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Conserved domains on  [gi|578811016|ref|XP_006714886|]
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butyrophilin-like protein 9 isoform X3 [Homo sapiens]

Protein Classification

PRY/SPRY domain-containing protein; RING finger and SPRY domain-containing protein( domain architecture ID 10861259)

PRY/SPRY domain-containing family protein, 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; RING finger and SPRY domain-containing protein similar to Salmo salar tripartite motif-containing protein 39

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SPRY_PRY_C-I_1 cd13733
PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM5, TRIM6, TRIM7, ...
322-496 4.99e-89

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: 270.89  E-value: 4.99e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 322 DVTLDPASAHPSLEVSEDGKSVSSRGAPPGPAPGHpQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGACLAAVPRA 401
Cdd:cd13733    1 DVTLDPDTAHPNLILSEDLKSVRYGDKRQNLPDNP-ERFDTCVCVLGSEGFSSGRHYWEVEVGGKTDWDLGVARESVNRK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 402 GPARLSPAAGYWVLGLWNGCEYFVLAPHRVALTLRVPPRRLGVFLDYEAGELSFFNVSDGSHIFTFHDTFSGALCAYFRP 481
Cdd:cd13733   80 GKITLSPENGYWTVGLRNGNEYKALTSPSTPLSLREKPQKVGVFLDYEEGQVSFYNVDDGSHIYTFTDCFTEKLYPYFSP 159
                        170
                 ....*....|....*
gi 578811016 482 RAHDGGEHPDPLTIC 496
Cdd:cd13733  160 CLNDGGKNSAPLIIC 174
IgV_MOG_like cd05713
Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here ...
39-151 3.26e-60

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: 193.95  E-value: 3.26e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016  39 KVLGPEYPILALVGEEVEFPCHLWPQLDAQQMEIRWFRSQTFNVVHLYQEQQELPGRQMPAFRNRTKLVKDDIAYGSVVL 118
Cdd:cd05713    2 SVIGPTEPILALVGEDAELPCHLSPKMSAEHMEVRWFRSQFSPVVHLYRDGQDQEEEQMPEYRGRTELLKDAIAEGSVAL 81
                         90       100       110
                 ....*....|....*....|....*....|...
gi 578811016 119 QLHSIIPSDKGTYGCRFHSDNFSGEALWELEVA 151
Cdd:cd05713   82 RIHNVRPSDEGQYTCFFRSGSFYEEATLELKVA 114
 
Name Accession Description Interval E-value
SPRY_PRY_C-I_1 cd13733
PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM5, TRIM6, TRIM7, ...
322-496 4.99e-89

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: 270.89  E-value: 4.99e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 322 DVTLDPASAHPSLEVSEDGKSVSSRGAPPGPAPGHpQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGACLAAVPRA 401
Cdd:cd13733    1 DVTLDPDTAHPNLILSEDLKSVRYGDKRQNLPDNP-ERFDTCVCVLGSEGFSSGRHYWEVEVGGKTDWDLGVARESVNRK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 402 GPARLSPAAGYWVLGLWNGCEYFVLAPHRVALTLRVPPRRLGVFLDYEAGELSFFNVSDGSHIFTFHDTFSGALCAYFRP 481
Cdd:cd13733   80 GKITLSPENGYWTVGLRNGNEYKALTSPSTPLSLREKPQKVGVFLDYEEGQVSFYNVDDGSHIYTFTDCFTEKLYPYFSP 159
                        170
                 ....*....|....*
gi 578811016 482 RAHDGGEHPDPLTIC 496
Cdd:cd13733  160 CLNDGGKNSAPLIIC 174
IgV_MOG_like cd05713
Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here ...
39-151 3.26e-60

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: 193.95  E-value: 3.26e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016  39 KVLGPEYPILALVGEEVEFPCHLWPQLDAQQMEIRWFRSQTFNVVHLYQEQQELPGRQMPAFRNRTKLVKDDIAYGSVVL 118
Cdd:cd05713    2 SVIGPTEPILALVGEDAELPCHLSPKMSAEHMEVRWFRSQFSPVVHLYRDGQDQEEEQMPEYRGRTELLKDAIAEGSVAL 81
                         90       100       110
                 ....*....|....*....|....*....|...
gi 578811016 119 QLHSIIPSDKGTYGCRFHSDNFSGEALWELEVA 151
Cdd:cd05713   82 RIHNVRPSDEGQYTCFFRSGSFYEEATLELKVA 114
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
375-498 5.01e-22

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: 91.59  E-value: 5.01e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016   375 GRHYWEVHVGRRSRWFLGACLAAVPRAGPARLSPAAGYWVLGLWNGCEYFVLAPHRVALTLRVPPRRLGVFLDYEAGELS 454
Cdd:smart00449   2 GRHYFEVEIGDGGHWRVGVATKSVPRGYFALLGEDKGSWGYDGDGGKKYHNSTGPEYGLPLQEPGDVIGCFLDLEAGTIS 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 578811016   455 FFNVSDGSHIFTFHD-TFSGALCAYFRPRAHDGGehpdPLTICPL 498
Cdd:smart00449  82 FYKNGKYLHGLAFFDvKFSGPLYPAFSLGSGNSV----RLNFGPL 122
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
376-479 7.76e-22

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: 90.87  E-value: 7.76e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016  376 RHYWEVHVGRRSR--WFLGACLAAVPRAGPARLSPAAGYWVLGLWNGCEYFVLAPHRVALTLRVPPRRLGVFLDYEAGEL 453
Cdd:pfam00622   1 RHYFEVEIFGQDGggWRVGWATKSVPRKGERFLGDESGSWGYDGWTGKKYWASTSPLTGLPLFEPGDVIGCFLDYEAGTI 80
                          90       100
                  ....*....|....*....|....*..
gi 578811016  454 SFFNVSdGSHIFTFHD-TFSGALCAYF 479
Cdd:pfam00622  81 SFTKNG-KSLGYAFRDvPFAGPLFPAV 106
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
43-143 1.23e-09

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: 55.54  E-value: 1.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016   43 PEYPILALVGEEVEFPCHLWPQLDAQQMEIRWFR----SQTFNVVHLYQeqqelPGRQMPAFRNRTKLvKDDIAYGSVVL 118
Cdd:pfam07686   2 TPREVTVALGGSVTLPCTYSSSMSEASTSVYWYRqppgKGPTFLIAYYS-----NGSEEGVKKGRFSG-RGDPSNGDGSL 75
                          90       100
                  ....*....|....*....|....*
gi 578811016  119 QLHSIIPSDKGTYGCRFHSDNFSGE 143
Cdd:pfam07686  76 TIQNLTLSDSGTYTCAVIPSGEGVF 100
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
46-150 7.11e-08

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: 49.81  E-value: 7.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016    46 PILALVGEEVEFPCHLWPQLDAQqmeIRWFRsqtfnvvhlyqeqqelPGRQMPAFRNRTKLVKDDiayGSVVLQLHSIIP 125
Cdd:smart00410   3 SVTVKEGESVTLSCEASGSPPPE---VTWYK----------------QGGKLLAESGRFSVSRSG---STSTLTISNVTP 60
                           90       100
                   ....*....|....*....|....*
gi 578811016   126 SDKGTYGCRFHSDNFSGEALWELEV 150
Cdd:smart00410  61 EDSGTYTCAATNSSGSASSGTTLTV 85
 
Name Accession Description Interval E-value
SPRY_PRY_C-I_1 cd13733
PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM5, TRIM6, TRIM7, ...
322-496 4.99e-89

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: 270.89  E-value: 4.99e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 322 DVTLDPASAHPSLEVSEDGKSVSSRGAPPGPAPGHpQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGACLAAVPRA 401
Cdd:cd13733    1 DVTLDPDTAHPNLILSEDLKSVRYGDKRQNLPDNP-ERFDTCVCVLGSEGFSSGRHYWEVEVGGKTDWDLGVARESVNRK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 402 GPARLSPAAGYWVLGLWNGCEYFVLAPHRVALTLRVPPRRLGVFLDYEAGELSFFNVSDGSHIFTFHDTFSGALCAYFRP 481
Cdd:cd13733   80 GKITLSPENGYWTVGLRNGNEYKALTSPSTPLSLREKPQKVGVFLDYEEGQVSFYNVDDGSHIYTFTDCFTEKLYPYFSP 159
                        170
                 ....*....|....*
gi 578811016 482 RAHDGGEHPDPLTIC 496
Cdd:cd13733  160 CLNDGGKNSAPLIIC 174
SPRY_PRY_TRIM39 cd13745
PRY/SPRY domain in tripartite motif-binding protein 39 (TRIM39) and TRIM39-like; This domain, ...
319-497 6.58e-71

