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Conserved domains on  [gi|767958435|ref|XP_011517382|]
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FSD1-like protein isoform X10 [Homo sapiens]

Protein Classification

fibronectin type III domain-containing protein( domain architecture ID 10046220)

fibronectin type III (FN3) domain-containing protein may be involved in specific interactions with other molecules through its FN3 domain

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SPRY_PRY_FSD1 cd12901
Fibronectin type III and SPRY containing 1 (FSD1) domain includes PRY at the N-terminus; This ...
83-297 1.60e-140

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: 395.73  E-value: 1.60e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435  83 FNLDNSSSHLNLKVEDTCVEWDPTGGKGQEsKIKGKENKGsvhvtslkkhtRSGTPSPKRTSV----GSRPPAVRGSRDR 158
Cdd:cd12901    1 FKLDASSSHQNLKVEDLSVEWDATGGKVLQ-KIKGRENDG-----------RSRTASPRNSSArcqsPKRMPSARGGRDR 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 159 FTGESYTVLGDTAIESGQHYWEVKAQKDCKSYSVGVAYKTLGKFDQLGKTNTSWCIHVNNWLQNTFAAKHNNKVKALDVT 238
Cdd:cd12901   69 FTAESYTVLGDTLIDGGQHYWEVRAQKDSKAFSVGVAYRSLGKFDQLGKTNASWCLHVNNWLQNSFAAKHNNKAKTLDVP 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767958435 239 VPEKIGVFCDFDGGQLSFYDANSKQLLYSFKTKFTQPVLPGFMVWCGGLSLSTGMQVPS 297
Cdd:cd12901  149 VPDRIGVYCDFDEGQLSFYNARTKQLLHTFKMKFTQPVLPAFMVWCGGLSVSTGLQVPS 207
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
2-78 1.69e-07

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 48.65  E-value: 1.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435   2 PEEDN-KIDHFILEHRKTNFDGlprvkdercWEIIDN--IKGTEYTLSGLKFDSKYmNFRVRACNKAVAGEYSDPVTLET 78
Cdd:cd00063   24 PEDDGgPITGYVVEYREKGSGD---------WKEVEVtpGSETSYTLTGLKPGTEY-EFRVRAVNGGGESPPSESVTVTT 93
 
Name Accession Description Interval E-value
SPRY_PRY_FSD1 cd12901
Fibronectin type III and SPRY containing 1 (FSD1) domain includes PRY at the N-terminus; This ...
83-297 1.60e-140

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: 395.73  E-value: 1.60e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435  83 FNLDNSSSHLNLKVEDTCVEWDPTGGKGQEsKIKGKENKGsvhvtslkkhtRSGTPSPKRTSV----GSRPPAVRGSRDR 158
Cdd:cd12901    1 FKLDASSSHQNLKVEDLSVEWDATGGKVLQ-KIKGRENDG-----------RSRTASPRNSSArcqsPKRMPSARGGRDR 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 159 FTGESYTVLGDTAIESGQHYWEVKAQKDCKSYSVGVAYKTLGKFDQLGKTNTSWCIHVNNWLQNTFAAKHNNKVKALDVT 238
Cdd:cd12901   69 FTAESYTVLGDTLIDGGQHYWEVRAQKDSKAFSVGVAYRSLGKFDQLGKTNASWCLHVNNWLQNSFAAKHNNKAKTLDVP 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767958435 239 VPEKIGVFCDFDGGQLSFYDANSKQLLYSFKTKFTQPVLPGFMVWCGGLSLSTGMQVPS 297
Cdd:cd12901  149 VPDRIGVYCDFDEGQLSFYNARTKQLLHTFKMKFTQPVLPAFMVWCGGLSVSTGLQVPS 207
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
174-286 1.62e-14

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: 68.86  E-value: 1.62e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435   174 SGQHYWEVKAQKDcKSYSVGVAYKT--LGKFDQLGKTNTSWCIH---VNNWlqntfaakHNNKVKALDVTVPEK---IGV 245
Cdd:smart00449   1 SGRHYFEVEIGDG-GHWRVGVATKSvpRGYFALLGEDKGSWGYDgdgGKKY--------HNSTGPEYGLPLQEPgdvIGC 71
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 767958435   246 FCDFDGGQLSFYDANSKQLLYSFKT-KFTQPVLPGFMVWCGG 286
Cdd:smart00449  72 FLDLEAGTISFYKNGKYLHGLAFFDvKFSGPLYPAFSLGSGN 113
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
177-280 1.27e-08

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: 52.35  E-value: 1.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435  177 HYWEVKAQKDCK-SYSVGVAYKT--LGKFDQLGKTNTSWCIHVNN---WLQNTFAAKHNNKVKALDVtvpekIGVFCDFD 250
Cdd:pfam00622   2 HYFEVEIFGQDGgGWRVGWATKSvpRKGERFLGDESGSWGYDGWTgkkYWASTSPLTGLPLFEPGDV-----IGCFLDYE 76
                          90       100       110
                  ....*....|....*....|....*....|.
gi 767958435  251 GGQLSFYDaNSKQLLYSFKT-KFTQPVLPGF 280
Cdd:pfam00622  77 AGTISFTK-NGKSLGYAFRDvPFAGPLFPAV 106
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
2-78 1.69e-07

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 48.65  E-value: 1.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435   2 PEEDN-KIDHFILEHRKTNFDGlprvkdercWEIIDN--IKGTEYTLSGLKFDSKYmNFRVRACNKAVAGEYSDPVTLET 78
Cdd:cd00063   24 PEDDGgPITGYVVEYREKGSGD---------WKEVEVtpGSETSYTLTGLKPGTEY-EFRVRAVNGGGESPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
2-65 2.32e-03

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 36.44  E-value: 2.32e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767958435     2 PEEDNKIDHFILEHRKTNfdglpRVKDERCWEIIDNIKGTEYTLSGLKFDSKYmNFRVRACNKA 65
Cdd:smart00060  23 PPPDDGITGYIVGYRVEY-----REEGSEWKEVNVTPSSTSYTLTGLKPGTEY-EFRVRAVNGA 80
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
32-78 4.93e-03

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 38.44  E-value: 4.93e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 767958435  32 WEIIDNIKGTEYTLSGLKFDSKYmNFRVRACNKA-VAGEYSDPVTLET 78
Cdd:COG3401  276 FTKVATVTTTSYTDTGLTNGTTY-YYRVTAVDAAgNESAPSNVVSVTT 322
 
Name Accession Description Interval E-value
SPRY_PRY_FSD1 cd12901
Fibronectin type III and SPRY containing 1 (FSD1) domain includes PRY at the N-terminus; This ...
83-297 1.60e-140

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: 395.73  E-value: 1.60e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435  83 FNLDNSSSHLNLKVEDTCVEWDPTGGKGQEsKIKGKENKGsvhvtslkkhtRSGTPSPKRTSV----GSRPPAVRGSRDR 158
Cdd:cd12901    1 FKLDASSSHQNLKVEDLSVEWDATGGKVLQ-KIKGRENDG-----------RSRTASPRNSSArcqsPKRMPSARGGRDR 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 159 FTGESYTVLGDTAIESGQHYWEVKAQKDCKSYSVGVAYKTLGKFDQLGKTNTSWCIHVNNWLQNTFAAKHNNKVKALDVT 238
Cdd:cd12901   69 FTAESYTVLGDTLIDGGQHYWEVRAQKDSKAFSVGVAYRSLGKFDQLGKTNASWCLHVNNWLQNSFAAKHNNKAKTLDVP 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767958435 239 VPEKIGVFCDFDGGQLSFYDANSKQLLYSFKTKFTQPVLPGFMVWCGGLSLSTGMQVPS 297
Cdd:cd12901  149 VPDRIGVYCDFDEGQLSFYNARTKQLLHTFKMKFTQPVLPAFMVWCGGLSVSTGLQVPS 207
SPRY_PRY_C-II cd13734
PRY/SPRY domain in tripartite motif-containing proteins 1, 9, 18, 36, 46, 67,76 (TRIM1, TRIM9, ...
83-289 3.02e-62

