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Conserved domains on  [gi|1370472444|ref|XP_024306768|]
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E3 ubiquitin-protein ligase RNF135 isoform X2 [Homo sapiens]

Protein Classification

SPRY domain-containing protein; PRY/SPRY domain-containing protein( domain architecture ID 10191516)

SPRY (SPla and the RYanodine receptor) domain-containing protein similar to yeast SSH4 (suppressor of SHR3 null mutation protein 4); the SPRY domain is a protein interaction module found in proteins implicated in important biological pathways, including those that regulate innate and adaptive immunity| 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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPRY_PRY_RNF135 cd12902
PRY/SPRY domain in RING finger protein RNF135; This domain, consisting of the distinct ...
 80-247 3.80e-115

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: 326.78  E-value: 3.80e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  80 PTFNLKSLSCSLEVSKDSRTVTVSHRPQPYRWSCERFSTSQVLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSRDQVL 159
Cdd:cd12902     1 PTFDLRSLSCSLEVSEDSRKVTVSHGPQAYAWSPDRFSISQVLCSQAFSSGQHYWEVDTRQCSHWAVGVASWEMSRDQML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 160 GRTMDSCCVEWKGTSQLSAWHMVKETVLGSDRPGVVGIWLNLEEGKLAFYSVDNQEKLLYECTISASSPLYPAFWLYGLH 239
Cdd:cd12902    81 GRTMDSWCIEWKGTGQLSAWHMNKETVLGSDKPRVVGIWLDLEEGKLAFYSVANQERLLHECEVSASSPLHPAFWLYGLE 160


                  ....*...
gi 1370472444 240 PGNYLIIK 247
Cdd:cd12902   161 PGNSLIIK 168
 
Name Accession Description Interval E-value
SPRY_PRY_RNF135 cd12902
PRY/SPRY domain in RING finger protein RNF135; This domain, consisting of the distinct ...
 80-247 3.80e-115

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: 326.78  E-value: 3.80e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  80 PTFNLKSLSCSLEVSKDSRTVTVSHRPQPYRWSCERFSTSQVLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSRDQVL 159
Cdd:cd12902     1 PTFDLRSLSCSLEVSEDSRKVTVSHGPQAYAWSPDRFSISQVLCSQAFSSGQHYWEVDTRQCSHWAVGVASWEMSRDQML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 160 GRTMDSCCVEWKGTSQLSAWHMVKETVLGSDRPGVVGIWLNLEEGKLAFYSVDNQEKLLYECTISASSPLYPAFWLYGLH 239
Cdd:cd12902    81 GRTMDSWCIEWKGTGQLSAWHMNKETVLGSDKPRVVGIWLDLEEGKLAFYSVANQERLLHECEVSASSPLHPAFWLYGLE 160


                  ....*...
gi 1370472444 240 PGNYLIIK 247
Cdd:cd12902   161 PGNSLIIK 168
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 129-237 1.87e-18

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: 78.49  E-value: 1.87e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  129 SGKHYWEVDTRNCSHWAVGVASWEMSRDQV--LGRTMDSCCVEWKGTSQLSAWHmVKETVLGSDRPG-VVGIWLNLEEGK 205
Cdd:smart00449   1 SGRHYFEVEIGDGGHWRVGVATKSVPRGYFalLGEDKGSWGYDGDGGKKYHNST-GPEYGLPLQEPGdVIGCFLDLEAGT 79

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1370472444  206 LAFYSVDNQEKLLYECTISASSPLYPAFWLYG 237
Cdd:smart00449  80 ISFYKNGKYLHGLAFFDVKFSGPLYPAFSLGS 111
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 131-236 1.47e-11

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: 60.05  E-value: 1.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 131 KHYWEV--DTRNCSHWAVGVASWEMSR--DQVLGRTMDSCCVEwkGTSQLSAWH-MVKETVLGSDRPG-VVGIWLNLEEG 204
Cdd:pfam00622   1 RHYFEVeiFGQDGGGWRVGWATKSVPRkgERFLGDESGSWGYD--GWTGKKYWAsTSPLTGLPLFEPGdVIGCFLDYEAG 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1370472444 205 KLAFYsvDNQEKLLYECTI-SASSPLYPAFWLY 236
Cdd:pfam00622  79 TISFT--KNGKSLGYAFRDvPFAGPLFPAVSLG 109
 
Name Accession Description Interval E-value
SPRY_PRY_RNF135 cd12902
PRY/SPRY domain in RING finger protein RNF135; This domain, consisting of the distinct ...
 80-247 3.80e-115

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: 326.78  E-value: 3.80e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  80 PTFNLKSLSCSLEVSKDSRTVTVSHRPQPYRWSCERFSTSQVLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSRDQVL 159
Cdd:cd12902     1 PTFDLRSLSCSLEVSEDSRKVTVSHGPQAYAWSPDRFSISQVLCSQAFSSGQHYWEVDTRQCSHWAVGVASWEMSRDQML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 160 GRTMDSCCVEWKGTSQLSAWHMVKETVLGSDRPGVVGIWLNLEEGKLAFYSVDNQEKLLYECTISASSPLYPAFWLYGLH 239
Cdd:cd12902    81 GRTMDSWCIEWKGTGQLSAWHMNKETVLGSDKPRVVGIWLDLEEGKLAFYSVANQERLLHECEVSASSPLHPAFWLYGLE 160


                  ....*...
gi 1370472444 240 PGNYLIIK 247
Cdd:cd12902   161 PGNSLIIK 168
SPRY_PRY_C-I_2 cd12891
PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM14-like, ...
 80-247 1.36e-57

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: 180.91  E-value: 1.36e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  80 PTFNLKSLSCSLEVSKDSRTVTVSHRPQPYRWSCERFSTSQVLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSR---D 156
Cdd:cd12891     1 LTLDPNTAHNNLALSGDLKTVTCSSENQHYPDSPERFTHSQVLSTQSFSSGRHYWEVEVSESGGWSVGVAYPSIERkgdE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 157 QVLGRTMDSCCVEWKGtSQLSAWHMVKETVLGSDRPGVVGIWLNLEEGKLAFYSVDNQEKLLYECTISASSPLYPAFWLY 236
Cdd:cd12891    81 SRIGRNDKSWCLEWQD-KSFSAWHNNEETPLPSVSSRRLGVYLDYEAGRLSFYELSDPIRHLHTFTATFTEPLHPAFWVL 159

                         170
                  ....*....|.
gi 1370472444 237 GlhpGNYLIIK 247
Cdd:cd12891   160 E---GGWIRIK 167
SPRY_PRY cd12874
PRY/SPRY domain, also known as B30.2; This domain contains residues in the N-terminus that ...
 80-247 3.61e-52

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: 167.10  E-value: 3.61e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  80 PTFNLKSLSCSLEVSKDSRTVTVSHRPQ-PYRWSCERFSTSQVLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSRDQV 158
Cdd:cd12874     1 LTFDPDTAHLNLILSDDLRSVRVGDISQhPPEPPPRFFECWQVLGSQSFSSGRHYWEVDVQDDSSWYVGVTYKSLPRKGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 159 ---LGRTMDSCCVEWKGtSQLSAWHMVKETVLGSDRPGVVGIWLNLEEGKLAFYSVDNQEKLLYECTISASSPLYPAFWL 235
Cdd:cd12874    81 msnLGRNNGSWCLEWRE-NEFSAWHNNPETRLPVTPPRRLGVFLDCDGGSLSFYGVTDGVQLLYTFKAKFTEPLYPAFWL 159

                         170
                  ....*....|..
gi 1370472444 236 YGlhpGNYLIIK 247
Cdd:cd12874   160 GE---GSTLSIC 168
SPRY_PRY_TRIM25 cd13736
PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25); This domain, consisting of ...
 81-236 1.48e-27

