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Conserved domains on  [gi|2462542783|ref|XP_054233276|]
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fibronectin type III and SPRY domain-containing protein 2 isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SPRY_PRY_TRIM76_like cd12899
PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76)-like; This domain is ...
488-663 7.40e-123

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: 362.18  E-value: 7.40e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 488 YFRLNKDTCHPWLTISEDGLTAVRSERRTPARELSPSDTHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADVR 567
Cdd:cd12899     1 YFHLNEDTAHPLLSISEDGFTVVYGEEELPARDLSFSDNSFTRCVAVMGSLIPVRGKHYWEVEVDEQTEYRVGVAFEDTQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 568 KQEDLGANCLSWCMRHTFASSRHKYEFLHNRTTPDIRITVPPKKIGILLDYEHSKLSFFNVDLSQHLYTFSCQLHKFVHP 647
Cdd:cd12899    81 RNGYLGANNTSWCMRHIITPSRHKYEFLHNGWTPDIRITVPPKKIGILLDYDSGRLSFFNVDLAQHLYTFSCQFQHFVHP 160
                         170
                  ....*....|....*.
gi 2462542783 648 CFSLEKPGCLKVHNGI 663
Cdd:cd12899   161 CFSLEKPGALKVHNGI 176
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
295-380 1.76e-14

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: 69.18  E-value: 1.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783  295 PSAPViNPQVPNSaTGSSVRVCWSLYSDDTVESYQLSYRpVQDSSPGTDQAEFTVTVKETYCSVTNLVPNTQYEFWVTAH 374
Cdd:smart00060   1 PSPPS-NLRVTDV-TSTSVTLSWEPPPDDGITGYIVGYR-VEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                   ....*.
gi 2462542783  375 NRAGPS 380
Cdd:smart00060  78 NGAGEG 83
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
294-484 4.52e-11

Fibronectin type 3 domain [General function prediction only];


The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 65.79  E-value: 4.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 294 APSAPViNPQVpNSATGSSVRVCWSLYSDDTVESYQLsYRpvQDSSPGTdqaeFTV--TVKETYCSVTNLVPNTQYEFWV 371
Cdd:COG3401   232 PPSAPT-GLTA-TADTPGSVTLSWDPVTESDATGYRV-YR--SNSGDGP----FTKvaTVTTTSYTDTGLTNGTTYYYRV 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 372 TAHNRAG----PSPSSERAVYMTAPSPPIIKTKEIRSCEEAVLIcWESGNLNPVDSYTVELTQAESPEASGVTESVVGip 447
Cdd:COG3401   303 TAVDAAGnesaPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLS-WTASSDADVTGYNVYRSTSGGGTYTKIAETVTT-- 379
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462542783 448 TCESVVQLQPGRSYIIYVRALNMGGP-SVRSEPATVHT 484
Cdd:COG3401   380 TSYTDTGLTPGTTYYYKVTAVDAAGNeSAPSEEVSATT 417
Bbox_SF super family cl00034
B-box-type zinc finger superfamily; The B-box-type zinc finger is a short zinc binding domain ...
178-205 5.87e-04

B-box-type zinc finger superfamily; The B-box-type zinc finger is a short zinc binding domain of around 40 amino acid residues in length. It has been found in transcription factors, ribonucleoproteins and proto-oncoproteins, such as in TRIM (tripartite motif) proteins that consist of an N-terminal RING finger (originally called an A-box), followed by 1-2 B-box domains and a coiled-coil domain (also called RBCC for Ring, B-box, Coiled-Coil). The B-box-type zinc finger often presents in combination with other motifs, like RING zinc finger, NHL motif, coiled-coil or RFP domain in functionally unrelated proteins, most likely mediating protein-protein interactions. Based on different consensus sequences and the spacing of the 7-8 zinc-binding residues, B-box-type zinc fingers can be divided into two groups, type 1 (Bbox1: C6H2) and type 2 (Bbox2: CHC3H2).


The actual alignment was detected with superfamily member cd19788:

Pssm-ID: 469587  Cd Length: 39  Bit Score: 37.83  E-value: 5.87e-04
                          10        20
                  ....*....|....*....|....*...
gi 2462542783 178 VFCVTCKTPIRAFQKVFDEHKEHEVIPL 205
Cdd:cd19788    12 IYCLTCEVPTCSMCKVFGAHKDCEVAPL 39
 
Name Accession Description Interval E-value
SPRY_PRY_TRIM76_like cd12899
PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76)-like; This domain is ...
488-663 7.40e-123

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: 362.18  E-value: 7.40e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 488 YFRLNKDTCHPWLTISEDGLTAVRSERRTPARELSPSDTHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADVR 567
Cdd:cd12899     1 YFHLNEDTAHPLLSISEDGFTVVYGEEELPARDLSFSDNSFTRCVAVMGSLIPVRGKHYWEVEVDEQTEYRVGVAFEDTQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 568 KQEDLGANCLSWCMRHTFASSRHKYEFLHNRTTPDIRITVPPKKIGILLDYEHSKLSFFNVDLSQHLYTFSCQLHKFVHP 647
Cdd:cd12899    81 RNGYLGANNTSWCMRHIITPSRHKYEFLHNGWTPDIRITVPPKKIGILLDYDSGRLSFFNVDLAQHLYTFSCQFQHFVHP 160
                         170
                  ....*....|....*.
gi 2462542783 648 CFSLEKPGCLKVHNGI 663
Cdd:cd12899   161 CFSLEKPGALKVHNGI 176
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
295-380 1.76e-14

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: 69.18  E-value: 1.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783  295 PSAPViNPQVPNSaTGSSVRVCWSLYSDDTVESYQLSYRpVQDSSPGTDQAEFTVTVKETYCSVTNLVPNTQYEFWVTAH 374
Cdd:smart00060   1 PSPPS-NLRVTDV-TSTSVTLSWEPPPDDGITGYIVGYR-VEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                   ....*.
gi 2462542783  375 NRAGPS 380
Cdd:smart00060  78 NGAGEG 83
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
542-659 1.76e-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: 70.40  E-value: 1.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783  542 RGHHYWEVEVDEHLDYRVGVAFADVR--KQEDLGANCLSWCMRhtfASSRHKYeflHNRTTPDIRITV--PPKKIGILLD 617
Cdd:smart00449   1 SGRHYFEVEIGDGGHWRVGVATKSVPrgYFALLGEDKGSWGYD---GDGGKKY---HNSTGPEYGLPLqePGDVIGCFLD 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2462542783  618 YEHSKLSFFNV-DLSQHLYTFSCQLHKFVHPCFSLEKPGCLKV 659
Cdd:smart00449  75 LEAGTISFYKNgKYLHGLAFFDVKFSGPLYPAFSLGSGNSVRL 117
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
295-390 3.34e-13

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: 65.60  E-value: 3.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 295 PSAPViNPQVpNSATGSSVRVCWSLYSDDT--VESYQLSYRPVQDSSPGTDQaefTVTVKETYCSVTNLVPNTQYEFWVT 372
Cdd:cd00063     1 PSPPT-NLRV-TDVTSTSVTLSWTPPEDDGgpITGYVVEYREKGSGDWKEVE---VTPGSETSYTLTGLKPGTEYEFRVR 75
                          90
                  ....*....|....*...
gi 2462542783 373 AHNRAGPSPSSERAVYMT 390
Cdd:cd00063    76 AVNGGGESPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
293-383 2.32e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.20  E-value: 2.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 293 PAPSAPVINPQvpnsaTGSSVRVCWS--LYSDDTVESYQLSYRPVQDSSPGTdqaEFTVTVKETYCSVTNLVPNTQYEFW 370
Cdd:pfam00041   1 SAPSNLTVTDV-----TSTSLTVSWTppPDGNGPITGYEVEYRPKNSGEPWN---EITVPGTTTSVTLTGLKPGTEYEVR 72
                          90
                  ....*....|...
gi 2462542783 371 VTAHNRAGPSPSS 383
Cdd:pfam00041  73 VQAVNGGGEGPPS 85
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
294-484 4.52e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 65.79  E-value: 4.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 294 APSAPViNPQVpNSATGSSVRVCWSLYSDDTVESYQLsYRpvQDSSPGTdqaeFTV--TVKETYCSVTNLVPNTQYEFWV 371
Cdd:COG3401   232 PPSAPT-GLTA-TADTPGSVTLSWDPVTESDATGYRV-YR--SNSGDGP----FTKvaTVTTTSYTDTGLTNGTTYYYRV 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 372 TAHNRAG----PSPSSERAVYMTAPSPPIIKTKEIRSCEEAVLIcWESGNLNPVDSYTVELTQAESPEASGVTESVVGip 447
Cdd:COG3401   303 TAVDAAGnesaPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLS-WTASSDADVTGYNVYRSTSGGGTYTKIAETVTT-- 379
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462542783 448 TCESVVQLQPGRSYIIYVRALNMGGP-SVRSEPATVHT 484
Cdd:COG3401   380 TSYTDTGLTPGTTYYYKVTAVDAAGNeSAPSEEVSATT 417
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
545-662 1.41e-09

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: 56.20  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 545 HYWEVEVDEHLD--YRVGVAFADVRKQ--EDLGANCLSWCMrhtfasSRHKYEFLHNRTTPDIR--ITVPPKKIGILLDY 618
Cdd:pfam00622   2 HYFEVEIFGQDGggWRVGWATKSVPRKgeRFLGDESGSWGY------DGWTGKKYWASTSPLTGlpLFEPGDVIGCFLDY 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462542783 619 EHSKLSFFNVdLSQHLYTFS-CQLHKFVHPCFSLEKPGCLKVHNG 662
Cdd:pfam00622  76 EAGTISFTKN-GKSLGYAFRdVPFAGPLFPAVSLGAGEGLKFNFG 119
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
392-484 7.82e-09

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: 53.27  E-value: 7.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 392 PSPPI-IKTKEIRSceEAVLICWE--SGNLNPVDSYTVELTQAESPEASGVTESVVGIPTCEsVVQLQPGRSYIIYVRAL 468
Cdd:cd00063     1 PSPPTnLRVTDVTS--TSVTLSWTppEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYT-LTGLKPGTEYEFRVRAV 77
                          90
                  ....*....|....*.
gi 2462542783 469 NMGGPSVRSEPATVHT 484
Cdd:cd00063    78 NGGGESPPSESVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
278-445 4.88e-08

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 56.16  E-value: 4.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 278 DFSDVEqlmgSINTIPAPSAPVINPQVpNSATGSSVRVCWSLYSDDTVESYQLsYRpvqDSSPGTDQAEFTVTVKETYCS 357
Cdd:COG3401   313 APSNVV----SVTTDLTPPAAPSGLTA-TAVGSSSITLSWTASSDADVTGYNV-YR---STSGGGTYTKIAETVTTTSYT 383
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 358 VTNLVPNTQYEFWVTAHNRAGP-SPSSERAVYMTAPSPPIIKTKEIRSceeavlicweSGNLNPVDSYTVELTQAESPEA 436
Cdd:COG3401   384 DTGLTPGTTYYYKVTAVDAAGNeSAPSEEVSATTASAASGESLTASVD----------AVPLTDVAGATAAASAASNPGV 453

