Its immunoreactivity is severely decreased in affected brain areas in Parkinson's disease and dementia with Lewy bodies, possibly playing an important role in the regulation of neuronal function and participating in pathological process of Lewy body disease through its ligase. TRIM36 interacts with centromere protein-H, one of the kinetochore proteins and possibly associates with chromosome segregation; an excess of TRIM36 may cause chromosomal instability. TRIM46 has not yet been characterized. TRIM67 negatively regulates Ras activity via degradation of 80K-H, leading to neural differentiation, including neuritogenesis. TRIM76 (also known as cardiomyopathy-associated protein 5 or CMYA5) is a muscle-specific member of the TRIM superfamily, but lacks the RING domain. It is possibly involved in protein kinase A signaling as well as vesicular trafficking. It has also been implicated in Duchenne muscular dystrophy and cardiac disease. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site.


Pssm-ID: 293969 [Multi-domain]  Cd Length: 166  Bit Score: 123.55  E-value: 2.86e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 241 TLDPDTAHPKLILSEDQRCVRLGDRRQPV--PDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRKg 318
Cdd:cd13734   2 KLDPKTAHRKLRLSNDNLTVEYDPEGSKDqaAVLPRRFTGSPAVLGDVAISSGRHYWEVSVSRSTSYRVGVAYKSAPRD- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 319 kvtasPANGH----WLLRQSrGNEYEALTSPQTS-FRLKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTFTHNFSGPLRP 393
Cdd:cd13734  81 -----EDLGKnstsWCLSRD-NNRYTARHDGKVVdLRVTGHPARIGVLLDYDNGTLSFYDAESKQHLYTFHVDFEGPVCP 154

                ..
gi 19923536 394 FF 395
Cdd:cd13734 155 AF 156
SPRY_PRY_TRIM22 cd15824
PRY/SPRY domain in tripartite motif-containing protein 22 (TRIM22), also known as RING finger ...
236-412 7.64e-32

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.


Pssm-ID: 293996 [Multi-domain]  Cd Length: 198  Bit Score: 120.72  E-value: 7.64e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 236 HFVAVTLDPDTAHPKLILSEDQRCVRLGDR---RQPVPDNPQRFDfvvsILGSEYFTTGCHYWEVYVGDKTKWILGVCSE 312
Cdd:cd15824   1 YWVDVMLNPVNAVSNVVVSADQRQVTVVHIcmfRNSNPCDFSAFD----VLGCQYFSSGKYYWEVDVSGKIAWILGVYSK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 313 SVSRKGKVTA-----------------SPANGHWLLRQSRGNEYEALTSPQTS------FRLKEPPRCVGIFLDYEAGVI 369
Cdd:cd15824  77 RNNLNKRKSSgfafdpnvnhpnvysryRPQNGYWVIGLQNESEYNAFEDSSSSdpkvltLSMAVPPHRVGVFLDYEAGTV 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 19923536 370 SFYNVTNK-SHIFTFTH-NFSGPLRPFFEPClhdggKNTAPLVIC 412
Cdd:cd15824 157 SFFNVTNHgSLIYKFSKcCFSQPVYPYFNPW-----NCPAPMTLC 196
SPRY_PRY_TRIM14 cd13738
PRY/SPRY domain of tripartite motif-binding protein 14 (TRIM14); This is a TRIM14 domain ...
241-395 1.96e-31

PRY/SPRY domain of tripartite motif-binding protein 14 (TRIM14); This is a TRIM14 domain family 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. TRIM14 domains have yet to be characterized. These B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. It belongs to Class IV TRIM protein family which has members involved in antiviral immunity at various levels of interferon signaling cascade.


Pssm-ID: 293973 [Multi-domain]  Cd Length: 173  Bit Score: 118.73  E-value: 1.96e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 241 TLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTK-WILGVCSESVSRKGK 319
Cdd:cd13738   2 TLEPDTLHPRLRLSDDRLTVSCGWLGTLGLCPPQRFDKLWQVLSRDSFFSGRHYWEVDLQEAGAgWWVGAAYPSIGRKGD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 320 VTASPAN---GHWLLRQSrGNEYEALTSPQ-TSFRLKEPPRCVGIFLDYEAGVISFYNVTNK-SHIFTFTHNFSGPLRPF 394
Cdd:cd13738  82 SEAARLGwnrQSWCLKRY-DLEYWAFHDGQrSRLRPEDDPDRLGVFLDYEAGILSFYDVTGGmTHLHTFRATFQEPLYPA 160

                .
gi 19923536 395 F 395
Cdd:cd13738 161 L 161
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
291-414 1.24e-29

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


Pssm-ID: 214669  Cd Length: 122  Bit Score: 112.00  E-value: 1.24e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536    291 GCHYWEVYVGDKTKWILGVCSESVSRKGKVTASPANGHWLLRQSRGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVIS 370
Cdd:smart00449   2 GRHYFEVEIGDGGHWRVGVATKSVPRGYFALLGEDKGSWGYDGDGGKKYHNSTGPEYGLPLQEPGDVIGCFLDLEAGTIS 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 19923536    371 FYNVTNKSHIFTFTH-NFSGPLRPFFepCLhdGGKNTAPLVICSE 414
Cdd:smart00449  82 FYKNGKYLHGLAFFDvKFSGPLYPAF--SL--GSGNSVRLNFGPL 122
SPRY_PRY_TRIM4 cd15809
PRY/SPRY domain in tripartite motif-binding protein 4 (TRIM4), also known as RING finger ...
238-395 3.51e-29

PRY/SPRY domain in tripartite motif-binding protein 4 (TRIM4), also known as RING finger protein 87 (RNF87); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM4 which is also known as RING finger protein 87 (RNF87). TRIM4 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. It is a positive regulator of RIG-I-mediated interferon (IFN) induction. It regulates virus-induced IFN induction and cellular antiviral innate immunity by targeting RIG-I for K63-linked poly-ubiquitination. Over-expression of TRIM4 enhances virus-triggered activation of transcription factors IRF3 and NF-kappaB, as well as IFN-beta induction. Expression of TRIM4 differs significantly in Huntington's Disease (HD) neural cells when compared with wild-type controls, possibly impacting down-regulation of the Huntingtin (HTT) gene, which is involved in the regulation of diverse cellular activities that are impaired in Huntington's Disease (HD) cells.


