NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1907094698|ref|XP_036014111|]
View 

cardiomyopathy-associated protein 5 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SPRY super family cl02614
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 3492-3654 3.66e-84

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.


The actual alignment was detected with superfamily member cd12898:

Pssm-ID: 470632  Cd Length: 171  Bit Score: 273.73  E-value: 3.66e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3492 GTRFLLLRETAHPALQISAN-GTVISFSERRR----LTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAGA 3566
Cdd:cd12898      1 GTRFLLLRETAHPALHISSDrGTVIYFHERRRkmssLTECPSVLGEELPSCGQYYWETTVTRCPAYRLGICSSSASQAGA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3567 LGQGETSWYMHC---SEPQRYTFFYSGIVSEVHATERPARVGILLDYTNQRLLFINAESGQLLFIVRHRFNEGVHPAFAL 3643
Cdd:cd12898     81 LGEGSTSWCLHCvptSEPCRYTLLHSGIVSDVFVTERPARVGTLLDYNNGRLIFINAESGQLLGIFRHRFAQPCHPAFAL 160

                          170
                   ....*....|.
gi 1907094698 3644 EKPGRCTLHLG 3654
Cdd:cd12898    161 EKPGKLELHMG 171
PTZ00341 super family cl31759
Ring-infected erythrocyte surface antigen; Provisional
 489-640 1.35e-06

Ring-infected erythrocyte surface antigen; Provisional


The actual alignment was detected with superfamily member PTZ00341:

Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 54.79  E-value: 1.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698  489 EPIVHREEEHAPEPivhREEEHAPESivHREEEHAPESIVQREEEHAPEPESIVHREEEHAPGPvpivHREEEHVPELES 568
Cdd:PTZ00341   434 ESVEDNEEEHSGDA---NEEELSVDE--HVEEHNADDSGEQQSDDESGEHQSVNEIVEEQSVNE----HVEEPTVADIVE 504

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907094698  569 iVHRGEEHAPEPIVHRDEGHapepivHREEEHVPEPIVhrDEGHAPEPIVhREEEHVPEPESIVHREEEHAP 640
Cdd:PTZ00341   505 -QETVDEHVEEPAVDENEEQ------QTADEHVEEPTI--AEEHVEEEIS-TAEEHIEEPASDVQQDSEAAP 566
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 3309-3397 1.45e-06

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: 49.03  E-value: 1.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3309 EPSSATSTTIAVYWSVNKED--VVDSFQVYCVEEPQDD-QEINELVeeyrltVKESCCIFEDLEPDRCYQVWVMAVNFTG 3385
Cdd:cd00063      8 RVTDVTSTSVTLSWTPPEDDggPITGYVVEYREKGSGDwKEVEVTP------GSETSYTLTGLKPGTEYEFRVRAVNGGG 81

                           90
                   ....*....|..
gi 1907094698 3386 CSLPSERAIFRT 3397
Cdd:cd00063     82 ESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 3404-3490 3.70e-05

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: 45.18  E-value: 3.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3404 IHVEDCTvcWNTATVRWRPANPEATE--TYTLEYCRQHSPEGEGLRSfSGIKGLQLKV-NLPPNDNYFFYVRATNASGTS 3480
Cdd:cd00063      7 LRVTDVT--STSVTLSWTPPEDDGGPitGYVVEYREKGSGDWKEVEV-TPGSETSYTLtGLKPGTEYEFRVRAVNGGGES 83

                           90
                   ....*....|
gi 1907094698 3481 EQSEAALIST 3490
Cdd:cd00063     84 PPSESVTVTT 93
CC_brat-like super family cl29238
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ...
 3141-3265 6.53e-05

coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family contains the coiled-coil (CC) region of Drosophila brain tumor (Brat), a translational repressor that belongs to the tripartite motif (TRIM) protein superfamily. TRIM proteins play important roles in various cellular processes and are involved in many diseases which consists of two B-box domains and a coiled-coil (CC) domain at the N-terminal region, and an NHL domain at the C-terminus. Brat localizes at the basal cortex during asymmetric division of Drosophila neuroblasts by directly interacting with the scaffolding protein Miranda (Mira), which it does through the CC-NHL domain tandem, indicating that the function of the Brat CC domain is to assemble Brat-NHL in dimeric form which is necessary for Mira binding. Brat CC forms an elongated antiparallel dimer similar to its other TRIM protein counterparts, but the overall length of Brat CC dimer is shorter than the TRIMs.