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: 224.04  E-value: 6.58e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 319 YAVDVTLDPASAHPSLEVSEDGKSVSsRGAPPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGACLAAV 398
Cdd:cd13745    1 FAVDVTLDPDTAHPNLVLSEDRKSVR-HGDTRQDLPDNPERFDTYPCVLGAEGFTGGRHYWEVEVGDKTEWTLGVCRESV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 399 PRAGPARLSPAAGYWVLGLWNGcEYFVLAPHRVALTLRVPPRRLGVFLDYEAGELSFFNVSDGSHIFTFHDTFSGALCAY 478
Cdd:cd13745   80 SRKGEVTLSPENGYWTVWLRDG-KYEALTSPPTPLPVSVRPSRVGIFLDYEAGEVSFYNVTDRSHLFTFTDTFSGTLRPY 158
                        170
                 ....*....|....*....
gi 578811016 479 FRPRAHDGGEHPDPLTICP 497
Cdd:cd13745  159 FYPGLNAGGKNAAPLIICP 177
SPRY_PRY_TRIM20 cd15813
PRY/SPRY domain in tripartite motif-binding protein 20 (TRIM20), also known as pyrin; This ...
313-496 1.71e-64

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: 207.69  E-value: 1.71e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 313 WRAAQKYAVDVTLDPASAHPSLEVSEDGKSVSSRGAPPGPAPGHpQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLG 392
Cdd:cd15813    1 LRAAQAHAVNVTLDPETAHPNLIFSDDLKSVRLGNKWDRLPDNP-ERFDSCIIVLGSPSFTSGRHYWEVEVGDKTGWILG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 393 ACLAAVPRAGPARLSPAAGYWVLGLWNGCEYFVLAPHRVALTLRVPPRRLGVFLDYEAGELSFFNVSDGSHIFTFHDTFS 472
Cdd:cd15813   80 VCKASVSRKGSMTLSPENGYWVVMMTKRNEYQASTSPPTRLWLREPPRRVGIFLDYEAGDISFYNVTAKSHIYTFTSFSS 159
                        170       180
                 ....*....|....*....|....*
gi 578811016 473 -GALCAYFRPRAHDGGEHPDPLTIC 496
Cdd:cd15813  160 sGPLQPIFSPGTHDGGKNMDPLTIC 184
SPRY_PRY_BTN1_2 cd15819
butyrophilin subfamily member A1 and A2 (BTN1A and BTN2A); This domain, consisting of the ...
320-496 1.91e-61

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: 199.37  E-value: 1.91e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 320 AVDVTLDPASAHPSLEVSEDGKSVSsRGAPPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGACLAAVP 399
Cdd:cd15819    1 AVNVTLDPDTAHPALILSEDGRSVT-WGETRQDLPENPERFDSLPCVLGQEGFTSGRHYWEVEVGDRTSWDLGVCRDNVM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 400 RAGPARLSPAAGYWVLGLWNGcEYFVLAPHRVALTLRVPPRRLGVFLDYEAGELSFFNVSDGSHIFTF-HDTFSGALCAY 478
Cdd:cd15819   80 RKGRVTLSPENGFWAIRLYGN-EYWALTSPETPLTLKEPPRRVGIFLDYEAGDVSFYNMTDGSHIYTFpQTAFSGPLRPF 158
                        170
                 ....*....|....*...
gi 578811016 479 FRPRAHDggehPDPLTIC 496
Cdd:cd15819  159 FRLWSSD----SGPLTIC 172
IgV_MOG_like cd05713
Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here ...
39-151 3.26e-60

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: 193.95  E-value: 3.26e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016  39 KVLGPEYPILALVGEEVEFPCHLWPQLDAQQMEIRWFRSQTFNVVHLYQEQQELPGRQMPAFRNRTKLVKDDIAYGSVVL 118
Cdd:cd05713    2 SVIGPTEPILALVGEDAELPCHLSPKMSAEHMEVRWFRSQFSPVVHLYRDGQDQEEEQMPEYRGRTELLKDAIAEGSVAL 81
                         90       100       110
                 ....*....|....*....|....*....|...
gi 578811016 119 QLHSIIPSDKGTYGCRFHSDNFSGEALWELEVA 151
Cdd:cd05713   82 RIHNVRPSDEGQYTCFFRSGSFYEEATLELKVA 114
SPRY_PRY_TRIM75 cd15829
PRY/SPRY domain of tripartite motif-binding protein 75 (TRIM75); This domain, consisting of ...
314-496 5.01e-55

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: 183.26  E-value: 5.01e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 314 RAAQKYAVDVTLDPASAHPSLEVSEDGKSVSSrGAPPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGA 393
Cdd:cd15829   12 KIIKKFRVDVTLDPETAHPNLLVSEDKKCVTF-TKKKQRVPDSPKRFTVNPVVLGFPGFHSGRHFWEVEVGDKPEWAVGV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 394 CLAAVPRAGPARLSPAAGYWVLGLWNGCeYFVLAPHRVALTLRVPPRRLGVFLDYEAGELSFFNVSDGSHIFTFHDTFSG 473
Cdd:cd15829   91 CKDSLSTKARRPPSGQQGCWRIQLQGGD-YDAPGAVPPPLLLEVKPRGIGVFLDYELGEISFYNMPEKSHIHTFTDTFSG 169
                        170       180
                 ....*....|....*....|...
gi 578811016 474 ALCAYFRPrahdgGEHPDPLTIC 496
Cdd:cd15829  170 PLRPYFYV-----GPDSKPLRIC 187
SPRY_PRY_RFPL cd15821
Ret finger protein-like (RFPL), includes RFP1, 2, 3, 4; This domain, consisting of the ...
318-496 6.14e-54

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: 179.82  E-value: 6.14e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 318 KYAVDVTLDPASAHPSLEVSEDGKSVSSRGAPPGPAPGHpQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGACLAA 397
Cdd:cd15821    1 KFQVDMTLDVDTANNYLIISEDLRSVRCGCFRQNRKELA-ERFDDALCVLGSPRFTSGRHYWEVDVGTSTEWDLGVCRES 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 398 VPRAGPARLSPAAGYWVLGLWNGCEYFVLAPHRVALTLRVPPRRLGVFLDYEAGELSFFNVSDGSHIFTFHDTF-SGALC 476
Cdd:cd15821   80 VNRQGPIELSPEHGFWTVSLRDGSVFFASTVPLTVLWVNPRLHRVGIFLDMEMGTISFYDVSDGSHIFTFTKISaEEPLR 159
                        170       180
                 ....*....|....*....|
gi 578811016 477 AYFRPRAHDGGEHpDPLTIC 496
Cdd:cd15821  160 PFFAPANPYGDDQ-GVLSIC 178
SPRY_PRY_BTN3 cd15820
PRY/SPRY domain of butyrophilin 3 (BTN3), includes BTN3A1, BTN3A2, BTN3A3 as well as BTN-like ...
320-497 1.33e-51

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: 173.77  E-value: 1.33e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 320 AVDVTLDPASAHPSLEVSEDGKSVSsRGAPPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGACLAAVP 399
Cdd:cd15820    3 PADVILDPDTANPILLISEDQRSLQ-WADEPQNLPDNPKRFDWHYCVLGCKSFTSGRHFWEVEVGDRKEWYVGVCRENVE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 400 RAGPARLSPAAGYWVLGLWNGCEYFVLAPHRVALTLRVPPRRLGVFLDYEAGELSFFNVSDGSHIFTF-HDTFSGALCAY 478
Cdd:cd15820   82 RKLWVKMAPENGFWTIGLSDGNDYQALTDPRTKLTIANPPQRVGVFLDYETGEVSFYNAMDGSHIYTFpHTSFSGPLYPV 161
                        170
                 ....*....|....*....
gi 578811016 479 FRPRAHDggehPDPLTICP 497
Cdd:cd15820  162 FRLLSWD----PTALTICP 176
SPRY_PRY_TRIM58 cd15816
PRY/SPRY domain in tripartite motif-binding protein 58 (TRIM58), also known as BIA2; This ...
322-479 1.06e-49

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: 168.43  E-value: 1.06e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 322 DVTLDPASAHPSLEVSEDGKSVSSrGAPPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGACLAAVPRA 401
Cdd:cd15816    1 DVKLDPATAHPSLLLTADLRSVQD-GELWRDVPGNPERFDTWPCVLGLQSFSSGRHYWEVAVGEKAEWGLGVCQDSAPRK 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578811016 402 GPARLSPAAGYWVLGLWNGCEYFVLAPHRVALTLRVPPRRLGVFLDYEAGELSFFNVSDGSHIFTFHDTFSGALCAYF 479
Cdd:cd15816   80 GETTPSPENGVWAVWLLKGNEYMVLASPSVPLLQLRRPRRVGVFLDYEAGEISFYNVTAGSHIYTFRQLFSGILRPYF 157
SPRY_PRY_TRIM60 cd15828
PRY/SPRY domain of tripartite motif-binding protein 60 (TRIM60) also known as RING finger ...
314-497 7.18e-48