Pssm-ID: 293981  Cd Length: 191  Bit Score: 113.39  E-value: 3.51e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 238 VAVTLDPDTAHPKLILSEDQRCVRLGDRRQPVP------------DNPQ-------RFDFVVSILGSEYFTTGCHYWEVY 298
Cdd:cd15809   3 VAVNLAEDTAHPKLVFSQEGRYVKNGASASSWPlfstawsyftgwRNPQkttqfveRFQHLPCVLGKNVFTSGKHYWEVE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 299 VGDKTKWILGVCSESV-SRKGKVTASPANGHWLLRQSRGNeYEALTSPQTSFRLKEP-PRCVGIFLDYEAGVISFYNVTN 376
Cdd:cd15809  83 NRDSLEIAVGVCREDVmGITDGSEMSPHVGIWAICWSSAG-YRPLTSSPVSPTKQEPaLHRVGVFLDHGAGEVSFYSAVD 161
                       170
                ....*....|....*....
gi 19923536 377 KSHIFTFTHNFSGPLRPFF 395
Cdd:cd15809 162 GVHLHTFSCPLVSRLRPFF 180
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
293-395 5.58e-29

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.


Pssm-ID: 459877  Cd Length: 121  Bit Score: 110.51  E-value: 5.58e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536   293 HYWEVYVG--DKTKWILGVCSESVSRKGKVTASPANGHWLLRQSRGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVIS 370
Cdd:pfam00622   2 HYFEVEIFgqDGGGWRVGWATKSVPRKGERFLGDESGSWGYDGWTGKKYWASTSPLTGLPLFEPGDVIGCFLDYEAGTIS 81
                          90       100
                  ....*....|....*....|....*.
gi 19923536   371 FYNVtNKSHIFTFTH-NFSGPLRPFF 395
Cdd:pfam00622  82 FTKN-GKSLGYAFRDvPFAGPLFPAV 106
SPRY_PRY_SNTX cd16040
Stonustoxin subunit alpha or SNTX subunit alpha; This domain, consisting of the distinct ...
241-395 6.97e-29

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.


Pssm-ID: 294002 [Multi-domain]  Cd Length: 180  Bit Score: 112.19  E-value: 6.97e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 241 TLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFtTGCHYWEVYVGDKtKWILGVCSESVSRKGKV 320
Cdd:cd16040  12 TLDPNTAHRNLSLSEGNRKVTRVKEEQPYPDHPERFDYWPQVLCREGL-SGRCYWEVEWSGG-GVDIAVAYKGISRKGDG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 321 TASpANGH----WLLRQSRG-------NEYEALTSPQTSFRlkeppRcVGIFLDYEAGVISFYNVTNK-SHIFTFTHNFS 388
Cdd:cd16040  90 DDS-RFGYndksWSLECSPSgysfwhnNKKTEISVPSSSSS-----R-VGVYLDHSAGTLSFYSVSDTmTLLHTVQTTFT 162

                ....*..
gi 19923536 389 GPLRPFF 395
Cdd:cd16040 163 EPLYPGF 169
SPRY_PRY_TRIM76_like cd12899
PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76)-like; This domain is ...
242-398 4.11e-26

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.


Pssm-ID: 293956 [Multi-domain]  Cd Length: 176  Bit Score: 104.48  E-value: 4.11e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 242 LDPDTAHPKLILSEDQRCVRLGDRRQPVPD---NPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRKG 318
Cdd:cd12899   4 LNEDTAHPLLSISEDGFTVVYGEEELPARDlsfSDNSFTRCVAVMGSLIPVRGKHYWEVEVDEQTEYRVGVAFEDTQRNG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 319 KVTASpaNGHWLLRQ----SRgNEYEALTSPQT-SFRLKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTfthnFSGPLRP 393
Cdd:cd12899  84 YLGAN--NTSWCMRHiitpSR-HKYEFLHNGWTpDIRITVPPKKIGILLDYDSGRLSFFNVDLAQHLYT----FSCQFQH 156

                ....*
gi 19923536 394 FFEPC 398
Cdd:cd12899 157 FVHPC 161
PRY pfam13765
SPRY-associated domain; PRY is a 50-60 amino acids domain associated with SPRY domains, ...
240-288 3.77e-24

SPRY-associated domain; PRY is a 50-60 amino acids domain associated with SPRY domains, adjacent to its N-terminal. PRY and SPRY domains are structurally very similar and consist of a beta sandwich fold. Distant homologs are domains in butyrophilin/marenostrin/pyrin, evolutionarily more ancient than SPRY/B30.2 counterpart.


Pssm-ID: 463976  Cd Length: 49  Bit Score: 94.47  E-value: 3.77e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 19923536   240 VTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYF 288
Cdd:pfam13765   1 VTLDPNTAHPSLVLSEDLKSVRYGDERQNVPDNPERFDSWPCVLGSEGF 49
SPRY_PRY_RNF135 cd12902
PRY/SPRY domain in RING finger protein RNF135; This domain, consisting of the distinct ...
241-395 1.12e-23

PRY/SPRY domain in RING finger protein RNF135; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of the RING finger protein RNF135 (also known as Riplet/RNF135), which ubiquitinates RIG-I (retinoic acid-inducible gene-I) to promote interferon-beta induction during the early phase of viral infection. Normally, RIG-I is activated by TRIM25 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. However, RNF135, consisting of an N-terminal RING finger domain, C-terminal SPRY and PRY motifs and showing sequence similarity to TRIM25, acts as an alternative factor that promotes RIG-I activation independent of TRIM25.


Pssm-ID: 293959 [Multi-domain]  Cd Length: 168  Bit Score: 97.20  E-value: 1.12e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 241 TLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDfVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRKGKV 320
Cdd:cd12902   2 TFDLRSLSCSLEVSEDSRKVTVSHGPQAYAWSPDRFS-ISQVLCSQAFSSGQHYWEVDTRQCSHWAVGVASWEMSRDQML 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19923536 321 --TASPanghWLLRQSRGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTN-KSHIFTFTHNFSGPLRPFF 395
Cdd:cd12902  81 grTMDS----WCIEWKGTGQLSAWHMNKETVLGSDKPRVVGIWLDLEEGKLAFYSVANqERLLHECEVSASSPLHPAF 154
PRY smart00589
associated with SPRY domains;
237-288 1.78e-21

associated with SPRY domains;


Pssm-ID: 128857  Cd Length: 52  Bit Score: 87.25  E-value: 1.78e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 19923536    237 FVAVTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYF 288
Cdd:smart00589   1 AVDVTLDPDTAHPYLLLSEDRRSVRYGDLKQSLPDNPERFDSYPCVLGSQGF 52
SPRY_PRY_TRIM16 cd12890
PRY/SPRY domain in tripartite motif-containing protein 16 (TRIM16); This domain, consisting of ...
240-395 2.53e-20

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.