The actual alignment was detected with superfamily member smart00502:

Pssm-ID: 475168  Cd Length: 127  Bit Score: 45.33  E-value: 6.53e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698  3141 KVQLGEFLENLQEKSLRIEAFVSEIESFFNTIEEKCSKNEKRLEMQNEEMMKRVLAQYDEKAQSFEEVKKKKMEFLHDQM 3220
Cdd:smart00502    2 REALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQL 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 1907094698  3221 VHFLQSMDTAKDTLETIVREAEELDETVFLASFEEINERLLSAME 3265
Cdd:smart00502   82 ESLTQKQEKLSHAINFTEEALNSGDPTELLLSKKLIIERLQNLLK 126
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
 373-560 7.16e-04

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.85  E-value: 7.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698  373 MEPPSIPATMVLERAKEELEQNAQGKESSEDDASVLTGSADDVQQEGLVSVNHSMPWEaekeslETGPPRPAPAIQEKFE 452
Cdd:PRK10263   341 TQTPPVASVDVPPAQPTVAWQPVPGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNEPLQ------QPVQPQQPYYAPAAEQ 414

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698  453 PDMEGLEPISTEKTEQASEYVTSSEPIVHREEEHAPEPivhrEEEHAPEPiVHREEEHAPESIVHREEEHAPESIvqrEE 532
Cdd:PRK10263   415 PAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQ----QSTFAPQS-TYQTEQTYQQPAAQEPLYQQPQPV---EQ 486

                          170       180
                   ....*....|....*....|....*...
gi 1907094698  533 EHAPEPESIVhreEEHAPGPVPIVHREE 560
Cdd:PRK10263   487 QPVVEPEPVV---EETKPARPPLYYFEE 511
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
 1762-2126 1.53e-03

104 kDa microneme/rhoptry antigen; Provisional


The actual alignment was detected with superfamily member PTZ00449:

Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 44.68  E-value: 1.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 1762 KPDGLVNQHEDRKPGTGQLESSESTDLMSEKlGAAPLDTDHTSETRNQETSKAPVSGEKLSQ--EPRRVQSKAVDDS-EE 1838
Cdd:PTZ00449   548 KPGETKEGEVGKKPGPAKEHKPSKIPTLSKK-PEFPKDPKHPKDPEEPKKPKRPRSAQRPTRpkSPKLPELLDIPKSpKR 626

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 1839 GRKLASGNVEVLTQSKSVP----AVKAKATPQPPETPEVTQKPSEKSLVTEQGL-PAEKGKKGIS------SFKSWMSSL 1907
Cdd:PTZ00449   627 PESPKSPKRPPPPQRPSSPerpeGPKIIKSPKPPKSPKPPFDPKFKEKFYDDYLdAAAKSKETKTtvvldeSFESILKET 706

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 1908 LFGS---------SIPDSKVSDNEDLETRPG-PSVEKAVPAIEPKGTVPAEVNIAEKPAVHSLPEVTVKLAEEPkgvsvk 1977
Cdd:PTZ00449   707 LPETpgtpfttprPLPPKLPRDEEFPFEPIGdPDAEQPDDIEFFTPPEEERTFFHETPADTPLPDILAEEFKEE------ 780

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 1978 sSISQDLKEKltflsnEDVLKQPKSNSENygQKELPGFSEGM--------GESLATSVGDKHPGIHPCSPMGEKVGMEEA 2049
Cdd:PTZ00449   781 -DIHAETGEP------DEAMKRPDSPSEH--EDKPPGDHPSLpkkrhrldGLALSTTDLESDAGRIAKDASGKIVKLKRS 851

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 2050 QNMAPLHITESQRRQKPEVSspsmwNISARKEEPSSDHKETWLSS----SDVVDRMPQK-----PKSAQSAFTRmnseEP 2120
Cdd:PTZ00449   852 KSFDDLTTVEEAEEMGAEAR-----KIVVDDDGTEADDEDTHPPEekhkSEVRRRRPPKkpskpKKPSKPKKPK----KP 922


                   ....*.
gi 1907094698 2121 ASMILP 2126
Cdd:PTZ00449   923 DSAFIP 928
 
Name Accession Description Interval E-value
SPRY_PRY_TRIM76 cd12898
PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76), also called ...
 3492-3654 3.66e-84

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: 273.73  E-value: 3.66e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3492 GTRFLLLRETAHPALQISAN-GTVISFSERRR----LTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAGA 3566
Cdd:cd12898      1 GTRFLLLRETAHPALHISSDrGTVIYFHERRRkmssLTECPSVLGEELPSCGQYYWETTVTRCPAYRLGICSSSASQAGA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3567 LGQGETSWYMHC---SEPQRYTFFYSGIVSEVHATERPARVGILLDYTNQRLLFINAESGQLLFIVRHRFNEGVHPAFAL 3643
Cdd:cd12898     81 LGEGSTSWCLHCvptSEPCRYTLLHSGIVSDVFVTERPARVGTLLDYNNGRLIFINAESGQLLGIFRHRFAQPCHPAFAL 160

                          170
                   ....*....|.
gi 1907094698 3644 EKPGRCTLHLG 3654
Cdd:cd12898    161 EKPGKLELHMG 171
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 3537-3654 6.89e-10

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: 59.23  E-value: 6.89e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698  3537 CGQHYWETTVADSPAYRLGICTSSAVRAGALGQGET--SWYMHCSEPQRYtffYSGIVSE--VHATERPARVGILLDYTN 3612
Cdd:smart00449    1 SGRHYFEVEIGDGGHWRVGVATKSVPRGYFALLGEDkgSWGYDGDGGKKY---HNSTGPEygLPLQEPGDVIGCFLDLEA 77

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 1907094698  3613 QRLLFINAESGQLLFIVRH-RFNEGVHPAFALEKPGRCTLHLG 3654
Cdd:smart00449   78 GTISFYKNGKYLHGLAFFDvKFSGPLYPAFSLGSGNSVRLNFG 120
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 489-640 1.35e-06