                  ....*....
gi 2462542783 437 SGVTESVVG 445
Cdd:COG3401   454 SAAVLADGG 462
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
392-474 2.15e-05

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: 43.37  E-value: 2.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783  392 PSPPIIKTKEIRSceEAVLICWESGNLNPVDSYTVELTQAESPEASGVTESVVGIPTCESVVQ-LQPGRSYIIYVRALNM 470
Cdd:smart00060   2 SPPSNLRVTDVTS--TSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTgLKPGTEYEFRVRAVNG 79

                   ....
gi 2462542783  471 GGPS 474
Cdd:smart00060  80 AGEG 83
Bbox2_MuRF cd19788
B-box-type 2 zinc finger found in muscle-specific RING finger protein (MuRF) family; This ...
178-205 5.87e-04

B-box-type 2 zinc finger found in muscle-specific RING finger protein (MuRF) family; This family corresponds to a group of striated muscle-specific tripartite motif (TRIM) proteins, including TRIM63/MuRF-1, TRIM55/MuRF-2, and TRIM54/MuRF-3, which function as E3 ubiquitin ligases in ubiquitin-mediated muscle protein turnover. They are tightly developmentally regulated in skeletal muscle and associate with different cytoskeleton components, such as microtubules, Z-disks and M-bands, as well as with metabolic enzymes and nuclear proteins. They also cooperate with diverse proteins implicated in selective protein degradation by the proteasome and autophagosome, and target proteins of metabolic regulation, sarcomere assembly and transcriptional regulation. Moreover, MURFs display variable fibre-type preferences. TRIM63/MuRF-1 is predominantly fast (type II) fibre-associated in skeletal muscle. TRIM55/MuRF-2 is predominantly slow-fibre associated. TRIM54/MuRF-3 is ubiquitously present. They play an active role in microtubule-mediated sarcomere assembly. MuRFs belong to the C-II subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, and an acidic residue-rich (AR) domain positioned C-terminal to the RBCC domain. They also harbor a MURF family-specific conserved box (MFC) between its RING-HC finger and Bbox domains. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380846  Cd Length: 39  Bit Score: 37.83  E-value: 5.87e-04
                          10        20
                  ....*....|....*....|....*...
gi 2462542783 178 VFCVTCKTPIRAFQKVFDEHKEHEVIPL 205
Cdd:cd19788    12 IYCLTCEVPTCSMCKVFGAHKDCEVAPL 39
fn3 pfam00041
Fibronectin type III domain;
420-477 5.95e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 39.32  E-value: 5.95e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462542783 420 PVDSYTVELTQAESPEASgVTESVVGIPTCESVVQLQPGRSYIIYVRALNMGGPSVRS 477
Cdd:pfam00041  29 PITGYEVEYRPKNSGEPW-NEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPPS 85
 
Name Accession Description Interval E-value
SPRY_PRY_TRIM76_like cd12899
PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76)-like; This domain is ...
488-663 7.40e-123

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: 362.18  E-value: 7.40e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 488 YFRLNKDTCHPWLTISEDGLTAVRSERRTPARELSPSDTHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADVR 567
Cdd:cd12899     1 YFHLNEDTAHPLLSISEDGFTVVYGEEELPARDLSFSDNSFTRCVAVMGSLIPVRGKHYWEVEVDEQTEYRVGVAFEDTQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 568 KQEDLGANCLSWCMRHTFASSRHKYEFLHNRTTPDIRITVPPKKIGILLDYEHSKLSFFNVDLSQHLYTFSCQLHKFVHP 647
Cdd:cd12899    81 RNGYLGANNTSWCMRHIITPSRHKYEFLHNGWTPDIRITVPPKKIGILLDYDSGRLSFFNVDLAQHLYTFSCQFQHFVHP 160
                         170
                  ....*....|....*.
gi 2462542783 648 CFSLEKPGCLKVHNGI 663
Cdd:cd12899   161 CFSLEKPGALKVHNGI 176
SPRY_PRY_C-II cd13734
PRY/SPRY domain in tripartite motif-containing proteins 1, 9, 18, 36, 46, 67,76 (TRIM1, TRIM9, ...
489-660 1.28e-49

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: 170.54  E-value: 1.28e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 489 FRLNKDTCHPWLTISEDGLTAVRSERRTPARElSPSDTHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADVRK 568
Cdd:cd13734     1 FKLDPKTAHRKLRLSNDNLTVEYDPEGSKDQA-AVLPRRFTGSPAVLGDVAISSGRHYWEVSVSRSTSYRVGVAYKSAPR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 569 QEDLGANCLSWCMRHTFassrHKYEFLHNRTTPDIRITVPPKKIGILLDYEHSKLSFFNVDLSQHLYTFSCQLHKFVHPC 648
Cdd:cd13734    80 DEDLGKNSTSWCLSRDN----NRYTARHDGKVVDLRVTGHPARIGVLLDYDNGTLSFYDAESKQHLYTFHVDFEGPVCPA 155
                         170
                  ....*....|..
gi 2462542783 649 FSLEkPGCLKVH 660
Cdd:cd13734   156 FAVW-NGSLTLH 166
SPRY_PRY_TRIM76 cd12898
PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76), also called ...
486-662 5.29e-36

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: 133.13  E-value: 5.29e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 486 GSYFRLNKDTCHPWLTISEDGLTAVRSERRtpaRELSPSDTHftrCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFAD 565
Cdd:cd12898     1 GTRFLLLRETAHPALHISSDRGTVIYFHER---RRKMSSLTE---CPSVLGEELPSCGQYYWETTVTRCPAYRLGICSSS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 566 VRKQEDLGANCLSWCMRHTFASSRHKYEFLHNRTTPDIRITVPPKKIGILLDYEHSKLSFFNVDLSQHLYTFSCQLHKFV 645
Cdd:cd12898    75 ASQAGALGEGSTSWCLHCVPTSEPCRYTLLHSGIVSDVFVTERPARVGTLLDYNNGRLIFINAESGQLLGIFRHRFAQPC 154
                         170
                  ....*....|....*..
gi 2462542783 646 HPCFSLEKPGCLKVHNG 662
Cdd:cd12898   155 HPAFALEKPGKLELHMG 171
SPRY_PRY_C-I_1 cd13733
PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM5, TRIM6, TRIM7, ...
494-651 1.03e-28

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: 112.57  E-value: 1.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 494 DTCHPWLTISEDGlTAVRseRRTPARELSPSDTHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADV-RKqedl 572
Cdd:cd13733     7 DTAHPNLILSEDL-KSVR--YGDKRQNLPDNPERFDTCVCVLGSEGFSSGRHYWEVEVGGKTDWDLGVARESVnRK---- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 573 GANCLS-----WCMRHTfasSRHKYEFLHNRTTPdIRITVPPKKIGILLDYEHSKLSFFNVDLSQHLYTFSCQLHKFVHP 647
Cdd:cd13733    80 GKITLSpengyWTVGLR---NGNEYKALTSPSTP-LSLREKPQKVGVFLDYEEGQVSFYNVDDGSHIYTFTDCFTEKLYP 155

                  ....
gi 2462542783 648 CFSL 651
Cdd:cd13733   156 YFSP 159
SPRY_PRY_TRIM18 cd12892
PRY/SPRY domain of TRIM18/MID1, also known as FXY or RNF59; This domain, consisting of the ...
489-669 3.69e-23

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: 97.00  E-value: 3.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 489 FRLNKDTCHPWLTISEDGLTAVRSErrTPARElSPSDTHFTR--CVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADV 566
Cdd:cd12892     2 FKLDPKSAHRKLKVSHDNLTVERDE--TSSKK-SHTPERFTSqgSYGVAGNVFIDSGRHYWEVVISGSTWYAIGIAYKSA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 567 RKQEDLGANCLSW--CMRHTFASSRHKYEFLHNRTTPDIRitvppkKIGILLDYEHSKLSFFNVDLSQHLYTFSCQLHKF 644
Cdd:cd12892    79 PKHEWIGKNSASWvlCRCNNNWVVRHNSKEIPIEPSPHLR------RVGILLDYDNGSLSFYDALNSIHLYTFDIAFAQP 152
                         170       180
                  ....*....|....*....|....*
gi 2462542783 645 VHPCFSLEKPgCLKVHNGISMPKHV 669
Cdd:cd12892   153 VCPTFTVWNK-CLTILTGLPIPDHL 176
SPRY_PRY_TRIM39 cd13745
PRY/SPRY domain in tripartite motif-binding protein 39 (TRIM39) and TRIM39-like; This domain, ...
491-655 3.37e-22

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: 94.23  E-value: 3.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 491 LNKDTCHPWLTISEDGLTAVRSERR-----TPARelspsdthFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFAD 565
Cdd:cd13745     7 LDPDTAHPNLVLSEDRKSVRHGDTRqdlpdNPER--------FDTYPCVLGAEGFTGGRHYWEVEVGDKTEWTLGVCRES 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 566 V-RKQE-DLGANCLSWCMRHtfasSRHKYEFLHNRTTPdIRITVPPKKIGILLDYEHSKLSFFNVDLSQHLYTFSCQLHK 643
Cdd:cd13745    79 VsRKGEvTLSPENGYWTVWL----RDGKYEALTSPPTP-LPVSVRPSRVGIFLDYEAGEVSFYNVTDRSHLFTFTDTFSG 153
                         170
                  ....*....|..
gi 2462542783 644 FVHPCFSlekPG 655
Cdd:cd13745   154 TLRPYFY---PG 162
SPRY_PRY_C-I_2 cd12891
PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM14-like, ...
491-659 2.58e-21

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: 91.15  E-value: 2.58e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 491 LNKDTCHPWLTISEDgLTAVRSERRTPARELSPsdTHFTRCvAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADVRKQE 570
Cdd:cd12891     3 LDPNTAHNNLALSGD-LKTVTCSSENQHYPDSP--ERFTHS-QVLSTQSFSSGRHYWEVEVSESGGWSVGVAYPSIERKG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 571 D---LGANCLSWCMRHtfasSRHKYEFLHNRTTPDIRiTVPPKKIGILLDYEHSKLSFFNV-DLSQHLYTFSCQLHKFVH 646
Cdd:cd12891    79 DesrIGRNDKSWCLEW----QDKSFSAWHNNEETPLP-SVSSRRLGVYLDYEAGRLSFYELsDPIRHLHTFTATFTEPLH 153
                         170
                  ....*....|...
gi 2462542783 647 PCFSLEKPGCLKV 659
Cdd:cd12891   154 PAFWVLEGGWIRI 166
SPRY_PRY_TRIM14 cd13738
PRY/SPRY domain of tripartite motif-binding protein 14 (TRIM14); This is a TRIM14 domain ...
491-651 7.11e-21