Pssm-ID: 293948  Cd Length: 182  Bit Score: 88.29  E-value: 2.53e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 240 VTLDPDTAHPKLILSEDQRCV-RLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWIlGVCSESVSRKG 318
Cdd:cd12890  11 LTFDPDTAHRYLRLTEDNRKVtNTTPWEHPYPDHPERFEHWRQVLSQQSLYLGRYYFEVEISGEGTYV-GLTYKSIDRKG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 319 KVTASPANGH---WLLrQSRGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTNKSH--IFTFTHNFSGPLRP 393
Cdd:cd12890  90 SESNSCISGNnfsWCL-QWNGKEFSAWHSDVETPLKKGPFTRLGIYLDYPGGTLSFYGVEDDGMtlLHKFQCKFTEPLYP 168

                ..
gi 19923536 394 FF 395
Cdd:cd12890 169 AF 170
SPRY_PRY_TRIM18 cd12892
PRY/SPRY domain of TRIM18/MID1, also known as FXY or RNF59; This domain, consisting of the ...
242-395 5.26e-20

PRY/SPRY domain of TRIM18/MID1, also known as FXY or RNF59; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is at the C-terminus of the overall domain architecture of MID1 (also known as FXY, RNF59, TRIM18) gene represented by a RING finger domain (RING), two B-box motifs (BBOX), coiled-coil C-terminal to Bbox domain (BBC) and fibronectin type 3 domain (FN3). Mutations in the human MID1 gene result in X-linked Opitz G/BBB syndrome (OS), a disorder affecting development of midline structures, causing craniofacial, urogenital, gastrointestinal and cardiovascular abnormalities. A unique MID1 gene mutation located in a variable loop in the SPRY domain alters conformation of the binding pocket and may affect the binding affinity to the PRY/SPRY domain.


Pssm-ID: 240472  Cd Length: 177  Bit Score: 87.37  E-value: 5.26e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 242 LDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVS--ILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRK-- 317
Cdd:cd12892   4 LDPKSAHRKLKVSHDNLTVERDETSSKKSHTPERFTSQGSygVAGNVFIDSGRHYWEVVISGSTWYAIGIAYKSAPKHew 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 318 -GKVTAS----PANGHWLLRQsrgNEYEALTSPQTSFRLkepprcVGIFLDYEAGVISFYNVTNKSHIFTFTHNFSGPLR 392
Cdd:cd12892  84 iGKNSASwvlcRCNNNWVVRH---NSKEIPIEPSPHLRR------VGILLDYDNGSLSFYDALNSIHLYTFDIAFAQPVC 154

                ...
gi 19923536 393 PFF 395
Cdd:cd12892 155 PTF 157
SPRY_BSPRY cd12904
SPRY domain in Ro-Ret family; This domain, named BSPRY, has been identified in the Ro-Ret ...
240-395 2.05e-19

SPRY domain in Ro-Ret family; This domain, named BSPRY, has been identified in the Ro-Ret family, since the protein is composed of a B-box, an alpha-helical coiled coil and a SPRY domain. The gene for BSPRY resides on human chromosome 9 and is specifically expressed in testis. The function of BSPRY is not known, but several related proteins of the RING-Box-coiled-coil (RBCC) family have been implicated in cell transformation.


Pssm-ID: 293961 [Multi-domain]  Cd Length: 171  Bit Score: 85.16  E-value: 2.05e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 240 VTLDPDTAHPKLILSEDQRCVRLGDR--RQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRK 317
Cdd:cd12904   1 LRFDERTVSPLLSLSEDRRTLTFSPKkaRQSPPDDPERFDHWPNALASLSFSSGTHAWVVDVGKSCAYKVGVCYGSLERK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 318 GkvTASPAN-GH----WLLRQSRGnEYEALTSPQ-TSFRLKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTFTHNFSGPL 391
Cdd:cd12904  81 G--SGNEARlGYnafsWVFSRYDG-EFSFSHNGQhVPLELLKCPARVGVLLDWPSQELLFYDPDSCTVLHSHREAFAAPL 157

                ....
gi 19923536 392 RPFF 395
Cdd:cd12904 158 LPVF 161
SPRY_PRY_SPRYD4 cd12903
PRY/SPRY domain containing protein 4 (SPRYD4); This domain, consisting of the distinct ...
242-402 2.77e-18

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.


Pssm-ID: 293960  Cd Length: 169  Bit Score: 82.11  E-value: 2.77e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 242 LDPDTAHPKLILSEDQRCVR---LGDRRQPVPDNPQRF-DFVVsILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRK 317
Cdd:cd12903   3 LDERTAHSSLDLFKKDTGVIyrmLGVDPTKVPQNPERFrDWAV-VLGDTPVTSGRHYWEVTVKRSQEFRIGVADVDMSRD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 318 GKVTASpaNGHWLLRQSRGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTFTHNFSGPLRPFFep 397
Cdd:cd12903  82 ECIGTN--ESSWVFAYAQRKWYAMVANETVPVPLVGKPDRVGLLLDYEAGKLSLVDVEKNSVVHTMSAEFRGPVVPAF-- 157

                ....*
gi 19923536 398 CLHDG 402
Cdd:cd12903 158 ALWDG 162
SPRY_PRY_TRIM76 cd12898
PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76), also called ...
245-395 1.44e-17

PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76), also called cardiomyopathy-associated protein 5; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is 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. It has also been implicated in Duchenne muscular dystrophy and cardiac disease; gene polymorphism of TRIM76 is associated with left ventricular wall thickness in patients with hypertension while its interactions with M-band titin and calpain 3 link it to tibial and limb-girdle muscular dystrophies.


Pssm-ID: 293955  Cd Length: 171  Bit Score: 79.97  E-value: 1.44e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 245 DTAHPKLILSEDQRCVR-LGDRRQPVPDNPQrfdfVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRKGKVTAS 323
Cdd:cd12898   9 ETAHPALHISSDRGTVIyFHERRRKMSSLTE----CPSVLGEELPSCGQYYWETTVTRCPAYRLGICSSSASQAGALGEG 84
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19923536 324 PANghWLLR---QSRGNEYEALTSP-QTSFRLKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTFTHNFSGPLRPFF 395
Cdd:cd12898  85 STS--WCLHcvpTSEPCRYTLLHSGiVSDVFVTERPARVGTLLDYNNGRLIFINAESGQLLGIFRHRFAQPCHPAF 158
SPRY_PRY_TRIM1 cd13739
PRY/SPRY domain of tripartite motif-binding protein 1 (TRIM1) or MID2; This domain, consisting ...
242-395 3.11e-17

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.