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 54.79  E-value: 1.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698  489 EPIVHREEEHAPEPivhREEEHAPESivHREEEHAPESIVQREEEHAPEPESIVHREEEHAPGPvpivHREEEHVPELES 568
Cdd:PTZ00341   434 ESVEDNEEEHSGDA---NEEELSVDE--HVEEHNADDSGEQQSDDESGEHQSVNEIVEEQSVNE----HVEEPTVADIVE 504

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907094698  569 iVHRGEEHAPEPIVHRDEGHapepivHREEEHVPEPIVhrDEGHAPEPIVhREEEHVPEPESIVHREEEHAP 640
Cdd:PTZ00341   505 -QETVDEHVEEPAVDENEEQ------QTADEHVEEPTI--AEEHVEEEIS-TAEEHIEEPASDVQQDSEAAP 566
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 3540-3655 1.41e-06

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: 50.03  E-value: 1.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3540 HYWETTV--ADSPAYRLGICTSSAVRAGALGQGET--SWYMHCSEPQRYTffysgiVSEVHATERPA-----RVGILLDY 3610
Cdd:pfam00622    2 HYFEVEIfgQDGGGWRVGWATKSVPRKGERFLGDEsgSWGYDGWTGKKYW------ASTSPLTGLPLfepgdVIGCFLDY 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1907094698 3611 TNQRLLFINAEsGQLLFIVRH-RFNEGVHPAFALEKPGRCTLHLGL 3655
Cdd:pfam00622   76 EAGTISFTKNG-KSLGYAFRDvPFAGPLFPAVSLGAGEGLKFNFGL 120
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 3309-3397 1.45e-06

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: 49.03  E-value: 1.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3309 EPSSATSTTIAVYWSVNKED--VVDSFQVYCVEEPQDD-QEINELVeeyrltVKESCCIFEDLEPDRCYQVWVMAVNFTG 3385
Cdd:cd00063      8 RVTDVTSTSVTLSWTPPEDDggPITGYVVEYREKGSGDwKEVEVTP------GSETSYTLTGLKPGTEYEFRVRAVNGGG 81

                           90
                   ....*....|..
gi 1907094698 3386 CSLPSERAIFRT 3397
Cdd:cd00063     82 ESPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 3300-3387 3.95e-06

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: 47.61  E-value: 3.95e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698  3300 PQPPRLEPqepSSATSTTIAVYWSVNKEDVVDSFQVYCVEEpqdDQEINELVEEYRLTVKESCCIFEDLEPDRCYQVWVM 3379
Cdd:smart00060    2 SPPSNLRV---TDVTSTSVTLSWEPPPDDGITGYIVGYRVE---YREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVR 75


                    ....*...
gi 1907094698  3380 AVNFTGCS 3387
Cdd:smart00060   76 AVNGAGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 3404-3490 3.70e-05

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: 45.18  E-value: 3.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3404 IHVEDCTvcWNTATVRWRPANPEATE--TYTLEYCRQHSPEGEGLRSfSGIKGLQLKV-NLPPNDNYFFYVRATNASGTS 3480
Cdd:cd00063      7 LRVTDVT--STSVTLSWTPPEDDGGPitGYVVEYREKGSGDWKEVEV-TPGSETSYTLtGLKPGTEYEFRVRAVNGGGES 83

                           90
                   ....*....|
gi 1907094698 3481 EQSEAALIST 3490
Cdd:cd00063     84 PPSESVTVTT 93
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
 3141-3265 6.53e-05

B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains


Pssm-ID: 128778  Cd Length: 127  Bit Score: 45.33  E-value: 6.53e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698  3141 KVQLGEFLENLQEKSLRIEAFVSEIESFFNTIEEKCSKNEKRLEMQNEEMMKRVLAQYDEKAQSFEEVKKKKMEFLHDQM 3220
Cdd:smart00502    2 REALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQL 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 1907094698  3221 VHFLQSMDTAKDTLETIVREAEELDETVFLASFEEINERLLSAME 3265
Cdd:smart00502   82 ESLTQKQEKLSHAINFTEEALNSGDPTELLLSKKLIIERLQNLLK 126
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 373-560 7.16e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.85  E-value: 7.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698  373 MEPPSIPATMVLERAKEELEQNAQGKESSEDDASVLTGSADDVQQEGLVSVNHSMPWEaekeslETGPPRPAPAIQEKFE 452
Cdd:PRK10263   341 TQTPPVASVDVPPAQPTVAWQPVPGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNEPLQ------QPVQPQQPYYAPAAEQ 414

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698  453 PDMEGLEPISTEKTEQASEYVTSSEPIVHREEEHAPEPivhrEEEHAPEPiVHREEEHAPESIVHREEEHAPESIvqrEE 532
Cdd:PRK10263   415 PAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQ----QSTFAPQS-TYQTEQTYQQPAAQEPLYQQPQPV---EQ 486

                          170       180
                   ....*....|....*....|....*...
gi 1907094698  533 EHAPEPESIVhreEEHAPGPVPIVHREE 560
Cdd:PRK10263   487 QPVVEPEPVV---EETKPARPPLYYFEE 511
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 3404-3480 7.35e-04