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: 90.23  E-value: 7.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 491 LNKDTCHPWLTISEDGLTAVRSERRTpareLSPSDT-HFTRCVAVMGNLIPVRGHHYWEVEVDEH-LDYRVGVAFADVRK 568
Cdd:cd13738     3 LEPDTLHPRLRLSDDRLTVSCGWLGT----LGLCPPqRFDKLWQVLSRDSFFSGRHYWEVDLQEAgAGWWVGAAYPSIGR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 569 QED-----LGANCLSWCMRhtfassRHKYEF--LHNRTTPDIRITVPPKKIGILLDYEHSKLSFFNVDLS-QHLYTFSCQ 640
Cdd:cd13738    79 KGDseaarLGWNRQSWCLK------RYDLEYwaFHDGQRSRLRPEDDPDRLGVFLDYEAGILSFYDVTGGmTHLHTFRAT 152
                         170
                  ....*....|.
gi 2462542783 641 LHKFVHPCFSL 651
Cdd:cd13738   153 FQEPLYPALRL 163
SPRY_PRY_TRIM1 cd13739
PRY/SPRY domain of tripartite motif-binding protein 1 (TRIM1) or MID2; This domain, consisting ...
489-651 8.45e-21

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: 90.07  E-value: 8.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 489 FRLNKDTCHPWLTISEDGLTAVRSERrTPARELSPSDTHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADVRK 568
Cdd:cd13739     1 FKLDPKMAHKKLKISNDGLQMEKDES-SLKKSHTPERFSGTGCYGAAGNIFIDSGCHYWEVVVGSSTWYAIGIAYKSAPK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 569 QEDLGANCLSWCMrhtfasSRHKYEFLHNRTTPDIRITVPP--KKIGILLDYEHSKLSFFNVDLSQHLYTFSCQLHKFVH 646
Cdd:cd13739    80 NEWIGKNSSSWVF------SRCNNNFVVRHNNKEMLVDVPPqlKRLGVLLDYDNNMLSFYDPANSLHLHTFEVSFILPVC 153

                  ....*
gi 2462542783 647 PCFSL 651
Cdd:cd13739   154 PTFTI 158
SPRY_PRY_TRIM20 cd15813
PRY/SPRY domain in tripartite motif-binding protein 20 (TRIM20), also known as pyrin; This ...
491-639 1.02e-20

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


Pssm-ID: 293985  Cd Length: 184  Bit Score: 90.20  E-value: 1.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 491 LNKDTCHPWLTISEDgLTAVRSERRTPARELSPSdtHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADVRKQe 570
Cdd:cd15813    13 LDPETAHPNLIFSDD-LKSVRLGNKWDRLPDNPE--RFDSCIIVLGSPSFTSGRHYWEVEVGDKTGWILGVCKASVSRK- 88
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462542783 571 dlGANCLS-----WCMRHTfasSRHKYEFLHNRTTPdIRITVPPKKIGILLDYEHSKLSFFNVDLSQHLYTFSC 639
Cdd:cd15813    89 --GSMTLSpengyWVVMMT---KRNEYQASTSPPTR-LWLREPPRRVGIFLDYEAGDISFYNVTAKSHIYTFTS 156
SPRY_PRY cd12874
PRY/SPRY domain, also known as B30.2; This domain contains residues in the N-terminus that ...
491-651 4.37e-20

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: 87.75  E-value: 4.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 491 LNKDTCHPWLTISEDgLTAVRSERrtPARELSPSDTHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADVRKQE 570
Cdd:cd12874     3 FDPDTAHLNLILSDD-LRSVRVGD--ISQHPPEPPPRFFECWQVLGSQSFSSGRHYWEVDVQDDSSWYVGVTYKSLPRKG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 571 D---LGANCLSWC---MRHTFASSrhkyeflHNRTTPDIRITvPPKKIGILLDYEHSKLSFFNV-DLSQHLYTFSCQLHK 643
Cdd:cd12874    80 KmsnLGRNNGSWClewRENEFSAW-------HNNPETRLPVT-PPRRLGVFLDCDGGSLSFYGVtDGVQLLYTFKAKFTE 151

                  ....*...
gi 2462542783 644 FVHPCFSL 651
Cdd:cd12874   152 PLYPAFWL 159
SPRY_PRY_TRIM7_like cd12888
PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7)-like, including TRIM7, TRIM10, ...
491-658 5.06e-20

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: 87.61  E-value: 5.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 491 LNKDTCHPWLTISEDGltavRSERRTPAR-ELSPSDTHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADVRKQ 569
Cdd:cd12888     4 LDPDTAHPRLVLSEDR----KSVRWGDTRqDLPDNPERFDTWPCVLGCEGFTSGRHYWEVEVGDGGGWAVGVARESVRRK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 570 EDLGANCLS--WCMRhtfassrhKYEFLHN-RTTPDIRITVP--PKKIGILLDYEHSKLSFFNVDLSQHLYTF--SCQLH 642
Cdd:cd12888    80 GEISFSPEEgiWAVG--------QWGGQYWaLTSPETPLPLSevPRRIRVYLDYEGGQVAFFDADNEAPIFTFppASFAG 151
                         170
                  ....*....|....*.
gi 2462542783 643 KFVHPCFSLEKPGCLK 658
Cdd:cd12888   152 ERIFPWFWVGKGSQLK 167
SPRY_PRY_TRIM69 cd15818
PRY/SPRY domain in tripartite motif-binding protein 69 (TRIM69), also known as RING finger ...
487-649 1.30e-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: 84.08  E-value: 1.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 487 SYFRLNKDTCHPWLTISEDgLTAVRserRTPARELSPSD-THFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFAD 565
Cdd:cd15818    13 SLITLDPKTAHPNLILSED-LTCVW---HGDTKQMLPDNpERFDSSVAVLGSEGFTSGKHYWEVEVAKKTKWTLGVVRES 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 566 VRKQedlGANCLS-----WCMRhtfasSRHKYEF----LHNRTtpdIRITVPPKKIGILLDYEHSKLSFFNVDLSQHLYT 636
Cdd:cd15818    89 INRK---GNCPLSpedgfWLLR-----LRNQNELkaldVPSFS---LTLTSNLNKVGIYLDYEGGQVSFYNANTMSHIYT 157
                         170
                  ....*....|...
gi 2462542783 637 FSCQLHKFVHPCF 649
Cdd:cd15818   158 FSDTFTEKIYPYF 170
SPRY_PRY_A33L cd12905
zinc-binding protein A33-like; This domain, consisting of the distinct N-terminal PRY ...
491-650 1.34e-18

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: 84.00  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 491 LNKDTCHPWLTISEDGLTAVRSERRTPARelsPSDTHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADVRKQE 570
Cdd:cd12905     8 FDPETAHPSLILSRDLTAVTESDEMQPYP---RSPKRFLQCVNVLASQGFQSGRHYWEVWVGSKTKWDLGVASESVDRQA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 571 --DLGANCLSWCMRhtfassrhkyefLHNR------TTPDIRITV--PPKKIGILLDYEHSKLSFFNVDLSQHLYTFS-- 638
Cdd:cd12905    85 rvKLCPENGYWTLR------------LRNGdeywagTQPWTRLRVtsRPQRIGVFLDCEERKVSFYNADDMSLLYSFHqg 152
                         170
                  ....*....|....
gi 2462542783 639 --CQLHKFVHPCFS 650
Cdd:cd12905   153 prGKVFPFFSTCFS 166
SPRY_PRY_BTN1_2 cd15819
butyrophilin subfamily member A1 and A2 (BTN1A and BTN2A); This domain, consisting of the ...
491-657 7.16e-18

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: 81.50  E-value: 7.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 491 LNKDTCHPWLTISEDGltavRSERRTPARELSPSDTH-FTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADVRKQ 569
Cdd:cd15819     6 LDPDTAHPALILSEDG----RSVTWGETRQDLPENPErFDSLPCVLGQEGFTSGRHYWEVEVGDRTSWDLGVCRDNVMRK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 570 edlGANCLS-----WCMRhtfaSSRHKYEFLhnrTTPDIRITV--PPKKIGILLDYEHSKLSFFNVDLSQHLYTFS-CQL 641
Cdd:cd15819    82 ---GRVTLSpengfWAIR----LYGNEYWAL---TSPETPLTLkePPRRVGIFLDYEAGDVSFYNMTDGSHIYTFPqTAF 151
                         170
                  ....*....|....*...
gi 2462542783 642 HKFVHPCFSL--EKPGCL 657
Cdd:cd15819   152 SGPLRPFFRLwsSDSGPL 169
SPRY_PRY_TRIM35 cd12893
PRY/SPRY domain in tripartite motif-containing protein 35 (TRIM35); This PRY/SPRY domain is ...
491-656 1.29e-17

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: 80.75  E-value: 1.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 491 LNKDTCHPWLTISEDgLTAVR--SERRT----PARelspsdthFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFA 564
Cdd:cd12893     4 LDPNTAHPWLSLSED-LTSVRysSEKQQlpdnPER--------FDPYPCVLGSEGFTSGKHSWDVEVGDNTSWMLGVAKE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 565 DVRKQEDLGANCLS--WCMRHtfasSRHKYEFLHNrTTPDIRITV--PPKKIGILLDYEHSKLSFFNVDLSQHLYTFScq 640
Cdd:cd12893    75 SVQRKGKFTLSPESgfWTIGF----SEGKYSARTS-PEPRTPLRVkqKPQRIRVQLDWDRGKVSFSDPDTNTHIHTFT-- 147
                         170
                  ....*....|....*....
gi 2462542783 641 lHKFVH---PCFSlekPGC 656
Cdd:cd12893   148 -HTFTErvfPYFY---TGC 162
SPRY_PRY_FSD1 cd12901
Fibronectin type III and SPRY containing 1 (FSD1) domain includes PRY at the N-terminus; This ...
489-666 1.52e-16

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: 78.72  E-value: 1.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 489 FRLNKDTCHPWLTISE---------------------DGLTAVRSERRTPARELSP--------SDTHFT-RCVAVMGNL 538
Cdd:cd12901     1 FKLDASSSHQNLKVEDlsvewdatggkvlqkikgrenDGRSRTASPRNSSARCQSPkrmpsargGRDRFTaESYTVLGDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 539 IPVRGHHYWEVEVD-EHLDYRVGVAFADVRKQEDLGANCLSWC------MRHTFASSrhkyeflHNRTTPDIRITVPpKK 611
Cdd:cd12901    81 LIDGGQHYWEVRAQkDSKAFSVGVAYRSLGKFDQLGKTNASWClhvnnwLQNSFAAK-------HNNKAKTLDVPVP-DR 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462542783 612 IGILLDYEHSKLSFFNVDLSQHLYTFSCQLHKFVHPCFSLeKPGCLKVHNGISMP 666
Cdd:cd12901   153 IGVYCDFDEGQLSFYNARTKQLLHTFKMKFTQPVLPAFMV-WCGGLSVSTGLQVP 206
SPRY_PRY_SPRYD4 cd12903
PRY/SPRY domain containing protein 4 (SPRYD4); This domain, consisting of the distinct ...
534-662 1.98e-16