Pssm-ID: 293974  Cd Length: 170  Bit Score: 79.29  E-value: 3.11e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 242 LDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSI--LGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRK-- 317
Cdd:cd13739   3 LDPKMAHKKLKISNDGLQMEKDESSLKKSHTPERFSGTGCYgaAGNIFIDSGCHYWEVVVGSSTWYAIGIAYKSAPKNew 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 318 -GKVTA----SPANGHWLLRQsrgNEYEAL--TSPQTsfrlkeppRCVGIFLDYEAGVISFYNVTNKSHIFTFTHNFSGP 390
Cdd:cd13739  83 iGKNSSswvfSRCNNNFVVRH---NNKEMLvdVPPQL--------KRLGVLLDYDNNMLSFYDPANSLHLHTFEVSFILP 151

                ....*
gi 19923536 391 LRPFF 395
Cdd:cd13739 152 VCPTF 156
SPRY_PRY_TRIM25 cd13736
PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25); This domain, consisting of ...
240-395 1.64e-16

PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM25 proteins (composed of RING/B-box/coiled-coil core and also known as RBCC proteins). 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.


Pssm-ID: 293971 [Multi-domain]  Cd Length: 169  Bit Score: 76.84  E-value: 1.64e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 240 VTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRKGK 319
Cdd:cd13736   1 VIFDYNTAHNKVSLSENYTKASVSDDPQNYREHPQRFTYCSQVLGLHCFKQGIHYWEVELQKNNFCGVGICYGSMDRQGP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 320 VTASPANGH-WLLR------QSRGNEYE-ALTSPQtsfrlkepPRCVGIFLDYEAGVISFYNVTNKSHIF-TFTHNFSGP 390
Cdd:cd13736  81 ESRLGRNSEsWCVEwfnvkiSAWHNNVEkTLPSTK--------ATRVGVLLNCDHGFVIFFAVQDKVHLMyKFKVDFTEA 152

                ....*
gi 19923536 391 LRPFF 395
Cdd:cd13736 153 LYPAF 157
SPRY_PRY_TRIM65 cd12896
PRY/SPRY domain in tripartite motif-containing domain 65 (TRIM65); This domain, consisting of ...
241-395 9.75e-15

PRY/SPRY domain in tripartite motif-containing domain 65 (TRIM65); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM65 proteins (composed of RING/B-box/coiled-coil core and also known as RBCC proteins). The SPRY/PRY combination is a possible component of immune defense. This protein family has not been characterized.


Pssm-ID: 293953 [Multi-domain]  Cd Length: 182  Bit Score: 72.10  E-value: 9.75e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 241 TLDPDTAHPKLILS-EDQRCVRLGDRRQPVPDNPQRFDfVVSILGSEYFTTGCHYWEVYVGDKTKwILGVCSESVSRKgK 319
Cdd:cd12896  13 TFDPRTANKYLELSrQNRRAKHGRSAARGVPASPGSFE-LWQVQCTQSFQHGHHYWEVEVSSHSV-TLGVTYPGLPRH-K 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 320 VTASPAN-----GHWLLrQSRGNEYEALTSPQTSfRLKEPP-RCVGIFLDYEAGVISFYNVTNK-SHIFTFTHNFSGPLR 392
Cdd:cd12896  90 QGGHKDNigrnpCSWGL-QIQEDSLQAWHNGRAQ-KLQGVSyRLLGVDLDLEAGTLTFYGLEPGtQRLHTFHAIFTQPLY 167

                ...
gi 19923536 393 PFF 395
Cdd:cd12896 168 PVF 170
IgV_B7-H3 cd20934
Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint ...
39-146 1.62e-14

Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint molecules; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H3 also known as CD276), a member of the B7 family of immune checkpoint molecules. B7-H3 is an important immune checkpoint member of the B7 family and shares homology with other B7 ligands such as programmed death ligand 1 (PD-L1). The B7 family molecules interact with CD28 on T-cells to provide co-stimulatory signals that regulate T-cell activation and T-helper cell differentiation. Although B7-H3 has been shown to have both co-stimulatory and co-inhibitory effects on T-cell responses, the most current studies describe B7-H3 as a T cell inhibitor that promotes tumor aggressiveness and proliferation. Moreover, B7-H3 is highly overexpressed on a wide range of human solid cancers and promotes tumor growth, metastasis, and drug resistance. Thus, B7-H3 expression in tumors often correlates with both negative prognosis and poor clinical outcome in cancer patients. B7-H3 protein contains a predicted signal peptide, V- and C-like Ig domains (IgV and IgC), a transmembrane region, and an intracellular tail.


Pssm-ID: 409528  Cd Length: 115  Bit Score: 69.55  E-value: 1.62e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536  39 VALLGGTAELLCPLSLWPGTVPKEVR--WlrsPFPQRSQAVHIFRDGKDQDEDLMPEYKGRTVLVRDA-QEGSVTLQILD 115
Cdd:cd20934   8 VALVGTDATLRCSFSPEPGFSLAQLSvfW---QLTDTKQLVHSFTESQDQGRDQGSAYANRTALFPDLlAQGNASLRLQR 84
                        90       100       110
                ....*....|....*....|....*....|.
gi 19923536 116 VRLEDQGSYRCLIQVGNLSKEdTVILQVAAP 146
Cdd:cd20934  85 VRVADEGSYTCFVSVQDFGSA-AVSLQVAAP 114
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
42-128 3.60e-10

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 57.08  E-value: 3.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536    42 LGGTAELLCPLSLWPGTVPKEVRWLRSPFPQRSQAVHIFRDGKDQdedlMPEYKGRTVLVRDAQEGSVTLQILDVRLEDQ 121
Cdd:pfam07686  10 LGGSVTLPCTYSSSMSEASTSVYWYRQPPGKGPTFLIAYYSNGSE----EGVKKGRFSGRGDPSNGDGSLTIQNLTLSDS 85

                  ....*..
gi 19923536   122 GSYRCLI 128
Cdd:pfam07686  86 GTYTCAV 92
IgV_HHLA2 cd16091
Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are ...
63-143 1.01e-09

Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are composed of the immunoglobulin variable (IgV) region in HERV-H LTR-associating 2 (HHLA2; also known as B7-H7/B7 homolog 7). HHLA2 is a member of the B7 family of immune regulatory proteins. Mature human HHLA2 consists of an extracellular domain (ECD) with three immunoglobulin-like domains, a transmembrane segment, and a cytoplasmic domain. HHLA2 is widely expressed in human cancers including non-small cell lung carcinoma (NSCLS), triple negative breast cancer (TNBC), and melanoma, but has limited expression on normal tissues. Interestingly, unlike other members of B7 family, HHLA2 is not expressed in mice or rats. HHLA2 functions as a T cell coinhibitory molecules as it inhibits the proliferation of activated CD4(+) and CD8(+) T cells and their cytokine production. Furthermore, HHLA2 is constitutively expressed on the surface of human monocytes and is induced on B cells after stimulation, however it is not inducible on T cells.