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: 41.06  E-value: 7.35e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907094698  3404 IHVEDCTvcWNTATVRWRPANPEATETYTLEYCRQHSPEGEGLRSFSGI-KGLQLKV-NLPPNDNYFFYVRATNASGTS 3480
Cdd:smart00060    7 LRVTDVT--STSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTpSSTSYTLtGLKPGTEYEFRVRAVNGAGEG 83
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 1762-2126 1.53e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 44.68  E-value: 1.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 1762 KPDGLVNQHEDRKPGTGQLESSESTDLMSEKlGAAPLDTDHTSETRNQETSKAPVSGEKLSQ--EPRRVQSKAVDDS-EE 1838
Cdd:PTZ00449   548 KPGETKEGEVGKKPGPAKEHKPSKIPTLSKK-PEFPKDPKHPKDPEEPKKPKRPRSAQRPTRpkSPKLPELLDIPKSpKR 626

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 1839 GRKLASGNVEVLTQSKSVP----AVKAKATPQPPETPEVTQKPSEKSLVTEQGL-PAEKGKKGIS------SFKSWMSSL 1907
Cdd:PTZ00449   627 PESPKSPKRPPPPQRPSSPerpeGPKIIKSPKPPKSPKPPFDPKFKEKFYDDYLdAAAKSKETKTtvvldeSFESILKET 706

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 1908 LFGS---------SIPDSKVSDNEDLETRPG-PSVEKAVPAIEPKGTVPAEVNIAEKPAVHSLPEVTVKLAEEPkgvsvk 1977
Cdd:PTZ00449   707 LPETpgtpfttprPLPPKLPRDEEFPFEPIGdPDAEQPDDIEFFTPPEEERTFFHETPADTPLPDILAEEFKEE------ 780

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 1978 sSISQDLKEKltflsnEDVLKQPKSNSENygQKELPGFSEGM--------GESLATSVGDKHPGIHPCSPMGEKVGMEEA 2049
Cdd:PTZ00449   781 -DIHAETGEP------DEAMKRPDSPSEH--EDKPPGDHPSLpkkrhrldGLALSTTDLESDAGRIAKDASGKIVKLKRS 851

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 2050 QNMAPLHITESQRRQKPEVSspsmwNISARKEEPSSDHKETWLSS----SDVVDRMPQK-----PKSAQSAFTRmnseEP 2120
Cdd:PTZ00449   852 KSFDDLTTVEEAEEMGAEAR-----KIVVDDDGTEADDEDTHPPEekhkSEVRRRRPPKkpskpKKPSKPKKPK----KP 922


                   ....*.
gi 1907094698 2121 ASMILP 2126
Cdd:PTZ00449   923 DSAFIP 928
fn3 pfam00041
Fibronectin type III domain;
3311-3390 2.27e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 39.71  E-value: 2.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3311 SSATSTTIAVYWS--VNKEDVVDSFQVYC--VEEPQDDQEINELVEEYRLTVKesccifeDLEPDRCYQVWVMAVNFTGC 3386
Cdd:pfam00041    9 TDVTSTSLTVSWTppPDGNGPITGYEVEYrpKNSGEPWNEITVPGTTTSVTLT-------GLKPGTEYEVRVQAVNGGGE 81


                   ....
gi 1907094698 3387 SLPS 3390
Cdd:pfam00041   82 GPPS 85
 
Name Accession Description Interval E-value
SPRY_PRY_TRIM76 cd12898
PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76), also called ...
 3492-3654 3.66e-84

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: 273.73  E-value: 3.66e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3492 GTRFLLLRETAHPALQISAN-GTVISFSERRR----LTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAGA 3566
Cdd:cd12898      1 GTRFLLLRETAHPALHISSDrGTVIYFHERRRkmssLTECPSVLGEELPSCGQYYWETTVTRCPAYRLGICSSSASQAGA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3567 LGQGETSWYMHC---SEPQRYTFFYSGIVSEVHATERPARVGILLDYTNQRLLFINAESGQLLFIVRHRFNEGVHPAFAL 3643
Cdd:cd12898     81 LGEGSTSWCLHCvptSEPCRYTLLHSGIVSDVFVTERPARVGTLLDYNNGRLIFINAESGQLLGIFRHRFAQPCHPAFAL 160

                          170
                   ....*....|.
gi 1907094698 3644 EKPGRCTLHLG 3654
Cdd:cd12898    161 EKPGKLELHMG 171
SPRY_PRY_C-II cd13734
PRY/SPRY domain in tripartite motif-containing proteins 1, 9, 18, 36, 46, 67,76 (TRIM1, TRIM9, ...
 3495-3652 1.47e-52

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: 183.25  E-value: 1.47e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3495 FLLLRETAHPALQISANGTVISFSE----------RRRLTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRA 3564
Cdd:cd13734      1 FKLDPKTAHRKLRLSNDNLTVEYDPegskdqaavlPRRFTGSPAVLGDVAISSGRHYWEVSVSRSTSYRVGVAYKSAPRD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3565 GALGQGETSWYMHCSEpQRYTFFYSGIVSEVHATERPARVGILLDYTNQRLLFINAESGQLLFIVRHRFNEGVHPAFALE 3644
Cdd:cd13734     81 EDLGKNSTSWCLSRDN-NRYTARHDGKVVDLRVTGHPARIGVLLDYDNGTLSFYDAESKQHLYTFHVDFEGPVCPAFAVW 159