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: 77.49  E-value: 1.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 534 VMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADVRKQEDLGANCLSWcmrhTFA-SSRHKYEFLHNRTTPdIRITVPPKKI 612
Cdd:cd12903    46 VLGDTPVTSGRHYWEVTVKRSQEFRIGVADVDMSRDECIGTNESSW----VFAyAQRKWYAMVANETVP-VPLVGKPDRV 120
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462542783 613 GILLDYEHSKLSFFNVDLSQHLYTFSCQLHKFVHPCFSLEKpGCLKVHNG 662
Cdd:cd12903   121 GLLLDYEAGKLSLVDVEKNSVVHTMSAEFRGPVVPAFALWD-GELLTHSG 169
SPRY_PRY_TRIM11 cd15811
PRY/SPRY domain of tripartite motif-binding protein 11 (TRIM11), also known as RING finger ...
491-638 8.00e-16

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: 75.76  E-value: 8.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 491 LNKDTCHPWLTISEDGltavRSERRTPARELSP-SDTHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADVRKQ 569
Cdd:cd15811     4 LDPDTANPELVLSEDR----RSVRRGDLRQALPdSPERFDPGPCVLGRERFTSGRHYWEVEVGDRTSWALGVCKENVNRK 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462542783 570 E--DLGANCLSWCMrhTFASSrhkYEFLHNRTTPDIRitVPPKKIGILLDYEHSKLSFFNVDLSQHLYTFS 638
Cdd:cd15811    80 EkgELSAGNGFWIL--VFLGN---YYSSERRTFAPLR--DPPRRVGIFLDYEAGHLSFYSATDGSLLFIFP 143
SPRY_PRY_TRIM41 cd13741
PRY/SPRY domain in tripartite motif-binding protein 41 (TRIM41); This domain, consisting of ...
491-655 4.13e-15

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: 74.41  E-value: 4.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 491 LNKDTCHPWLTISEDGLTAVRSERRtpaRELSPSDTHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADVRKQE 570
Cdd:cd13741     4 LDPDTAHPALLLSPDRRGVRLAERR---QEVPEHPKRFSADCCVLGAQGFRSGRHYWEVEVGGRRGWAVGAARESTHHKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 571 DLGANCLSWCMRHTFASS-RHKYEFLHNRTTPDIRITV-------------------------PPKKIGILLDYEHSKLS 624
Cdd:cd13741    81 KVGSGGSSVSSGDASSSRhHHRRRRLHLPQQPLLQREVwcvgtngkryqaqssteqtllspseKPRRFGVYLDYEAGRLG 160
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462542783 625 FFNVDLSQHLYTFSCQLH-KFVHPCFSLEKPG 655
Cdd:cd13741   161 FYNAETLAHVHTFSAAFLgERVFPFFRVLSKG 192
SPRY_PRY_BTN3 cd15820
PRY/SPRY domain of butyrophilin 3 (BTN3), includes BTN3A1, BTN3A2, BTN3A3 as well as BTN-like ...
491-638 7.27e-15

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: 72.85  E-value: 7.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 491 LNKDTCHPWLTISEDgltaVRSERRTPARELSP-SDTHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADVRKQ 569
Cdd:cd15820     8 LDPDTANPILLISED----QRSLQWADEPQNLPdNPKRFDWHYCVLGCKSFTSGRHFWEVEVGDRKEWYVGVCRENVERK 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462542783 570 EDLGANCLS--WCMRhtfASSRHKYeflHNRTTPDIRITV--PPKKIGILLDYEHSKLSFFNVDLSQHLYTFS 638
Cdd:cd15820    84 LWVKMAPENgfWTIG---LSDGNDY---QALTDPRTKLTIanPPQRVGVFLDYETGEVSFYNAMDGSHIYTFP 150
SPRY_PRY_TRIM60 cd15828
PRY/SPRY domain of tripartite motif-binding protein 60 (TRIM60) also known as RING finger ...
491-650 1.53e-14

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: 72.32  E-value: 1.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 491 LNKDTCHPWLTISEDGlTAVRSERRTpaRELSPSDTHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGV---AFADVR 567
Cdd:cd15828    14 LDPETAHPQLTVSEDR-KSVLYGEMK--QNVCYNPRRFYLCPAVLGSEGFHSGRQYWEVEVGDKPEWTLGVcqdCLPRNW 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 568 KQEDLGANCLsWCMRHTFASSrhkYEFLHNRTTpDIRITVPPKKIGILLDYEHSKLSFFNVDLSQHLYTFSCQLHKFVHP 647
Cdd:cd15828    91 SNQPSVQDGL-WAIGRYSESN---YVALGPKKI-QLLPKVRPSKIGIFLDYELGEVSFYNMNDRSLLYTFSDSFTGTLWP 165

                  ...
gi 2462542783 648 CFS 650
Cdd:cd15828   166 YFY 168
SPRY_PRY_TRIM60_75 cd15817
PRY/SPRY domain of tripartite motif-binding protein 60 and 75 (TRIM60 and TRIM75); This domain, ...
491-651 1.74e-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: 71.81  E-value: 1.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 491 LNKDTCHPWLTISEDGlTAVRSERRTPARELSPSdtHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADVRKQE 570
Cdd:cd15817     4 LDPETAHPNLIVSEDR-KAVRYRRMKPNCPYDPR--RFTVYPAVLGSEGFDSGRHFWEVEVGGKGEWILGVCKDSLPRNA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 571 DLGANCLSWCMRhtFASSRHKYEFLHNRTTPDIrITVPPKKIGILLDYEHSKLSFFNVDLSQHLYTFSCQLHKFVHPCFS 650
Cdd:cd15817    81 QDPPSPLGGCWQ--IGRYMSGYVASGPKTTQLL-PVVKPSRIGIFLDYELGEVSFYNMNDRSHLYTFTDTFTGKLIPYFY 157

                  .
gi 2462542783 651 L 651
Cdd:cd15817   158 V 158
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
295-380 1.76e-14

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: 69.18  E-value: 1.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783  295 PSAPViNPQVPNSaTGSSVRVCWSLYSDDTVESYQLSYRpVQDSSPGTDQAEFTVTVKETYCSVTNLVPNTQYEFWVTAH 374
Cdd:smart00060   1 PSPPS-NLRVTDV-TSTSVTLSWEPPPDDGITGYIVGYR-VEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                   ....*.
gi 2462542783  375 NRAGPS 380
Cdd:smart00060  78 NGAGEG 83
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
542-659 1.76e-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: 70.40  E-value: 1.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783  542 RGHHYWEVEVDEHLDYRVGVAFADVR--KQEDLGANCLSWCMRhtfASSRHKYeflHNRTTPDIRITV--PPKKIGILLD 617
Cdd:smart00449   1 SGRHYFEVEIGDGGHWRVGVATKSVPrgYFALLGEDKGSWGYD---GDGGKKY---HNSTGPEYGLPLqePGDVIGCFLD 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2462542783  618 YEHSKLSFFNV-DLSQHLYTFSCQLHKFVHPCFSLEKPGCLKV 659
Cdd:smart00449  75 LEAGTISFYKNgKYLHGLAFFDVKFSGPLYPAFSLGSGNSVRL 117
SPRY_PRY_TRIM15 cd15826
PRY/SPRY domain in tripartite motif-binding protein 15 (TRIM15); This domain, consisting of ...
491-655 1.08e-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: 69.51  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 491 LNKDTCHPWLTISEDgLTAVRSERRTPARELSPsdTHFTRCVAVMGNLIPVRGHHYWEVEVD--EHLDYRVGVAFADVRK 568
Cdd:cd15826     4 LDPQTASGSLVLSED-RKSVRYTRQKQNLPDSP--LRFDGLPAVLGSPGFSSGRHRWQVEVQlgDGGGCTVGVAGESVRR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 569 QEDLGancLS-----WCMRhtFASSRhkyefLHNRTTP--DIRITVPPKKIGILLDYEHSKLSFFNVDLSQHLYTFSCQL 641
Cdd:cd15826    81 KGEMG---LSaedgvWAVI--LSHQQ-----CWASTSPgtDLPLSEIPRRVGVALDYEAGTVTLTNAETQEPIFTFTASF 150
                         170
                  ....*....|....
gi 2462542783 642 HKFVHPCFSLEKPG 655
Cdd:cd15826   151 SGKVFPFFAVWKKG 164
SPRY_PRY_TRIM67_9 cd12889
PRY/SPRY domain in tripartite motif-containing proteins, TRIM9 and TRIM67; This domain, ...
487-666 1.12e-13

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: 69.58  E-value: 1.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 487 SYFRLNKDTCHPWLTISEDGLTAvrserrtparelspSDTHFTRCVaVMGNLIPVRGHHYWEVEVDE---HLDYRVGVAF 563
Cdd:cd12889     8 AWFTFDPSTSHPDIILSNDNMTV--------------TCNSYEDRV-VLGSVGFSRGVHYWEVTIDRydgHPDPAFGVAR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 564 ADVRKQEDLGANCLSWCMrhTFASSRHkyEFLHN-----RTtpDIRITVpPKKIGILLDYEHSKLSFFNVDLSQHLYTFS 638
Cdd:cd12889    73 IDVNKDKMLGKDDKGWSM--YIDNNRS--WFLHNnehsnRT--EGGITV-GSVVGVLLDLDRHTLSFYVNDEPQGPIAFR 145
                         170       180
                  ....*....|....*....|....*...
gi 2462542783 639 cQLHKFVHPCFSLEKPGCLKVHNGISMP 666
Cdd:cd12889   146 -NLPGVFYPAVSLNRNVQVTLHTGLEPP 172
SPRY_PRY_SNTX cd16040
Stonustoxin subunit alpha or SNTX subunit alpha; This domain, consisting of the distinct ...
491-637 1.89e-13

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: 69.05  E-value: 1.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 491 LNKDTCHPWLTISEDGLTAVRSERrtparELSPSDtH---FTRCVAVMGNLiPVRGHHYWEVE-----VDehldyrVGVA 562
Cdd:cd16040    13 LDPNTAHRNLSLSEGNRKVTRVKE-----EQPYPD-HperFDYWPQVLCRE-GLSGRCYWEVEwsgggVD------IAVA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 563 FADV-RKQED----LGANCLSWCMRhtfaSSRHKYEFLHNRTTPDIRITVPP-KKIGILLDYEHSKLSFFNV-DLSQHLY 635
Cdd:cd16040    80 YKGIsRKGDGddsrFGYNDKSWSLE----CSPSGYSFWHNNKKTEISVPSSSsSRVGVYLDHSAGTLSFYSVsDTMTLLH 155