Pssm-ID: 409512  Cd Length: 107  Bit Score: 55.86  E-value: 1.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536  63 VRWLRspfPQRSQAVHIFRDGKDQDEDLMPEYKGRTVLVRDA-QEGSVTLQILDVRLEDQGSYRCLIQVGNLSKEDTVIL 141
Cdd:cd16091  29 IHWYK---QDSDIKVHSYYYGKDQLESQDQRYRNRTSLFKDQiSNGNASLLLRRVQLQDEGRYKCYTSTIIGNQESFVNL 105

                ..
gi 19923536 142 QV 143
Cdd:cd16091 106 KV 107
IgV_B7-H4 cd20984
Immunoglobulin Variable (IgV) domain of B7-H4; The members here are composed of the ...
39-128 1.11e-09

Immunoglobulin Variable (IgV) domain of B7-H4; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H4 (also known as B7-S1, B7x, or Vtcn1). B7-H4 is one of the B7 family of immune-regulatory ligands that act as negative regulators of T cell function; it contains one IgV domain and one IgC domain. The B7-family consists of structurally related cell-surface protein ligands, which bind to receptors on lymphocytes that regulate immune responses. The binding of B7-H4 to unidentified receptors results in the inhibition of TCR-mediated T cell proliferation, cell-cycle progression and IL-2 production. As a co-inhibitory molecule, B7-H4 is widely expressed in tumor tissues and its expression is significantly associated with poor prognosis in human cancers such as glioma, pancreatic cancer, oral squamous cell carcinoma, renal cell carcinoma, and lung cancer.


Pssm-ID: 409576  Cd Length: 110  Bit Score: 55.68  E-value: 1.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536  39 VALLGGTAELLCPLSLWPGTVPKEVRWLRSpfpQRSQAVHIFRDGKDQDEDLMPEYKGRT-VLVRDAQEGSVTLQILDVR 117
Cdd:cd20984   8 AGNIGEDGILSCTFTPDIKLSDIVIQWLKE---GDSGLVHEFKEGKDELSRQSPMFRGRTsLFADQVHVGNASLRLKNVQ 84
                        90
                ....*....|.
gi 19923536 118 LEDQGSYRCLI 128
Cdd:cd20984  85 LTDAGTYLCII 95
SPRY_PRY_FSD1 cd12901
Fibronectin type III and SPRY containing 1 (FSD1) domain includes PRY at the N-terminus; This ...
281-395 1.86e-09

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.


Pssm-ID: 293958  Cd Length: 207  Bit Score: 57.53  E-value: 1.86e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 281 SILGSEYFTTGCHYWEV-YVGDKTKWILGVCSESVSR---KGKVTAS---PANgHWL---LRQSRGNEYEALTSPQtsfr 350
Cdd:cd12901  75 TVLGDTLIDGGQHYWEVrAQKDSKAFSVGVAYRSLGKfdqLGKTNASwclHVN-NWLqnsFAAKHNNKAKTLDVPV---- 149
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 19923536 351 lkepPRCVGIFLDYEAGVISFYNVTNKSHIFTFTHNFSGPLRPFF 395
Cdd:cd12901 150 ----PDRIGVYCDFDEGQLSFYNARTKQLLHTFKMKFTQPVLPAF 190
IGv smart00406
Immunoglobulin V-Type;
45-128 1.21e-08

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 52.00  E-value: 1.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536     45 TAELLCplSLWPGTVPK-EVRWLRSPfpQRSQAVHIFRDGKDQDEDLMPEYKGRTVLVRDAQEGSVTLQILDVRLEDQGS 123
Cdd:smart00406   1 SVTLSC--KFSGSTFSSyYVSWVRQP--PGKGLEWLGYIGSNGSSYYQESYKGRFTISKDTSKNDVSLTISNLRVEDTGT 76

                   ....*
gi 19923536    124 YRCLI 128
Cdd:smart00406  77 YYCAV 81
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
291-404 1.34e-08

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.


Pssm-ID: 293931  Cd Length: 118  Bit Score: 52.82  E-value: 1.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 291 GCHYWEVYVGDKTK--WILGVCSESVSRKGKVTASPANGHWLL---RQSRGNEYealTSPQTSFRLKEPPRcVGIFLDYE 365
Cdd:cd11709   1 GKWYWEVRVDSGNGglIQVGWATKSFSLDGEGGVGDDEESWGYdgsRLRKGHGG---SSGPGGRPWKSGDV-VGCLLDLD 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 19923536 366 AGVISFYNvtNKSHIFTFTHNF---SGPLRPFFEPCLHDGGK 404
Cdd:cd11709  77 EGTLSFSL--NGKDLGVAFTNLflkGGGLYPAVSLGSGQGVT 116
IgV_CD86 cd16087
Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 86; The members here ...
40-129 5.09e-07

Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 86; The members here are composed of the immunoglobulin variable region (IgV) in the Cluster of Differentiation (CD) 86). Glycoproteins B7-1 (also known as cluster of differentiation (CD) 80) and B7-2 (also known as CD86) are expressed on antigen-presenting cells and deliver the co-stimulatory signal through CD28 and CTLA-4 (also known as CD152) on T cells. signaling through CD28 augments the T-cell response, whereas CTLA-4 signaling attenuates it. The CTLA-4 and B7-2 monomers are both two-layer beta-sandwiches that display the chain topology characteristic of the immunoglobulin variable (V-type) domains present in antigen receptors. The front and back sheets of B7-2 are composed of AGFCC'C" and BED strands, respectively. Members of the IgV family are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 409508  Cd Length: 108  Bit Score: 48.09  E-value: 5.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536  40 ALLGGTAELLCPLSLWPGTVPKE--VRWLRspfpQRSQAVHIFRDGKDQDEDLMPEYKGRTVLVRDaqegSVTLQILDVR 117
Cdd:cd16087   5 AYFNETAYLPCQFKNPQNISLSElvVFWQD----QKKLVLYELYLGKEKLDNVNSKYIGRTSFDQE----NWTLQLHNVQ 76
                        90
                ....*....|..
gi 19923536 118 LEDQGSYRCLIQ 129
Cdd:cd16087  77 IKDQGTYQCFIH 88
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
38-143 6.56e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 47.11  E-value: 6.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536     38 HVALLGGTAELLCPLSlwpGTVPKEVRWLRspfpqrsqavhifrdgkdqDEDLMPEYKGRTVLVRDaqEGSVTLQILDVR 117
Cdd:smart00410   4 VTVKEGESVTLSCEAS---GSPPPEVTWYK-------------------QGGKLLAESGRFSVSRS--GSTSTLTISNVT 59
                           90       100
                   ....*....|....*....|....*.
gi 19923536    118 LEDQGSYRCLIQVGNLSKEDTVILQV 143
Cdd:smart00410  60 PEDSGTYTCAATNSSGSASSGTTLTV 85
SPRY_PRY_TRIM25-like cd13737
PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25)-like; This domain, ...
242-393 2.69e-06

PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25)-like; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of proteins similar to TRIM25 (composed of RING/B-box/coiled-coil core and also known as RBCC proteins). 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.