                   ....*...
gi 1907094698 3645 kPGRCTLH 3652
Cdd:cd13734    160 -NGSLTLH 166
SPRY_PRY_TRIM76_like cd12899
PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76)-like; This domain is ...
 3495-3655 2.08e-34

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: 131.45  E-value: 2.08e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3495 FLLLRETAHPALQISANGTVISFSERR-----------RLTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVR 3563
Cdd:cd12899      2 FHLNEDTAHPLLSISEDGFTVVYGEEElpardlsfsdnSFTRCVAVMGSLIPVRGKHYWEVEVDEQTEYRVGVAFEDTQR 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3564 AGALGQGETSWYM-HCSEPQR--YTFFYSGIVSEVHATERPARVGILLDYTNQRLLFINAESGQLLFIVRHRFNEGVHPA 3640
Cdd:cd12899     82 NGYLGANNTSWCMrHIITPSRhkYEFLHNGWTPDIRITVPPKKIGILLDYDSGRLSFFNVDLAQHLYTFSCQFQHFVHPC 161

                          170
                   ....*....|....*
gi 1907094698 3641 FALEKPGRCTLHLGL 3655
Cdd:cd12899    162 FSLEKPGALKVHNGI 176
SPRY_BSPRY cd12904
SPRY domain in Ro-Ret family; This domain, named BSPRY, has been identified in the Ro-Ret ...
 3501-3642 1.90e-19

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


Pssm-ID: 293961 [Multi-domain]  Cd Length: 171  Bit Score: 88.25  E-value: 1.90e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3501 TAHPALQISANGTVISFSERR----------RLTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAGA---- 3566
Cdd:cd12904      7 TVSPLLSLSEDRRTLTFSPKKarqsppddpeRFDHWPNALASLSFSSGTHAWVVDVGKSCAYKVGVCYGSLERKGSgnea 86

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907094698 3567 -LGQGETSWYMHCSEpQRYTFFYSGIVSEVHATERPARVGILLDYTNQRLLFINAESGQLLFIVRHRFNEGVHPAFA 3642
Cdd:cd12904     87 rLGYNAFSWVFSRYD-GEFSFSHNGQHVPLELLKCPARVGVLLDWPSQELLFYDPDSCTVLHSHREAFAAPLLPVFA 162
SPRY_PRY cd12874
PRY/SPRY domain, also known as B30.2; This domain contains residues in the N-terminus that ...
 3500-3643 2.18e-16

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: 79.66  E-value: 2.18e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3500 ETAHPALQISANGTVIS--------FSERRRLTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAGA---LG 3568
Cdd:cd12874      6 DTAHLNLILSDDLRSVRvgdisqhpPEPPPRFFECWQVLGSQSFSSGRHYWEVDVQDDSSWYVGVTYKSLPRKGKmsnLG 85

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907094698 3569 QGETSWYMHCSEpQRYTFFYSGIVSEVHATErPARVGILLDYTNQRLLFIN-AESGQLLFIVRHRFNEGVHPAFAL 3643
Cdd:cd12874     86 RNNGSWCLEWRE-NEFSAWHNNPETRLPVTP-PRRLGVFLDCDGGSLSFYGvTDGVQLLYTFKAKFTEPLYPAFWL 159
SPRY_PRY_C-I_1 cd13733
PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM5, TRIM6, TRIM7, ...
 3500-3641 3.26e-15

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: 76.36  E-value: 3.26e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3500 ETAHPALQISANGTVISFSERR--------RLTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAGAL---- 3567
Cdd:cd13733      7 DTAHPNLILSEDLKSVRYGDKRqnlpdnpeRFDTCVCVLGSEGFSSGRHYWEVEVGGKTDWDLGVARESVNRKGKItlsp 86

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907094698 3568 GQGetSWYMHCSEPQRYTFFYSGIVSeVHATERPARVGILLDYTNQRLLFINAESGQLLFIVRHRFNEGVHPAF 3641
Cdd:cd13733     87 ENG--YWTVGLRNGNEYKALTSPSTP-LSLREKPQKVGVFLDYEEGQVSFYNVDDGSHIYTFTDCFTEKLYPYF 157
SPRY_PRY_SPRYD4 cd12903
PRY/SPRY domain containing protein 4 (SPRYD4); This domain, consisting of the distinct ...
 3522-3643 3.61e-15

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: 75.95  E-value: 3.61e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3522 RLTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAGALGQGETSW---YMHcsepQRYTFFYSGIVSEVHAT 3598
Cdd:cd12903     39 RFRDWAVVLGDTPVTSGRHYWEVTVKRSQEFRIGVADVDMSRDECIGTNESSWvfaYAQ----RKWYAMVANETVPVPLV 114

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1907094698 3599 ERPARVGILLDYTNQRLLFINAESGQLLFIVRHRFNEGVHPAFAL 3643
Cdd:cd12903    115 GKPDRVGLLLDYEAGKLSLVDVEKNSVVHTMSAEFRGPVVPAFAL 159
SPRY_PRY_TRIM35 cd12893
PRY/SPRY domain in tripartite motif-containing protein 35 (TRIM35); This PRY/SPRY domain is ...
 3501-3641 3.85e-15