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: 195.19  E-value: 3.02e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435  83 FNLDNSSSHLNLKVED--TCVEWDPTGGKGQESkikgkenkgsvhvtslkkhtrsgtpspkrtsvgsrppavrgSRDRFT 160
Cdd:cd13734    1 FKLDPKTAHRKLRLSNdnLTVEYDPEGSKDQAA-----------------------------------------VLPRRF 39
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 161 GESYTVLGDTAIESGQHYWEVKAQKDCkSYSVGVAYKTLGKFDQLGKTNTSWCIHVNNwlqNTFAAKHNNKVKALDVTV- 239
Cdd:cd13734   40 TGSPAVLGDVAISSGRHYWEVSVSRST-SYRVGVAYKSAPRDEDLGKNSTSWCLSRDN---NRYTARHDGKVVDLRVTGh 115
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767958435 240 PEKIGVFCDFDGGQLSFYDANSKQLLYSFKTKFTQPVLPGFMVWCGGLSL 289
Cdd:cd13734  116 PARIGVLLDYDNGTLSFYDAESKQHLYTFHVDFEGPVCPAFAVWNGSLTL 165
SPRY_PRY cd12874
PRY/SPRY domain, also known as B30.2; This domain contains residues in the N-terminus that ...
83-290 2.68e-58

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: 185.20  E-value: 2.68e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435  83 FNLDNSSSHLNLKVEDT--CVEWDPTGGKGQEskikgkenkgsvhvtslkkhtrsgtpspkrtsvgsrppavrgsRDRFT 160
Cdd:cd12874    1 LTFDPDTAHLNLILSDDlrSVRVGDISQHPPE-------------------------------------------PPPRF 37
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 161 GESYTVLGDTAIESGQHYWEVKAQkDCKSYSVGVAYKTL---GKFDQLGKTNTSWCIHVNNwlqNTFAAKHNNKVKALDV 237
Cdd:cd12874   38 FECWQVLGSQSFSSGRHYWEVDVQ-DDSSWYVGVTYKSLprkGKMSNLGRNNGSWCLEWRE---NEFSAWHNNPETRLPV 113
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767958435 238 TVPEKIGVFCDFDGGQLSFYDAN-SKQLLYSFKTKFTQPVLPGFMVW-CGGLSLS 290
Cdd:cd12874  114 TPPRRLGVFLDCDGGSLSFYGVTdGVQLLYTFKAKFTEPLYPAFWLGeGSTLSIC 168
SPRY_PRY_C-I_2 cd12891
PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM14-like, ...
141-286 7.50e-35

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: 124.67  E-value: 7.50e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 141 KRTSVGSRPPAVRGSRDRFTgeSYTVLGDTAIESGQHYWEVKAQKdCKSYSVGVAYKTL---GKFDQLGKTNTSWCIHVN 217
Cdd:cd12891   19 KTVTCSSENQHYPDSPERFT--HSQVLSTQSFSSGRHYWEVEVSE-SGGWSVGVAYPSIerkGDESRIGRNDKSWCLEWQ 95
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 218 NwlqNTFAAKHNNKVKALDVTVPEKIGVFCDFDGGQLSFYD-ANSKQLLYSFKTKFTQPVLPGFMVWCGG 286
Cdd:cd12891   96 D---KSFSAWHNNEETPLPSVSSRRLGVYLDYEAGRLSFYElSDPIRHLHTFTATFTEPLHPAFWVLEGG 162
SPRY_PRY_TRIM18 cd12892
PRY/SPRY domain of TRIM18/MID1, also known as FXY or RNF59; This domain, consisting of the ...
83-296 9.40e-32

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: 117.03  E-value: 9.40e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435  83 FNLDNSSSHLNLKV--EDTCVEWDPTGGKgqeskikgkenkgsvhvtslKKHTRsgtpspkrtsvgsrppavrgsrDRFT 160
Cdd:cd12892    2 FKLDPKSAHRKLKVshDNLTVERDETSSK--------------------KSHTP----------------------ERFT 39
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 161 GE-SYTVLGDTAIESGQHYWEVKAQKDcKSYSVGVAYKTLGKFDQLGKTNTSWCIHVNNwlqNTFAAKHNNKVKALDVTv 239
Cdd:cd12892   40 SQgSYGVAGNVFIDSGRHYWEVVISGS-TWYAIGIAYKSAPKHEWIGKNSASWVLCRCN---NNWVVRHNSKEIPIEPS- 114
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767958435 240 PE--KIGVFCDFDGGQLSFYDANSKQLLYSFKTKFTQPVLPGFMVWCGGLSLSTGMQVP 296
Cdd:cd12892  115 PHlrRVGILLDYDNGSLSFYDALNSIHLYTFDIAFAQPVCPTFTVWNKCLTILTGLPIP 173
SPRY_PRY_RNF135 cd12902
PRY/SPRY domain in RING finger protein RNF135; This domain, consisting of the distinct ...
137-296 1.42e-27

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: 105.67  E-value: 1.42e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 137 TPSPKRTSVGSRPPAVRGSRDRFTGESytVLGDTAIESGQHYWEVKAQKdCKSYSVGVAYKTLGKFDQLGKTNTSWCIHV 216
Cdd:cd12902   15 SEDSRKVTVSHGPQAYAWSPDRFSISQ--VLCSQAFSSGQHYWEVDTRQ-CSHWAVGVASWEMSRDQMLGRTMDSWCIEW 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 217 NNWLQntFAAKHNNKVKALDVTVPEKIGVFCDFDGGQLSFYD-ANSKQLLYSFKTKFTQPVLPGFmvWCGGLSLSTGMQV 295
Cdd:cd12902   92 KGTGQ--LSAWHMNKETVLGSDKPRVVGIWLDLEEGKLAFYSvANQERLLHECEVSASSPLHPAF--WLYGLEPGNSLII 167

                 .
gi 767958435 296 P 296
Cdd:cd12902  168 K 168
SPRY_PRY_TRIM1 cd13739
PRY/SPRY domain of tripartite motif-binding protein 1 (TRIM1) or MID2; This domain, consisting ...
83-293 2.06e-25

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: 100.09  E-value: 2.06e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435  83 FNLDNSSSHLNLKVEDTCVEWDPtggkgQESkikgkenkgsvhvtSLKKhtrSGTPspkrtsvgsrppavrgsrDRFTGE 162
Cdd:cd13739    1 FKLDPKMAHKKLKISNDGLQMEK-----DES--------------SLKK---SHTP------------------ERFSGT 40
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 163 -SYTVLGDTAIESGQHYWEVkAQKDCKSYSVGVAYKTLGKFDQLGKTNTSWCIHVNNwlqNTFAAKHNNKVKALDVTvPE 241
Cdd:cd13739   41 gCYGAAGNIFIDSGCHYWEV-VVGSSTWYAIGIAYKSAPKNEWIGKNSSSWVFSRCN---NNFVVRHNNKEMLVDVP-PQ 115
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767958435 242 --KIGVFCDFDGGQLSFYDANSKQLLYSFKTKFTQPVLPGFMVWCGGLSLSTGM 293
Cdd:cd13739  116 lkRLGVLLDYDNNMLSFYDPANSLHLHTFEVSFILPVCPTFTIWNKSLMILSGL 169
SPRY_PRY_TRIM76 cd12898
PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76), also called ...
150-280 9.14e-24

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: 95.38  E-value: 9.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 150 PAVRGSRDRFTGESY--------------TVLGDTAIESGQHYWEVKAQkDCKSYSVGVAYKTLGKFDQLGKTNTSWCIH 215
Cdd:cd12898   13 PALHISSDRGTVIYFherrrkmssltecpSVLGEELPSCGQYYWETTVT-RCPAYRLGICSSSASQAGALGEGSTSWCLH 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767958435 216 -VNNWLQNTFAAKHNNKVKALDVT-VPEKIGVFCDFDGGQLSFYDANSKQLLYSFKTKFTQPVLPGF 280
Cdd:cd12898   92 cVPTSEPCRYTLLHSGIVSDVFVTeRPARVGTLLDYNNGRLIFINAESGQLLGIFRHRFAQPCHPAF 158
SPRY_PRY_SNTX cd16040
Stonustoxin subunit alpha or SNTX subunit alpha; This domain, consisting of the distinct ...
174-286 1.25e-23