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: 164.00  E-value: 7.18e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 314 RAAQKYAVDVTLDPASAHPSLEVSEDGKSVSSRGAPPGPAPGHpQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGA 393
Cdd:cd15828    3 RIIKRFQVDVTLDPETAHPQLTVSEDRKSVLYGEMKQNVCYNP-RRFYLCPAVLGSEGFHSGRQYWEVEVGDKPEWTLGV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 394 CLAAVPRAGPARLSPAAGYWVLGLWNGCEYFVLAPHRVALTLRVPPRRLGVFLDYEAGELSFFNVSDGSHIFTFHDTFSG 473
Cdd:cd15828   82 CQDCLPRNWSNQPSVQDGLWAIGRYSESNYVALGPKKIQLLPKVRPSKIGIFLDYELGEVSFYNMNDRSLLYTFSDSFTG 161
                        170       180
                 ....*....|....*....|....
gi 578811016 474 ALCAYFrprahDGGEHPDPLTICP 497
Cdd:cd15828  162 TLWPYF-----YTGTDSEPLKICT 180
SPRY_PRY_TRIM11 cd15811
PRY/SPRY domain of tripartite motif-binding protein 11 (TRIM11), also known as RING finger ...
322-496 1.61e-44

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: 154.73  E-value: 1.61e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 322 DVTLDPASAHPSLEVSEDGKSVSsRGAPPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGACLAAVPRA 401
Cdd:cd15811    1 DVTLDPDTANPELVLSEDRRSVR-RGDLRQALPDSPERFDPGPCVLGRERFTSGRHYWEVEVGDRTSWALGVCKENVNRK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 402 GPARLSPAAGYWVLGLWNgceYFVLAPHRVALTLRVPPRRLGVFLDYEAGELSFFNVSDGSHIFTFHDT-FSGALCAYFR 480
Cdd:cd15811   80 EKGELSAGNGFWILVFLG---NYYSSERRTFAPLRDPPRRVGIFLDYEAGHLSFYSATDGSLLFIFPETpFSGTLRPLFS 156
                        170
                 ....*....|....*.
gi 578811016 481 PRAHDggehPDPLTIC 496
Cdd:cd15811  157 PLSSS----PTPMTIC 168
SPRY_PRY_TRIM69 cd15818
PRY/SPRY domain in tripartite motif-binding protein 69 (TRIM69), also known as RING finger ...
323-495 1.13e-43

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: 153.04  E-value: 1.13e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 323 VTLDPASAHPSLEVSEDGKSVSsRGAPPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGACLAAVPRAG 402
Cdd:cd15818   15 ITLDPKTAHPNLILSEDLTCVW-HGDTKQMLPDNPERFDSSVAVLGSEGFTSGKHYWEVEVAKKTKWTLGVVRESINRKG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 403 PARLSPAAGYWVLGLWNGCEYFVLAPHRVALTLRVPPRRLGVFLDYEAGELSFFNVSDGSHIFTFHDTFSGALCAYFRPR 482
Cdd:cd15818   94 NCPLSPEDGFWLLRLRNQNELKALDVPSFSLTLTSNLNKVGIYLDYEGGQVSFYNANTMSHIYTFSDTFTEKIYPYFCPC 173
                        170
                 ....*....|...
gi 578811016 483 AHDGGEHPDPLTI 495
Cdd:cd15818  174 LNDSGENKEPLKI 186
SPRY_PRY_A33L cd12905
zinc-binding protein A33-like; This domain, consisting of the distinct N-terminal PRY ...
323-496 6.29e-43

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: 150.64  E-value: 6.29e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 323 VTLDPASAHPSLEVSEDGKSVSSRGAPPGPAPGHpQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGACLAAVPRAG 402
Cdd:cd12905    6 LTFDPETAHPSLILSRDLTAVTESDEMQPYPRSP-KRFLQCVNVLASQGFQSGRHYWEVWVGSKTKWDLGVASESVDRQA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 403 PARLSPAAGYWVLGLWNGCEYFVLAPHRVALTLRVPPRRLGVFLDYEAGELSFFNVSDGSHIFTFHDTFSGALCAYFRPR 482
Cdd:cd12905   85 RVKLCPENGYWTLRLRNGDEYWAGTQPWTRLRVTSRPQRIGVFLDCEERKVSFYNADDMSLLYSFHQGPRGKVFPFFSTC 164
                        170
                 ....*....|....
gi 578811016 483 AHDGGEHPDPLTIC 496
Cdd:cd12905  165 FSDDGQNAEPMRLL 178
SPRY_PRY_TRIM27 cd15814
PRY/SPRY domain in tripartite motif-containing protein 27 (TRIM27), also known as RING finger ...
320-497 6.40e-42

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: 148.30  E-value: 6.40e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 320 AVDVTLDPASAHPSLEVSEDGKSVSSrGAPPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGACLAAVP 399
Cdd:cd15814    1 SVDVTLDPDTAYPSLILSDNLRQVRY-SYLQQDLPDNPERFNLFPCVLGSPCFIAGRHYWEVEVGDKAKWTIGVCEDSVC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 400 RAGPARLSPAAGYWVLGLWNGCEYFVLAPHRVALTLRVPPRRLGVFLDYEAGELSFFNVSDGSHIFTF-HDTFSGALCAY 478
Cdd:cd15814   80 RKGGVTSAPQNGFWAVSLWYGKEYWALTSPMTALPLRTPLQRVGIFLDYDAGEVSFYNVTERCHTFTFsHATFCGPVRPY 159
                        170
                 ....*....|....*....
gi 578811016 479 FRpRAHDGGEHPDPLTICP 497
Cdd:cd15814  160 FS-LSYSGGKSAAPLIICP 177
SPRY_PRY_TRIM38 cd15815
PRY/SPRY domain of tripartite motif-binding protein 38 (TRIM38), also known as Ring finger ...
319-480 6.84e-42

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: 148.27  E-value: 6.84e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 319 YAVDVTLDPASAHPSLEVSEDGKSVSsRGAPPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGACLAAV 398
Cdd:cd15815   11 HQVSVTLDPDTAHPELTLSKDQRQVT-YGRCQENLDASPKRFTVLPCVLGCEGFTSGRHYFEVDVGEGTGWDVGVCLENV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 399 PRAGPARLSPAAGYWVLGLWNGCEYFVLAPHRVALTLRVPPRRLGVFLDYEAGELSFFNVSDGSHIFTF-HDTFSGALCA 477
Cdd:cd15815   90 QRGFGMKQEPEFGFWTIRLCEEDGYVALTSPPTPLPLREKPLVVGVFLDYEAGLVSFYNMTTGSHIFTFpKASFSDTLRP 169

                 ...
gi 578811016 478 YFR 480
Cdd:cd15815  170 YFQ 172
SPRY_PRY_TRIM35 cd12893
PRY/SPRY domain in tripartite motif-containing protein 35 (TRIM35); This PRY/SPRY domain is ...
323-497 1.96e-41

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: 146.62  E-value: 1.96e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 323 VTLDPASAHPSLEVSEDGKSVSsRGAPPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGACLAAVPRAG 402
Cdd:cd12893    2 VTLDPNTAHPWLSLSEDLTSVR-YSSEKQQLPDNPERFDPYPCVLGSEGFTSGKHSWDVEVGDNTSWMLGVAKESVQRKG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 403 PARLSPAAGYWVLGLWNGcEYFVLAPH--RVALTLRVPPRRLGVFLDYEAGELSFFNVSDGSHIFTFHDTFSGALCAYFR 480
Cdd:cd12893   81 KFTLSPESGFWTIGFSEG-KYSARTSPepRTPLRVKQKPQRIRVQLDWDRGKVSFSDPDTNTHIHTFTHTFTERVFPYFY 159
                        170
                 ....*....|....*..
gi 578811016 481 PrahdgGEHPDPLTICP 497
Cdd:cd12893  160 T-----GCKSEPLRILP 171
SPRY_PRY_TRIM60_75 cd15817
PRY/SPRY domain of tripartite motif-binding protein 60 and 75 (TRIM60 and TRIM75); This domain, ...
322-496 2.41e-41

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: 146.15  E-value: 2.41e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 322 DVTLDPASAHPSLEVSEDGKSVSSRGAPPGPAPGHpQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGACLAAVPRA 401
Cdd:cd15817    1 DLILDPETAHPNLIVSEDRKAVRYRRMKPNCPYDP-RRFTVYPAVLGSEGFDSGRHFWEVEVGGKGEWILGVCKDSLPRN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 402 GPARLSPAAGYWVLGLWNGcEYFVLAPHRVALTLRVPPRRLGVFLDYEAGELSFFNVSDGSHIFTFHDTFSGALCAYFRP 481
Cdd:cd15817   80 AQDPPSPLGGCWQIGRYMS-GYVASGPKTTQLLPVVKPSRIGIFLDYELGEVSFYNMNDRSHLYTFTDTFTGKLIPYFYV 158
                        170
                 ....*....|....*
gi 578811016 482 rahdgGEHPDPLTIC 496
Cdd:cd15817  159 -----GPDSEPLTIC 168
SPRY_PRY_TRIM5_6_22_34 cd15810
PRY/SPRY domain of tripartite motif-binding protein 5, 6, 22 and 34 (TRIM5, TRIM6, TRIM22 and ...
322-496 2.39e-39