                  ..
gi 2462542783 636 TF 637
Cdd:cd16040   156 TV 157
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
295-390 3.34e-13

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: 65.60  E-value: 3.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 295 PSAPViNPQVpNSATGSSVRVCWSLYSDDT--VESYQLSYRPVQDSSPGTDQaefTVTVKETYCSVTNLVPNTQYEFWVT 372
Cdd:cd00063     1 PSPPT-NLRV-TDVTSTSVTLSWTPPEDDGgpITGYVVEYREKGSGDWKEVE---VTPGSETSYTLTGLKPGTEYEFRVR 75
                          90
                  ....*....|....*...
gi 2462542783 373 AHNRAGPSPSSERAVYMT 390
Cdd:cd00063    76 AVNGGGESPPSESVTVTT 93
SPRY_PRY_TRIM21 cd12900
PRY/SPRY domain in tripartite motif-binding protein 21 (TRIM21) also known as 52kD ...
486-650 5.50e-13

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: 67.60  E-value: 5.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 486 GSYFRLNKDTCHPWLTISEDgltavRSERR---TPaRELSPSDTHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVA 562
Cdd:cd12900     2 MVHITLDPDTANPWLILSKD-----RRQVRlgdTH-QNVPENEERFDNYPMVLGAQRFNSGKHYWEVDVTGKEAWDLGVC 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 563 FADVRKQedlGANCLS-----WcmrhTFASSRHKYEFLHNRTTPdIRITVPPKKIGILLDYEHSKLSFFNV-DLSQHLYT 636
Cdd:cd12900    76 RDSVRRK---GQFLLSpengfW----TIWLWNKKYEAGTSPQTT-LHLQVPPCQVGIFLDYEAGVVSFYNItDHGSLIYT 147
                         170
                  ....*....|....*
gi 2462542783 637 FS-CQLHKFVHPCFS 650
Cdd:cd12900   148 FSeCAFTGPLRPFFN 162
SPRY_PRY_TRIM65 cd12896
PRY/SPRY domain in tripartite motif-containing domain 65 (TRIM65); This domain, consisting of ...
543-651 1.38e-12

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


Pssm-ID: 293953 [Multi-domain]  Cd Length: 182  Bit Score: 66.71  E-value: 1.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 543 GHHYWEVEVDEHLDYrVGVAFADVRKQE------DLGANCLSW--CMRhtfassRHKYEFLHNRTTPDIRiTVPPKKIGI 614
Cdd:cd12896    63 GHHYWEVEVSSHSVT-LGVTYPGLPRHKqgghkdNIGRNPCSWglQIQ------EDSLQAWHNGRAQKLQ-GVSYRLLGV 134
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2462542783 615 LLDYEHSKLSFFNV-DLSQHLYTFSCQLHKFVHPCFSL 651
Cdd:cd12896   135 DLDLEAGTLTFYGLePGTQRLHTFHAIFTQPLYPVFWL 172
fn3 pfam00041
Fibronectin type III domain;
293-383 2.32e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.20  E-value: 2.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 293 PAPSAPVINPQvpnsaTGSSVRVCWS--LYSDDTVESYQLSYRPVQDSSPGTdqaEFTVTVKETYCSVTNLVPNTQYEFW 370
Cdd:pfam00041   1 SAPSNLTVTDV-----TSTSLTVSWTppPDGNGPITGYEVEYRPKNSGEPWN---EITVPGTTTSVTLTGLKPGTEYEVR 72
                          90
                  ....*....|...
gi 2462542783 371 VTAHNRAGPSPSS 383
Cdd:pfam00041  73 VQAVNGGGEGPPS 85
SPRY_PRY_TRIM75 cd15829
PRY/SPRY domain of tripartite motif-binding protein 75 (TRIM75); This domain, consisting of ...
491-637 3.78e-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: 3.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 491 LNKDTCHPWLTISEDGlTAVRSERRTpaRELSPSDTHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADV---R 567
Cdd:cd15829    23 LDPETAHPNLLVSEDK-KCVTFTKKK--QRVPDSPKRFTVNPVVLGFPGFHSGRHFWEVEVGDKPEWAVGVCKDSLstkA 99
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462542783 568 KQEDLGANClSWCMRhtfassrhkyefLHN-------RTTPDIRITVPPKKIGILLDYEHSKLSFFNVDLSQHLYTF 637
Cdd:cd15829   100 RRPPSGQQG-CWRIQ------------LQGgdydapgAVPPPLLLEVKPRGIGVFLDYELGEISFYNMPEKSHIHTF 163
SPRY_PRY_TRIM38 cd15815
PRY/SPRY domain of tripartite motif-binding protein 38 (TRIM38), also known as Ring finger ...
491-637 9.37e-12

PRY/SPRY domain of tripartite motif-binding protein 38 (TRIM38), also known as Ring finger protein 15 (RNF15); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM38, which is also known as RING finger protein 15 (RNF15) or RORET. TRIM38 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. TRIM38 has been shown to act as a suppressor in TOLL-like receptor (TLR)-mediated interferon (IFN)-beta induction by promoting degradation of TRAF6 and NAP1 through the ubiquitin-proteasome system. Another study has shown that TRIM38 may act as a novel negative regulator for TLR3-mediated IFN-beta signaling by targeting TRIF for degradation. TRIM38 has been identified as a critical negative regulator in TNFalpha- and IL-1beta-triggered activation of NF-kappaB and MAP Kinases (MAPKs); it causes degradation of two essential cellular components, TGFbeta-associated kinase 1 (TAK1)-associating chaperones 2 and 3 (TAB2/3). The degradation is promoted through a lysosomal-dependent pathway, which requires the C-terminal PRY-SPRY of TRIM38. Enterovirus 71 infection induces degradation of TRIM38, suggesting that TRIM38 may play a role in viral infections.


Pssm-ID: 293987 [Multi-domain]  Cd Length: 182  Bit Score: 64.29  E-value: 9.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 491 LNKDTCHPWLTISEDGLTAVRserRTPARELSPSDTHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADV---- 566
Cdd:cd15815    17 LDPDTAHPELTLSKDQRQVTY---GRCQENLDASPKRFTVLPCVLGCEGFTSGRHYFEVDVGEGTGWDVGVCLENVqrgf 93
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462542783 567 -RKQEdlgANCLSWCMRhtfASSRHKYEFLHNRTTPdIRITVPPKKIGILLDYEHSKLSFFNVDLSQHLYTF 637
Cdd:cd15815    94 gMKQE---PEFGFWTIR---LCEEDGYVALTSPPTP-LPLREKPLVVGVFLDYEAGLVSFYNMTTGSHIFTF 158
SPRY_PRY_TRIM25 cd13736
PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25); This domain, consisting of ...
491-649 9.84e-12

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: 63.75  E-value: 9.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 491 LNKDTCHPWLTISEDGLTAVRSErrTPArELSPSDTHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADVRKQ- 569
Cdd:cd13736     3 FDYNTAHNKVSLSENYTKASVSD--DPQ-NYREHPQRFTYCSQVLGLHCFKQGIHYWEVELQKNNFCGVGICYGSMDRQg 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 570 --EDLGANCLSWCMRHtFASsrhKYEFLHNrttpDIRITVP---PKKIGILLDYEHSKLSFFNVDLSQHL-YTFSCQLHK 643
Cdd:cd13736    80 peSRLGRNSESWCVEW-FNV---KISAWHN----NVEKTLPstkATRVGVLLNCDHGFVIFFAVQDKVHLmYKFKVDFTE 151

                  ....*.
gi 2462542783 644 FVHPCF 649
Cdd:cd13736   152 ALYPAF 157
SPRY_PRY_RFPL cd15821
Ret finger protein-like (RFPL), includes RFP1, 2, 3, 4; This domain, consisting of the ...
491-638 2.00e-11

Ret finger protein-like (RFPL), includes RFP1, 2, 3, 4; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of RFPL protein family, which includes RFPL1, RFPL2, RFPL3 and RFPL4. In humans, RFPL transcripts can be detected at the onset of neurogenesis in differentiating human embryonic stem cells, and in the developing human neocortex. The human RFPL1, 2, 3 genes have a role in neocortex development. RFPL1 is a primate-specific target gene of Pax6, a key transcription factor for pancreas, eye and neocortex development; human RFPL1 decreases cell number through its RFPL-defining motif (RDM) and SPRY domains. The RFPL4 (also known as RFPL4A) gene encodes a putative E3 ubiquitin-protein ligase expressed in adult germ cells and interacts with oocyte proteins of the ubiquitin-proteasome degradation pathway.


Pssm-ID: 293993 [Multi-domain]  Cd Length: 178  Bit Score: 63.10  E-value: 2.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 491 LNKDTCHPWLTISEDgLTAVRSERRTPARELSPSDTHFTRCVavMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADVRKQe 570
Cdd:cd15821     8 LDVDTANNYLIISED-LRSVRCGCFRQNRKELAERFDDALCV--LGSPRFTSGRHYWEVDVGTSTEWDLGVCRESVNRQ- 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462542783 571 dlGANCLS-----WCM----RHTFASSrhkyeflhnrTTPDIRITVPPK--KIGILLDYEHSKLSFFNVDLSQHLYTFS 638
Cdd:cd15821    84 --GPIELSpehgfWTVslrdGSVFFAS----------TVPLTVLWVNPRlhRVGIFLDMEMGTISFYDVSDGSHIFTFT 150
SPRY_PRY_TRIM50 cd13743
PRY/SPRY domain in tripartite motif-binding protein 50 (TRIM50); This domain, consisting of ...
490-649 3.11e-11

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: 62.90  E-value: 3.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 490 RLNKDTCHPWLTISEdGLTAVrsERRTPARELSPSDTHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADVRKQ 569
Cdd:cd13743    15 KLDPLTAHPMLELSK-GNTVV--ECGLLAQRLPSNPERFDYSNCVLASRGFSSGKHYWEVVVGSKSKWRLGLIKGTTSRK 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 570 EDLGANCLSWCMRHTFASSRHKYEFLHNRTTpdIRITVPPKKIGILLDYEHSKLSFFNVDLSQHL---YTFSCQLHKFVH 646
Cdd:cd13743    92 GKLNKSPENGVWLIGLKEGRVYEAFANPRVP--LPLSTRPQRIGVFLDYEKGELTFYNADSPDELvpiYTFQAEFQGKLY 169

                  ...
gi 2462542783 647 PCF 649
Cdd:cd13743   170 PLL 172
SPRY_PRY_TRIM5_6_22_34 cd15810
PRY/SPRY domain of tripartite motif-binding protein 5, 6, 22 and 34 (TRIM5, TRIM6, TRIM22 and ...
491-653 4.06e-11