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: 76.13  E-value: 3.85e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3501 TAHPALQISANGTVISFSERR--------RLTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAGALGQGET 3572
Cdd:cd12893      8 TAHPWLSLSEDLTSVRYSSEKqqlpdnpeRFDPYPCVLGSEGFTSGKHSWDVEVGDNTSWMLGVAKESVQRKGKFTLSPE 87

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907094698 3573 S--WYMhCSEPQRYTFFYSGI-VSEVHATERPARVGILLDYTNQRLLFINAESGQLLFIVRHRFNEGVHPAF 3641
Cdd:cd12893     88 SgfWTI-GFSEGKYSARTSPEpRTPLRVKQKPQRIRVQLDWDRGKVSFSDPDTNTHIHTFTHTFTERVFPYF 158
SPRY_PRY_TRIM39 cd13745
PRY/SPRY domain in tripartite motif-binding protein 39 (TRIM39) and TRIM39-like; This domain, ...
 3500-3641 5.42e-15

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: 75.74  E-value: 5.42e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3500 ETAHPALQISANGTVISFSERR--------RLTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAG--ALGQ 3569
Cdd:cd13745     10 DTAHPNLVLSEDRKSVRHGDTRqdlpdnpeRFDTYPCVLGAEGFTGGRHYWEVEVGDKTEWTLGVCRESVSRKGevTLSP 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3570 GETSW--------YMHCSEPqrytffysgiVSEVHATERPARVGILLDYTNQRLLFINAESGQLLFIVRHRFNEGVHPAF 3641
Cdd:cd13745     90 ENGYWtvwlrdgkYEALTSP----------PTPLPVSVRPSRVGIFLDYEAGEVSFYNVTDRSHLFTFTDTFSGTLRPYF 159
SPRY_PRY_TRIM15 cd15826
PRY/SPRY domain in tripartite motif-binding protein 15 (TRIM15); This domain, consisting of ...
 3500-3651 1.36e-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: 71.44  E-value: 1.36e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3500 ETAHPALQISANGTVISFSERR--------RLTEIPSVLGEELPACGQHYWETTV--ADSPAYRLGICTSSAVRAGALG- 3568
Cdd:cd15826      7 QTASGSLVLSEDRKSVRYTRQKqnlpdsplRFDGLPAVLGSPGFSSGRHRWQVEVqlGDGGGCTVGVAGESVRRKGEMGl 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3569 -QGETSWYMHCSEPQRYTFFYSGivSEVHATERPARVGILLDYTNQRLLFINAESGQLLFIVRHRFNEGVHPAFALEKPG 3647
Cdd:cd15826     87 sAEDGVWAVILSHQQCWASTSPG--TDLPLSEIPRRVGVALDYEAGTVTLTNAETQEPIFTFTASFSGKVFPFFAVWKKG 164


                   ....
gi 1907094698 3648 RCTL 3651
Cdd:cd15826    165 SRLT 168
SPRY_PRY_TRIM75 cd15829
PRY/SPRY domain of tripartite motif-binding protein 75 (TRIM75); This domain, consisting of ...
 3500-3641 4.82e-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: 67.31  E-value: 4.82e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3500 ETAHPALQISANGTVISFSERR--------RLTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAG--ALGQ 3569
Cdd:cd15829     26 ETAHPNLLVSEDKKCVTFTKKKqrvpdspkRFTVNPVVLGFPGFHSGRHFWEVEVGDKPEWAVGVCKDSLSTKArrPPSG 105

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907094698 3570 GETSWymhCSEPQRYTFFYSGIV-SEVHATERPARVGILLDYTNQRLLFINAESGQLLFIVRHRFNEGVHPAF 3641
Cdd:cd15829    106 QQGCW---RIQLQGGDYDAPGAVpPPLLLEVKPRGIGVFLDYELGEISFYNMPEKSHIHTFTDTFSGPLRPYF 175
SPRY_PRY_TRIM50 cd13743
PRY/SPRY domain in tripartite motif-binding protein 50 (TRIM50); This domain, consisting of ...
 3501-3641 5.19e-12

PRY/SPRY domain in tripartite motif-binding protein 50 (TRIM50); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM50. TRIM50, an E3 ubiquitin ligase, is deleted in Williams-Beuren (WBS) syndrome, a multi-system neurodevelopmental disorder caused by the deletion of contiguous genes at chromosome region 7q11.23. It is specifically expressed in gastric parietal cells and may play an essential role in tubulovesicular dynamics. It also interacts with and increases the level of p62, a multifunctional adaptor protein that is implicated in various cellular processes such as the autophagy clearance of polyubiquitinated protein aggregates.