Pssm-ID: 293972  Cd Length: 172  Bit Score: 47.56  E-value: 2.69e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 242 LDPDTAHPKLIL-SEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKtkWI-LGVCSESVSRKGK 319
Cdd:cd13737   3 FDPNTASEELFLfKETHSVLNMGILLESFFGPCQGFNHWPQVLCTRSLCEGCHYWEAEVSNS--WVcLGVTYSYSHPTGK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536 320 vtaspANGHWLLRQSRGN---EYEAL----------TSPQTSFRlkeppRCVGIFLDYEAGVISFYNVTNK-SHIFTFTH 385
Cdd:cd13737  81 -----SCIFYLIGRNPYSwclEWDSLkfsvwhnniqTVVHGSYY-----KTIGVLLDYAAGSLTFYGVANTmNLIYRFLT 150

                ....*...
gi 19923536 386 NFSGPLRP 393
Cdd:cd13737 151 TFTEPLYP 158
IgV_CAR_like cd20960
Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and ...
43-126 9.25e-06

Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins; The members here are composed of the Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins. CAR, which is encoded by human CXADR gene, is a cell adhesion molecule of the Immunoglobulin (Ig) superfamily. The CAR acts as a type I membrane receptor for group B1-B6 coxsackie viruses and subgroup C adenoviruses. For instance, adenovirus interacts with the coxsackievirus and adenovirus receptor to enter epithelial airway cells. The CAR is also shown to be involved in physiological processes such as neuronal and heart development, epithelial tight junction integrity, and tumor suppression. The CAR is a component of the epithelial apical junction complex that may function as a homophilic cell adhesion molecule and is essential for tight junction integrity. The CAR is also involved in transepithelial migration of leukocytes through adhesive interactions with JAML a transmembrane protein of the plasma membrane of leukocytes. The interaction between both receptors also mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. The CAR is composed of one V-set and one C2-set Ig module, a single transmembrane helix, and an intracellular domain. This group belongs to the V-set of IgSF domains, having A, B, E and D strands in one beta-sheet and A', G, F, C, C' and C" in the other


Pssm-ID: 409552  Cd Length: 114  Bit Score: 44.75  E-value: 9.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536  43 GGTAELLCPLSLWPGTVPK-EVRWLRSPfPQRSQAVHIFRDGKDQDEDLMPEYKGRTVLVRDAQEGSVTLQILDVRLEDQ 121
Cdd:cd20960  15 GENVTLPCHHQLGLEDQGTlDIEWLLLP-SDKVEKVVITYSGDRVYNHYYPALKGRVAFTSNDLSGDASLNISNLKLSDT 93

                ....*
gi 19923536 122 GSYRC 126
Cdd:cd20960  94 GTYQC 98
IgV_PDl1 cd20947
Immunoglobulin Variable (IgV) domain of Programmed death ligand 1 (PD-L1); The members here ...
87-131 1.54e-05

Immunoglobulin Variable (IgV) domain of Programmed death ligand 1 (PD-L1); The members here are composed of the immunoglobulin variable (IgV) domain of Programmed death ligand 1 (PD-L1; also known as Cluster of Differentiation 274 (CD274)). PD-L1 is a cell-surface ligand that competes with PD-L2 for binding to the immunosuppressive receptor programmed death-1 (PD-1). PD-1 is a member of the B7 family that plays an important role in negatively regulating immune responses upon interaction with its two ligands, PD-L1 or PD-L2. Like PD-L2, PD-L1 interacts with PD-1 and suppresses T cell proliferation and cytokine production. The PD-1 receptor is expressed on the surface of activated T cells, while PD-L1 is expressed on cancer cells. When PD-1 and PD-L1 bind together, they form a molecular shield protecting tumor cells from being destroyed by the immune system. Thus, inhibiting the binding of PD-L1 to PD-1 with an antibody leads to killing of tumor cells by T cells. PD-1 inhibitors (such as Pembrolizumab, Nivolumab, and Cemiplimab) and PD-L1 inhibitors (such as Atezolizumab, Avelumab, and Durvalumab ) are an emerging class of immunotherapy that stimulate lymphocytes against tumor cells.


Pssm-ID: 409539  Cd Length: 110  Bit Score: 43.77  E-value: 1.54e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 19923536  87 DEDLMPE---YKGRTVLVRDA-QEGSVTLQILDVRLEDQGSYRCLIQVG 131
Cdd:cd20947  51 EEDLKVQhssYRQRARLLKDQlSLGNAALQITDVKLQDAGVYRCMISYG 99
IgV_VCBP cd20963
Immunoglobulin Variable region-containing chitin-binding proteins; an immunoglobulin V-set ...
39-137 2.54e-05

Immunoglobulin Variable region-containing chitin-binding proteins; an immunoglobulin V-set domain; The members here are composed of the immunoglobulin variable (IgV) region-containing chitin-binding proteins (VCBPs). VCBPs are secreted, immune-type molecules that have been identified in both amphioxus and sea squirt (Ciona intestinalis). VCBPs, which consist of a leader peptide, two tandem N-terminal immunoglobulin V-type domains and a single C-terminal chitin-binding domain, belong to a multigene family encoding secreted proteins. The VCBPs were identified first in the cephalochordate Branchiostoma floridae and show structural similarities with V-type domains of immunoglobulins and T cell receptors, suggesting that VCBPs represent a unique gut-associated form of innate immune proteins. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as, T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as, butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the V-set of IgSF domains, having A, B, E and D strands in one beta-sheet and A', G, F, C, C' and C" in the other.


Pssm-ID: 409555  Cd Length: 123  Bit Score: 43.76  E-value: 2.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536  39 VALLGGTAELLCPLSLWPGTVPKEVRWLRSPFPQRSQAV----HIFRDGKDQDEDLMPEYKGRTVLVRDAQEgsvTLQIL 114
Cdd:cd20963  13 DPTWGNRVELPCSYTISPAAQPPTITWLKGISVDRAEVVfkgfKYWNETSSSGEVYFGDYAGRASVASLTQP---TLVLT 89
                        90       100
                ....*....|....*....|...
gi 19923536 115 DVRLEDQGSYRCliQVGNLSKED 137
Cdd:cd20963  90 DLKFDDWGRYWC--RVANWSQRD 110
SPRY_PRY_TRIM67_9 cd12889
PRY/SPRY domain in tripartite motif-containing proteins, TRIM9 and TRIM67; This domain, ...
241-299 4.70e-05

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.