PRY/SPRY domain of tripartite motif-binding protein 5, 6, 22 and 34 (TRIM5, TRIM6, TRIM22 and TRIM34); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of very close paralogs, TRIM5, TRIM6, TRIM22 and TRIM34. These domains are composed of RING/B-box/coiled-coil core and are also known as RBCC proteins. They form a locus of four closely related TRIM genes within an olfactory receptor-rich region on chromosome 11 of the human genome. Genetic analysis of this locus indicates that these four genes have evolved by gene duplication from a common ancestral gene. All genes in the TRIM6/TRIM34/TRIM5/TRIM22 locus are type I interferon inducible, with TRIM5 and TRIM22 possessing antiviral properties. TRIM5 promotes innate immune signaling by activating the TAK1 kinase complex by cooperating with the heterodimeric E2, UBC13/UEV1A. It also stimulates NFkB and AP-1 signaling, and the transcription of inflammatory cytokines and chemokines, amplifying these activities upon retroviral infection. Interaction of its PRY-SPRY or cyclophilin domains with the retroviral capsid lattice stimulates the formation of a complementary lattice by TRIM5, with greatly increased TRIM5 E3 activity, and host cell signal transduction. TRIM6 is selectively expressed in embryonic stem (ES) cells and interacts with the proto-oncogene product Myc, maintaining the pluripotency of the ES cells. TRIM6, together with E2 Ubiquitin conjugase (UbE2K) and K48-linked poly-Ub chains, is critical for the IkappaB kinase epsilon (IKKepsilon) branch of type I interferon (IFN-I) signaling pathway and subsequent establishment of a protective antiviral response. TRIM22 plays an integral role in the host innate immune response to viruses; it has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. Altered TRIM22 expression has also been associated with multiple sclerosis, cancer, and autoimmune disease. While the PRY-SPRY domain of TRIM5a provides specificity and the capsid recognition motif to retroviral restriction, TRIM34 binds HIV-1 capsid but does not restrict HIV-1 infection.


Pssm-ID: 293982 [Multi-domain]  Cd Length: 189  Bit Score: 62.50  E-value: 4.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 491 LNKDTCHPWLTISEDGltavRSERRTPARELSPSDTHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAfadVRKQE 570
Cdd:cd15810     4 LNPVNISLNIVISEDQ----RQVRIVPPQTSGQALTNNNYDFGVLGSQYFSSGKHYWEVDVSKKSAWILGVC---SHKRS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 571 DLGANCLSWCMRHTFASSRH---------------KYEFLHNRTTPD-----IRITVPPKKIGILLDYEHSKLSFFNVdl 630
Cdd:cd15810    77 DAMTKSNANQINHQNVYSRYqpqygywviglqnesEYNAFEDSSSFNphvltLSVTVPPHRVGVFLDYEAGTVSFFNV-- 154
                         170       180
                  ....*....|....*....|....*..
gi 2462542783 631 SQH---LYTFS-CQLHKFVHPCFSLEK 653
Cdd:cd15810   155 TNHgslIYKFSkCCFSTTVCPYFNPWN 181
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
294-484 4.52e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 65.79  E-value: 4.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 294 APSAPViNPQVpNSATGSSVRVCWSLYSDDTVESYQLsYRpvQDSSPGTdqaeFTV--TVKETYCSVTNLVPNTQYEFWV 371
Cdd:COG3401   232 PPSAPT-GLTA-TADTPGSVTLSWDPVTESDATGYRV-YR--SNSGDGP----FTKvaTVTTTSYTDTGLTNGTTYYYRV 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 372 TAHNRAG----PSPSSERAVYMTAPSPPIIKTKEIRSCEEAVLIcWESGNLNPVDSYTVELTQAESPEASGVTESVVGip 447
Cdd:COG3401   303 TAVDAAGnesaPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLS-WTASSDADVTGYNVYRSTSGGGTYTKIAETVTT-- 379
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462542783 448 TCESVVQLQPGRSYIIYVRALNMGGP-SVRSEPATVHT 484
Cdd:COG3401   380 TSYTDTGLTPGTTYYYKVTAVDAAGNeSAPSEEVSATT 417
SPRY_PRY_RNF135 cd12902
PRY/SPRY domain in RING finger protein RNF135; This domain, consisting of the distinct ...
497-651 3.61e-10

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


Pssm-ID: 293959 [Multi-domain]  Cd Length: 168  Bit Score: 59.07  E-value: 3.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 497 HPWLTISEDGLTAVRSERRTPARElspSDTHFTRCvAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADVRKQEDLGANC 576
Cdd:cd12902     9 SCSLEVSEDSRKVTVSHGPQAYAW---SPDRFSIS-QVLCSQAFSSGQHYWEVDTRQCSHWAVGVASWEMSRDQMLGRTM 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462542783 577 LSWCMRHtfaSSRHKYEFLHNRTTPDIRiTVPPKKIGILLDYEHSKLSFFNVDLSQHL-YTFSCQLHKFVHPCFSL 651
Cdd:cd12902    85 DSWCIEW---KGTGQLSAWHMNKETVLG-SDKPRVVGIWLDLEEGKLAFYSVANQERLlHECEVSASSPLHPAFWL 156
SPRY_BSPRY cd12904
SPRY domain in Ro-Ret family; This domain, named BSPRY, has been identified in the Ro-Ret ...
490-638 8.37e-10

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: 58.20  E-value: 8.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 490 RLNKDTCHPWLTISEDGLTAVRSERRtpARELSPSD-THFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADV-R 567
Cdd:cd12904     2 RFDERTVSPLLSLSEDRRTLTFSPKK--ARQSPPDDpERFDHWPNALASLSFSSGTHAWVVDVGKSCAYKVGVCYGSLeR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 568 K----QEDLGANCLSWCMrhtfasSRH--KYEFLHNRTTPDIRITVPPKKIGILLDYEHSKLSFFNVD----LSQHLYTF 637
Cdd:cd12904    80 KgsgnEARLGYNAFSWVF------SRYdgEFSFSHNGQHVPLELLKCPARVGVLLDWPSQELLFYDPDsctvLHSHREAF 153

                  .
gi 2462542783 638 S 638
Cdd:cd12904   154 A 154
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
545-662 1.41e-09

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: 56.20  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 545 HYWEVEVDEHLD--YRVGVAFADVRKQ--EDLGANCLSWCMrhtfasSRHKYEFLHNRTTPDIR--ITVPPKKIGILLDY 618
Cdd:pfam00622   2 HYFEVEIFGQDGggWRVGWATKSVPRKgeRFLGDESGSWGY------DGWTGKKYWASTSPLTGlpLFEPGDVIGCFLDY 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462542783 619 EHSKLSFFNVdLSQHLYTFS-CQLHKFVHPCFSLEKPGCLKVHNG 662
Cdd:pfam00622  76 EAGTISFTKN-GKSLGYAFRdVPFAGPLFPAVSLGAGEGLKFNFG 119
SPRY_PRY_TRIM58 cd15816
PRY/SPRY domain in tripartite motif-binding protein 58 (TRIM58), also known as BIA2; This ...
490-649 1.49e-09

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: 57.49  E-value: 1.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 490 RLNKDTCHPWLTISEDgLTAVRSERrtPARELSPSDTHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADV-RK 568
Cdd:cd15816     3 KLDPATAHPSLLLTAD-LRSVQDGE--LWRDVPGNPERFDTWPCVLGLQSFSSGRHYWEVAVGEKAEWGLGVCQDSApRK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 569 QE-----DLGANCLsWCMRHTfassrhKYEFLHNRTTPDIRITvPPKKIGILLDYEHSKLSFFNVDLSQHLYTFSCQLHK 643
Cdd:cd15816    80 GEttpspENGVWAV-WLLKGN------EYMVLASPSVPLLQLR-RPRRVGVFLDYEAGEISFYNVTAGSHIYTFRQLFSG 151

                  ....*.
gi 2462542783 644 FVHPCF 649
Cdd:cd15816   152 ILRPYF 157
SPRY_PRY_TRIM27 cd15814
PRY/SPRY domain in tripartite motif-containing protein 27 (TRIM27), also known as RING finger ...
491-655 1.49e-09

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: 57.78  E-value: 1.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 491 LNKDTCHPWLTISeDGLTAVRSERRTpaRELSPSDTHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADVRKQE 570
Cdd:cd15814     6 LDPDTAYPSLILS-DNLRQVRYSYLQ--QDLPDNPERFNLFPCVLGSPCFIAGRHYWEVEVGDKAKWTIGVCEDSVCRKG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 571 DLGANCLSWCMRHTFASSRHKYEFLHNRTTPDIRitVPPKKIGILLDYEHSKLSFFNVDLSQHLYTFS-CQLHKFVHPCF 649
Cdd:cd15814    83 GVTSAPQNGFWAVSLWYGKEYWALTSPMTALPLR--TPLQRVGIFLDYDAGEVSFYNVTERCHTFTFShATFCGPVRPYF 160

                  ....*.
gi 2462542783 650 SLEKPG 655
Cdd:cd15814   161 SLSYSG 166
SPRY_PRY_TRIM62 cd13744
PRY/SPRY domain in tripartite motif-binding protein 62 (TRIM62); This domain, consisting of ...
482-655 1.71e-09

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


Pssm-ID: 293978  Cd Length: 188  Bit Score: 57.70  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 482 VHTIGSYFRLNKDTCHPWLTISEDgLTAVRSERRTPaRELSPSDTHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGV 561
Cdd:cd13744     7 IHPVPAALTLDPVTAHQRLILSDD-CTIVAYGNLHP-QPLQDSPKRFDVEVSVLGSEGFSGGVHYWEVVVSEKTQWMIGL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 562 AFADVRK------QEDLGANCLSWCMRHTFASSrhkyeflhnrTTPDIRITVPPK--KIGILLDYEHSKLSFFNVDLSQH 633
Cdd:cd13744    85 AHEAVSRkgsiqiQPGRGFYCIVMHDGNQYSAC----------TEPWTRLNVKSKleKVGVYLDYDKGLLIFYNADDMSW 154
                         170       180
                  ....*....|....*....|..
gi 2462542783 634 LYTFScqlHKFVHPCFSLEKPG 655
Cdd:cd13744   155 LYTFR---EKFPGKLCSYFSPG 173
SPRY_PRY_TRIM4 cd15809
PRY/SPRY domain in tripartite motif-binding protein 4 (TRIM4), also known as RING finger ...
491-651 2.61e-09