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: 103.81  E-value: 1.48e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  81 TFNLKSLSCSLEVSKDSRTVTVSHRPQPYRWSCERFS-TSQVLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSR---D 156
Cdd:cd13736     2 IFDYNTAHNKVSLSENYTKASVSDDPQNYREHPQRFTyCSQVLGLHCFKQGIHYWEVELQKNNFCGVGICYGSMDRqgpE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 157 QVLGRTMDSCCVEWKgTSQLSAWHMVKETVLGSDRPGVVGIWLNLEEGKLAFYSVDNQEKLLYECTISASSPLYPAFWLY 236
Cdd:cd13736    82 SRLGRNSESWCVEWF-NVKISAWHNNVEKTLPSTKATRVGVLLNCDHGFVIFFAVQDKVHLMYKFKVDFTEALYPAFWVF 160
SPRY_PRY_C-II cd13734
PRY/SPRY domain in tripartite motif-containing proteins 1, 9, 18, 36, 46, 67,76 (TRIM1, TRIM9, ...
 82-233 1.04e-23

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: 93.50  E-value: 1.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  82 FNL--KSLSCSLEVSKDSRTVTV-SHRPQPYRWSCERFST--SQVLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSRD 156
Cdd:cd13734     1 FKLdpKTAHRKLRLSNDNLTVEYdPEGSKDQAAVLPRRFTgsPAVLGDVAISSGRHYWEVSVSRSTSYRVGVAYKSAPRD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370472444 157 QVLGRTMDSCCVEWKGTSqLSAWHMVKETVLGSDR-PGVVGIWLNLEEGKLAFYSVDNQeKLLYECTISASSPLYPAF 233
Cdd:cd13734    81 EDLGKNSTSWCLSRDNNR-YTARHDGKVVDLRVTGhPARIGVLLDYDNGTLSFYDAESK-QHLYTFHVDFEGPVCPAF 156
SPRY_PRY_TRIM65 cd12896
PRY/SPRY domain in tripartite motif-containing domain 65 (TRIM65); This domain, consisting of ...
 81-235 1.33e-22

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: 90.97  E-value: 1.33e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  81 TFNLKSLSCSLEVSKDSRTVtvSHRPQPYRWSCER---FSTSQVLCSQALSSGKHYWEVdtRNCSHWA-VGVASWEMSRD 156
Cdd:cd12896    13 TFDPRTANKYLELSRQNRRA--KHGRSAARGVPASpgsFELWQVQCTQSFQHGHHYWEV--EVSSHSVtLGVTYPGLPRH 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 157 QVLGRT----MDSC----CVEwkgTSQLSAWHMVKETVLGSDRPGVVGIWLNLEEGKLAFYSVDNQEKLLYECTISASSP 228
Cdd:cd12896    89 KQGGHKdnigRNPCswglQIQ---EDSLQAWHNGRAQKLQGVSYRLLGVDLDLEAGTLTFYGLEPGTQRLHTFHAIFTQP 165


                  ....*..
gi 1370472444 229 LYPAFWL 235
Cdd:cd12896   166 LYPVFWL 172
SPRY_PRY_SNTX cd16040
Stonustoxin subunit alpha or SNTX subunit alpha; This domain, consisting of the distinct ...
 91-236 1.33e-20

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: 85.62  E-value: 1.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  91 LEVSKDSRTVTVSHRPQPYRWSCERFST-SQVLCSQALSsGKHYWEVDtRNCSHWAVGVASWEMSR-----DQVLGRTMD 164
Cdd:cd16040    22 LSLSEGNRKVTRVKEEQPYPDHPERFDYwPQVLCREGLS-GRCYWEVE-WSGGGVDIAVAYKGISRkgdgdDSRFGYNDK 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370472444 165 SCCVEWKGTSqLSAWHMVKETVL-----GSDRpgvVGIWLNLEEGKLAFYSVDNQEKLLYecTISA--SSPLYPAFWLY 236
Cdd:cd16040   100 SWSLECSPSG-YSFWHNNKKTEIsvpssSSSR---VGVYLDHSAGTLSFYSVSDTMTLLH--TVQTtfTEPLYPGFGVG 172
SPRY_PRY_C-I_1 cd13733
PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM5, TRIM6, TRIM7, ...
 90-241 5.71e-20

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: 84.07  E-value: 5.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  90 SLEVSKDSRTVTVSHRPQPYRWSCERFSTS-QVLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSRDqvlGRTMDS--- 165
Cdd:cd13733    12 NLILSEDLKSVRYGDKRQNLPDNPERFDTCvCVLGSEGFSSGRHYWEVEVGGKTDWDLGVARESVNRK---GKITLSpen 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 166 --CCVEWKGTSQLSAWHMVKETVLGSDRPGVVGIWLNLEEGKLAFYSVDNQEkLLY---ECTisaSSPLYPAFWLYGLHP 240
Cdd:cd13733    89 gyWTVGLRNGNEYKALTSPSTPLSLREKPQKVGVFLDYEEGQVSFYNVDDGS-HIYtftDCF---TEKLYPYFSPCLNDG 164


                  .
gi 1370472444 241 G 241
Cdd:cd13733   165 G 165
SPRY_PRY_A33L cd12905
zinc-binding protein A33-like; This domain, consisting of the distinct N-terminal PRY ...
 81-233 4.38e-19

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: 81.69  E-value: 4.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  81 TFNLKSLSCSLEVSKDSRTVTVSHRPQPYRWSCERFSTS-QVLCSQALSSGKHYWEVDTRNCSHWAVGVASwemsrDQVL 159
Cdd:cd12905     7 TFDPETAHPSLILSRDLTAVTESDEMQPYPRSPKRFLQCvNVLASQGFQSGRHYWEVWVGSKTKWDLGVAS-----ESVD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 160 GRTMDSCCVE--------------WKGTsqlSAWhmVKETVlgSDRPGVVGIWLNLEEGKLAFYSVDNQeKLLYECTISA 225
Cdd:cd12905    82 RQARVKLCPEngywtlrlrngdeyWAGT---QPW--TRLRV--TSRPQRIGVFLDCEERKVSFYNADDM-SLLYSFHQGP 153


                  ....*...
gi 1370472444 226 SSPLYPAF 233
Cdd:cd12905   154 RGKVFPFF 161
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 129-237 1.87e-18

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: 78.49  E-value: 1.87e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  129 SGKHYWEVDTRNCSHWAVGVASWEMSRDQV--LGRTMDSCCVEWKGTSQLSAWHmVKETVLGSDRPG-VVGIWLNLEEGK 205
Cdd:smart00449   1 SGRHYFEVEIGDGGHWRVGVATKSVPRGYFalLGEDKGSWGYDGDGGKKYHNST-GPEYGLPLQEPGdVIGCFLDLEAGT 79

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1370472444  206 LAFYSVDNQEKLLYECTISASSPLYPAFWLYG 237
Cdd:smart00449  80 ISFYKNGKYLHGLAFFDVKFSGPLYPAFSLGS 111
SPRY_PRY_TRIM75 cd15829
PRY/SPRY domain of tripartite motif-binding protein 75 (TRIM75); This domain, consisting of ...
 57-235 2.02e-17

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: 77.33  E-value: 2.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  57 CPLPDQsHPALRR-ASRFAQWAI------HPtfnlkslscSLEVSKDSRTVTVSHRPQPYRWSCERFSTSQ-VLCSQALS 128
Cdd:cd15829     1 CSFPPQ-YSALQKiIKKFRVDVTldpetaHP---------NLLVSEDKKCVTFTKKKQRVPDSPKRFTVNPvVLGFPGFH 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 129 SGKHYWEVDTRNCSHWAVGVASWEMSRDQVLGRTMDSCC--VEWKGTSqLSAWHMVKETVLGSDRPGVVGIWLNLEEGKL 206
Cdd:cd15829    71 SGRHFWEVEVGDKPEWAVGVCKDSLSTKARRPPSGQQGCwrIQLQGGD-YDAPGAVPPPLLLEVKPRGIGVFLDYELGEI 149