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: 95.25  E-value: 1.25e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 174 SGQHYWEVkaQKDCKSYSVGVAYKTL---GKFDQ--LGKTNTSWCIhvnNWLQNTFAAKHNNKVKALDVTVPE--KIGVF 246
Cdd:cd16040   60 SGRCYWEV--EWSGGGVDIAVAYKGIsrkGDGDDsrFGYNDKSWSL---ECSPSGYSFWHNNKKTEISVPSSSssRVGVY 134
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767958435 247 CDFDGGQLSFYDANSK-QLLYSFKTKFTQPVLPGFMVWCGG 286
Cdd:cd16040  135 LDHSAGTLSFYSVSDTmTLLHTVQTTFTEPLYPGFGVGYGS 175
SPRY_PRY_TRIM25 cd13736
PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25); This domain, consisting of ...
144-290 3.05e-21

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: 88.79  E-value: 3.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 144 SVGSRPPAVRGSRDRFTGESyTVLGDTAIESGQHYWEVKAQKD--CksySVGVAYKTL---GKFDQLGKTNTSWCIHvnn 218
Cdd:cd13736   22 SVSDDPQNYREHPQRFTYCS-QVLGLHCFKQGIHYWEVELQKNnfC---GVGICYGSMdrqGPESRLGRNSESWCVE--- 94
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958435 219 WLQNTFAAKHNNKVKALDVTVPEKIGVFCDFDGGQLSFYDANSK-QLLYSFKTKFTQPVLPGFMVWCGGLSLS 290
Cdd:cd13736   95 WFNVKISAWHNNVEKTLPSTKATRVGVLLNCDHGFVIFFAVQDKvHLMYKFKVDFTEALYPAFWVFSAGTTLS 167
SPRY_PRY_TRIM76_like cd12899
PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76)-like; This domain is ...
166-280 1.42e-20

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: 87.15  E-value: 1.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 166 VLGDTAIESGQHYWEVKAQKDCKsYSVGVAYKTLGKFDQLGKTNTSWCI-HVNNWLQNTFAAKHNNKVKALDVTV-PEKI 243
Cdd:cd12899   47 VMGSLIPVRGKHYWEVEVDEQTE-YRVGVAFEDTQRNGYLGANNTSWCMrHIITPSRHKYEFLHNGWTPDIRITVpPKKI 125
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767958435 244 GVFCDFDGGQLSFYDANSKQLLYSFKTKFTQPVLPGF 280
Cdd:cd12899  126 GILLDYDSGRLSFFNVDLAQHLYTFSCQFQHFVHPCF 162
SPRY_PRY_TRIM14 cd13738
PRY/SPRY domain of tripartite motif-binding protein 14 (TRIM14); This is a TRIM14 domain ...
166-290 3.09e-20

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: 85.99  E-value: 3.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 166 VLGDTAIESGQHYWEVKAQKDCKSYSVGVAYKTLGK-----FDQLGKTNTSWCIH---VNNWlqntfaAKHNNKVKALDV 237
Cdd:cd13738   43 VLSRDSFFSGRHYWEVDLQEAGAGWWVGAAYPSIGRkgdseAARLGWNRQSWCLKrydLEYW------AFHDGQRSRLRP 116
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767958435 238 TV-PEKIGVFCDFDGGQLSFYDANSKQL-LYSFKTKFTQPVLPGFMVWCGGLSLS 290
Cdd:cd13738  117 EDdPDRLGVFLDYEAGILSFYDVTGGMThLHTFRATFQEPLYPALRLWEGSISIC 171
SPRY_PRY_SPRYD4 cd12903
PRY/SPRY domain containing protein 4 (SPRYD4); This domain, consisting of the distinct ...
145-287 4.33e-20

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: 85.58  E-value: 4.33e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 145 VGSRPPAVRGSRDRFTgESYTVLGDTAIESGQHYWEVKAQKDcKSYSVGVAYKTLGKFDQLGKTNTSWcihVNNWLQNT- 223
Cdd:cd12903   26 LGVDPTKVPQNPERFR-DWAVVLGDTPVTSGRHYWEVTVKRS-QEFRIGVADVDMSRDECIGTNESSW---VFAYAQRKw 100
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767958435 224 FAAKHNNKVKALDVTVPEKIGVFCDFDGGQLSFYDANSKQLLYSFKTKFTQPVLPGFMVWCGGL 287
Cdd:cd12903  101 YAMVANETVPVPLVGKPDRVGLLLDYEAGKLSLVDVEKNSVVHTMSAEFRGPVVPAFALWDGEL 164
SPRY_PRY_C-I_1 cd13733
PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM5, TRIM6, TRIM7, ...
139-280 1.99e-19

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: 83.68  E-value: 1.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 139 SPKRTSV--GSRPPAVRGSRDRFTgESYTVLGDTAIESGQHYWEVKAqKDCKSYSVGVAYKTLgkfDQLGKTNTS----- 211
Cdd:cd13733   16 SEDLKSVryGDKRQNLPDNPERFD-TCVCVLGSEGFSSGRHYWEVEV-GGKTDWDLGVARESV---NRKGKITLSpengy 90
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767958435 212 WCIhvnnWLQNtfaakhNNKVKALD--------VTVPEKIGVFCDFDGGQLSFYDANSKQLLYSFKTKFTQPVLPGF 280
Cdd:cd13733   91 WTV----GLRN------GNEYKALTspstplslREKPQKVGVFLDYEEGQVSFYNVDDGSHIYTFTDCFTEKLYPYF 157
SPRY_PRY_TRIM69 cd15818
PRY/SPRY domain in tripartite motif-binding protein 69 (TRIM69), also known as RING finger ...
163-280 5.68e-18

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: 80.23  E-value: 5.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 163 SYTVLGDTAIESGQHYWEVKAQKDCKsYSVGVAYKTLGKFDQ--LGKTNTSWCIhvnnWLQNtfaakhNNKVKALDV--- 237
Cdd:cd15818   54 SVAVLGSEGFTSGKHYWEVEVAKKTK-WTLGVVRESINRKGNcpLSPEDGFWLL----RLRN------QNELKALDVpsf 122
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767958435 238 -----TVPEKIGVFCDFDGGQLSFYDANSKQLLYSFKTKFTQPVLPGF 280
Cdd:cd15818  123 sltltSNLNKVGIYLDYEGGQVSFYNANTMSHIYTFSDTFTEKIYPYF 170
SPRY_PRY_TRIM65 cd12896
PRY/SPRY domain in tripartite motif-containing domain 65 (TRIM65); This domain, consisting of ...
148-290 2.01e-17

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: 78.65  E-value: 2.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 148 RPPAVRGSRDRFTGESYTVLGDTAIESGQHYWEVKAQKdcKSYSVGVAYKTL------GKFDQLGKTNTSW--CIHvnnw 219
Cdd:cd12896   36 RSAARGVPASPGSFELWQVQCTQSFQHGHHYWEVEVSS--HSVTLGVTYPGLprhkqgGHKDNIGRNPCSWglQIQ---- 109
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958435 220 lQNTFAAKHNNKVKALDVTVPEKIGVFCDFDGGQLSFY-DANSKQLLYSFKTKFTQPVLPGFmvW-CGGLSLS 290
Cdd:cd12896  110 -EDSLQAWHNGRAQKLQGVSYRLLGVDLDLEAGTLTFYgLEPGTQRLHTFHAIFTQPLYPVF--WlLEGRTLT 179
SPRY_BSPRY cd12904
SPRY domain in Ro-Ret family; This domain, named BSPRY, has been identified in the Ro-Ret ...
128-282 5.64e-17

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: 77.08  E-value: 5.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 128 SLKKHTRSGTPSPKRTSVgsrppAVRGSRDRFtgESY-TVLGDTAIESGQHYWEVKAQKDCkSYSVGVAYKTL-----GK 201
Cdd:cd12904   13 SLSEDRRTLTFSPKKARQ-----SPPDDPERF--DHWpNALASLSFSSGTHAWVVDVGKSC-AYKVGVCYGSLerkgsGN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 202 FDQLGKTNTSWcihVNNWLQNTFAAKHNNKVKALDVT-VPEKIGVFCDFDGGQLSFYDANSKQLLYSFKTKFTQPVLPGF 280
Cdd:cd12904   85 EARLGYNAFSW---VFSRYDGEFSFSHNGQHVPLELLkCPARVGVLLDWPSQELLFYDPDSCTVLHSHREAFAAPLLPVF 161