Pssm-ID: 293947  Cd Length: 172  Bit Score: 43.77  E-value: 4.70e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 19923536 241 TLDPDTAHPKLILSEDQRCVRLgdrrqpvpdnpQRFDFVVsILGSEYFTTGCHYWEVYV 299
Cdd:cd12889  11 TFDPSTSHPDIILSNDNMTVTC-----------NSYEDRV-VLGSVGFSRGVHYWEVTI 57
IgV_CRIg cd16089
Immunoglobulin variable (IgV)-like domain in complement receptor of the immunoglobulin ...
44-143 1.61e-04

Immunoglobulin variable (IgV)-like domain in complement receptor of the immunoglobulin superfamily (CRIg); The members here are composed of the immunoglobulin variable (IgV) region of the complement receptor of the immunoglobulin superfamily (CRIg). The N-terminal domain of CRIg (also known as Z39Ig and V-set and Ig domain-containing 4 (VSIG4) belongs to the IgV family of immunoglobulin-like domains while the C-terminal domain of CRIg belongs to the IgC family of immunoglobulin-like domains. Like all members of this family, the CRIg domain contains two beta-sheets: one composed of strands A', G, F, C, C' and C", and the other of strands B, E and D. The complement system is an important part of the innate immune system and is required for removal of pathogens from the bloodstream. After exposure to pathogens, the third component of the complement system, C3, is cleaved to C3b which, after recruitment of factor B, initiates formation of the alternative pathway convertases. CRIg, a complement receptor expressed on macrophages, binds to C3b and iC3b mediating phagocytosis of the particles. It is also a potent inhibitor of the alternative pathway convertases and a negative regulator of T cell activation. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as, T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as, butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 409510  Cd Length: 117  Bit Score: 41.36  E-value: 1.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536  44 GTAELLCPLSLWPGTVPKEVRWLrspFPQRSQAVHIF-RDGKDqDEDLMPEYKGRTVLVRDAqEGSVTLQILDVRLEDQG 122
Cdd:cd16089  15 GSVNLPCTYVPEEGYTQVLVKWL---VQRDSDPVTIFlRDSSG-DHIQQAKYRGRLEVSKDT-PGDVSLQLDTLEMDDRG 89
                        90       100
                ....*....|....*....|....*.
gi 19923536 123 SYRCLI----QVGNLSK-EDTVILQV 143
Cdd:cd16089  90 HYTCQVtwqtPDGNLIVrEKTTELRV 115
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
93-142 2.04e-04

Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The members here are composed of the immunoglobulin (Ig)-like domain similar to that found in human cartilage link protein (LP; also called hyaluronan and proteoglycan link protein). In cartilage, chondroitin-keratan sulfate proteoglycan (CSPG), aggrecan, forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409461  Cd Length: 117  Bit Score: 40.77  E-value: 2.04e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 19923536  93 EYKGRtVLVRDAQEGSVTLQILDVRLEDQGSYRCliQVGNLSKEDTVILQ 142
Cdd:cd05877  63 SYQGR-VFLRRADDLDASLVITDLRLEDYGRYRC--EVIDGLEDESVVVA 109
IgV_1_MRC-OX-2_like cd05846
First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; ...
39-130 1.56e-03

First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of rat MRC OX-2 antigen (also known as CD200) and similar proteins. MRC OX-2 is a membrane glycoprotein expressed in a variety of lymphoid and non-lymphoid cells in rats. It has a similar broad distribution pattern in humans. MRC OX-2 may regulate myeloid cell activity. The protein has an extracellular portion containing two Ig-like domains, a transmembrane portion, and a cytoplasmic portion.


Pssm-ID: 409433  Cd Length: 108  Bit Score: 38.09  E-value: 1.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536  39 VALLGGTAELLCPLSLwpgtvPKEVR---WlrspfpQRSQAV---HIFRDGKDQDEDLMPEYKGRTVLVRDAQEGSvTLQ 112
Cdd:cd05846   9 RAVLGGNATLSCNLTL-----PEEVLqvtW------QKIKASspeNIVTYSKKYGVKIQPSYVRRISFTSSGLNST-SIT 76
                        90
                ....*....|....*...
gi 19923536 113 ILDVRLEDQGSYRCLIQV 130
Cdd:cd05846  77 IWNVTLEDEGCYKCLFNT 94
IgV_B7-H6 cd20981
Immunoglobulin variable (IgV) domain of B7-H6; The members here are composed of the ...
34-143 2.56e-03

Immunoglobulin variable (IgV) domain of B7-H6; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H6 (also known as NCR3LG1). B7-H6 contains one IgV domain and one IgC domain (IgV-IgC) and belongs to the B7-family, which consists of structurally related cell-surface protein ligands which bind to receptors on lymphocytes that regulate immune responses. B7-H6 is a ligand of NKp30, which is a member of CD28 family and an activating receptor of natural killer (NK) cells. The expression of NKp30 has been found in most of NK cells, which is involved in the process of tumor cell killing and interaction with antigen presenting cells (APCs) such as dendritic cells. Studies showed that NK cells eliminate B7-H6-expressing tumor cells either directly via cytotoxicity or indirectly by cytokine secretion. For instance, chimeric NKp30-expressing T cells responded to B7-H6(+) tumor cells and those T cells produced IFN-gamma and killed B7-H6-expressing tumor cells in vivo. B7-H6 mRNA is not found in normal cells, while high expression of B7-H6 is found in certain type tumor cells, such as lymphoma, leukemia, ovarian cancer, brain tumors, breast cancers, and various sarcomas. Since B7-H6 can bind NKp30 to exert anti-tumor effects by NK cells, which are able to recognize the difference between cancer cells and normal cells, B7-H6 may serve as a promising target for cancer immunotherapy.