                         170       180
                  ....*....|....*....|....*....
gi 1370472444 207 AFYSVdNQEKLLYECTISASSPLYPAFWL 235
Cdd:cd15829   150 SFYNM-PEKSHIHTFTDTFSGPLRPYFYV 177
SPRY_PRY_TRIM16 cd12890
PRY/SPRY domain in tripartite motif-containing protein 16 (TRIM16); This domain, consisting of ...
 73-235 3.25e-17

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: 76.74  E-value: 3.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  73 FAQWAIHPTFNLKSLSCSLEVSKDSRTVTVSHRPQ-PYRWSCERF-STSQVLCSQALSSGKHYWEVDTRNCSHWaVGVAS 150
Cdd:cd12890     4 FLKYAYPLTFDPDTAHRYLRLTEDNRKVTNTTPWEhPYPDHPERFeHWRQVLSQQSLYLGRYYFEVEISGEGTY-VGLTY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 151 WEMSRDqvlGRTMDSC--------CVEWKGTSqLSAWHMVKETVLGSDRPGVVGIWLNLEEGKLAFYSVDNQEKLL---Y 219
Cdd:cd12890    83 KSIDRK---GSESNSCisgnnfswCLQWNGKE-FSAWHSDVETPLKKGPFTRLGIYLDYPGGTLSFYGVEDDGMTLlhkF 158

                         170
                  ....*....|....*.
gi 1370472444 220 ECTIsaSSPLYPAFWL 235
Cdd:cd12890   159 QCKF--TEPLYPAFWL 172
SPRY_PRY_TRIM25-like cd13737
PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25)-like; This domain, ...
 120-232 3.48e-16

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: 73.75  E-value: 3.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 120 QVLCSQALSSGKHYWEVDTRNcSHWAVGVASWEMSRDQ------VLGRTMDSCCVEWKgTSQLSAWHMVKETVLGSDRPG 193
Cdd:cd13737    43 QVLCTRSLCEGCHYWEAEVSN-SWVCLGVTYSYSHPTGkscifyLIGRNPYSWCLEWD-SLKFSVWHNNIQTVVHGSYYK 120

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1370472444 194 VVGIWLNLEEGKLAFYSVDNQEKLLYECTISASSPLYPA 232
Cdd:cd13737   121 TIGVLLDYAAGSLTFYGVANTMNLIYRFLTTFTEPLYPA 159
SPRY_PRY_TRIM7_like cd12888
PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7)-like, including TRIM7, TRIM10, ...
 88-235 3.94e-16

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: 73.36  E-value: 3.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  88 SCSLEVSKDSRTVTVSHRPQPYRWSCERFSTSQ-VLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSRDqvlGRTmdSC 166
Cdd:cd12888    10 HPRLVLSEDRKSVRWGDTRQDLPDNPERFDTWPcVLGCEGFTSGRHYWEVEVGDGGGWAVGVARESVRRK---GEI--SF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 167 CVE--------WKGtsQLSAWHMVKETVLGSDRPGVVGIWLNLEEGKLAFYSVDNQEKLlyeCTISASSP----LYPAFW 234
Cdd:cd12888    85 SPEegiwavgqWGG--QYWALTSPETPLPLSEVPRRIRVYLDYEGGQVAFFDADNEAPI---FTFPPASFagerIFPWFW 159


                  .
gi 1370472444 235 L 235
Cdd:cd12888   160 V 160
SPRY_PRY_FSD1 cd12901
Fibronectin type III and SPRY containing 1 (FSD1) domain includes PRY at the N-terminus; This ...
 105-239 7.48e-15

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: 71.01  E-value: 7.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 105 RPQPYRWSCERFSTSQ--VLCSQALSSGKHYWEVD-TRNCSHWAVGVASWEMSRDQVLGRTMDSCCV---EWKGTSqLSA 178
Cdd:cd12901    58 RMPSARGGRDRFTAESytVLGDTLIDGGQHYWEVRaQKDSKAFSVGVAYRSLGKFDQLGKTNASWCLhvnNWLQNS-FAA 136

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370472444 179 WHMVKETVLGSDRPGVVGIWLNLEEGKLAFYSVDNQEkLLYECTISASSPLYPAF--WLYGLH 239
Cdd:cd12901   137 KHNNKAKTLDVPVPDRIGVYCDFDEGQLSFYNARTKQ-LLHTFKMKFTQPVLPAFmvWCGGLS 198
SPRY_PRY_TRIM14 cd13738
PRY/SPRY domain of tripartite motif-binding protein 14 (TRIM14); This is a TRIM14 domain ...
 80-237 1.48e-14

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: 69.43  E-value: 1.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  80 PTFNLKSLSCSLEVSKDSRTVTVSHRPQPYRWSCERF-STSQVLCSQALSSGKHYWEVDTRNCSH-WAVGVASWEMSRDQ 157
Cdd:cd13738     1 PTLEPDTLHPRLRLSDDRLTVSCGWLGTLGLCPPQRFdKLWQVLSRDSFFSGRHYWEVDLQEAGAgWWVGAAYPSIGRKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 158 V-----LGRTMDSCCVEwKGTSQLSAWHMVKET-VLGSDRPGVVGIWLNLEEGKLAFYSVDNQEKLLYECTISASSPLYP 231
Cdd:cd13738    81 DseaarLGWNRQSWCLK-RYDLEYWAFHDGQRSrLRPEDDPDRLGVFLDYEAGILSFYDVTGGMTHLHTFRATFQEPLYP 159


                  ....*.
gi 1370472444 232 AFWLYG 237
Cdd:cd13738   160 ALRLWE 165
SPRY_PRY_TRIM50_72 cd12897
PRY/SPRY domain in tripartite motif-binding (TRIM) proteins TRIM50 and TRIM72; This domain, ...
 81-233 2.52e-14

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: 69.18  E-value: 2.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  81 TFNLKSLSCSLEVSKDSRTVTVSHRPQPYRWSCERFSTSQ-VLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSRDQVL 159
Cdd:cd12897    15 TFDPATAHPLLVVSSGGTVVECGLQKQRRASQPERFDKSTcVVASQGFSEGEHYWEVVVGDKPRWALGVIKGTASRKGKL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 160 GRTMDS--CCVEWKGTSQLSAWHMVKET-VLGS-DRPGVVGIWLNLEEGKLAFYSVDNQE--KLLYECTISASSPLYPAF 233
Cdd:cd12897    95 HASPSHgvWLIGLKEGKVYEAHGEPKEPrPLRVaGRPHRIGVYLSFEDGVLSFFDASDPDdlRTLYTFQERFQGKLYPFF 174
SPRY_PRY_RFPL cd15821
Ret finger protein-like (RFPL), includes RFP1, 2, 3, 4; This domain, consisting of the ...
 91-233 5.90e-14

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: 67.72  E-value: 5.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  91 LEVSKDSRTVTVSHRPQPYRWSCERFSTSQ-VLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSR--DQVLGRTMDSCC 167
Cdd:cd15821    17 LIISEDLRSVRCGCFRQNRKELAERFDDALcVLGSPRFTSGRHYWEVDVGTSTEWDLGVCRESVNRqgPIELSPEHGFWT 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370472444 168 VEWKGTSQLSAwHMVKETVLG-SDRPGVVGIWLNLEEGKLAFYSVDNQEKLLYECTISASSPLYPAF 233
Cdd:cd15821    97 VSLRDGSVFFA-STVPLTVLWvNPRLHRVGIFLDMEMGTISFYDVSDGSHIFTFTKISAEEPLRPFF 162
SPRY_PRY_TRIM60_75 cd15817
PRY/SPRY domain of tripartite motif-binding protein 60 and 75 (TRIM60 and TRIM75); This domain, ...
 91-235 1.73e-13