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: 141.46  E-value: 2.39e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 322 DVTLDPASAHPSLEVSEDGKSVSSRGAPPGPAPGHpqRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGACLAAVPRA 401
Cdd:cd15810    1 DVTLNPVNISLNIVISEDQRQVRIVPPQTSGQALT--NNNYDFGVLGSQYFSSGKHYWEVDVSKKSAWILGVCSHKRSDA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 402 GP-------------ARLSPAAGYWVLGLWNGCEYFVL------APHRVALTLRVPPRRLGVFLDYEAGELSFFNVSD-G 461
Cdd:cd15810   79 MTksnanqinhqnvySRYQPQYGYWVIGLQNESEYNAFedsssfNPHVLTLSVTVPPHRVGVFLDYEAGTVSFFNVTNhG 158
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 578811016 462 SHIFTFHD-TFSGALCAYFRPRahdggEHPDPLTIC 496
Cdd:cd15810  159 SLIYKFSKcCFSTTVCPYFNPW-----NCPVPMTLC 189
SPRY_PRY_TRIM21 cd12900
PRY/SPRY domain in tripartite motif-binding protein 21 (TRIM21) also known as 52kD ...
319-498 4.15e-39

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: 140.79  E-value: 4.15e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 319 YAVDVTLDPASAHPSLEVSEDGKSVSsRGAPPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGACLAAV 398
Cdd:cd12900    1 HMVHITLDPDTANPWLILSKDRRQVR-LGDTHQNVPENEERFDNYPMVLGAQRFNSGKHYWEVDVTGKEAWDLGVCRDSV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 399 PRAGPARLSPAAGYWVLGLWNGcEYFVLAPHRVALTLRVPPRRLGVFLDYEAGELSFFNVSD-GSHIFTFHD-TFSGALC 476
Cdd:cd12900   80 RRKGQFLLSPENGFWTIWLWNK-KYEAGTSPQTTLHLQVPPCQVGIFLDYEAGVVSFYNITDhGSLIYTFSEcAFTGPLR 158
                        170       180
                 ....*....|....*....|..
gi 578811016 477 AYFRPRAHDGGEHPDPLTICPL 498
Cdd:cd12900  159 PFFNPGFNDSGGNAAPLTLCPL 180
SPRY_PRY_TRIM7_like cd12888
PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7)-like, including TRIM7, TRIM10, ...
322-467 1.40e-38

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: 138.85  E-value: 1.40e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 322 DVTLDPASAHPSLEVSEDGKSVSsRGAPPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGACLAAVPRA 401
Cdd:cd12888    1 NVTLDPDTAHPRLVLSEDRKSVR-WGDTRQDLPDNPERFDTWPCVLGCEGFTSGRHYWEVEVGDGGGWAVGVARESVRRK 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578811016 402 GPARLSPAAGYWVLGLWNGcEYFVLAPHRVALTLRVPPRRLGVFLDYEAGELSFFNVSDGSHIFTF 467
Cdd:cd12888   80 GEISFSPEEGIWAVGQWGG-QYWALTSPETPLPLSEVPRRIRVYLDYEGGQVAFFDADNEAPIFTF 144
SPRY_PRY_TRIM72 cd13742
PRY/SPRY domain in tripartite motif-binding protein 72 (TRIM72); This domain, consisting of ...
313-496 8.31e-37

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: 134.99  E-value: 8.31e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 313 WRAAQKYAVDVTLDPASAHPSLEVSEDGKSVSSRGAPPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLG 392
Cdd:cd13742    4 FRALMPALENLTFDPDTAHPYLVVSSDGKRVECADQKQAVSSDDPNRFDKANCVVSHQSFSEGEHYWEVIVGDKPRWALG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 393 ACLAAVPRAGPARLSPAAGYWVLGLWNGCEYFVLAPHRVALTLRVP--PRRLGVFLDYEAGELSFFNVSDGSHI---FTF 467
Cdd:cd13742   84 VISAEAGRKGRLHALPSNGFWLLGCKEGKVYEAHVEHKEPRALRVEgrPTRIGVYLSFSDGVLSFYDASDEDNLvqlFAF 163
                        170       180
                 ....*....|....*....|....*....
gi 578811016 468 HDTFSGALCAYFRPRAHDGGEHPDPLTIC 496
Cdd:cd13742  164 HERFPGPLYPFFDVCWHDKGKNSQPLKIF 192
SPRY_PRY_TRIM50_72 cd12897
PRY/SPRY domain in tripartite motif-binding (TRIM) proteins TRIM50 and TRIM72; This domain, ...
313-495 1.84e-36

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: 133.89  E-value: 1.84e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 313 WRAAQKYAVDVTLDPASAHPSLEVSEDGKSVSSrGAPPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLG 392
Cdd:cd12897    4 FRALMPALESLTFDPATAHPLLVVSSGGTVVEC-GLQKQRRASQPERFDKSTCVVASQGFSEGEHYWEVVVGDKPRWALG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 393 ACLAAVPRAGPARLSPAAGYWVLGLWNGCEYFVLAPHRVALTLRVP--PRRLGVFLDYEAGELSFFNVSDGSH---IFTF 467
Cdd:cd12897   83 VIKGTASRKGKLHASPSHGVWLIGLKEGKVYEAHGEPKEPRPLRVAgrPHRIGVYLSFEDGVLSFFDASDPDDlrtLYTF 162
                        170       180
                 ....*....|....*....|....*...
gi 578811016 468 HDTFSGALCAYFRPRAHDGGEHPDPLTI 495
Cdd:cd12897  163 QERFQGKLYPFFDVCWHDKGKNSQPLVL 190
SPRY_PRY cd12874
PRY/SPRY domain, also known as B30.2; This domain contains residues in the N-terminus that ...
323-481 6.09e-35

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: 128.96  E-value: 6.09e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 323 VTLDPASAHPSLEVSEDGKSVSSrGAPPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGACLAAVPRAG 402
Cdd:cd12874    1 LTFDPDTAHLNLILSDDLRSVRV-GDISQHPPEPPPRFFECWQVLGSQSFSSGRHYWEVDVQDDSSWYVGVTYKSLPRKG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 403 PA-RLSPAAGYWVLGlWNGCEYfvLAPHR-VALTLRV-PPRRLGVFLDYEAGELSFFNVSDG-SHIFTFHDTFSGALCAY 478
Cdd:cd12874   80 KMsNLGRNNGSWCLE-WRENEF--SAWHNnPETRLPVtPPRRLGVFLDCDGGSLSFYGVTDGvQLLYTFKAKFTEPLYPA 156

                 ...
gi 578811016 479 FRP 481
Cdd:cd12874  157 FWL 159
SPRY_PRY_TRIM5 cd15822
PRY/SPRY domain in tripartite motif-binding protein 5 (TRIM5), also known as RING finger ...
312-496 1.77e-34

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: 128.50  E-value: 1.77e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 312 EWRAAQKYAVDVTLDPaSAHPSLEVSEDGKSVSSRGAPPGPAPghpQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFL 391
Cdd:cd15822    3 ELTDVQRYWVHVTLDP-SNNKNIVISEDRRQVRYVRKQQRYNS---NGNNEDYGVLGSPSITSGKHYWEVDVSKKRAWIL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 392 GACLAAVPRAGP--------------ARLSPAAGYWVLGLWNGCEY--FV----LAPHRVALTLRVPPRRLGVFLDYEAG 451
Cdd:cd15822   79 GVCGGKYPNSTLkdfnkqgknnqkqcSNYQPKYGYWVIGLQNKSEYnaFEdsssSDPLILTLSLTVPPCRVGVFLDYEAG 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 578811016 452 ELSFFNVS-DGSHIFTFHD-TFSGALCAYFRPRahdggEHPDPLTIC 496
Cdd:cd15822  159 TVSFFNVTnHGFLIYKFSScSFSQEVFPYFNPM-----KCPVPMTLC 200
SPRY_PRY_TRIM50 cd13743
PRY/SPRY domain in tripartite motif-binding protein 50 (TRIM50); This domain, consisting of ...
325-495 3.24e-33

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: 124.91  E-value: 3.24e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 325 LDPASAHPSLEVSEDGKSVSSrGAPPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGACLAAVPRAGPA 404
Cdd:cd13743   16 LDPLTAHPMLELSKGNTVVEC-GLLAQRLPSNPERFDYSNCVLASRGFSSGKHYWEVVVGSKSKWRLGLIKGTTSRKGKL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 405 RLSPAAGYWVLGLWNGCEYFVLAPHRVALTLRVPPRRLGVFLDYEAGELSFFNVSDGSH---IFTFHDTFSGALCAYFRP 481
Cdd:cd13743   95 NKSPENGVWLIGLKEGRVYEAFANPRVPLPLSTRPQRIGVFLDYEKGELTFYNADSPDElvpIYTFQAEFQGKLYPLLDV 174
                        170
                 ....*....|....
gi 578811016 482 RAHDGGEHPDPLTI 495
Cdd:cd13743  175 CWHERGANKLPIIL 188
SPRY_PRY_TRIM62 cd13744
PRY/SPRY domain in tripartite motif-binding protein 62 (TRIM62); This domain, consisting of ...
323-495 1.00e-31