                 ..
gi 767958435 281 MV 282
Cdd:cd12904  162 AV 163
SPRY_PRY_TRIM60 cd15828
PRY/SPRY domain of tripartite motif-binding protein 60 (TRIM60) also known as RING finger ...
119-280 2.61e-15

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: 72.71  E-value: 2.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 119 ENKGSVHVTSLKKHTrsgTPSPKRTSVGsrpPAVRGSrdrftgESYTvlgdtaieSGQHYWEVKAQKDCKsYSVGVAYKT 198
Cdd:cd15828   27 EDRKSVLYGEMKQNV---CYNPRRFYLC---PAVLGS------EGFH--------SGRQYWEVEVGDKPE-WTLGVCQDC 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 199 L--GKFDQLGKTNTSWCIhvNNWLQNTFAAKHNNKVKALDVTVPEKIGVFCDFDGGQLSFYDANSKQLLYSFKTKFTQPV 276
Cdd:cd15828   86 LprNWSNQPSVQDGLWAI--GRYSESNYVALGPKKIQLLPKVRPSKIGIFLDYELGEVSFYNMNDRSLLYTFSDSFTGTL 163

                 ....
gi 767958435 277 LPGF 280
Cdd:cd15828  164 WPYF 167
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
174-286 1.62e-14

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: 68.86  E-value: 1.62e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435   174 SGQHYWEVKAQKDcKSYSVGVAYKT--LGKFDQLGKTNTSWCIH---VNNWlqntfaakHNNKVKALDVTVPEK---IGV 245
Cdd:smart00449   1 SGRHYFEVEIGDG-GHWRVGVATKSvpRGYFALLGEDKGSWGYDgdgGKKY--------HNSTGPEYGLPLQEPgdvIGC 71
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 767958435   246 FCDFDGGQLSFYDANSKQLLYSFKT-KFTQPVLPGFMVWCGG 286
Cdd:smart00449  72 FLDLEAGTISFYKNGKYLHGLAFFDvKFSGPLYPAFSLGSGN 113
SPRY_PRY_TRIM25-like cd13737
PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25)-like; This domain, ...
166-285 6.75e-14

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: 68.74  E-value: 6.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 166 VLGDTAIESGQHYWEVKAQKD--CksysVGVAYK---TLGK---FDQLGKTNTSWCIHvnnWLQNTFAAKHNNKVKALDV 237
Cdd:cd13737   44 VLCTRSLCEGCHYWEAEVSNSwvC----LGVTYSyshPTGKsciFYLIGRNPYSWCLE---WDSLKFSVWHNNIQTVVHG 116
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767958435 238 TVPEKIGVFCDFDGGQLSFYD-ANSKQLLYSFKTKFTQPVLPGFMVWCG 285
Cdd:cd13737  117 SYYKTIGVLLDYAAGSLTFYGvANTMNLIYRFLTTFTEPLYPAVMVSSG 165
SPRY_PRY_TRIM60_75 cd15817
PRY/SPRY domain of tripartite motif-binding protein 60 and 75 (TRIM60 and TRIM75); This domain, ...
141-282 8.55e-14

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: 68.34  E-value: 8.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 141 KRTSVGSRPPAVRGSRDRFTgeSY-TVLGDTAIESGQHYWEVKAqKDCKSYSVGVAYKTLGKFDQLGKTNTSWCIHVNNW 219
Cdd:cd15817   20 KAVRYRRMKPNCPYDPRRFT--VYpAVLGSEGFDSGRHFWEVEV-GGKGEWILGVCKDSLPRNAQDPPSPLGGCWQIGRY 96
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958435 220 LqNTFAAKHNNKVKALDVTVPEKIGVFCDFDGGQLSFYDANSKQLLYSFKTKFTQPVLPGFMV 282
Cdd:cd15817   97 M-SGYVASGPKTTQLLPVVKPSRIGIFLDYELGEVSFYNMNDRSHLYTFTDTFTGKLIPYFYV 158
SPRY_PRY_A33L cd12905
zinc-binding protein A33-like; This domain, consisting of the distinct N-terminal PRY ...
139-280 8.70e-14

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: 68.59  E-value: 8.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 139 SPKRTSV--GSRPPAVRGSRDRFTgESYTVLGDTAIESGQHYWEVKAQKDCKsYSVGVAYKTLGKFD--QLGKTNTSWCI 214
Cdd:cd12905   20 SRDLTAVteSDEMQPYPRSPKRFL-QCVNVLASQGFQSGRHYWEVWVGSKTK-WDLGVASESVDRQArvKLCPENGYWTL 97
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767958435 215 HVNNwlQNTFAAKHNNKVKALDVTVPEKIGVFCDFDGGQLSFYDANSKQLLYSFKTKFTQPVLPGF 280
Cdd:cd12905   98 RLRN--GDEYWAGTQPWTRLRVTSRPQRIGVFLDCEERKVSFYNADDMSLLYSFHQGPRGKVFPFF 161
SPRY_PRY_TRIM15 cd15826
PRY/SPRY domain in tripartite motif-binding protein 15 (TRIM15); This domain, consisting of ...
158-289 2.52e-13

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: 66.81  E-value: 2.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 158 RFTGESyTVLGDTAIESGQHYWEVKAQK-DCKSYSVGVAYKTLGKFDQLGKTNTS--WCIHVNNwlQNTFAAKHNNKVKA 234
Cdd:cd15826   37 RFDGLP-AVLGSPGFSSGRHRWQVEVQLgDGGGCTVGVAGESVRRKGEMGLSAEDgvWAVILSH--QQCWASTSPGTDLP 113
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767958435 235 LDVTvPEKIGVFCDFDGGQLSFYDANSKQLLYSFKTKFTQPVLPGFMVWCGGLSL 289
Cdd:cd15826  114 LSEI-PRRVGVALDYEAGTVTLTNAETQEPIFTFTASFSGKVFPFFAVWKKGSRL 167
SPRY_PRY_TRIM35 cd12893
PRY/SPRY domain in tripartite motif-containing protein 35 (TRIM35); This PRY/SPRY domain is ...
143-289 7.17e-13

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: 65.73  E-value: 7.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 143 TSV--GSRPPAVRGSRDRFTGeSYTVLGDTAIESGQHYWEVKAqKDCKSYSVGVAYKTL---GKFDqLGKTNTSWCIhvn 217
Cdd:cd12893   20 TSVrySSEKQQLPDNPERFDP-YPCVLGSEGFTSGKHSWDVEV-GDNTSWMLGVAKESVqrkGKFT-LSPESGFWTI--- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 218 nWLqntfaakHNNKVKALD-------VTV---PEKIGVFCDFDGGQLSFYDANSKQLLYSFKTKFTQPVLPGFMVWCGGL 287
Cdd:cd12893   94 -GF-------SEGKYSARTspeprtpLRVkqkPQRIRVQLDWDRGKVSFSDPDTNTHIHTFTHTFTERVFPYFYTGCKSE 165

                 ..
gi 767958435 288 SL 289
Cdd:cd12893  166 PL 167
SPRY_PRY_TRIM75 cd15829
PRY/SPRY domain of tripartite motif-binding protein 75 (TRIM75); This domain, consisting of ...
148-284 1.37e-12

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: 65.39  E-value: 1.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 148 RPPAVRGSRDRFTGESyTVLGDTAIESGQHYWEVKAqKDCKSYSVGVAYKTL--GKFDQLGKTNTSWCIHvnnWLQNTFA 225
Cdd:cd15829   46 KKQRVPDSPKRFTVNP-VVLGFPGFHSGRHFWEVEV-GDKPEWAVGVCKDSLstKARRPPSGQQGCWRIQ---LQGGDYD 120
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767958435 226 AKHNNKVKALDVTVPEKIGVFCDFDGGQLSFYDANSKQLLYSFKTKFTQPVLPGFMVWC 284
Cdd:cd15829  121 APGAVPPPLLLEVKPRGIGVFLDYELGEISFYNMPEKSHIHTFTDTFSGPLRPYFYVGP 179
SPRY_PRY_BTN3 cd15820
PRY/SPRY domain of butyrophilin 3 (BTN3), includes BTN3A1, BTN3A2, BTN3A3 as well as BTN-like ...
158-280 2.45e-12