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: 66.42  E-value: 1.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  91 LEVSKDSRTVTVSHRPQPYRWSCERFSTS-QVLCSQALSSGKHYWEVDTRNCSHWAVGVAswemsRDQVLGRTMDSCCVE 169
Cdd:cd15817    13 LIVSEDRKAVRYRRMKPNCPYDPRRFTVYpAVLGSEGFDSGRHFWEVEVGGKGEWILGVC-----KDSLPRNAQDPPSPL 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370472444 170 ---WK---GTSQLSAWHMVKETVLGSDRPGVVGIWLNLEEGKLAFYSVdNQEKLLYECTISASSPLYPAFWL 235
Cdd:cd15817    88 ggcWQigrYMSGYVASGPKTTQLLPVVKPSRIGIFLDYELGEVSFYNM-NDRSHLYTFTDTFTGKLIPYFYV 158
SPRY_PRY_BTN1_2 cd15819
butyrophilin subfamily member A1 and A2 (BTN1A and BTN2A); This domain, consisting of the ...
 90-245 1.96e-13

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: 66.10  E-value: 1.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  90 SLEVSKDSRTVTVSHRPQPYRWSCERF-STSQVLCSQALSSGKHYWEVDTRNCSHWAVGVAswemsRDQVL--GRTMDS- 165
Cdd:cd15819    14 ALILSEDGRSVTWGETRQDLPENPERFdSLPCVLGQEGFTSGRHYWEVEVGDRTSWDLGVC-----RDNVMrkGRVTLSp 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 166 ----CCVE------WKGTSqlsawhmvKETVLG-SDRPGVVGIWLNLEEGKLAFYSV-DNQEklLYECT-ISASSPLYPA 232
Cdd:cd15819    89 engfWAIRlygneyWALTS--------PETPLTlKEPPRRVGIFLDYEAGDVSFYNMtDGSH--IYTFPqTAFSGPLRPF 158

                         170
                  ....*....|...
gi 1370472444 233 FWLYGLHPGNYLI 245
Cdd:cd15819   159 FRLWSSDSGPLTI 171
SPRY_PRY_TRIM60 cd15828
PRY/SPRY domain of tripartite motif-binding protein 60 (TRIM60) also known as RING finger ...
 81-233 4.49e-13

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: 65.39  E-value: 4.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  81 TFNLKSLSCSLEVSKDSRTVTVSHRPQPYRWSCERFS-TSQVLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSRD--- 156
Cdd:cd15828    13 TLDPETAHPQLTVSEDRKSVLYGEMKQNVCYNPRRFYlCPAVLGSEGFHSGRQYWEVEVGDKPEWTLGVCQDCLPRNwsn 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 157 QVL--------GRTMDSCCVewkgtsqlsAWHMVKETVLGSDRPGVVGIWLNLEEGKLAFYSVDNQEkLLYECTISASSP 228
Cdd:cd15828    93 QPSvqdglwaiGRYSESNYV---------ALGPKKIQLLPKVRPSKIGIFLDYELGEVSFYNMNDRS-LLYTFSDSFTGT 162


                  ....*
gi 1370472444 229 LYPAF 233
Cdd:cd15828   163 LWPYF 167
SPRY_PRY_TRIM21 cd12900
PRY/SPRY domain in tripartite motif-binding protein 21 (TRIM21) also known as 52kD ...
 78-233 1.13e-12

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: 64.52  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  78 IHPTFNLKSLSCSLEVSKDSRTVTVSHRPQPYRWSCERFST-SQVLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSRD 156
Cdd:cd12900     3 VHITLDPDTANPWLILSKDRRQVRLGDTHQNVPENEERFDNyPMVLGAQRFNSGKHYWEVDVTGKEAWDLGVCRDSVRRK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 157 -QVLGRTMDSCCVEWKGTSQLSAWHMVKETVLGSDRPGVVGIWLNLEEGKLAFYSVDNQEKLLY---ECTIsaSSPLYPA 232
Cdd:cd12900    83 gQFLLSPENGFWTIWLWNKKYEAGTSPQTTLHLQVPPCQVGIFLDYEAGVVSFYNITDHGSLIYtfsECAF--TGPLRPF 160


                  .
gi 1370472444 233 F 233
Cdd:cd12900   161 F 161
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 130-237 1.63e-12

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: 62.45  E-value: 1.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 130 GKHYWEV--DTRNCSHWAVGVASWEMSRDQ--VLGRTMDSCCVEwkgTSQLSAWHMVKETVLGSD--RPGVVGIWLNLEE 203
Cdd:cd11709     1 GKWYWEVrvDSGNGGLIQVGWATKSFSLDGegGVGDDEESWGYD---GSRLRKGHGGSSGPGGRPwkSGDVVGCLLDLDE 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1370472444 204 GKLAFYSVDNQEKLLYECTISASSPLYPAFWLYG 237
Cdd:cd11709    78 GTLSFSLNGKDLGVAFTNLFLKGGGLYPAVSLGS 111
SPRY_PRY_TRIM50 cd13743
PRY/SPRY domain in tripartite motif-binding protein 50 (TRIM50); This domain, consisting of ...
 91-233 1.90e-12

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: 64.05  E-value: 1.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  91 LEVSKDSRTVTVSHRPQPYRWSCERFSTSQ-VLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSRDQVLGRTMDSCCve 169
Cdd:cd13743    25 LELSKGNTVVECGLLAQRLPSNPERFDYSNcVLASRGFSSGKHYWEVVVGSKSKWRLGLIKGTTSRKGKLNKSPENGV-- 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 170 W----KGTSQLSAWHMVKETVLGSDRPGVVGIWLNLEEGKLAFYSVDNQEKL--LYECTISASSPLYPAF 233
Cdd:cd13743   103 WliglKEGRVYEAFANPRVPLPLSTRPQRIGVFLDYEKGELTFYNADSPDELvpIYTFQAEFQGKLYPLL 172
SPRY_PRY_TRIM38 cd15815
PRY/SPRY domain of tripartite motif-binding protein 38 (TRIM38), also known as Ring finger ...
 90-211 4.33e-12

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: 62.75  E-value: 4.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  90 SLEVSKDSRTVTVSHRPQPYRWSCERFSTSQ-VLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSRDqvLGRTMDSCCV 168
Cdd:cd15815    25 ELTLSKDQRQVTYGRCQENLDASPKRFTVLPcVLGCEGFTSGRHYFEVDVGEGTGWDVGVCLENVQRG--FGMKQEPEFG 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370472444 169 EWkgtsqlsAWHMVKE----------TVLG-SDRPGVVGIWLNLEEGKLAFYSV 211
Cdd:cd15815   103 FW-------TIRLCEEdgyvaltsppTPLPlREKPLVVGVFLDYEAGLVSFYNM 149
SPRY_PRY_TRIM41 cd13741
PRY/SPRY domain in tripartite motif-binding protein 41 (TRIM41); This domain, consisting of ...
 60-233 7.63e-12

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: 62.47  E-value: 7.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  60 PDQSHPALrrasrfaqwaihptfnlkslscslEVSKDSRTVTVSHRPQPYRWSCERFSTSQ-VLCSQALSSGKHYWEVDT 138
Cdd:cd13741     6 PDTAHPAL------------------------LLSPDRRGVRLAERRQEVPEHPKRFSADCcVLGAQGFRSGRHYWEVEV 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 139 RNCSHWAVGVASWEMSRDQVLGRTMDSC------------------------------CVEWKGtSQLSAWHMVKETVLG 188
Cdd:cd13741    62 GGRRGWAVGAARESTHHKEKVGSGGSSVssgdasssrhhhrrrrlhlpqqpllqrevwCVGTNG-KRYQAQSSTEQTLLS 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1370472444 189 -SDRPGVVGIWLNLEEGKLAFYsvdNQEKLLYECTISAS---SPLYPAF 233
Cdd:cd13741   141 pSEKPRRFGVYLDYEAGRLGFY---NAETLAHVHTFSAAflgERVFPFF 186
SPRY_PRY_TRIM76 cd12898
PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76), also called ...
 91-242 1.01e-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: 61.48  E-value: 1.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  91 LEVSKDSRTVTVSHrpQPYRWSCERFSTSQVLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSRDQVLGRTMDSCCVEW 170
Cdd:cd12898    15 LHISSDRGTVIYFH--ERRRKMSSLTECPSVLGEELPSCGQYYWETTVTRCPAYRLGICSSSASQAGALGEGSTSWCLHC 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370472444 171 KGTSQLSAWHMVKETVLGS----DRPGVVGIWLNLEEGKLAFYSVDNqEKLLYECTISASSPLYPAFWLYglHPGN 242
Cdd:cd12898    93 VPTSEPCRYTLLHSGIVSDvfvtERPARVGTLLDYNNGRLIFINAES-GQLLGIFRHRFAQPCHPAFALE--KPGK 165
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 131-236 1.47e-11