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: 120.88  E-value: 1.00e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 323 VTLDPASAHPSLEVSEDGKSVSSRGAPPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGACLAAVPRAG 402
Cdd:cd13744   14 LTLDPVTAHQRLILSDDCTIVAYGNLHPQPLQDSPKRFDVEVSVLGSEGFSGGVHYWEVVVSEKTQWMIGLAHEAVSRKG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 403 PARLSPAAGYWVLGLWNGCEYFVLAPHRVALTLRVPPRRLGVFLDYEAGELSFFNVSDGSHIFTFHDTFSGALCAYFRP- 481
Cdd:cd13744   94 SIQIQPGRGFYCIVMHDGNQYSACTEPWTRLNVKSKLEKVGVYLDYDKGLLIFYNADDMSWLYTFREKFPGKLCSYFSPg 173
                        170
                 ....*....|....
gi 578811016 482 RAHDGGEHPDPLTI 495
Cdd:cd13744  174 QSHANGKNVQPLRI 187
SPRY_PRY_TRIM34 cd15825
PRY/SPRY domain in tripartite motif-containing protein 34 (TRIM34), also known as RING finger ...
321-497 2.03e-29

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: 114.16  E-value: 2.03e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 321 VDVTLDPASAHPSLEVSEDGKSVSSRGAPPGPapghpqrfSEQTCALSLERFSAGRHYWEVHVGRRSRWFLG------AC 394
Cdd:cd15825    2 VDFTLNPVNLNLNLVLSEDQRQVTSVPIWPFK--------CYNYGILGSQYFSSGKHYWEVDVSKKTAWILGvycrkrSR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 395 LAAVPRAGP------ARLSPAAGYWVLGLWNGCEYFVLA------PHRVALTLRVPPRRLGVFLDYEAGELSFFNVSD-G 461
Cdd:cd15825   74 TFKYVRQGKnhpnvySRYRPQYGYWVIGLQNKSEYYAFEdsstsdPKVLTLSVATPPHRVGVFLDYEAGTVSFFNVTNhG 153
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 578811016 462 SHIFTFHD-TFSGALCAYFRPrahdgGEHPDPLTICP 497
Cdd:cd15825  154 SLIYKFSKcCFSQPVYPYFNP-----WNCPAPMTLCP 185
SPRY_PRY_TRIM6 cd15823
PRY/SPRY domain in tripartite motif-binding protein 6 (TRIM6), also known as RING finger ...
319-481 5.35e-29

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: 113.03  E-value: 5.35e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 319 YAVDVTLDPASAHPSLEVSEDGKSVssRGAPPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGACLAAV 398
Cdd:cd15823    1 YWVDVTLNPHTANLNLVLSKNRRQV--RFVGAKLSGPSYLEEHYDCSVLGSQHFSSGKHYWEVDVTKKTAWILGVCSHSL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 399 P-----------RAGPARLSPAAGYWVLGLWNGCEY--FVLAPHRVALTLRVPPRRLGVFLDYEAGELSFFNVSD-GSHI 464
Cdd:cd15823   79 GptfsfnqyaqnHNAYSRYQPQSGYWVIGLQHNHEYraYEDSSTSLLLSMTVPPRRVGVFLDYEAGTVSFYNVTNhGFPI 158
                        170
                 ....*....|....*...
gi 578811016 465 FTFHD-TFSGALCAYFRP 481
Cdd:cd15823  159 YTFSKyYFPTTLCPYFNP 176
SPRY_PRY_TRIM22 cd15824
PRY/SPRY domain in tripartite motif-containing protein 22 (TRIM22), also known as RING finger ...
319-497 1.22e-28

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: 112.63  E-value: 1.22e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 319 YAVDVTLDPASAHPSLEVSEDGKSVssRGAPPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGAC--LA 396
Cdd:cd15824    1 YWVDVMLNPVNAVSNVVVSADQRQV--TVVHICMFRNSNPCDFSAFDVLGCQYFSSGKYYWEVDVSGKIAWILGVYskRN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 397 AVPRAGP---------------ARLSPAAGYWVLGLWNGCEYFVLA------PHRVALTLRVPPRRLGVFLDYEAGELSF 455
Cdd:cd15824   79 NLNKRKSsgfafdpnvnhpnvySRYRPQNGYWVIGLQNESEYNAFEdssssdPKVLTLSMAVPPHRVGVFLDYEAGTVSF 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 578811016 456 FNVSD-GSHIFTFHDT-FSGALCAYFRPrahdgGEHPDPLTICP 497
Cdd:cd15824  159 FNVTNhGSLIYKFSKCcFSQPVYPYFNP-----WNCPAPMTLCP 197
SPRY_PRY_C-II cd13734
PRY/SPRY domain in tripartite motif-containing proteins 1, 9, 18, 36, 46, 67,76 (TRIM1, TRIM9, ...
324-479 5.23e-28

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: 109.68  E-value: 5.23e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 324 TLDPASAHPSLEVSEDGKSVSSRG-APPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHVGRrSRWF-LGACLAAVPRA 401
Cdd:cd13734    2 KLDPKTAHRKLRLSNDNLTVEYDPeGSKDQAAVLPRRFTGSPAVLGDVAISSGRHYWEVSVSR-STSYrVGVAYKSAPRD 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578811016 402 GpaRLSPAAGYWVLGLWNGCEYFVLAPHRVALTLRVPPRRLGVFLDYEAGELSFFNVSDGSHIFTFHDTFSGALCAYF 479
Cdd:cd13734   81 E--DLGKNSTSWCLSRDNNRYTARHDGKVVDLRVTGHPARIGVLLDYDNGTLSFYDAESKQHLYTFHVDFEGPVCPAF 156
SPRY_PRY_TRIM17 cd15812
PRY/SPRY domain of tripartite motif-binding protein 17 (TRIM17), also known as testis RING ...
322-479 5.65e-28

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: 109.98  E-value: 5.65e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 322 DVTLDPASAHPSLEVSEdGKSVSSRGAPPGPAPGHPQRFSEQTCALSLERFSAGRHYWEV--HVGRRSRWFLGACLAAVP 399
Cdd:cd15812    1 DVVPDPSTAYPYLLLYE-SRQRRYLSTPPDGTPCSKDRFLAYPCAVGQETFSSGRHYWEVgmNLTGDALWALGVCRDNVS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 400 RAGPARLSPAAGYWVLGLWNGCEYFVLAPHRVALTLRVPPRRLGVFLDYEAGELSFFNVSDGSHIFTF-HDTFSGALCAY 478
Cdd:cd15812   80 RKDRVPKSPENGFWVVQLSKGKKYLSAMSALTPVTLTEPPSHMGIFLDFEAGEVSFYSVNDGSHLHTYsQAAFPGPLQPF 159

                 .
gi 578811016 479 F 479
Cdd:cd15812  160 F 160
SPRY_PRY_C-I_2 cd12891
PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM14-like, ...
323-480 7.23e-26

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: 103.87  E-value: 7.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 323 VTLDPASAHPSLEVSEDGKSVSSRGAPPGPAPGHpQRF-SEQTcaLSLERFSAGRHYWEVHVGRRSRWFLGACLAAVPRA 401
Cdd:cd12891    1 LTLDPNTAHNNLALSGDLKTVTCSSENQHYPDSP-ERFtHSQV--LSTQSFSSGRHYWEVEVSESGGWSVGVAYPSIERK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 402 GP-ARLSPAAGYWVLgLWNGCEYFVLApHRVALTLR-VPPRRLGVFLDYEAGELSFFNVSDG-SHIFTFHDTFSGALCAY 478
Cdd:cd12891   78 GDeSRIGRNDKSWCL-EWQDKSFSAWH-NNEETPLPsVSSRRLGVYLDYEAGRLSFYELSDPiRHLHTFTATFTEPLHPA 155

                 ..
gi 578811016 479 FR 480
Cdd:cd12891  156 FW 157
SPRY_PRY_TRIM41 cd13741
PRY/SPRY domain in tripartite motif-binding protein 41 (TRIM41); This domain, consisting of ...
322-480 1.52e-25

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: 104.07  E-value: 1.52e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 322 DVTLDPASAHPSLEVSEDGKSVSsRGAPPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGACLAAVPR- 400
Cdd:cd13741    1 DLTLDPDTAHPALLLSPDRRGVR-LAERRQEVPEHPKRFSADCCVLGAQGFRSGRHYWEVEVGGRRGWAVGAARESTHHk 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 401 --AGPARLSPAAGY-------------------------WVLGLwNGCEYFVL-APHRVALTLRVPPRRLGVFLDYEAGE 452
Cdd:cd13741   80 ekVGSGGSSVSSGDasssrhhhrrrrlhlpqqpllqrevWCVGT-NGKRYQAQsSTEQTLLSPSEKPRRFGVYLDYEAGR 158
                        170       180
                 ....*....|....*....|....*....
gi 578811016 453 LSFFNVSDGSHIFTFHDTFSGA-LCAYFR 480
Cdd:cd13741  159 LGFYNAETLAHVHTFSAAFLGErVFPFFR 187
SPRY_PRY_TRIM14 cd13738
PRY/SPRY domain of tripartite motif-binding protein 14 (TRIM14); This is a TRIM14 domain ...
324-480 1.53e-23