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: 64.37  E-value: 2.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 158 RFTGEsYTVLGDTAIESGQHYWEVKAqKDCKSYSVGVAYKTLGKFDQLGKT--NTSWCIHVNNwlQNTFAAKHNNKVKAL 235
Cdd:cd15820   41 RFDWH-YCVLGCKSFTSGRHFWEVEV-GDRKEWYVGVCRENVERKLWVKMApeNGFWTIGLSD--GNDYQALTDPRTKLT 116
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767958435 236 DVTVPEKIGVFCDFDGGQLSFYDANSKQLLYSF-KTKFTQPVLPGF 280
Cdd:cd15820  117 IANPPQRVGVFLDYETGEVSFYNAMDGSHIYTFpHTSFSGPLYPVF 162
SPRY_PRY_TRIM16 cd12890
PRY/SPRY domain in tripartite motif-containing protein 16 (TRIM16); This domain, consisting of ...
166-280 3.97e-12

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: 64.03  E-value: 3.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 166 VLGDTAIESGQHYWEVKAqKDCKSYsVGVAYKTLgkfDQLGK--------TNTSWCIHvnnWLQNTFAAKHNNKVKALDV 237
Cdd:cd12890   54 VLSQQSLYLGRYYFEVEI-SGEGTY-VGLTYKSI---DRKGSesnscisgNNFSWCLQ---WNGKEFSAWHSDVETPLKK 125
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767958435 238 TVPEKIGVFCDFDGGQLSFY--DANSKQLLYSFKTKFTQPVLPGF 280
Cdd:cd12890  126 GPFTRLGIYLDYPGGTLSFYgvEDDGMTLLHKFQCKFTEPLYPAF 170
SPRY_PRY_TRIM62 cd13744
PRY/SPRY domain in tripartite motif-binding protein 62 (TRIM62); This domain, consisting of ...
149-280 4.12e-12

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: 63.87  E-value: 4.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 149 PPAVRGSRDRFTGEsYTVLGDTAIESGQHYWEVKAQKDCKsYSVGVAYKTLGKFD--QLGKTNTSWCIHVNNwlQNTFAA 226
Cdd:cd13744   41 PQPLQDSPKRFDVE-VSVLGSEGFSGGVHYWEVVVSEKTQ-WMIGLAHEAVSRKGsiQIQPGRGFYCIVMHD--GNQYSA 116
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 227 ------KHNNKVKAldvtvpEKIGVFCDFDGGQLSFYDANSKQLLYSFKTKFTQPVLPGF 280
Cdd:cd13744  117 ctepwtRLNVKSKL------EKVGVYLDYDKGLLIFYNADDMSWLYTFREKFPGKLCSYF 170
SPRY_PRY_TRIM58 cd15816
PRY/SPRY domain in tripartite motif-binding protein 58 (TRIM58), also known as BIA2; This ...
146-282 5.14e-12

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: 63.27  E-value: 5.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 146 GSRPPAVRGSRDRFtgESY-TVLGDTAIESGQHYWEVkAQKDCKSYSVGVAYKTLGKfdqLGKTNTS-----WCIhvnnW 219
Cdd:cd15816   25 GELWRDVPGNPERF--DTWpCVLGLQSFSSGRHYWEV-AVGEKAEWGLGVCQDSAPR---KGETTPSpengvWAV----W 94
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767958435 220 L--QNTFAAKHNNKVKALDVTVPEKIGVFCDFDGGQLSFYDANSKQLLYSFKTKFTQPVLPGFMV 282
Cdd:cd15816   95 LlkGNEYMVLASPSVPLLQLRRPRRVGVFLDYEAGEISFYNVTAGSHIYTFRQLFSGILRPYFFV 159
SPRY_PRY_TRIM50 cd13743
PRY/SPRY domain in tripartite motif-binding protein 50 (TRIM50); This domain, consisting of ...
157-283 6.90e-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: 63.28  E-value: 6.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 157 DRFTgESYTVLGDTAIESGQHYWEVkaQKDCKS-YSVGVAYKTLGKFDQLGKT--NTSWCIHVNNwlQNTFAAKHNNKVK 233
Cdd:cd13743   48 ERFD-YSNCVLASRGFSSGKHYWEV--VVGSKSkWRLGLIKGTTSRKGKLNKSpeNGVWLIGLKE--GRVYEAFANPRVP 122
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767958435 234 ALDVTVPEKIGVFCDFDGGQLSFYDANSKQLL---YSFKTKFTQPVLPGF-MVW 283
Cdd:cd13743  123 LPLSTRPQRIGVFLDYEKGELTFYNADSPDELvpiYTFQAEFQGKLYPLLdVCW 176
SPRY_PRY_TRIM11 cd15811
PRY/SPRY domain of tripartite motif-binding protein 11 (TRIM11), also known as RING finger ...
139-280 7.61e-12

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: 62.67  E-value: 7.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 139 SPKRTSV--GSRPPAVRGSRDRFTgESYTVLGDTAIESGQHYWEVKAqKDCKSYSVGVAYKTLGKFD--QLGKTNTSWCI 214
Cdd:cd15811   16 SEDRRSVrrGDLRQALPDSPERFD-PGPCVLGRERFTSGRHYWEVEV-GDRTSWALGVCKENVNRKEkgELSAGNGFWIL 93
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 215 hvnnwlqnTFAAKHNNKVKALDVTV---PEKIGVFCDFDGGQLSFYDANSKQLLYSF-KTKFTQPVLPGF 280
Cdd:cd15811   94 --------VFLGNYYSSERRTFAPLrdpPRRVGIFLDYEAGHLSFYSATDGSLLFIFpETPFSGTLRPLF 155
SPRY_PRY_TRIM5_6_22_34 cd15810
PRY/SPRY domain of tripartite motif-binding protein 5, 6, 22 and 34 (TRIM5, TRIM6, TRIM22 and ...
139-283 8.98e-12

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: 62.88  E-value: 8.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 139 SPKRTSVGSRPPAVRGSRDRFTGESYTVLGDTAIESGQHYWEV--------------KAQKDCKSYSVGVAYKTLGKFDQ 204
Cdd:cd15810   16 SEDQRQVRIVPPQTSGQALTNNNYDFGVLGSQYFSSGKHYWEVdvskksawilgvcsHKRSDAMTKSNANQINHQNVYSR 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 205 LGKTNTSWCIHVNNWLQ-NTF--AAKHNNKVKALDVTV-PEKIGVFCDFDGGQLSFYD-ANSKQLLYSF-KTKFTQPVLP 278
Cdd:cd15810   96 YQPQYGYWVIGLQNESEyNAFedSSSFNPHVLTLSVTVpPHRVGVFLDYEAGTVSFFNvTNHGSLIYKFsKCCFSTTVCP 175

                 ....*
gi 767958435 279 GFMVW 283
Cdd:cd15810  176 YFNPW 180
SPRY_PRY_TRIM34 cd15825
PRY/SPRY domain in tripartite motif-containing protein 34 (TRIM34), also known as RING finger ...
159-283 1.19e-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: 62.55  E-value: 1.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 159 FTGESYTVLGDTAIESGQHYWEVKAQKD--------CKSYSVGVAYKTLGKFDQLGKT-----NTSWCIHVNNWLQ-NTF 224
Cdd:cd15825   32 FKCYNYGILGSQYFSSGKHYWEVDVSKKtawilgvyCRKRSRTFKYVRQGKNHPNVYSryrpqYGYWVIGLQNKSEyYAF 111
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767958435 225 --AAKHNNKVKALDVTVP-EKIGVFCDFDGGQLSFYD-ANSKQLLYSF-KTKFTQPVLPGFMVW 283
Cdd:cd15825  112 edSSTSDPKVLTLSVATPpHRVGVFLDYEAGTVSFFNvTNHGSLIYKFsKCCFSQPVYPYFNPW 175
SPRY_PRY_TRIM5 cd15822
PRY/SPRY domain in tripartite motif-binding protein 5 (TRIM5), also known as RING finger ...
162-280 2.68e-11