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: 60.05  E-value: 1.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 131 KHYWEV--DTRNCSHWAVGVASWEMSR--DQVLGRTMDSCCVEwkGTSQLSAWH-MVKETVLGSDRPG-VVGIWLNLEEG 204
Cdd:pfam00622   1 RHYFEVeiFGQDGGGWRVGWATKSVPRkgERFLGDESGSWGYD--GWTGKKYWAsTSPLTGLPLFEPGdVIGCFLDYEAG 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1370472444 205 KLAFYsvDNQEKLLYECTI-SASSPLYPAFWLY 236
Cdd:pfam00622  79 TISFT--KNGKSLGYAFRDvPFAGPLFPAVSLG 109
SPRY_PRY_TRIM34 cd15825
PRY/SPRY domain in tripartite motif-containing protein 34 (TRIM34), also known as RING finger ...
 81-233 1.55e-11

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: 61.39  E-value: 1.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  81 TFNLKSLSCSLEVSKDSRTVT-VSHRPqpyrWSCERFStsqVLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSRDQVL 159
Cdd:cd15825     5 TLNPVNLNLNLVLSEDQRQVTsVPIWP----FKCYNYG---ILGSQYFSSGKHYWEVDVSKKTAWILGVYCRKRSRTFKY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 160 GR---TMDSCCVEWK--------GTSQLSAWHMVKETVLGSDR---------PGVVGIWLNLEEGKLAFYSVDNQEKLLY 219
Cdd:cd15825    78 VRqgkNHPNVYSRYRpqygywviGLQNKSEYYAFEDSSTSDPKvltlsvatpPHRVGVFLDYEAGTVSFFNVTNHGSLIY 157

                         170
                  ....*....|....*
gi 1370472444 220 E-CTISASSPLYPAF 233
Cdd:cd15825   158 KfSKCCFSQPVYPYF 172
SPRY_PRY_TRIM39 cd13745
PRY/SPRY domain in tripartite motif-binding protein 39 (TRIM39) and TRIM39-like; This domain, ...
 91-233 2.15e-11

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: 60.72  E-value: 2.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  91 LEVSKDSRTVTVSHRPQPYRWSCERFSTS-QVLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSRD-QVLGRTMDSCCV 168
Cdd:cd13745    16 LVLSEDRKSVRHGDTRQDLPDNPERFDTYpCVLGAEGFTGGRHYWEVEVGDKTEWTLGVCRESVSRKgEVTLSPENGYWT 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370472444 169 EW--KG-----TSQLSAWHMvketvlgSDRPGVVGIWLNLEEGKLAFYSVDNQEKlLYECTISASSPLYPAF 233
Cdd:cd13745    96 VWlrDGkyealTSPPTPLPV-------SVRPSRVGIFLDYEAGEVSFYNVTDRSH-LFTFTDTFSGTLRPYF 159
SPRY_PRY_TRIM11 cd15811
PRY/SPRY domain of tripartite motif-binding protein 11 (TRIM11), also known as RING finger ...
 91-233 2.35e-11

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: 60.74  E-value: 2.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  91 LEVSKDSRTVTVSHRPQPYRWSCERFSTSQ-VLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSRdqvlgrtmdsccve 169
Cdd:cd15811    13 LVLSEDRRSVRRGDLRQALPDSPERFDPGPcVLGRERFTSGRHYWEVEVGDRTSWALGVCKENVNR-------------- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 170 wKGTSQLSA----WHMVketVLGS-------------DRPGVVGIWLNLEEGKLAFYSVDNQEKLLYECTISASSPLYPA 232
Cdd:cd15811    79 -KEKGELSAgngfWILV---FLGNyysserrtfaplrDPPRRVGIFLDYEAGHLSFYSATDGSLLFIFPETPFSGTLRPL 154


                  .
gi 1370472444 233 F 233
Cdd:cd15811   155 F 155
SPRY_PRY_TRIM15 cd15826
PRY/SPRY domain in tripartite motif-binding protein 15 (TRIM15); This domain, consisting of ...
 81-247 2.47e-11

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: 60.65  E-value: 2.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  81 TFNLKSLSCSLEVSKDSRTVTVSHRPQ-----PYRWSCErfstSQVLCSQALSSGKHYWEVDTR--NCSHWAVGVASWEM 153
Cdd:cd15826     3 TLDPQTASGSLVLSEDRKSVRYTRQKQnlpdsPLRFDGL----PAVLGSPGFSSGRHRWQVEVQlgDGGGCTVGVAGESV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 154 SRDQVLGRTMD----------SCCveWKGTSqlsawhmvKETVLG-SDRPGVVGIWLNLEEGKLAFYSVDNQEkLLYECT 222
Cdd:cd15826    79 RRKGEMGLSAEdgvwavilshQQC--WASTS--------PGTDLPlSEIPRRVGVALDYEAGTVTLTNAETQE-PIFTFT 147

                         170       180
                  ....*....|....*....|....*
gi 1370472444 223 ISASSPLYPAFWLYglHPGNYLIIK 247
Cdd:cd15826   148 ASFSGKVFPFFAVW--KKGSRLTLK 170
SPRY_BSPRY cd12904
SPRY domain in Ro-Ret family; This domain, named BSPRY, has been identified in the Ro-Ret ...
 81-233 2.91e-11

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: 60.51  E-value: 2.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  81 TFNLKSLSCSLEVSKDSRTVTVSHRP--QPYRWSCERF-STSQVLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSR-- 155
Cdd:cd12904     2 RFDERTVSPLLSLSEDRRTLTFSPKKarQSPPDDPERFdHWPNALASLSFSSGTHAWVVDVGKSCAYKVGVCYGSLERkg 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 156 ---DQVLGRTMDSccveW---KGTSQLSAWHMVKETVLG-SDRPGVVGIWLNLEEGKLAFYSVDNQeKLLYECTISASSP 228
Cdd:cd12904    82 sgnEARLGYNAFS----WvfsRYDGEFSFSHNGQHVPLElLKCPARVGVLLDWPSQELLFYDPDSC-TVLHSHREAFAAP 156


                  ....*
gi 1370472444 229 LYPAF 233
Cdd:cd12904   157 LLPVF 161
SPRY_PRY_TRIM5_6_22_34 cd15810
PRY/SPRY domain of tripartite motif-binding protein 5, 6, 22 and 34 (TRIM5, TRIM6, TRIM22 and ...
 80-233 3.21e-11

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: 60.57  E-value: 3.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  80 PTFNLKSLSCSLEVSKDSRTVTVSHrPQPYRWSCER-FSTSQVLCSQALSSGKHYWEVDTRNCSHWAVGVASWEM----- 153
Cdd:cd15810     2 VTLNPVNISLNIVISEDQRQVRIVP-PQTSGQALTNnNYDFGVLGSQYFSSGKHYWEVDVSKKSAWILGVCSHKRsdamt 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 154 -------------SRDQ------VLGRTMDSCCVEWKGTSQlSAWHMV--KETVLgsdrPGVVGIWLNLEEGKLAFYSVD 212
Cdd:cd15810    81 ksnanqinhqnvySRYQpqygywVIGLQNESEYNAFEDSSS-FNPHVLtlSVTVP----PHRVGVFLDYEAGTVSFFNVT 155