Pssm-ID: 409573  Cd Length: 114  Bit Score: 37.59  E-value: 2.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536  34 AGKFHVALLGGTAELLCPLslwPGTVPKEVR-----WLRSPfPQRSQAVHIFRDGKDQDEDLMPeykGRTVLVRDAQEGS 108
Cdd:cd20981   7 AGGTQITPLNDNVTIFCNI---FYSQPLNITsmgitWFRKS-LTFDKEVKVFEFFGDHQKAFRP---GAIVSPWRLKSGD 79
                        90       100       110
                ....*....|....*....|....*....|....*
gi 19923536 109 VTLQILDVRLEDQGSYRCLIQVGNLSKEDTVILQV 143
Cdd:cd20981  80 ASLQLPGVQLEEAGEYRCEVVVTPLKAQGTVQLEV 114
I-set pfam07679
Immunoglobulin I-set domain;
39-144 3.67e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 36.47  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536    39 VALLGGTAELLCPLSlwpGTVPKEVRWlrspfpqrsqavhiFRDGKDQDEDlmpeykgRTVLVRdAQEGSVTLQILDVRL 118
Cdd:pfam07679  11 EVQEGESARFTCTVT---GTPDPEVSW--------------FKDGQPLRSS-------DRFKVT-YEGGTYTLTISNVQP 65
                          90       100
                  ....*....|....*....|....*.
gi 19923536   119 EDQGSYRCliQVGNLSKEDTVILQVA 144
Cdd:pfam07679  66 DDSGKYTC--VATNSAGEAEASAELT 89
IgV_CD33 cd05712
Immunoglobulin Variable (IgV) domain at the N-terminus of CD33 and related Siglecs (sialic ...
65-125 4.01e-03

Immunoglobulin Variable (IgV) domain at the N-terminus of CD33 and related Siglecs (sialic acid-binding Ig-like lectins); The members here are composed of the immunoglobulin (Ig) domain at the N-terminus of Cluster of Differentiation (CD) 33 and related Siglecs (sialic acid-binding Ig-like lectins). Siglec refers to a structurally related protein family that specifically recognizes sialic acid in oligosaccharide chains of glycoproteins and glycolipids. Siglecs are type I transmembrane proteins, organized as an extracellular module composed of Ig-like domains, an N-terminal variable set of Ig-like carbohydrate recognition domains, and 1 to 16 constant Ig-like domains, followed by transmembrane and short cytoplasmic domains. Human Siglecs are classified into two subgroups, one subgroup is comprised of sialoadhesin (Siglec-1), CD22 (Siglec-2), and MAG, the other subgroup is comprised of CD33-related Siglecs which include CD33 (Siglec-3) and human Siglecs 5-11.


Pssm-ID: 409377  Cd Length: 119  Bit Score: 37.37  E-value: 4.01e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19923536  65 WLR-SPFPQRSQAVHIfrdgKDQDEDLMPEYKGRTVLVRDAQEGSVTLQILDVRLEDQGSYR 125
Cdd:cd05712  39 WYRgGPYPKYRPPVAT----NNRTREVHESTQGRFRLLGDPGKKNCSLSISDARPEDSGKYF 96
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
43-126 4.03e-03

Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin variable domain (IgV). The IgV family contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology, and are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E and, D strands in one sheet and A', G, F, C, C', and C" strands in the other.


Pssm-ID: 409355 [Multi-domain]  Cd Length: 111  Bit Score: 36.93  E-value: 4.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536  43 GGTAELLCPLSLWPGTVPkeVRWLRSPFPQRSQAVHIFRDGKDQDEDlmpEYKGRTVLVRDAQEgSVTLQILDVRLEDQG 122
Cdd:cd00099  13 GESVTLSCEVSSSFSSTY--IYWYRQKPGQGPEFLIYLSSSKGKTKG---GVPGRFSGSRDGTS-SFSLTISNLQPEDSG 86

                ....
gi 19923536 123 SYRC 126
Cdd:cd00099  87 TYYC 90
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
46-126 4.17e-03

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 35.77  E-value: 4.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536  46 AELLCPLSlwpGTVPKEVRWlrspfpqrsqavhiFRDGKDQDEDLMPEykgrtvlvRDAQEGSVTLQILDVRLEDQGSYR 125
Cdd:cd00096   1 VTLTCSAS---GNPPPTITW--------------YKNGKPLPPSSRDS--------RRSELGNGTLTISNVTLEDSGTYT 55

                .
gi 19923536 126 C 126
Cdd:cd00096  56 C 56
Ig_Versican cd05901
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
42-144 6.61e-03

Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), versican; The members here are composed of the immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), versican. In CSPGs, the Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, the CSPG aggrecan (not included in this group) forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Like aggrecan, versican has a wide distribution in connective tissue and extracellular matrices. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409482  Cd Length: 128  Bit Score: 36.86  E-value: 6.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536  42 LGGTAELLCPLSLWPgTVPKEVRWLRSPFPQRSQAVHIFRDGKDQDEDLM-----------PEYKGR-TVLVRDAQEGSV 109
Cdd:cd05901  11 LSGSVVLPCRFSTLP-TLPPSYNITSEFLRIKWTKIQVDKNGKDHKETTVlvaqngiikigQEYMGRvSVPSHPEDQGDA 89
                        90       100       110
                ....*....|....*....|....*....|....*
gi 19923536 110 TLQILDVRLEDQGSYRCLIQVGNLSKEDTVILQVA 144
Cdd:cd05901  90 SLTIVKLRASDAGVYRCEVMHGIEDTQDTVSLDVS 124
IgV_pIgR_like cd05716
Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The ...
38-142 7.60e-03

Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins. pIgR delivers dimeric IgA and pentameric IgM to mucosal secretions. Polymeric immunoglobulin (pIgs) are the first defense against pathogens and toxins. IgA and IgM can form polymers via an 18-residue extension at their C-termini referred to as the tailpiece. pIgR transports pIgs across mucosal epithelia into mucosal secretions. Human pIgR is a glycosylated type I transmembrane protein, comprised of a 620-residue extracellular region, a 23-residue transmembrane region, and a 103-residue cytoplasmic tail. The extracellular region contains five domains that share sequence similarity with Ig variable (v) regions. This group also contains the Ig-like extracellular domains of other receptors such as NK cell receptor Nkp44 and myeloid receptors, among others.


Pssm-ID: 409381  Cd Length: 100  Bit Score: 35.84  E-value: 7.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923536  38 HVALLGGTAELLCPLSLWPGTVPKevRWLRSpfpqrsqavhifRDGKDQDEDLMPEY--KGRTVLVRDAQEGSVTLQILD 115
Cdd:cd05716   7 VTGVEGGSVTIQCPYPPKYASSRK--YWCKW------------GSEGCQTLVSSEGVvpGGRISLTDDPDNGVFTVTLNQ 72
                        90       100
                ....*....|....*....|....*...
gi 19923536 116 VRLEDQGSYRCLI-QVGNLSKEDTVILQ 142
Cdd:cd05716  73 LRKEDAGWYWCGVgDDGDRGLTVQVKLV 100
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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