Pssm-ID: 293977  Cd Length: 189  Bit Score: 67.52  E-value: 5.19e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3501 TAHPALQISANGTVIS---FSERR-----RLTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAGALGQGET 3572
Cdd:cd13743     20 TAHPMLELSKGNTVVEcglLAQRLpsnpeRFDYSNCVLASRGFSSGKHYWEVVVGSKSKWRLGLIKGTTSRKGKLNKSPE 99

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907094698 3573 S--WYMHCSEPQRYTFFYSGIVSeVHATERPARVGILLDYTNQRLLFINAESGQ-LLFI--VRHRFNEGVHPAF 3641
Cdd:cd13743    100 NgvWLIGLKEGRVYEAFANPRVP-LPLSTRPQRIGVFLDYEKGELTFYNADSPDeLVPIytFQAEFQGKLYPLL 172
SPRY_PRY_FSD1 cd12901
Fibronectin type III and SPRY containing 1 (FSD1) domain includes PRY at the N-terminus; This ...
 3520-3659 5.37e-12

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: 67.93  E-value: 5.37e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3520 RRRLT-EIPSVLGEELPACGQHYWETTV-ADSPAYRLGICTSSAVRAGALGQGETSWYMHCSEPQRYTFfysgivSEVHA 3597
Cdd:cd12901     66 RDRFTaESYTVLGDTLIDGGQHYWEVRAqKDSKAFSVGVAYRSLGKFDQLGKTNASWCLHVNNWLQNSF------AAKHN 139

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907094698 3598 TER-------PARVGILLDYTNQRLLFINAESGQLLFIVRHRFNEGVHPAFALeKPGRCTLHLGLEPPD 3659
Cdd:cd12901    140 NKAktldvpvPDRIGVYCDFDEGQLSFYNARTKQLLHTFKMKFTQPVLPAFMV-WCGGLSVSTGLQVPS 207
SPRY_PRY_TRIM58 cd15816
PRY/SPRY domain in tripartite motif-binding protein 58 (TRIM58), also known as BIA2; This ...
 3501-3641 8.16e-12

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


Pssm-ID: 293988 [Multi-domain]  Cd Length: 168  Bit Score: 66.35  E-value: 8.16e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3501 TAHPALQISANGTVISFSER--------RRLTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRagalgQGET 3572
Cdd:cd15816      8 TAHPSLLLTADLRSVQDGELwrdvpgnpERFDTWPCVLGLQSFSSGRHYWEVAVGEKAEWGLGVCQDSAPR-----KGET 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907094698 3573 S-------WYMHCSEPQRYTFFYSGIVSEVHaTERPARVGILLDYTNQRLLFINAESGQLLFIVRHRFNEGVHPAF 3641
Cdd:cd15816     83 TpspengvWAVWLLKGNEYMVLASPSVPLLQ-LRRPRRVGVFLDYEAGEISFYNVTAGSHIYTFRQLFSGILRPYF 157
SPRY_PRY_TRIM60 cd15828
PRY/SPRY domain of tripartite motif-binding protein 60 (TRIM60) also known as RING finger ...
 3496-3641 1.15e-11

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: 66.16  E-value: 1.15e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3496 LLLRETAHPALQISANGTVISFSER--------RRLTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSS------- 3560
Cdd:cd15828     13 TLDPETAHPQLTVSEDRKSVLYGEMkqnvcynpRRFYLCPAVLGSEGFHSGRQYWEVEVGDKPEWTLGVCQDClprnwsn 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3561 --AVRAG--ALGQGETSWYMHCSePQRytffySGIVSEVhateRPARVGILLDYTNQRLLFINAESGQLLFIVRHRFNEG 3636
Cdd:cd15828     93 qpSVQDGlwAIGRYSESNYVALG-PKK-----IQLLPKV----RPSKIGIFLDYELGEVSFYNMNDRSLLYTFSDSFTGT 162


                   ....*
gi 1907094698 3637 VHPAF 3641
Cdd:cd15828    163 LWPYF 167
SPRY_PRY_TRIM62 cd13744
PRY/SPRY domain in tripartite motif-binding protein 62 (TRIM62); This domain, consisting of ...
 3501-3648 1.70e-11

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: 65.79  E-value: 1.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3501 TAHPALQISANGTVISF----------SERRRLTEIpSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAGAL--- 3567
Cdd:cd13744     20 TAHQRLILSDDCTIVAYgnlhpqplqdSPKRFDVEV-SVLGSEGFSGGVHYWEVVVSEKTQWMIGLAHEAVSRKGSIqiq 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3568 -GQGETSWYMH-------CSEPQrytffysgivSEVHATERPARVGILLDYTNQRLLFINAESGQLLFIVRHRFNEGVHP 3639
Cdd:cd13744     99 pGRGFYCIVMHdgnqysaCTEPW----------TRLNVKSKLEKVGVYLDYDKGLLIFYNADDMSWLYTFREKFPGKLCS 168


                   ....*....
gi 1907094698 3640 AFAlekPGR 3648
Cdd:cd13744    169 YFS---PGQ 174
SPRY_PRY_TRIM60_75 cd15817
PRY/SPRY domain of tripartite motif-binding protein 60 and 75 (TRIM60 and TRIM75); This domain, ...
 3500-3641 1.80e-11