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: 61.86  E-value: 2.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 162 ESYTVLGDTAIESGQHYWEVK-AQKD-------CKSYSvGVAYKTLGKFDQLGKTNTS--------WCIhvnnWLQNTF- 224
Cdd:cd15822   49 EDYGVLGSPSITSGKHYWEVDvSKKRawilgvcGGKYP-NSTLKDFNKQGKNNQKQCSnyqpkygyWVI----GLQNKSe 123
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767958435 225 ------AAKHNNKVKALDVTVPEK-IGVFCDFDGGQLSFYDA-NSKQLLYSFKT-KFTQPVLPGF 280
Cdd:cd15822  124 ynafedSSSSDPLILTLSLTVPPCrVGVFLDYEAGTVSFFNVtNHGFLIYKFSScSFSQEVFPYF 188
SPRY_PRY_TRIM41 cd13741
PRY/SPRY domain in tripartite motif-binding protein 41 (TRIM41); This domain, consisting of ...
139-286 3.77e-11

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: 61.32  E-value: 3.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 139 SPKRTSV--GSRPPAVRGSRDRFTGEsYTVLGDTAIESGQHYWEVKAQKDcKSYSVGVAYKTLGKFDQLGKTNTS----- 211
Cdd:cd13741   16 SPDRRGVrlAERRQEVPEHPKRFSAD-CCVLGAQGFRSGRHYWEVEVGGR-RGWAVGAARESTHHKEKVGSGGSSvssgd 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 212 -------------------------WCIHVNNwlqNTFAAKHNNKVKALDVT-VPEKIGVFCDFDGGQLSFYDANSKQLL 265
Cdd:cd13741   94 asssrhhhrrrrlhlpqqpllqrevWCVGTNG---KRYQAQSSTEQTLLSPSeKPRRFGVYLDYEAGRLGFYNAETLAHV 170
                        170       180
                 ....*....|....*....|..
gi 767958435 266 YSFKTKF-TQPVLPGFMVWCGG 286
Cdd:cd13741  171 HTFSAAFlGERVFPFFRVLSKG 192
SPRY_PRY_TRIM21 cd12900
PRY/SPRY domain in tripartite motif-binding protein 21 (TRIM21) also known as 52kD ...
124-280 7.93e-11

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: 60.28  E-value: 7.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 124 VHVTsLKKHTRSG----TPSPKRTSVGSRPPAVRGSRDRFtgESY-TVLGDTAIESGQHYWEVKAQKDcKSYSVGV---A 195
Cdd:cd12900    3 VHIT-LDPDTANPwlilSKDRRQVRLGDTHQNVPENEERF--DNYpMVLGAQRFNSGKHYWEVDVTGK-EAWDLGVcrdS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 196 YKTLGKFdQLGKTNTSWCIhvnnWLQNTFAAKHNNKVKALDVTVPE-KIGVFCDFDGGQLSFYD-ANSKQLLYSF-KTKF 272
Cdd:cd12900   79 VRRKGQF-LLSPENGFWTI----WLWNKKYEAGTSPQTTLHLQVPPcQVGIFLDYEAGVVSFYNiTDHGSLIYTFsECAF 153

                 ....*...
gi 767958435 273 TQPVLPGF 280
Cdd:cd12900  154 TGPLRPFF 161
SPRY_PRY_TRIM7_like cd12888
PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7)-like, including TRIM7, TRIM10, ...
158-290 7.17e-10

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: 57.18  E-value: 7.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 158 RFTGEsYTVLGDTAIESGQHYWEVKAQkDCKSYSVGVAYKTLGK-----FDQLGKTntsWCIHVNNWLqntFAAKHNNKV 232
Cdd:cd12888   37 RFDTW-PCVLGCEGFTSGRHYWEVEVG-DGGGWAVGVARESVRRkgeisFSPEEGI---WAVGQWGGQ---YWALTSPET 108
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767958435 233 KALDVTVPEKIGVFCDFDGGQLSFYDANSKQLLYSFKTKF--TQPVLPGFMVWCG-GLSLS 290
Cdd:cd12888  109 PLPLSEVPRRIRVYLDYEGGQVAFFDADNEAPIFTFPPASfaGERIFPWFWVGKGsQLKLC 169
SPRY_PRY_BTN1_2 cd15819
butyrophilin subfamily member A1 and A2 (BTN1A and BTN2A); This domain, consisting of the ...
166-283 1.17e-09

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: 56.47  E-value: 1.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 166 VLGDTAIESGQHYWEVKAQkDCKSYSVGVAYKTLGKfdqlgktntSWCIHVNNwlQNTFAA--KHNNKVKALdvTVPE-- 241
Cdd:cd15819   46 VLGQEGFTSGRHYWEVEVG-DRTSWDLGVCRDNVMR---------KGRVTLSP--ENGFWAirLYGNEYWAL--TSPEtp 111
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767958435 242 --------KIGVFCDFDGGQLSFYDANSKQLLYSF-KTKFTQPVLPGFMVW 283
Cdd:cd15819  112 ltlkepprRVGIFLDYEAGDVSFYNMTDGSHIYTFpQTAFSGPLRPFFRLW 162
SPRY_PRY_TRIM17 cd15812
PRY/SPRY domain of tripartite motif-binding protein 17 (TRIM17), also known as testis RING ...
139-300 3.36e-09

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: 55.28  E-value: 3.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 139 SPKRTSVGSRPPAVRGSRDRFTGESYTVlGDTAIESGQHYWEVKAQKDCKS-YSVGVAYKTLGKFDQLGKT--NTSWCIh 215
Cdd:cd15812   18 SRQRRYLSTPPDGTPCSKDRFLAYPCAV-GQETFSSGRHYWEVGMNLTGDAlWALGVCRDNVSRKDRVPKSpeNGFWVV- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 216 vnnwlQNTFAAKHNNKVKALD-VTV---PEKIGVFCDFDGGQLSFYDANSKQLLYSF-KTKFTQPVLPGFmvwCGGlSLS 290
Cdd:cd15812   96 -----QLSKGKKYLSAMSALTpVTLtepPSHMGIFLDFEAGEVSFYSVNDGSHLHTYsQAAFPGPLQPFF---CLG-APK 166
                        170
                 ....*....|
gi 767958435 291 TGMQVPSAVR 300
Cdd:cd15812  167 SGQMVISTVT 176
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
177-280 1.27e-08

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: 52.35  E-value: 1.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435  177 HYWEVKAQKDCK-SYSVGVAYKT--LGKFDQLGKTNTSWCIHVNN---WLQNTFAAKHNNKVKALDVtvpekIGVFCDFD 250
Cdd:pfam00622   2 HYFEVEIFGQDGgGWRVGWATKSvpRKGERFLGDESGSWGYDGWTgkkYWASTSPLTGLPLFEPGDV-----IGCFLDYE 76
                          90       100       110
                  ....*....|....*....|....*....|.
gi 767958435  251 GGQLSFYDaNSKQLLYSFKT-KFTQPVLPGF 280
Cdd:pfam00622  77 AGTISFTK-NGKSLGYAFRDvPFAGPLFPAV 106
SPRY_PRY_TRIM67_9 cd12889
PRY/SPRY domain in tripartite motif-containing proteins, TRIM9 and TRIM67; This domain, ...
160-296 2.35e-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: 52.63  E-value: 2.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 160 TGESY---TVLGDTAIESGQHYWEVK-----AQKDCksySVGVAYKTLGKFDQLGKTNTSWCIHVNN---WLQNtfAAKH 228
Cdd:cd12889   31 TCNSYedrVVLGSVGFSRGVHYWEVTidrydGHPDP---AFGVARIDVNKDKMLGKDDKGWSMYIDNnrsWFLH--NNEH 105
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767958435 229 NNKVKAlDVTVPEKIGVFCDFDGGQLSFYDANSKQLLYSFKTKFTQpVLPGFMVWCG-GLSLSTGMQVP 296
Cdd:cd12889  106 SNRTEG-GITVGSVVGVLLDLDRHTLSFYVNDEPQGPIAFRNLPGV-FYPAVSLNRNvQVTLHTGLEPP 172
SPRY_PRY_TRIM27 cd15814
PRY/SPRY domain in tripartite motif-containing protein 27 (TRIM27), also known as RING finger ...
166-288 2.52e-08