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: 57.15  E-value: 2.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 491 LNKDTCHPWLTISEDGL----TAVRSER-------------RTPARElSPSDTHFTRCVAVMGNLIPVRGHHYWEVEVDE 553
Cdd:cd15809     7 LAEDTAHPKLVFSQEGRyvknGASASSWplfstawsyftgwRNPQKT-TQFVERFQHLPCVLGKNVFTSGKHYWEVENRD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 554 HLDYRVGVAFADV-------RKQEDLGANCLSWcmrhtfasSRHKYEFLHNRTTPDIRITVPPKKIGILLDYEHSKLSFF 626
Cdd:cd15809    86 SLEIAVGVCREDVmgitdgsEMSPHVGIWAICW--------SSAGYRPLTSSPVSPTKQEPALHRVGVFLDHGAGEVSFY 157
                         170       180
                  ....*....|....*....|....*
gi 2462542783 627 NVDLSQHLYTFSCQLHKFVHPCFSL 651
Cdd:cd15809   158 SAVDGVHLHTFSCPLVSRLRPFFWL 182
SPRY_PRY_TRIM50_72 cd12897
PRY/SPRY domain in tripartite motif-binding (TRIM) proteins TRIM50 and TRIM72; This domain, ...
490-649 5.28e-09

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: 56.47  E-value: 5.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 490 RLNKDTCHPWLTISEDGLTAVRSERRTPARElspSDTHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADVRKQ 569
Cdd:cd12897    15 TFDPATAHPLLVVSSGGTVVECGLQKQRRAS---QPERFDKSTCVVASQGFSEGEHYWEVVVGDKPRWALGVIKGTASRK 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 570 EDLGANCLSWCMRHTFASSRHKYEFLHNRTTPDIRITVPPKKIGILLDYEHSKLSFFNVDLSQH---LYTFSCQLHKFVH 646
Cdd:cd12897    92 GKLHASPSHGVWLIGLKEGKVYEAHGEPKEPRPLRVAGRPHRIGVYLSFEDGVLSFFDASDPDDlrtLYTFQERFQGKLY 171

                  ...
gi 2462542783 647 PCF 649
Cdd:cd12897   172 PFF 174
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
392-484 7.82e-09

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: 53.27  E-value: 7.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 392 PSPPI-IKTKEIRSceEAVLICWE--SGNLNPVDSYTVELTQAESPEASGVTESVVGIPTCEsVVQLQPGRSYIIYVRAL 468
Cdd:cd00063     1 PSPPTnLRVTDVTS--TSVTLSWTppEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYT-LTGLKPGTEYEFRVRAV 77
                          90
                  ....*....|....*.
gi 2462542783 469 NMGGPSVRSEPATVHT 484
Cdd:cd00063    78 NGGGESPPSESVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
278-445 4.88e-08

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 56.16  E-value: 4.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 278 DFSDVEqlmgSINTIPAPSAPVINPQVpNSATGSSVRVCWSLYSDDTVESYQLsYRpvqDSSPGTDQAEFTVTVKETYCS 357
Cdd:COG3401   313 APSNVV----SVTTDLTPPAAPSGLTA-TAVGSSSITLSWTASSDADVTGYNV-YR---STSGGGTYTKIAETVTTTSYT 383
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 358 VTNLVPNTQYEFWVTAHNRAGP-SPSSERAVYMTAPSPPIIKTKEIRSceeavlicweSGNLNPVDSYTVELTQAESPEA 436
Cdd:COG3401   384 DTGLTPGTTYYYKVTAVDAAGNeSAPSEEVSATTASAASGESLTASVD----------AVPLTDVAGATAAASAASNPGV 453

                  ....*....
gi 2462542783 437 SGVTESVVG 445
Cdd:COG3401   454 SAAVLADGG 462
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
290-482 1.27e-07

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 55.01  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 290 NTIPAPSAPVINPQVPNSATGSSVRVCWSLYSDDTVESYQLSYRPVQDSSPGTDQAEFTVTVKETYCSVTNLVPNTQYEF 369
Cdd:COG3401   128 ATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYY 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 370 WVTAHNRAGPSPSSERA---VYMTAPSPPI-IKTKEIRSceEAVLICWESGNLNPVDSYTVELtqaeSPEASGVTESVVG 445
Cdd:COG3401   208 RVAATDTGGESAPSNEVsvtTPTTPPSAPTgLTATADTP--GSVTLSWDPVTESDATGYRVYR----SNSGDGPFTKVAT 281
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2462542783 446 IPTCESVVQ-LQPGRSYIIYVRALN-MGGPSVRSEPATV 482
Cdd:COG3401   282 VTTTSYTDTgLTNGTTYYYRVTAVDaAGNESAPSNVVSV 320
SPRY_PRY_TRIM6 cd15823
PRY/SPRY domain in tripartite motif-binding protein 6 (TRIM6), also known as RING finger ...
522-638 1.81e-07

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: 51.79  E-value: 1.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 522 SPSDTHFTrcVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADVRKqedlgANCLSWCMRHTFASSR------------ 589
Cdd:cd15823    36 SYLEEHYD--CSVLGSQHFSSGKHYWEVDVTKKTAWILGVCSHSLGP-----TFSFNQYAQNHNAYSRyqpqsgywvigl 108
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462542783 590 -HKYE---FLHNRTTPDIRITVPPKKIGILLDYEHSKLSFFNVdlSQH---LYTFS 638
Cdd:cd15823   109 qHNHEyraYEDSSTSLLLSMTVPPRRVGVFLDYEAGTVSFYNV--TNHgfpIYTFS 162
SPRY_PRY_TRIM5 cd15822
PRY/SPRY domain in tripartite motif-binding protein 5 (TRIM5), also known as RING finger ...
534-653 1.88e-07

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: 51.84  E-value: 1.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 534 VMGNLIPVRGHHYWEVEVDEHLDYRVGVAfadvrkqedlGANCLSwCMRHTFASSRH-----------KYEF----LHNR 598
Cdd:cd15822    53 VLGSPSITSGKHYWEVDVSKKRAWILGVC----------GGKYPN-STLKDFNKQGKnnqkqcsnyqpKYGYwvigLQNK 121
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462542783 599 ---------TTPDIRI-----TVPPKKIGILLDYEHSKLSFFNVdlSQH---LYTFS-CQLHKFVHPCFSLEK 653
Cdd:cd15822   122 seynafedsSSSDPLIltlslTVPPCRVGVFLDYEAGTVSFFNV--TNHgflIYKFSsCSFSQEVFPYFNPMK 192
SPRY_PRY_TRIM34 cd15825
PRY/SPRY domain in tripartite motif-containing protein 34 (TRIM34), also known as RING finger ...
543-650 2.36e-07

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: 51.38  E-value: 2.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 543 GHHYWEVEVDEHLDYRVGV-------AFADVRKQEDLGANCLSWCMRHTF----ASSRHKYEFLHNRTTPDIRI-----T 606
Cdd:cd15825    48 GKHYWEVDVSKKTAWILGVycrkrsrTFKYVRQGKNHPNVYSRYRPQYGYwvigLQNKSEYYAFEDSSTSDPKVltlsvA 127
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462542783 607 VPPKKIGILLDYEHSKLSFFNVdlSQH---LYTFS-CQLHKFVHPCFS 650
Cdd:cd15825   128 TPPHRVGVFLDYEAGTVSFFNV--TNHgslIYKFSkCCFSQPVYPYFN 173
SPRY_PRY_TRIM10 cd15827
PRY/SPRY domain of tripartite motif-binding protein 10 (TRIM10) also known as hematopoietic ...
487-651 1.35e-06

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: 49.06  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 487 SYFRLNKDTCHPWLTISEDGLTAvrseRRTPARELSP-SDTHFTRCVAVMGNLIPVRGHHYWEVEVDehLDY----RVGV 561
Cdd:cd15827     2 AHISLDPQTSHPKLLLSEDHQRA----RFSYKWQNSPdNPQRFDRATCVLAHDGFTGGRHTWVVSVD--LAHggscTVGV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 562 AFADVRK--------QEDLGANCLSWcmrhTFASSRHKYEflhnrttpdIRITVP--PKKIGILLDYEHSKLSFFNVDLS 631
Cdd:cd15827    76 VSEDVRRkgelrlrpEEGVWAVRLAW----GFVSALGSFP---------TRLALEeqPRQVRVSLDYEVGWVTFVNAVTQ 142
                         170       180
                  ....*....|....*....|
gi 2462542783 632 QHLYTFSCQLHKFVHPCFSL 651
Cdd:cd15827   143 EPIYTFTASFTQKVFPFFGL 162
SPRY_PRY_TRIM22 cd15824
PRY/SPRY domain in tripartite motif-containing protein 22 (TRIM22), also known as RING finger ...
543-651 1.39e-06

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: 49.46  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 543 GHHYWEVEVDEHLDYRVGVaFADVRKQEDLGANCLSW--CMRHTFASSRHK---------------YEFLHNRTTPDIRI 605
Cdd:cd15824    55 GKYYWEVDVSGKIAWILGV-YSKRNNLNKRKSSGFAFdpNVNHPNVYSRYRpqngywviglqneseYNAFEDSSSSDPKV 133
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462542783 606 -----TVPPKKIGILLDYEHSKLSFFNVdlSQH---LYTFS-CQLHKFVHPCFSL 651
Cdd:cd15824   134 ltlsmAVPPHRVGVFLDYEAGTVSFFNV--TNHgslIYKFSkCCFSQPVYPYFNP 186
SPRY_PRY_TRIM72 cd13742
PRY/SPRY domain in tripartite motif-binding protein 72 (TRIM72); This domain, consisting of ...
494-649 1.86e-06

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: 49.09  E-value: 1.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 494 DTCHPWLTISEDGLTAVRSERRTPARELSPSdtHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADVRKQEDLG 573
Cdd:cd13742    19 DTAHPYLVVSSDGKRVECADQKQAVSSDDPN--RFDKANCVVSHQSFSEGEHYWEVIVGDKPRWALGVISAEAGRKGRLH 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 574 A---NCLsWCMrhTFASSRHKYEFLHNRTTPDIRITVPPKKIGILLDYEHSKLSFFNV---DLSQHLYTFSCQLHKFVHP 647
Cdd:cd13742    97 AlpsNGF-WLL--GCKEGKVYEAHVEHKEPRALRVEGRPTRIGVYLSFSDGVLSFYDAsdeDNLVQLFAFHERFPGPLYP 173

                  ..
gi 2462542783 648 CF 649
Cdd:cd13742   174 FF 175
SPRY_PRY_TRIM17 cd15812
PRY/SPRY domain of tripartite motif-binding protein 17 (TRIM17), also known as testis RING ...
543-638 1.88e-06

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: 48.73  E-value: 1.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 543 GHHYWEVEVDEHLD--YRVGVAFADVRKQEDLGAnclswCMRHTF----ASSRHKYEFLHNRTTPdIRITVPPKKIGILL 616
Cdd:cd15812    53 GRHYWEVGMNLTGDalWALGVCRDNVSRKDRVPK-----SPENGFwvvqLSKGKKYLSAMSALTP-VTLTEPPSHMGIFL 126
                          90       100
                  ....*....|....*....|..
gi 2462542783 617 DYEHSKLSFFNVDLSQHLYTFS 638
Cdd:cd15812   127 DFEAGEVSFYSVNDGSHLHTYS 148
SPRY_PRY_TRIM7 cd13740
PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7); This domain, consisting of the ...
490-651 6.15e-06