                         170       180
                  ....*....|....*....|....
gi 1370472444 213 NQEKLLY---ECtiSASSPLYPAF 233
Cdd:cd15810   156 NHGSLIYkfsKC--CFSTTVCPYF 177
SPRY_PRY_SPRYD4 cd12903
PRY/SPRY domain containing protein 4 (SPRYD4); This domain, consisting of the distinct ...
 114-236 3.91e-11

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: 59.77  E-value: 3.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 114 ERFST-SQVLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSRDQVLGrtMDSCcvEWKGTSQLSAWH-MV---KETVLG 188
Cdd:cd12903    38 ERFRDwAVVLGDTPVTSGRHYWEVTVKRSQEFRIGVADVDMSRDECIG--TNES--SWVFAYAQRKWYaMVaneTVPVPL 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1370472444 189 SDRPGVVGIWLNLEEGKLAFYSVDnQEKLLYECTISASSPLYPAFWLY 236
Cdd:cd12903   114 VGKPDRVGLLLDYEAGKLSLVDVE-KNSVVHTMSAEFRGPVVPAFALW 160
SPRY_PRY_TRIM35 cd12893
PRY/SPRY domain in tripartite motif-containing protein 35 (TRIM35); This PRY/SPRY domain is ...
 91-237 4.61e-11

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: 59.57  E-value: 4.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  91 LEVSKDSRTVTVSHRPQPYRWSCERFSTSQ-VLCSQALSSGKHYWEVDTRNCSHWAVGVASweMSRDQvlGRTMDSC--- 166
Cdd:cd12893    13 LSLSEDLTSVRYSSEKQQLPDNPERFDPYPcVLGSEGFTSGKHSWDVEVGDNTSWMLGVAK--ESVQR--KGKFTLSpes 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370472444 167 ---CVE-WKGtsQLSAWHMVKE-TVLG-SDRPGVVGIWLNLEEGKLAFYSVDNqEKLLYECTISASSPLYPAFWLYG 237
Cdd:cd12893    89 gfwTIGfSEG--KYSARTSPEPrTPLRvKQKPQRIRVQLDWDRGKVSFSDPDT-NTHIHTFTHTFTERVFPYFYTGC 162
SPRY_PRY_TRIM69 cd15818
PRY/SPRY domain in tripartite motif-binding protein 69 (TRIM69), also known as RING finger ...
 114-233 6.55e-11

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: 59.82  E-value: 6.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 114 ERFSTS-QVLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSRDQVLGRT-MDSCCVEW-KGTSQLSAWHMVKETVLGSD 190
Cdd:cd15818    49 ERFDSSvAVLGSEGFTSGKHYWEVEVAKKTKWTLGVVRESINRKGNCPLSpEDGFWLLRlRNQNELKALDVPSFSLTLTS 128

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1370472444 191 RPGVVGIWLNLEEGKLAFYSVDNQEKlLYECTISASSPLYPAF 233
Cdd:cd15818   129 NLNKVGIYLDYEGGQVSFYNANTMSH-IYTFSDTFTEKIYPYF 170
SPRY_PRY_TRIM58 cd15816
PRY/SPRY domain in tripartite motif-binding protein 58 (TRIM58), also known as BIA2; This ...
 90-235 1.35e-10

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: 58.26  E-value: 1.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  90 SLEVSKDSRTVTVSHRPQPYRWSCERFST-SQVLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSRDqvlGRTMDS--- 165
Cdd:cd15816    12 SLLLTADLRSVQDGELWRDVPGNPERFDTwPCVLGLQSFSSGRHYWEVAVGEKAEWGLGVCQDSAPRK---GETTPSpen 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370472444 166 -CCVEW--KGTSqlsawHMVKET----VLGSDRPGVVGIWLNLEEGKLAFYSVDNqEKLLYECTISASSPLYPAFWL 235
Cdd:cd15816    89 gVWAVWllKGNE-----YMVLASpsvpLLQLRRPRRVGVFLDYEAGEISFYNVTA-GSHIYTFRQLFSGILRPYFFV 159
SPRY_PRY_TRIM20 cd15813
PRY/SPRY domain in tripartite motif-binding protein 20 (TRIM20), also known as pyrin; This ...
 91-233 1.98e-10

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: 58.23  E-value: 1.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  91 LEVSKDSRTVTVSHRPQPYRWSCERF-STSQVLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSRDQVLGRT------- 162
Cdd:cd15813    22 LIFSDDLKSVRLGNKWDRLPDNPERFdSCIIVLGSPSFTSGRHYWEVEVGDKTGWILGVCKASVSRKGSMTLSpengywv 101

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370472444 163 -MDSCCVEWKGTSQLSAWHMVKETvlgsdrPGVVGIWLNLEEGKLAFYSVDNQEkLLYECTISASS-PLYPAF 233
Cdd:cd15813   102 vMMTKRNEYQASTSPPTRLWLREP------PRRVGIFLDYEAGDISFYNVTAKS-HIYTFTSFSSSgPLQPIF 167
SPRY_PRY_TRIM47 cd15808
PRY/SPRY domain in tripartite motif-containing protein 47 (TRIM47), also known as RING finger ...
 106-231 2.00e-10

PRY/SPRY domain in tripartite motif-containing protein 47 (TRIM47), also known as RING finger protein 100 (RNF100) or Gene overexpressed in astrocytoma protein (GOA); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM47, also known as GOA (Gene overexpressed in astrocytoma protein) or RNF100 (RING finger protein 100). TRIM47 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. It is highly expressed in kidney tubular cells, but lowly 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; astrocytoma, also known as cerebral astrocytoma, is a malignant glioma that arises from astrocytes. Genome wide studies on white matter lesions have identified a novel locus on chromosome 17q25 harboring several genes such as TRIM47 and TRIM65 which pinpoints to possible novel mechanisms leading to these lesions.


Pssm-ID: 293980  Cd Length: 206  Bit Score: 58.74  E-value: 2.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 106 PQPYRWSCERFS-TSQVLCSQALSSGKHYWEVDTrnCSHW-AVGVASWEMSRDQV-----LGRTMDSCCVEWKGTSqLSA 178
Cdd:cd15808    35 PISYPESPTRFThCEQVLGEGALDRGTYYWEVEI--IEGWvSVGVMAEDFSPREPydrgrLGRNAHSCCLQWNGRN-FSV 111

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370472444 179 WHMVKETVLGSDRPGVVGIWLNLEEGKLAFYSV-DNQEKLLYECTIS-------ASSPLYP 231
Cdd:cd15808   112 WFHGLEAPLPHPFSPTVGVCLEYADRALAFYAVrDGKVSLLRRLKASrprrggpPASPLDP 172
SPRY_PRY_BTN3 cd15820
PRY/SPRY domain of butyrophilin 3 (BTN3), includes BTN3A1, BTN3A2, BTN3A3 as well as BTN-like ...
 91-240 2.36e-10

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: 57.82  E-value: 2.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  91 LEVSKDSRTVTVSHRPQPYRWSCERFST-SQVLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSR-DQVlgrTMDSCCV 168
Cdd:cd15820    17 LLISEDQRSLQWADEPQNLPDNPKRFDWhYCVLGCKSFTSGRHFWEVEVGDRKEWYVGVCRENVERkLWV---KMAPENG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 169 EWkgTSQLSawHMVKETVLGSDR--------PGVVGIWLNLEEGKLAFYSVDNQEKLLYECTISASSPLYPAFWLYGLHP 240
Cdd:cd15820    94 FW--TIGLS--DGNDYQALTDPRtkltianpPQRVGVFLDYETGEVSFYNAMDGSHIYTFPHTSFSGPLYPVFRLLSWDP 169
SPRY_PRY_TRIM72 cd13742
PRY/SPRY domain in tripartite motif-binding protein 72 (TRIM72); This domain, consisting of ...
 81-233 6.27e-10