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: 97.55  E-value: 1.53e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 324 TLDPASAHPSLEVSEDGKSVSsRGAPPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHVGRRSR-WFLGACLAAVPRAG 402
Cdd:cd13738    2 TLEPDTLHPRLRLSDDRLTVS-CGWLGTLGLCPPQRFDKLWQVLSRDSFFSGRHYWEVDLQEAGAgWWVGAAYPSIGRKG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 403 P---ARLSPAAGYWVLGLWNgCEYFVLAP-HRVALTLRVPPRRLGVFLDYEAGELSFFNVSDG-SHIFTFHDTFSGALCA 477
Cdd:cd13738   81 DseaARLGWNRQSWCLKRYD-LEYWAFHDgQRSRLRPEDDPDRLGVFLDYEAGILSFYDVTGGmTHLHTFRATFQEPLYP 159

                 ...
gi 578811016 478 YFR 480
Cdd:cd13738  160 ALR 162
SPRY_PRY_TRIM7 cd13740
PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7); This domain, consisting of the ...
322-471 8.36e-23

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: 95.41  E-value: 8.36e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 322 DVTLDPASAHPSLEVSEDGKSVSSrGAPPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGACLAAVPRA 401
Cdd:cd13740    1 ELTLDPDSANPRLILSLDLKSVRL-GERAQDLPNHPCRFDTNTRVLASCGFSSGRHHWEVEVGSKDGWAFGVARESVRRK 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 402 GPARLSPAAGYWVLGLWNGCEYFVLAPHRVALTLRvPPRRLGVFLDYEAGELSFFNVSDGSHIFTFHDTF 471
Cdd:cd13740   80 GLTPFTPEEGVWALQLNGGQYWAVTSPERTPLSCG-HLSRVRVALDLEVGAVSFYAAEDMRHIYTFRVNF 148
SPRY_PRY_TRIM15 cd15826
PRY/SPRY domain in tripartite motif-binding protein 15 (TRIM15); This domain, consisting of ...
323-479 2.94e-22

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: 93.78  E-value: 2.94e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 323 VTLDPASAHPSLEVSEDGKSVSsRGAPPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHVGRRSrwfLGACLA-----A 397
Cdd:cd15826    2 VTLDPQTASGSLVLSEDRKSVR-YTRQKQNLPDSPLRFDGLPAVLGSPGFSSGRHRWQVEVQLGD---GGGCTVgvageS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 398 VPRAGPARLSPAAGYWVLGLWNGCEYFVLAPHrVALTLRVPPRRLGVFLDYEAGELSFFNVSDGSHIFTFHDTFSGALCA 477
Cdd:cd15826   78 VRRKGEMGLSAEDGVWAVILSHQQCWASTSPG-TDLPLSEIPRRVGVALDYEAGTVTLTNAETQEPIFTFTASFSGKVFP 156

                 ..
gi 578811016 478 YF 479
Cdd:cd15826  157 FF 158
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
375-498 5.01e-22

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: 91.59  E-value: 5.01e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016   375 GRHYWEVHVGRRSRWFLGACLAAVPRAGPARLSPAAGYWVLGLWNGCEYFVLAPHRVALTLRVPPRRLGVFLDYEAGELS 454
Cdd:smart00449   2 GRHYFEVEIGDGGHWRVGVATKSVPRGYFALLGEDKGSWGYDGDGGKKYHNSTGPEYGLPLQEPGDVIGCFLDLEAGTIS 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 578811016   455 FFNVSDGSHIFTFHD-TFSGALCAYFRPRAHDGGehpdPLTICPL 498
Cdd:smart00449  82 FYKNGKYLHGLAFFDvKFSGPLYPAFSLGSGNSV----RLNFGPL 122
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
376-479 7.76e-22

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: 90.87  E-value: 7.76e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016  376 RHYWEVHVGRRSR--WFLGACLAAVPRAGPARLSPAAGYWVLGLWNGCEYFVLAPHRVALTLRVPPRRLGVFLDYEAGEL 453
Cdd:pfam00622   1 RHYFEVEIFGQDGggWRVGWATKSVPRKGERFLGDESGSWGYDGWTGKKYWASTSPLTGLPLFEPGDVIGCFLDYEAGTI 80
                          90       100
                  ....*....|....*....|....*..
gi 578811016  454 SFFNVSdGSHIFTFHD-TFSGALCAYF 479
Cdd:pfam00622  81 SFTKNG-KSLGYAFRDvPFAGPLFPAV 106
SPRY_PRY_SNTX cd16040
Stonustoxin subunit alpha or SNTX subunit alpha; This domain, consisting of the distinct ...
318-480 3.56e-18

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: 82.15  E-value: 3.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 318 KYAVDVTLDPASAHPSLEVSEDGKSVSsRGAPPGPAPGHPQRFSEQTCALSLERFSaGRHYWEVHVgRRSRWFLGACLAA 397
Cdd:cd16040    6 KYACQLTLDPNTAHRNLSLSEGNRKVT-RVKEEQPYPDHPERFDYWPQVLCREGLS-GRCYWEVEW-SGGGVDIAVAYKG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 398 VPRAGPARLSpAAGY----WVLG-------LW-NGCEYFVLAPhrvaltlRVPPRRLGVFLDYEAGELSFFNVSDG-SHI 464
Cdd:cd16040   83 ISRKGDGDDS-RFGYndksWSLEcspsgysFWhNNKKTEISVP-------SSSSSRVGVYLDHSAGTLSFYSVSDTmTLL 154
                        170
                 ....*....|....*.
gi 578811016 465 FTFHDTFSGALCAYFR 480
Cdd:cd16040  155 HTVQTTFTEPLYPGFG 170
SPRY_PRY_TRIM10 cd15827
PRY/SPRY domain of tripartite motif-binding protein 10 (TRIM10) also known as hematopoietic ...
323-479 5.77e-18

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: 81.42  E-value: 5.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 323 VTLDPASAHPSLEVSEDGKSVSSrGAPPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHV--GRRSRWFLGACLAAVPR 400
Cdd:cd15827    4 ISLDPQTSHPKLLLSEDHQRARF-SYKWQNSPDNPQRFDRATCVLAHDGFTGGRHTWVVSVdlAHGGSCTVGVVSEDVRR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 401 AGPARLSPAAGYWVLGLWNGceyFVLA----PHRvaLTLRVPPRRLGVFLDYEAGELSFFNVSDGSHIFTFHDTFSGALC 476
Cdd:cd15827   83 KGELRLRPEEGVWAVRLAWG---FVSAlgsfPTR--LALEEQPRQVRVSLDYEVGWVTFVNAVTQEPIYTFTASFTQKVF 157

                 ...
gi 578811016 477 AYF 479
Cdd:cd15827  158 PFF 160
SPRY_PRY_TRIM4 cd15809
PRY/SPRY domain in tripartite motif-binding protein 4 (TRIM4), also known as RING finger ...
319-479 4.99e-17

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: 79.49  E-value: 4.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 319 YAVDVTLDPASAHPSLEVSEDGK------SVSSRGAPPGP------------APGHPQRFSEQTCALSLERFSAGRHYWE 380
Cdd:cd15809    1 FQVAVNLAEDTAHPKLVFSQEGRyvkngaSASSWPLFSTAwsyftgwrnpqkTTQFVERFQHLPCVLGKNVFTSGKHYWE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 381 VHVGRRSRWFLGACLAAVPR-AGPARLSPAAGYWVLGlWNGCEYFVLAPHRVALTLRVP-PRRLGVFLDYEAGELSFFNV 458
Cdd:cd15809   81 VENRDSLEIAVGVCREDVMGiTDGSEMSPHVGIWAIC-WSSAGYRPLTSSPVSPTKQEPaLHRVGVFLDHGAGEVSFYSA 159
                        170       180
                 ....*....|....*....|.
gi 578811016 459 SDGSHIFTFHDTFSGALCAYF 479
Cdd:cd15809  160 VDGVHLHTFSCPLVSRLRPFF 180
SPRY_BSPRY cd12904
SPRY domain in Ro-Ret family; This domain, named BSPRY, has been identified in the Ro-Ret ...
323-479 7.66e-16

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: 75.15  E-value: 7.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 323 VTLDPASAHPSLEVSEDGKSVS-SRGAPPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGACLAAVPRA 401
Cdd:cd12904    1 LRFDERTVSPLLSLSEDRRTLTfSPKKARQSPPDDPERFDHWPNALASLSFSSGTHAWVVDVGKSCAYKVGVCYGSLERK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 402 GP---ARLSPAAGYWVLGLWNGCEYFVLAPHRVALTLRVPPRRLGVFLDYEAGELSFFNVSDGSHIFTFHDTFSGALCAY 478
Cdd:cd12904   81 GSgneARLGYNAFSWVFSRYDGEFSFSHNGQHVPLELLKCPARVGVLLDWPSQELLFYDPDSCTVLHSHREAFAAPLLPV 160