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: 46.87  E-value: 6.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 490 RLNKDTCHPWLTISEDgLTAVRSERRtpARELSPSDTHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADVRKQ 569
Cdd:cd13740     3 TLDPDSANPRLILSLD-LKSVRLGER--AQDLPNHPCRFDTNTRVLASCGFSSGRHHWEVEVGSKDGWAFGVARESVRRK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 570 edlGANCLS-----WCMRHTfaSSRHkyeflhnrttpdIRITVPPK---------KIGILLDYEHSKLSFFNVDLSQHLY 635
Cdd:cd13740    80 ---GLTPFTpeegvWALQLN--GGQY------------WAVTSPERtplscghlsRVRVALDLEVGAVSFYAAEDMRHIY 142
                         170
                  ....*....|....*.
gi 2462542783 636 TFSCQLHKFVHPCFSL 651
Cdd:cd13740   143 TFRVNFQERVFPLFSV 158
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
543-651 1.81e-05

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: 44.34  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 543 GHHYWEVEVD--EHLDYRVGVA--FADVRKQEDLGANCLSWCMRHTFASSRHKYeflhnRTTPDIRITVPPKKIGILLDY 618
Cdd:cd11709     1 GKWYWEVRVDsgNGGLIQVGWAtkSFSLDGEGGVGDDEESWGYDGSRLRKGHGG-----SSGPGGRPWKSGDVVGCLLDL 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2462542783 619 EHSKLSFF-NVDLSQHLYTFSCQLHKFVHPCFSL 651
Cdd:cd11709    76 DEGTLSFSlNGKDLGVAFTNLFLKGGGLYPAVSL 109
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
392-474 2.15e-05

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: 43.37  E-value: 2.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783  392 PSPPIIKTKEIRSceEAVLICWESGNLNPVDSYTVELTQAESPEASGVTESVVGIPTCESVVQ-LQPGRSYIIYVRALNM 470
Cdd:smart00060   2 SPPSNLRVTDVTS--TSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTgLKPGTEYEFRVRAVNG 79

                   ....
gi 2462542783  471 GGPS 474
Cdd:smart00060  80 AGEG 83
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
308-376 8.00e-05

Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple acid phosphatase proteins.


Pssm-ID: 465220 [Multi-domain]  Cd Length: 93  Bit Score: 42.01  E-value: 8.00e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462542783 308 ATGSSVRVCWslYSDDTVESYQLSYRPVQDSSPGTDQAEFTVTVKETYCS-------VTNLVPNTQYEFWVTAHNR 376
Cdd:pfam16656  10 GDSTSMTVSW--VTPSAVTSPVVQYGTSSSALTSTATATSSTYTTGDGGTgyihratLTGLEPGTTYYYRVGDDNG 83
SPRY_SOCS3 cd12876
SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY ...
533-626 1.13e-04

SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY domain-containing SOCS box protein family (SPSB1-4, also known as SSB-1 to -4) is composed of a central SPRY protein interaction domain and a C-terminal SOCS box. All four SPSB proteins interact with c-Met, the hepatocyte growth factor receptor, but SOCS3 regulates cellular response to a variety of cytokines such as leukemia inhibitory factor (LIF) and interleukin 6. SOCS3, along with SOCS1, are expressed by immune cells and cells of the central nervous system (CNS) and have the potential to impact immune processes within the CNS. In non-small cell lung cancer (NSCLC), SOCS3 is silenced and proline-rich tyrosine kinase 2 (Pyk2) is over-expressed; it has been suggested that SOCS3 could be an effective way to prevent the progression of NSCLC due to its role in regulating Pyk2 expression.


Pssm-ID: 293936  Cd Length: 185  Bit Score: 43.30  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 533 AVMGNLIPVRGHHYWEVEVDEHL---DYRVGVAFADVRKQED-------LGANCLSWCMrhtfassRHKYEFLHN-RTTP 601
Cdd:cd12876    34 AVRGTKPLTNGQHYWEIKMSSPVygtDMMVGVGTKKADLHAYryefcslLGEDEESWGL-------SYKGLLWHDgQSRP 106
                          90       100       110
                  ....*....|....*....|....*....|
gi 2462542783 602 -----DIRITVppkkIGILLDYEHSKLSFF 626
Cdd:cd12876   107 ytspfGNQGTI----IGVHLDMWRGTLTFY 132
COG3979 COG3979
Chitodextrinase [Carbohydrate transport and metabolism];
294-393 2.45e-04

Chitodextrinase [Carbohydrate transport and metabolism];


Pssm-ID: 443178 [Multi-domain]  Cd Length: 369  Bit Score: 43.99  E-value: 2.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 294 APSAPViNPQVPNsATGSSVRVCWSlYSDDT--VESYQLsYRpvqdsspGTDQAEfTVTVKETYcSVTNLVPNTQYEFWV 371
Cdd:COG3979     2 APTAPT-GLTASN-VTSSSVSLSWD-ASTDNvgVTGYDV-YR-------GGDQVA-TVTGLTAW-TVTGLTPGTEYTFTV 68
                          90       100
                  ....*....|....*....|...
gi 2462542783 372 TAHNRAG-PSPSSERAVYMTAPS 393
Cdd:COG3979    69 GACDAAGnVSAASGTSTAMFGGS 91
SPRY_PRY_TRIM47 cd15808
PRY/SPRY domain in tripartite motif-containing protein 47 (TRIM47), also known as RING finger ...
524-628 2.82e-04

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


Pssm-ID: 293980  Cd Length: 206  Bit Score: 42.56  E-value: 2.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542783 524 SDTHFTRCVAVMGNLIPVRGHHYWEVEVDEHLdYRVGVAFADVRKQED-----LGANCLSWCMRHtfaSSRHKYEFLHNR 598
Cdd:cd15808    41 SPTRFTHCEQVLGEGALDRGTYYWEVEIIEGW-VSVGVMAEDFSPREPydrgrLGRNAHSCCLQW---NGRNFSVWFHGL 116
                          90       100       110
                  ....*....|....*....|....*....|
gi 2462542783 599 TTPDIRITVPpkKIGILLDYEHSKLSFFNV 628
Cdd:cd15808   117 EAPLPHPFSP--TVGVCLEYADRALAFYAV 144
Bbox2_MuRF cd19788
B-box-type 2 zinc finger found in muscle-specific RING finger protein (MuRF) family; This ...
178-205 5.87e-04

B-box-type 2 zinc finger found in muscle-specific RING finger protein (MuRF) family; This family corresponds to a group of striated muscle-specific tripartite motif (TRIM) proteins, including TRIM63/MuRF-1, TRIM55/MuRF-2, and TRIM54/MuRF-3, which function as E3 ubiquitin ligases in ubiquitin-mediated muscle protein turnover. They are tightly developmentally regulated in skeletal muscle and associate with different cytoskeleton components, such as microtubules, Z-disks and M-bands, as well as with metabolic enzymes and nuclear proteins. They also cooperate with diverse proteins implicated in selective protein degradation by the proteasome and autophagosome, and target proteins of metabolic regulation, sarcomere assembly and transcriptional regulation. Moreover, MURFs display variable fibre-type preferences. TRIM63/MuRF-1 is predominantly fast (type II) fibre-associated in skeletal muscle. TRIM55/MuRF-2 is predominantly slow-fibre associated. TRIM54/MuRF-3 is ubiquitously present. They play an active role in microtubule-mediated sarcomere assembly. MuRFs belong to the C-II subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, and an acidic residue-rich (AR) domain positioned C-terminal to the RBCC domain. They also harbor a MURF family-specific conserved box (MFC) between its RING-HC finger and Bbox domains. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380846  Cd Length: 39  Bit Score: 37.83  E-value: 5.87e-04
                          10        20
                  ....*....|....*....|....*...
gi 2462542783 178 VFCVTCKTPIRAFQKVFDEHKEHEVIPL 205
Cdd:cd19788    12 IYCLTCEVPTCSMCKVFGAHKDCEVAPL 39
fn3 pfam00041
Fibronectin type III domain;
420-477 5.95e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 39.32  E-value: 5.95e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462542783 420 PVDSYTVELTQAESPEASgVTESVVGIPTCESVVQLQPGRSYIIYVRALNMGGPSVRS 477
Cdd:pfam00041  29 PITGYEVEYRPKNSGEPW-NEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPPS 85
Bbox2_MuRF3_C-II cd19833
B-box-type 2 zinc finger found in muscle-specific RING finger protein 3 (MuRF-3) and similar ...
178-206 1.74e-03

B-box-type 2 zinc finger found in muscle-specific RING finger protein 3 (MuRF-3) and similar proteins; MuRF-3, also known as tripartite motif-containing protein 54 (TRIM54), or RING finger protein 30 (RNF30), is an E3 ubiquitin-protein ligase in ubiquitin-mediated muscle protein turnover. It is ubiquitously detected in all fibre types, and is developmentally upregulated, associates with microtubules, the sarcomeric M-line and Z-line, and is required for microtubule stability and myogenesis. It associates with glutamylated microtubules during skeletal muscle development, and is required for skeletal myoblast differentiation and development of cellular microtubular networks. MuRF-3 controls the degradation of four-and-a-half LIM domain (FHL2) and gamma-filamin and is required for maintenance of ventricular integrity after myocardial infarction (MI). MuRF-3 belongs to the C-II subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, and an acidic residue-rich (AR) domain. It also harbors a MURF family-specific conserved box (MFC) between its RING-HC finger and Bbox domains. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380891  Cd Length: 43  Bit Score: 36.59  E-value: 1.74e-03
                          10        20
                  ....*....|....*....|....*....
gi 2462542783 178 VFCVTCKTPIRAFQKVFDEHKEHEVIPLN 206
Cdd:cd19833    13 IYCLSCEVPTCSLCKVFGAHKDCEVAPLP 41
PRY pfam13765
SPRY-associated domain; PRY is a 50-60 amino acids domain associated with SPRY domains, ...
491-536 4.12e-03

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


Pssm-ID: 463976  Cd Length: 49  Bit Score: 35.53  E-value: 4.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2462542783 491 LNKDTCHPWLTISEDGLTAVRSERRtpaRELSPSDTHFTRCVAVMG 536
Cdd:pfam13765   3 LDPNTAHPSLVLSEDLKSVRYGDER---QNVPDNPERFDSWPCVLG 45
PRY smart00589
associated with SPRY domains;
491-537 5.57e-03

associated with SPRY domains;


Pssm-ID: 128857  Cd Length: 52  Bit Score: 35.24  E-value: 5.57e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2462542783  491 LNKDTCHPWLTISEDGLTAVRSERRTPARElSPSdtHFTRCVAVMGN 537
Cdd:smart00589   6 LDPDTAHPYLLLSEDRRSVRYGDLKQSLPD-NPE--RFDSYPCVLGS 49
 
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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