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: 57.18  E-value: 6.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  81 TFNLKSLSCSLEVSKDSRTVTVSHRPQPYRWS-CERFSTSQ-VLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSRDQV 158
Cdd:cd13742    15 TFDPDTAHPYLVVSSDGKRVECADQKQAVSSDdPNRFDKANcVVSHQSFSEGEHYWEVIVGDKPRWALGVISAEAGRKGR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 159 LGRTMDS-----CCVEWKgTSQLSAWHMVKETVLGSDRPGVVGIWLNLEEGKLAFYSVDNQEKL--LYECTISASSPLYP 231
Cdd:cd13742    95 LHALPSNgfwllGCKEGK-VYEAHVEHKEPRALRVEGRPTRIGVYLSFSDGVLSFYDASDEDNLvqLFAFHERFPGPLYP 173


                  ..
gi 1370472444 232 AF 233
Cdd:cd13742   174 FF 175
SPRY_PRY_TRIM62 cd13744
PRY/SPRY domain in tripartite motif-binding protein 62 (TRIM62); This domain, consisting of ...
 78-217 6.04e-09

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: 54.24  E-value: 6.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  78 IHP-----TFNLKSLSCSLEVSKDSRTVTVSH-RPQPYRWSCERFSTS-QVLCSQALSSGKHYWEVDTRNCSHWAVGVAS 150
Cdd:cd13744     7 IHPvpaalTLDPVTAHQRLILSDDCTIVAYGNlHPQPLQDSPKRFDVEvSVLGSEGFSGGVHYWEVVVSEKTQWMIGLAH 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370472444 151 WEMSRDQVL----GRTMdsCCVEWKGTSQLSAWHMVKETVLGSDRPGVVGIWLNLEEGKLAFYSVDNQEKL 217
Cdd:cd13744    87 EAVSRKGSIqiqpGRGF--YCIVMHDGNQYSACTEPWTRLNVKSKLEKVGVYLDYDKGLLIFYNADDMSWL 155
SPRY_PRY_TRIM5 cd15822
PRY/SPRY domain in tripartite motif-binding protein 5 (TRIM5), also known as RING finger ...
 64-233 1.14e-08

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: 53.38  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  64 HPALRRASRFaqWAiHPTFNLKSLScSLEVSKDSRTVTVSHRPQPYRWSCERFSTSqVLCSQALSSGKHYWEVDTRNCSH 143
Cdd:cd15822     1 FNELTDVQRY--WV-HVTLDPSNNK-NIVISEDRRQVRYVRKQQRYNSNGNNEDYG-VLGSPSITSGKHYWEVDVSKKRA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 144 WAVGVASWE------MSRDQVLGRTMDSC------CVEW----KGTSQLSAWhmvKETVLG---------SDRPGVVGIW 198
Cdd:cd15822    76 WILGVCGGKypnstlKDFNKQGKNNQKQCsnyqpkYGYWviglQNKSEYNAF---EDSSSSdpliltlslTVPPCRVGVF 152

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1370472444 199 LNLEEGKLAFYSVDNQEKLLYE-CTISASSPLYPAF 233
Cdd:cd15822   153 LDYEAGTVSFFNVTNHGFLIYKfSSCSFSQEVFPYF 188
SPRY_PRY_TRIM67_9 cd12889
PRY/SPRY domain in tripartite motif-containing proteins, TRIM9 and TRIM67; This domain, ...
 81-215 2.17e-08

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: 52.24  E-value: 2.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  81 TFNLKSLSCSLEVSKDSRTVTvshrpqpyrwsCERFSTSQVLCSQALSSGKHYWE--VDTR-NCSHWAVGVASWEMSRDQ 157
Cdd:cd12889    11 TFDPSTSHPDIILSNDNMTVT-----------CNSYEDRVVLGSVGFSRGVHYWEvtIDRYdGHPDPAFGVARIDVNKDK 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370472444 158 VLGRTMdsccvewKGTS-----QLSaWHMVKE-----TVLGSDRPGVVGIWLNLEEGKLAFYsVDNQE 215
Cdd:cd12889    80 MLGKDD-------KGWSmyidnNRS-WFLHNNehsnrTEGGITVGSVVGVLLDLDRHTLSFY-VNDEP 138
SPRY_PRY_TRIM18 cd12892
PRY/SPRY domain of TRIM18/MID1, also known as FXY or RNF59; This domain, consisting of the ...
 85-233 5.30e-08

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: 51.16  E-value: 5.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  85 KSLSCSLEVSKDSRTVTVSHRPQPYRWSCERFsTSQ----VLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSRDQVLG 160
Cdd:cd12892     7 KSAHRKLKVSHDNLTVERDETSSKKSHTPERF-TSQgsygVAGNVFIDSGRHYWEVVISGSTWYAIGIAYKSAPKHEWIG 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370472444 161 RTMDS-----CCVEWkgtsqlSAWHMVKET-VLGSDRPGVVGIWLNLEEGKLAFYSVDNQEKlLYECTISASSPLYPAF 233
Cdd:cd12892    86 KNSASwvlcrCNNNW------VVRHNSKEIpIEPSPHLRRVGILLDYDNGSLSFYDALNSIH-LYTFDIAFAQPVCPTF 157
SPRY_PRY_TRIM22 cd15824
PRY/SPRY domain in tripartite motif-containing protein 22 (TRIM22), also known as RING finger ...
 93-233 5.90e-08

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: 51.39  E-value: 5.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  93 VSKDSRTVTVSHrPQPYRWSCER-FSTSQVLCSQALSSGKHYWEVDTRNCSHWAVGVASW----------------EMSR 155
Cdd:cd15824    18 VSADQRQVTVVH-ICMFRNSNPCdFSAFDVLGCQYFSSGKYYWEVDVSGKIAWILGVYSKrnnlnkrkssgfafdpNVNH 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 156 DQVLGRTMDSCCVEWKGTSQLSAWHMVKE---------TVLGSDRPGVVGIWLNLEEGKLAFYSVDNQEKLLYE---CTI 223
Cdd:cd15824    97 PNVYSRYRPQNGYWVIGLQNESEYNAFEDssssdpkvlTLSMAVPPHRVGVFLDYEAGTVSFFNVTNHGSLIYKfskCCF 176

                         170
                  ....*....|
gi 1370472444 224 saSSPLYPAF 233
Cdd:cd15824   177 --SQPVYPYF 184
SPRY_PRY_TRIM17 cd15812
PRY/SPRY domain of tripartite motif-binding protein 17 (TRIM17), also known as testis RING ...
 125-235 1.51e-07

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: 49.88  E-value: 1.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 125 QALSSGKHYWEVDTRNCSH--WAVGVAswemsRDQVLGRTMDSCCVE---W-----KGTSQLSAWHMVKeTVLGSDRPGV 194
Cdd:cd15812    48 ETFSSGRHYWEVGMNLTGDalWALGVC-----RDNVSRKDRVPKSPEngfWvvqlsKGKKYLSAMSALT-PVTLTEPPSH 121

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1370472444 195 VGIWLNLEEGKLAFYSVDNQEKLLYECTISASSPLYPAFWL 235
Cdd:cd15812   122 MGIFLDFEAGEVSFYSVNDGSHLHTYSQAAFPGPLQPFFCL 162
SPRY_PRY_TRIM4 cd15809
PRY/SPRY domain in tripartite motif-binding protein 4 (TRIM4), also known as RING finger ...
 106-235 4.15e-07

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: 49.06  E-value: 4.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 106 PQPYRWSCERFS-TSQVLCSQALSSGKHYWEVDTRNCSHWAVGVAswemsRDQVLGRTMDSCCVEWKGT-----SQLSAW 179
Cdd:cd15809    50 PQKTTQFVERFQhLPCVLGKNVFTSGKHYWEVENRDSLEIAVGVC-----REDVMGITDGSEMSPHVGIwaicwSSAGYR 124

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370472444 180 HMVKETVLGSDR---PGVVGIWLNLEEGKLAFYSVDNQEKlLYECTISASSPLYPAFWL 235
Cdd:cd15809   125 PLTSSPVSPTKQepaLHRVGVFLDHGAGEVSFYSAVDGVH-LHTFSCPLVSRLRPFFWL 182
SPRY_PRY_TRIM7 cd13740
PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7); This domain, consisting of the ...
 80-233 6.52e-07