                 .
gi 578811016 479 F 479
Cdd:cd12904  161 F 161
SPRY_PRY_TRIM18 cd12892
PRY/SPRY domain of TRIM18/MID1, also known as FXY or RNF59; This domain, consisting of the ...
325-479 6.83e-15

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: 72.74  E-value: 6.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 325 LDPASAHPSLEVSEDGKSVSsRGAPPGPAPGHPQRFSEQ-TCALSLERF-SAGRHYWEVHVGRRSRWFLGACLAAVPRAg 402
Cdd:cd12892    4 LDPKSAHRKLKVSHDNLTVE-RDETSSKKSHTPERFTSQgSYGVAGNVFiDSGRHYWEVVISGSTWYAIGIAYKSAPKH- 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578811016 403 pARLSPAAGYWVLGLWNGCeyFVLAPHRVALTLRVPP--RRLGVFLDYEAGELSFFNVSDGSHIFTFHDTFSGALCAYF 479
Cdd:cd12892   82 -EWIGKNSASWVLCRCNNN--WVVRHNSKEIPIEPSPhlRRVGILLDYDNGSLSFYDALNSIHLYTFDIAFAQPVCPTF 157
SPRY_PRY_TRIM76_like cd12899
PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76)-like; This domain is ...
325-471 1.80e-14

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: 71.35  E-value: 1.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 325 LDPASAHPSLEVSEDGKSV--SSRGAPPGPAPGHPQRFSEQTCAL-SLERFSaGRHYWEVHVGRRSRWFLGACLAAVPRA 401
Cdd:cd12899    4 LNEDTAHPLLSISEDGFTVvyGEEELPARDLSFSDNSFTRCVAVMgSLIPVR-GKHYWEVEVDEQTEYRVGVAFEDTQRN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 402 GpaRLSPAAGYWvlglwngCEYFVLAPHRVA-----------LTLRVPPRRLGVFLDYEAGELSFFNVSDGSHIFTFHDT 470
Cdd:cd12899   83 G--YLGANNTSW-------CMRHIITPSRHKyeflhngwtpdIRITVPPKKIGILLDYDSGRLSFFNVDLAQHLYTFSCQ 153

                 .
gi 578811016 471 F 471
Cdd:cd12899  154 F 154
SPRY_PRY_TRIM1 cd13739
PRY/SPRY domain of tripartite motif-binding protein 1 (TRIM1) or MID2; This domain, consisting ...
325-479 3.70e-14

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: 70.43  E-value: 3.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 325 LDPASAHPSLEVSEDGKSVSsRGAPPGPAPGHPQRFSEQTC--ALSLERFSAGRHYWEVHVGRRSRWFLGACLAAVPRAg 402
Cdd:cd13739    3 LDPKMAHKKLKISNDGLQME-KDESSLKKSHTPERFSGTGCygAAGNIFIDSGCHYWEVVVGSSTWYAIGIAYKSAPKN- 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578811016 403 pARLSPAAGYWVLGLWNgcEYFVLAPHRVALTLRVPP--RRLGVFLDYEAGELSFFNVSDGSHIFTFHDTFSGALCAYF 479
Cdd:cd13739   81 -EWIGKNSSSWVFSRCN--NNFVVRHNNKEMLVDVPPqlKRLGVLLDYDNNMLSFYDPANSLHLHTFEVSFILPVCPTF 156
IgV_B7-H4 cd20984
Immunoglobulin Variable (IgV) domain of B7-H4; The members here are composed of the ...
48-150 1.57e-13

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: 66.85  E-value: 1.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016  48 LALVGEEVEFPCHLWPQLDAQQMEIRWFRSQTFNVVHLYQEQQELPGRQMPAFRNRTKLVKDDIAYGSVVLQLHSIIPSD 127
Cdd:cd20984    8 AGNIGEDGILSCTFTPDIKLSDIVIQWLKEGDSGLVHEFKEGKDELSRQSPMFRGRTSLFADQVHVGNASLRLKNVQLTD 87
                         90       100
                 ....*....|....*....|...
gi 578811016 128 KGTYGCRFHSDNFSGEALWELEV 150
Cdd:cd20984   88 AGTYLCIISNSKGTGNANMEYKT 110
SPRY_PRY_TRIM16 cd12890
PRY/SPRY domain in tripartite motif-containing protein 16 (TRIM16); This domain, consisting of ...
318-460 4.91e-13

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: 67.49  E-value: 4.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 318 KYAVDVTLDPASAHPSLEVSEDGKSVSSRGAPPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHVgRRSRWFLGACLAA 397
Cdd:cd12890    6 KYAYPLTFDPDTAHRYLRLTEDNRKVTNTTPWEHPYPDHPERFEHWRQVLSQQSLYLGRYYFEVEI-SGEGTYVGLTYKS 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578811016 398 VPRAGPARLSPAAGY---WVLGlWNGCEYfvLAPHR-VALTLRVPP-RRLGVFLDYEAGELSFFNVSD 460
Cdd:cd12890   85 IDRKGSESNSCISGNnfsWCLQ-WNGKEF--SAWHSdVETPLKKGPfTRLGIYLDYPGGTLSFYGVED 149
SPRY_PRY_SPRYD4 cd12903
PRY/SPRY domain containing protein 4 (SPRYD4); This domain, consisting of the distinct ...
325-479 2.12e-12

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: 65.55  E-value: 2.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 325 LDPASAHPSLEVSEDGKSVSSRG--APPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGACLAAVPR-- 400
Cdd:cd12903    3 LDERTAHSSLDLFKKDTGVIYRMlgVDPTKVPQNPERFRDWAVVLGDTPVTSGRHYWEVTVKRSQEFRIGVADVDMSRde 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 401 -AGPARLSpaagyWVLGLWNGCEYFVLAPHRVALTLRVPPRRLGVFLDYEAGELSFFNVSDGSHIFTFHDTFSGALCAYF 479
Cdd:cd12903   83 cIGTNESS-----WVFAYAQRKWYAMVANETVPVPLVGKPDRVGLLLDYEAGKLSLVDVEKNSVVHTMSAEFRGPVVPAF 157
SPRY_PRY_TRIM65 cd12896
PRY/SPRY domain in tripartite motif-containing domain 65 (TRIM65); This domain, consisting of ...
317-475 7.49e-12

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: 64.01  E-value: 7.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 317 QKYAVDVTLDPASAHPSLEVSEDGKSVSSRGAPPGPAPGHPQRFS--EQTCAlslERFSAGRHYWEVHVGRRSRwFLGAC 394
Cdd:cd12896    6 WKDYRNLTFDPRTANKYLELSRQNRRAKHGRSAARGVPASPGSFElwQVQCT---QSFQHGHHYWEVEVSSHSV-TLGVT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 395 LAAVPRAGPAR------LSPaaGYWVLGLWNGCeyfVLAPHR-VALTLRVPP-RRLGVFLDYEAGELSFFNVSDG-SHIF 465
Cdd:cd12896   82 YPGLPRHKQGGhkdnigRNP--CSWGLQIQEDS---LQAWHNgRAQKLQGVSyRLLGVDLDLEAGTLTFYGLEPGtQRLH 156
                        170
                 ....*....|
gi 578811016 466 TFHDTFSGAL 475
Cdd:cd12896  157 TFHAIFTQPL 166
SPRY_PRY_TRIM25 cd13736
PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25); This domain, consisting of ...
323-479 1.34e-11

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: 62.98  E-value: 1.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 323 VTLDPASAHPSLEVSEDgKSVSSRGAPPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGACLAAVPRAG 402
Cdd:cd13736    1 VIFDYNTAHNKVSLSEN-YTKASVSDDPQNYREHPQRFTYCSQVLGLHCFKQGIHYWEVELQKNNFCGVGICYGSMDRQG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 403 P-ARLSPAAGYWVLglwngcEYF---VLAPHR-VALTLRVP-PRRLGVFLDYEAGELSFFNVSDGSHIF-TFHDTFSGAL 475
Cdd:cd13736   80 PeSRLGRNSESWCV------EWFnvkISAWHNnVEKTLPSTkATRVGVLLNCDHGFVIFFAVQDKVHLMyKFKVDFTEAL 153

                 ....
gi 578811016 476 CAYF 479
Cdd:cd13736  154 YPAF 157
SPRY_PRY_TRIM76 cd12898
PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76), also called ...
329-472 1.72e-11