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: 52.77  E-value: 2.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 166 VLGDTAIESGQHYWEVKAQKDCKsYSVGVAYKTLGKFDQL--GKTNTSWCIHVnnWLQNTFAAKhNNKVKALDVTVP-EK 242
Cdd:cd15814   46 VLGSPCFIAGRHYWEVEVGDKAK-WTIGVCEDSVCRKGGVtsAPQNGFWAVSL--WYGKEYWAL-TSPMTALPLRTPlQR 121
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767958435 243 IGVFCDFDGGQLSFYDANSKQLLYSFK-TKFTQPVLPGF-MVWCGGLS 288
Cdd:cd15814  122 VGIFLDYDAGEVSFYNVTERCHTFTFShATFCGPVRPYFsLSYSGGKS 169
SPRY_PRY_TRIM22 cd15824
PRY/SPRY domain in tripartite motif-containing protein 22 (TRIM22), also known as RING finger ...
163-283 2.57e-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: 53.31  E-value: 2.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 163 SYTVLGDTAIESGQHYWEV--------------KAQKDCKSYSVGVAYKTLGK----FDQLGKTNTSWCIHVNNWLQ-NT 223
Cdd:cd15824   43 AFDVLGCQYFSSGKYYWEVdvsgkiawilgvysKRNNLNKRKSSGFAFDPNVNhpnvYSRYRPQNGYWVIGLQNESEyNA 122
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767958435 224 FAAKHNNKVKALDVTV---PEKIGVFCDFDGGQLSFYD-ANSKQLLYSF-KTKFTQPVLPGFMVW 283
Cdd:cd15824  123 FEDSSSSDPKVLTLSMavpPHRVGVFLDYEAGTVSFFNvTNHGSLIYKFsKCCFSQPVYPYFNPW 187
SPRY_PRY_TRIM39 cd13745
PRY/SPRY domain in tripartite motif-binding protein 39 (TRIM39) and TRIM39-like; This domain, ...
158-280 4.07e-08

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: 52.24  E-value: 4.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 158 RFTgeSY-TVLGDTAIESGQHYWEVKAqKDCKSYSVGVAYKTL---GKFDqLGKTNTSWCIhvnnWLQNtfaakhnNKVK 233
Cdd:cd13745   40 RFD--TYpCVLGAEGFTGGRHYWEVEV-GDKTEWTLGVCRESVsrkGEVT-LSPENGYWTV----WLRD-------GKYE 104
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767958435 234 A-------LDVTV-PEKIGVFCDFDGGQLSFYDANSKQLLYSFKTKFTQPVLPGF 280
Cdd:cd13745  105 AltspptpLPVSVrPSRVGIFLDYEAGEVSFYNVTDRSHLFTFTDTFSGTLRPYF 159
SPRY_PRY_TRIM50_72 cd12897
PRY/SPRY domain in tripartite motif-binding (TRIM) proteins TRIM50 and TRIM72; This domain, ...
153-283 5.39e-08

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: 52.23  E-value: 5.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 153 RGSRDRFTGESYTVLGDTAIESGQHYWEVKAQkDCKSYSVGVAYKTLGKFDQLGKT--NTSWCIHVNnwlQNTFAAKHNN 230
Cdd:cd12897   43 RASQPERFDKSTCVVASQGFSEGEHYWEVVVG-DKPRWALGVIKGTASRKGKLHASpsHGVWLIGLK---EGKVYEAHGE 118
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 231 KVKALDVTV---PEKIGVFCDFDGGQLSFYDANSK---QLLYSFKTKFTQPVLPGFMV-W 283
Cdd:cd12897  119 PKEPRPLRVagrPHRIGVYLSFEDGVLSFFDASDPddlRTLYTFQERFQGKLYPFFDVcW 178
SPRY_PRY_TRIM7 cd13740
PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7); This domain, consisting of the ...
141-282 6.29e-08

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: 51.50  E-value: 6.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 141 KRTSVGSRPPAVRGSRDRFTGESyTVLGDTAIESGQHYWEVK-AQKDckSYSVGVAYKTLGK--FDQLGKTNTSWCIHVN 217
Cdd:cd13740   20 KSVRLGERAQDLPNHPCRFDTNT-RVLASCGFSSGRHHWEVEvGSKD--GWAFGVARESVRRkgLTPFTPEEGVWALQLN 96
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767958435 218 N---WLqntfaakhnnkvkaldVTVPE----------KIGVFCDFDGGQLSFYDANSKQLLYSFKTKFTQPVLPGFMV 282
Cdd:cd13740   97 GgqyWA----------------VTSPErtplscghlsRVRVALDLEVGAVSFYAAEDMRHIYTFRVNFQERVFPLFSV 158
SPRY_PRY_TRIM72 cd13742
PRY/SPRY domain in tripartite motif-binding protein 72 (TRIM72); This domain, consisting of ...
141-282 7.03e-08

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: 51.78  E-value: 7.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 141 KRTSVGSRPPAVRGSRDRFTGESYTVLGDTAIESGQHYWEVkAQKDCKSYSVGVAYKTLGKFDQLGKT--NTSWCIHVNN 218
Cdd:cd13742   32 KRVECADQKQAVSSDDPNRFDKANCVVSHQSFSEGEHYWEV-IVGDKPRWALGVISAEAGRKGRLHALpsNGFWLLGCKE 110
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767958435 219 wlQNTFAAKHNNK-VKALDVTV-PEKIGVFCDFDGGQLSFYDANSKQ---LLYSFKTKFTQPVLPGFMV 282
Cdd:cd13742  111 --GKVYEAHVEHKePRALRVEGrPTRIGVYLSFSDGVLSFYDASDEDnlvQLFAFHERFPGPLYPFFDV 177
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
2-78 1.69e-07

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 48.65  E-value: 1.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435   2 PEEDN-KIDHFILEHRKTNFDGlprvkdercWEIIDN--IKGTEYTLSGLKFDSKYmNFRVRACNKAVAGEYSDPVTLET 78
Cdd:cd00063   24 PEDDGgPITGYVVEYREKGSGD---------WKEVEVtpGSETSYTLTGLKPGTEY-EFRVRAVNGGGESPPSESVTVTT 93
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
175-257 3.92e-07

SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit Ryanodine receptor (hence the name), are homologous to B30.2. SPRY domains have been identified in at least 11 protein families, covering a wide range of functions, including regulation of cytokine signaling (SOCS), RNA metabolism (DDX1 and hnRNP), immunity to retroviruses (TRIM5alpha), intracellular calcium release (ryanodine receptors or RyR) and regulatory and developmental processes (HERC1 and Ash2L). B30.2 also contains residues in the N-terminus that form a distinct PRY domain structure; i.e. B30.2 domain consists of PRY and SPRY subdomains. B30.2 domains comprise the C-terminus of three protein families: BTNs (receptor glycoproteins of immunoglobulin superfamily); several TRIM proteins (composed of RING/B-box/coiled-coil or RBCC core); Stonutoxin (secreted poisonous protein of the stonefish Synanceia horrida). TRIM/RBCC proteins are involved in a variety of processes, including apoptosis, cell cycle regulation, cell growth, senescence, viral response, meiosis, cell differentiation, and vesicular transport. Genes belonging to this family are implicated in several human diseases that vary from cancer to rare genetic syndromes. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site. While SPRY domains are evolutionarily ancient, B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. Mutations found in the SPRY-containing proteins have shown to cause Mediterranean fever and Opitz syndrome.