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: 48.03  E-value: 6.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  80 PTFNLKSLSCSLEVSKDSRTVTVSHRPQPYRWSCERFST-SQVLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSRDQV 158
Cdd:cd13740     2 LTLDPDSANPRLILSLDLKSVRLGERAQDLPNHPCRFDTnTRVLASCGFSSGRHHWEVEVGSKDGWAFGVARESVRRKGL 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370472444 159 LGRTMDS--CCVEWKGtSQLSAWHMVKETVLGSDRPGVVGIWLNLEEGKLAFYSVDNQEKlLYECTISASSPLYPAF 233
Cdd:cd13740    82 TPFTPEEgvWALQLNG-GQYWAVTSPERTPLSCGHLSRVRVALDLEVGAVSFYAAEDMRH-IYTFRVNFQERVFPLF 156
SPRY_PRY_TRIM6 cd15823
PRY/SPRY domain in tripartite motif-binding protein 6 (TRIM6), also known as RING finger ...
 81-245 2.04e-06

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: 46.78  E-value: 2.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  81 TFNLKSLSCSLEVSKDSRTVTVSHRPQPYRWSCERFSTSQVLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSRDQVLG 160
Cdd:cd15823     6 TLNPHTANLNLVLSKNRRQVRFVGAKLSGPSYLEEHYDCSVLGSQHFSSGKHYWEVDVTKKTAWILGVCSHSLGPTFSFN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 161 RTMDSCCVEWKGTSQLSAW----HMVKETVLGSDR-----------PGVVGIWLNLEEGKLAFYSVDNQEKLLYECT-IS 224
Cdd:cd15823    86 QYAQNHNAYSRYQPQSGYWviglQHNHEYRAYEDSstslllsmtvpPRRVGVFLDYEAGTVSFYNVTNHGFPIYTFSkYY 165

                         170       180
                  ....*....|....*....|.
gi 1370472444 225 ASSPLYPAFwlyglHPGNYLI 245
Cdd:cd15823   166 FPTTLCPYF-----NPCNCVV 181
SPRY_PRY_TRIM76_like cd12899
PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76)-like; This domain is ...
 130-221 4.80e-06

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: 45.55  E-value: 4.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 130 GKHYWEVDTRNCSHWAVGVASWEMSRDQVLGRTMDSCCVEWKGTSQLSAWHMVKE----TVLGSDRPGVVGIWLNLEEGK 205
Cdd:cd12899    56 GKHYWEVEVDEQTEYRVGVAFEDTQRNGYLGANNTSWCMRHIITPSRHKYEFLHNgwtpDIRITVPPKKIGILLDYDSGR 135

                          90
                  ....*....|....*..
gi 1370472444 206 LAFYSVDNQEKLL-YEC 221
Cdd:cd12899   136 LSFFNVDLAQHLYtFSC 152
SPRY_PRY_TRIM36 cd12894
PRY/SPRY domain in tripartite motif-containing protein 36 (TRIM36); This domain, consisting of ...
 192-237 9.47e-06

PRY/SPRY domain in tripartite motif-containing protein 36 (TRIM36); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM36, a Class I TRIM protein. TRIM36 (also known as Haprin or RNF98) has a ubiquitin ligase activity and interacts with centromere protein-H, one of the kinetochore proteins. It has been shown that TRIM36 is potentially associated with chromosome segregation and that an excess of TRIM36 may cause chromosomal instability. In Xenopus laevis, TRIM36 is expressed during early embryogenesis and plays an important role in the arrangement of somites during their formation.


Pssm-ID: 293951  Cd Length: 204  Bit Score: 45.14  E-value: 9.47e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1370472444 192 PGVVGIWLNLEEGKLAFYSVDNQeKLLYECTISASSPLYPAFWLYG 237
Cdd:cd12894   149 PTRIGICLDYDKGKVGFYDADSM-KCLYERQVDCSGTMYPAFALMG 193
SPRY_PRY_TRIM1 cd13739
PRY/SPRY domain of tripartite motif-binding protein 1 (TRIM1) or MID2; This domain, consisting ...
 80-236 1.02e-05

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: 44.62  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  80 PTFNLKSLSCS---LEVSKDSRTVTVSHRPqpyrwscERFSTSQVLCSQA---LSSGKHYWEVDTRNCSHWAVGVASWEM 153
Cdd:cd13739     5 PKMAHKKLKISndgLQMEKDESSLKKSHTP-------ERFSGTGCYGAAGnifIDSGCHYWEVVVGSSTWYAIGIAYKSA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 154 SRDQVLGRTMDSCCVEwKGTSQLSAWHMVKETVLG-SDRPGVVGIWLNLEEGKLAFYSVDNQEKlLYECTISASSPLYPA 232
Cdd:cd13739    78 PKNEWIGKNSSSWVFS-RCNNNFVVRHNNKEMLVDvPPQLKRLGVLLDYDNNMLSFYDPANSLH-LHTFEVSFILPVCPT 155


                  ....
gi 1370472444 233 FWLY 236
Cdd:cd13739   156 FTIW 159
PRY smart00589
associated with SPRY domains;
77-127 9.08e-05

associated with SPRY domains;


Pssm-ID: 128857  Cd Length: 52  Bit Score: 39.10  E-value: 9.08e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1370472444   77 AIHPTFNLKSLSCSLEVSKDSRTVTVSHRPQPYRWSCERFST-SQVLCSQAL 127
Cdd:smart00589   1 AVDVTLDPDTAHPYLLLSEDRRSVRYGDLKQSLPDNPERFDSyPCVLGSQGF 52
SPRY_PRY_TRIM27 cd15814
PRY/SPRY domain in tripartite motif-containing protein 27 (TRIM27), also known as RING finger ...
 90-235 1.05e-04

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: 41.98  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444  90 SLEVSKDSRTVTVSHRPQPYRWSCERFSTSQ-VLCSQALSSGKHYWEVDTRNCSHWAVGVASwemsrdqvlgrtmDSCCV 168
Cdd:cd15814    14 SLILSDNLRQVRYSYLQQDLPDNPERFNLFPcVLGSPCFIAGRHYWEVEVGDKAKWTIGVCE-------------DSVCR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 169 EWKGTS-------QLSAWHMVKETVLGSDRPGV--------VGIWLNLEEGKLAFYSVDNQEKLLYECTISASSPLYPAF 233
Cdd:cd15814    81 KGGVTSapqngfwAVSLWYGKEYWALTSPMTALplrtplqrVGIFLDYDAGEVSFYNVTERCHTFTFSHATFCGPVRPYF 160


                  ..
gi 1370472444 234 WL 235
Cdd:cd15814   161 SL 162
SPRYD7 cd12880
SPRY domain-containing protein 7; This family contains SPRY domain-containing protein 7 (also ...
 121-233 1.28e-03

SPRY domain-containing protein 7; This family contains SPRY domain-containing protein 7 (also known as SPRY domain-containing protein 7 or CLL deletion region gene 6 protein homolog or CLLD6 or chronic lymphocytic leukemia deletion region gene 6 protein homolog). In humans, CLLD6 is highly expressed in heart, skeletal muscle, and testis as well as cancer cell lines. It also has cross-species conservation, suggesting that it is likely to carry out important cellular processes.


Pssm-ID: 293938  Cd Length: 160  Bit Score: 38.33  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472444 121 VLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSRDQV-LGRTMDSCCVEWKGTsqlsAWH------MVKETVLGSDrpg 193
Cdd:cd12880    20 ALANAPIVQDKAYFEVKIQSTGVWGVGLATRKTDLNRVpLGNDAESWVLRSDGT----IWHngevihKLKQLVEEGD--- 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1370472444 194 VVGIWLNleEGKLAFYSvdNQEKLlyECTISA-SSPLYPAF 233
Cdd:cd12880    93 VIGVTYD--HVELNFYL--NGKPL--DCPITGiKGTVYPVV 127
 
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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