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: 62.64  E-value: 1.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 329 SAHPSLEVSEDGKSVSSrgapPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHVGRRSRWFLGACLAAVPRAGParLSP 408
Cdd:cd12898   10 TAHPALHISSDRGTVIY----FHERRRKMSSLTECPSVLGEELPSCGQYYWETTVTRCPAYRLGICSSSASQAGA--LGE 83
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578811016 409 AAGYWVL---GLWNGCEYFVLApHRVALTLRVP--PRRLGVFLDYEAGELSFFNVSDGSHIFTFHDTFS 472
Cdd:cd12898   84 GSTSWCLhcvPTSEPCRYTLLH-SGIVSDVFVTerPARVGTLLDYNNGRLIFINAESGQLLGIFRHRFA 151
IgV_B7-H3 cd20934
Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint ...
43-151 1.86e-10

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: 58.38  E-value: 1.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016  43 PEYPILALVGEEVEFPCHLWPQ--LDAQQMEIRWFRSQTFNVVHLYQEQQELPGRQMPAFRNRTKLVKDDIAYGSVVLQL 120
Cdd:cd20934    3 PEDPVVALVGTDATLRCSFSPEpgFSLAQLSVFWQLTDTKQLVHSFTESQDQGRDQGSAYANRTALFPDLLAQGNASLRL 82
                         90       100       110
                 ....*....|....*....|....*....|.
gi 578811016 121 HSIIPSDKGTYGCRFHSDNFSGEALwELEVA 151
Cdd:cd20934   83 QRVRVADEGSYTCFVSVQDFGSAAV-SLQVA 112
SPRY_PRY_RNF135 cd12902
PRY/SPRY domain in RING finger protein RNF135; This domain, consisting of the distinct ...
324-460 1.91e-10

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: 59.84  E-value: 1.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 324 TLDPASAHPSLEVSEDGKSVSSRGAPPGPAPGHpQRFSEQTCALSlERFSAGRHYWEVHVGRRSRWFLGACLAAVPR--- 400
Cdd:cd12902    2 TFDLRSLSCSLEVSEDSRKVTVSHGPQAYAWSP-DRFSISQVLCS-QAFSSGQHYWEVDTRQCSHWAVGVASWEMSRdqm 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578811016 401 AGPARLS---PAAGYWVLGLWNGCEYFVLAPHRvaltlrvpPRRLGVFLDYEAGELSFFNVSD 460
Cdd:cd12902   80 LGRTMDSwciEWKGTGQLSAWHMNKETVLGSDK--------PRVVGIWLDLEEGKLAFYSVAN 134
IgV_HHLA2 cd16091
Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are ...
44-133 6.04e-10

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: 56.63  E-value: 6.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016  44 EYPILALVGEEVEFPCHLWPQLDAQqmeIRWFRSQTFNVVHLYQEQQELPGRQMPAFRNRTKLVKDDIAYGSVVLQLHSI 123
Cdd:cd16091    4 EVIVVCLLSEDCILPCSFTPGSEVV---IHWYKQDSDIKVHSYYYGKDQLESQDQRYRNRTSLFKDQISNGNASLLLRRV 80
                         90
                 ....*....|
gi 578811016 124 IPSDKGTYGC 133
Cdd:cd16091   81 QLQDEGRYKC 90
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
43-143 1.23e-09

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: 55.54  E-value: 1.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016   43 PEYPILALVGEEVEFPCHLWPQLDAQQMEIRWFR----SQTFNVVHLYQeqqelPGRQMPAFRNRTKLvKDDIAYGSVVL 118
Cdd:pfam07686   2 TPREVTVALGGSVTLPCTYSSSMSEASTSVYWYRqppgKGPTFLIAYYS-----NGSEEGVKKGRFSG-RGDPSNGDGSL 75
                          90       100
                  ....*....|....*....|....*
gi 578811016  119 QLHSIIPSDKGTYGCRFHSDNFSGE 143
Cdd:pfam07686  76 TIQNLTLSDSGTYTCAVIPSGEGVF 100
PRY smart00589
associated with SPRY domains;
320-372 2.49e-09

associated with SPRY domains;


Pssm-ID: 128857  Cd Length: 52  Bit Score: 52.96  E-value: 2.49e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 578811016   320 AVDVTLDPASAHPSLEVSEDGKSVSSRgAPPGPAPGHPQRFSEQTCALSLERF 372
Cdd:smart00589   1 AVDVTLDPDTAHPYLLLSEDRRSVRYG-DLKQSLPDNPERFDSYPCVLGSQGF 52
PRY pfam13765
SPRY-associated domain; PRY is a 50-60 amino acids domain associated with SPRY domains, ...
323-372 4.37e-08

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: 49.40  E-value: 4.37e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 578811016  323 VTLDPASAHPSLEVSEDGKSVsSRGAPPGPAPGHPQRFSEQTCALSLERF 372
Cdd:pfam13765   1 VTLDPNTAHPSLVLSEDLKSV-RYGDERQNVPDNPERFDSWPCVLGSEGF 49
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
46-150 7.11e-08

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: 49.81  E-value: 7.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016    46 PILALVGEEVEFPCHLWPQLDAQqmeIRWFRsqtfnvvhlyqeqqelPGRQMPAFRNRTKLVKDDiayGSVVLQLHSIIP 125
Cdd:smart00410   3 SVTVKEGESVTLSCEASGSPPPE---VTWYK----------------QGGKLLAESGRFSVSRSG---STSTLTISNVTP 60
                           90       100
                   ....*....|....*....|....*
gi 578811016   126 SDKGTYGCRFHSDNFSGEALWELEV 150
Cdd:smart00410  61 EDSGTYTCAATNSSGSASSGTTLTV 85
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
375-488 1.46e-07

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: 50.12  E-value: 1.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 375 GRHYWEVHV--GRRSRWFLGACLAAVPRAGPARLSPAAGYWVLGlwngCEYFVLAPHRVALTLRVPPR---RLGVFLDYE 449
Cdd:cd11709    1 GKWYWEVRVdsGNGGLIQVGWATKSFSLDGEGGVGDDEESWGYD----GSRLRKGHGGSSGPGGRPWKsgdVVGCLLDLD 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 578811016 450 AGELSFF-NVSDGSHIFTFHDTFSGALCAYFRPRAHDGGE 488
Cdd:cd11709   77 EGTLSFSlNGKDLGVAFTNLFLKGGGLYPAVSLGSGQGVT 116
SPRY_PRY_FSD1 cd12901
Fibronectin type III and SPRY containing 1 (FSD1) domain includes PRY at the N-terminus; This ...
374-472 1.78e-05

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: 45.97  E-value: 1.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 374 AGRHYWEVHVGRRSRWF-LGACLAAVPRAGpaRLSPAAGYWVLGLWNGCEYFVLAPH-RVALTLRVP-PRRLGVFLDYEA 450
Cdd:cd12901   84 GGQHYWEVRAQKDSKAFsVGVAYRSLGKFD--QLGKTNASWCLHVNNWLQNSFAAKHnNKAKTLDVPvPDRIGVYCDFDE 161
                         90       100
                 ....*....|....*....|..
gi 578811016 451 GELSFFNVSDGSHIFTFHDTFS 472
Cdd:cd12901  162 GQLSFYNARTKQLLHTFKMKFT 183
SPRY_PRY_TRIM67_9 cd12889
PRY/SPRY domain in tripartite motif-containing proteins, TRIM9 and TRIM67; This domain, ...
324-386 9.26e-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: 43.00  E-value: 9.26e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578811016 324 TLDPASAHPSLEVSEDGKSVSSRGappgpapghpqrfSEQTCALSLERFSAGRHYWEVHVGRR 386
Cdd:cd12889   11 TFDPSTSHPDIILSNDNMTVTCNS-------------YEDRVVLGSVGFSRGVHYWEVTIDRY 60
SPRY_PRY_TRIM25-like cd13737
PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25)-like; This domain, ...
325-475 7.54e-04

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: 40.63  E-value: 7.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 325 LDPASAHPSLEVSEDGKSVSSRGAPPGPAPGHPQRFSEQTCALSLERFSAGRHYWEVHVGrrSRWFlgaCLAAVPRAGPa 404
Cdd:cd13737    3 FDPNTASEELFLFKETHSVLNMGILLESFFGPCQGFNHWPQVLCTRSLCEGCHYWEAEVS--NSWV---CLGVTYSYSH- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016 405 RLSPAAGYWVLGL--------WNGCEYFVLAPHRVALTLRVPPRRLGVFLDYEAGELSFFNVSDG-SHIFTFHDTFSGAL 475
Cdd:cd13737   77 PTGKSCIFYLIGRnpyswcleWDSLKFSVWHNNIQTVVHGSYYKTIGVLLDYAAGSLTFYGVANTmNLIYRFLTTFTEPL 156
IGv smart00406
Immunoglobulin V-Type;
55-133 3.14e-03

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 36.59  E-value: 3.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811016    55 VEFPCHLWpQLDAQQMEIRWFRSQTFNVV-HLYQEQQELPGRQMPAFRNRTKLVKDDiAYGSVVLQLHSIIPSDKGTYGC 133
Cdd:smart00406   2 VTLSCKFS-GSTFSSYYVSWVRQPPGKGLeWLGYIGSNGSSYYQESYKGRFTISKDT-SKNDVSLTISNLRVEDTGTYYC 79
 
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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