Pssm-ID: 293931  Cd Length: 118  Bit Score: 48.20  E-value: 3.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 175 GQHYWEVKAQK-DCKSYSVGVA--YKTLGKFDQLGKTNTSWCIHVNNWLQNTFAAKHNN--KVKALDVtvpekIGVFCDF 249
Cdd:cd11709    1 GKWYWEVRVDSgNGGLIQVGWAtkSFSLDGEGGVGDDEESWGYDGSRLRKGHGGSSGPGgrPWKSGDV-----VGCLLDL 75

                 ....*...
gi 767958435 250 DGGQLSFY 257
Cdd:cd11709   76 DEGTLSFS 83
SPRY_PRY_TRIM6 cd15823
PRY/SPRY domain in tripartite motif-binding protein 6 (TRIM6), also known as RING finger ...
152-280 1.39e-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: 47.93  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 152 VRGSRDRFTGESY-------TVLGDTAIESGQHYWEVKAQKDcKSYSVGVAYKTLG---KFDQLGKTNTSWCIHVNNWLQ 221
Cdd:cd15823   25 VRFVGAKLSGPSYleehydcSVLGSQHFSSGKHYWEVDVTKK-TAWILGVCSHSLGptfSFNQYAQNHNAYSRYQPQSGY 103
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767958435 222 NTFAAKHNNKVKA---------LDVTVP-EKIGVFCDFDGGQLSFYDANSKQL-LYSF-KTKFTQPVLPGF 280
Cdd:cd15823  104 WVIGLQHNHEYRAyedsstsllLSMTVPpRRVGVFLDYEAGTVSFYNVTNHGFpIYTFsKYYFPTTLCPYF 174
SPRY_PRY_TRIM36 cd12894
PRY/SPRY domain in tripartite motif-containing protein 36 (TRIM36); This domain, consisting of ...
139-286 2.52e-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: 47.45  E-value: 2.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 139 SPKRTSVGSRP--PAVRGSrDRFTGESYTVL----GDTAIESGQHYWEVKAQKDCKSYSVGVAYK-------------TL 199
Cdd:cd12894   17 NARRDSVESRAgfSLLLGA-ERIQVGCYTSLdyiiGDTGITKGKHFWAFRVEPYSYLVKVGVASDsklqewfhnprdiSS 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 200 GKFDQ-----LGKTNTSWCIH-----VNNWLQNTFAAK-------HNNKVkaldVTVPEKIGVFCDFDGGQLSFYDANSK 262
Cdd:cd12894   96 PRYDQdsghdSGSEDTSFDSSqpftlVTIGMKKLFIPKssassgdAENRV----LPLPTRIGICLDYDKGKVGFYDADSM 171
                        170       180
                 ....*....|....*....|....
gi 767958435 263 QLLYSFKTKFTQPVLPGFMVWCGG 286
Cdd:cd12894  172 KCLYERQVDCSGTMYPAFALMGSG 195
SPRY_PRY_TRIM4 cd15809
PRY/SPRY domain in tripartite motif-binding protein 4 (TRIM4), also known as RING finger ...
166-280 2.98e-06

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: 47.13  E-value: 2.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 166 VLGDTAIESGQHYWEVKaQKDCKSYSVGVAYKtlgkfDQLGKTNTS--------WCIHVNN---WLQNTFAAKHNNKVKA 234
Cdd:cd15809   66 VLGKNVFTSGKHYWEVE-NRDSLEIAVGVCRE-----DVMGITDGSemsphvgiWAICWSSagyRPLTSSPVSPTKQEPA 139
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767958435 235 LdvtvpEKIGVFCDFDGGQLSFYDANSKQLLYSFKTKFTQPVLPGF 280
Cdd:cd15809  140 L-----HRVGVFLDHGAGEVSFYSAVDGVHLHTFSCPLVSRLRPFF 180
SPRY_PRY_TRIM10 cd15827
PRY/SPRY domain of tripartite motif-binding protein 10 (TRIM10) also known as hematopoietic ...
240-290 2.06e-05

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


Pssm-ID: 293999 [Multi-domain]  Cd Length: 172  Bit Score: 44.44  E-value: 2.06e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767958435 240 PEKIGVFCDFDGGQLSFYDANSKQLLYSFKTKFTQPVLPGFMVWCGGLSLS 290
Cdd:cd15827  120 PRQVRVSLDYEVGWVTFVNAVTQEPIYTFTASFTQKVFPFFGLWGRGSSFS 170
SPRY_SOCS_Fbox cd12875
SPRY domain in Fbxo45 and suppressors of cytokine signaling (SOCS) proteins; This family ...
168-264 1.19e-04

SPRY domain in Fbxo45 and suppressors of cytokine signaling (SOCS) proteins; This family consists of the SPRY domain-containing SOCS box protein family (SPSB1-4, also known as SSB-1 to -4) as well as F-box protein 45 (Fbxo45), a novel synaptic E3 and ubiquitin ligase. The SPSB protein is composed of a central SPRY protein interaction domain and a C-terminal SOCS box. SPSB1, SPSB2, and SPSB4 interact with prostate apoptosis response protein 4 (Par-4) and are negative regulators that recruit the ECS E3 ubiquitin ligase complex to polyubiquitinate inducible nitric-oxide synthase (iNOS), resulting in its proteasomal degradation. Fbxo45 is related to this family; it is located N-terminal to the SPRY domain, and known to induce the degradation of a synaptic vesicle-priming factor, Munc13-1, via the SPRY domain, thus playing an important role in the regulation of neurotransmission by modulating Munc13-1 at the synapse. Suppressor of cytokine signaling (SOCS) proteins negatively regulate signaling from JAK-associated cytokine receptor complexes, and play key roles in the regulation of immune homeostasis.


Pssm-ID: 293935  Cd Length: 169  Bit Score: 42.06  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 168 GDTAIESGQHYWEVKAQKDCKSYS--VGVAYK-----TLGKFDQLGKTNTSWcihvnNWLQNTFAAKHNNKV-------K 233
Cdd:cd12875   35 GKKGYTRGLHAWEVKWISRPRGSHavVGVATKdaplqCDGYVTLLGSNSESW-----GWDLGDNKLYHNGKKvigsypaK 109
                         90       100       110
                 ....*....|....*....|....*....|.
gi 767958435 234 ALDVTVPEKIGVFCDFDGGQLSFyDANSKQL 264
Cdd:cd12875  110 SENYQVPDRILVILDMEDGTLAF-EANGEYL 139
SPRY_PRY_TRIM46 cd12895
PRY/SPRY domain in tripartite motif-containing protein 46 (TRIM46); This domain, consisting of ...
166-286 1.62e-03

PRY/SPRY domain in tripartite motif-containing protein 46 (TRIM46); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM46 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 yet been characterized.


Pssm-ID: 293952  Cd Length: 209  Bit Score: 39.08  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 166 VLGDTAIESGQHYW-----------------EVKAQK------------------------DCKSYSVGVAYKTLGkfdq 204
Cdd:cd12895   50 VVGDVAITQGRSYWacsvdpgsylvkvgvglESKLQEwfqlpqdvvsprydpdsghdsgaeDATVESPPFAFLTMG---- 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958435 205 LGKTNTSwcIHVNNWLQNTfaaKHNNKVKALDVTVPEKIGVFCDFDGGQLSFYDANSKQLLYSFKTKFTQPVLPGFMVWC 284
Cdd:cd12895  126 MGKIYLP--SSVSSGHGLT---GRDGPPAGCTVPLPPRLGICLDYEKGRVSFYDAVSFRPLWECPVDCSGPVCPAFCFIG 200

                 ..
gi 767958435 285 GG 286
Cdd:cd12895  201 GG 202
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
2-65 2.32e-03

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 36.44  E-value: 2.32e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767958435     2 PEEDNKIDHFILEHRKTNfdglpRVKDERCWEIIDNIKGTEYTLSGLKFDSKYmNFRVRACNKA 65
Cdd:smart00060  23 PPPDDGITGYIVGYRVEY-----REEGSEWKEVNVTPSSTSYTLTGLKPGTEY-EFRVRAVNGA 80
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
32-78 4.93e-03

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 38.44  E-value: 4.93e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 767958435  32 WEIIDNIKGTEYTLSGLKFDSKYmNFRVRACNKA-VAGEYSDPVTLET 78
Cdd:COG3401  276 FTKVATVTTTSYTDTGLTNGTTY-YYRVTAVDAAgNESAPSNVVSVTT 322
 
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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