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: 65.26  E-value: 1.80e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3500 ETAHPALQISANGTVISFSER--------RRLTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRA------- 3564
Cdd:cd15817      7 ETAHPNLIVSEDRKAVRYRRMkpncpydpRRFTVYPAVLGSEGFDSGRHFWEVEVGGKGEWILGVCKDSLPRNaqdppsp 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3565 ----GALGQGETSWymHCSEPqrytfFYSGIVSEVhateRPARVGILLDYTNQRLLFINAESGQLLFIVRHRFNEGVHPA 3640
Cdd:cd15817     87 lggcWQIGRYMSGY--VASGP-----KTTQLLPVV----KPSRIGIFLDYELGEVSFYNMNDRSHLYTFTDTFTGKLIPY 155


                   .
gi 1907094698 3641 F 3641
Cdd:cd15817    156 F 156
SPRY_PRY_C-I_2 cd12891
PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM14-like, ...
 3501-3645 2.25e-11

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: 64.96  E-value: 2.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3501 TAHPALQISANGTVISFS---ERRRLT----EIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAGA---LGQG 3570
Cdd:cd12891      7 TAHNNLALSGDLKTVTCSsenQHYPDSperfTHSQVLSTQSFSSGRHYWEVEVSESGGWSVGVAYPSIERKGDesrIGRN 86

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907094698 3571 ETSWYMHCSEPQrYTFFYSGIVSEVHATeRPARVGILLDYTNQRLLFINAESG-QLLFIVRHRFNEGVHPAFALEK 3645
Cdd:cd12891     87 DKSWCLEWQDKS-FSAWHNNEETPLPSV-SSRRLGVYLDYEAGRLSFYELSDPiRHLHTFTATFTEPLHPAFWVLE 160
SPRY_PRY_TRIM11 cd15811
PRY/SPRY domain of tripartite motif-binding protein 11 (TRIM11), also known as RING finger ...
 3500-3628 3.35e-11

PRY/SPRY domain of tripartite motif-binding protein 11 (TRIM11), also known as RING finger protein 92 (RNF92); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM11, also known as RING finger protein 92 (RNF92) or BIA1. TRIM11 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. It localizes to the nucleus and the cytoplasm; it is overexpressed in high-grade gliomas and promotes proliferation, invasion, migration and glial tumor growth. TRIM11 increases expression of dopamine beta-hydroxylase gene by interacting with the homeodomain transcription factor, PHOX2B, via the B30.2/SPRY domain, thus playing a potential role in the specification of noradrenergic (NA) neuron phenotype. It has also been shown that TRIM11 plays a critical role in the clearance of mutant PHOX2B, which causes congenital central hypoventilation syndrome, via the proteasome. TRIM11 binds a key component of the activator-mediated cofactor complex (ARC105), and destabilizes it, through the ubiquitin-proteasome system; ARC105 mediates chromatin-directed transcription activation and is a key regulatory factor for transforming growth factor beta (TGFbeta) signaling.


Pssm-ID: 293983 [Multi-domain]  Cd Length: 169  Bit Score: 64.59  E-value: 3.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3500 ETAHPALQISANGTVISFSERR--------RLTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVR--AGALGQ 3569
Cdd:cd15811      7 DTANPELVLSEDRRSVRRGDLRqalpdspeRFDPGPCVLGRERFTSGRHYWEVEVGDRTSWALGVCKENVNRkeKGELSA 86

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907094698 3570 GETSWYMhcsepqrytFFYSGIVSEVHAT-----ERPARVGILLDYTNQRLLFINAESGQLLFI 3628
Cdd:cd15811     87 GNGFWIL---------VFLGNYYSSERRTfaplrDPPRRVGIFLDYEAGHLSFYSATDGSLLFI 141
SPRY_PRY_TRIM50_72 cd12897
PRY/SPRY domain in tripartite motif-binding (TRIM) proteins TRIM50 and TRIM72; This domain, ...
 3501-3641 3.51e-11

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: 64.94  E-value: 3.51e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3501 TAHPALQISANGTVISFSER--------RRLTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAGALGQGET 3572
Cdd:cd12897     20 TAHPLLVVSSGGTVVECGLQkqrrasqpERFDKSTCVVASQGFSEGEHYWEVVVGDKPRWALGVIKGTASRKGKLHASPS 99

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907094698 3573 S--WYMHCSEPQRYTFFYSGIVSEV-HATERPARVGILLDYTNQRLLFINAESG---QLLFIVRHRFNEGVHPAF 3641
Cdd:cd12897    100 HgvWLIGLKEGKVYEAHGEPKEPRPlRVAGRPHRIGVYLSFEDGVLSFFDASDPddlRTLYTFQERFQGKLYPFF 174
SPRY_PRY_BTN1_2 cd15819
butyrophilin subfamily member A1 and A2 (BTN1A and BTN2A); This domain, consisting of the ...
 3500-3643 4.24e-11

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: 64.17  E-value: 4.24e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3500 ETAHPALQISANGTVISFSERR--------RLTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAGALgqge 3571
Cdd:cd15819      9 DTAHPALILSEDGRSVTWGETRqdlpenpeRFDSLPCVLGQEGFTSGRHYWEVEVGDRTSWDLGVCRDNVMRKGRV---- 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3572 tswymhCSEPQ-------RYTFFYSGIVS-EVHAT--ERPARVGILLDYTNQRLLFINAESGQLLFIVRH-RFNEGVHPA 3640
Cdd:cd15819     85 ------TLSPEngfwairLYGNEYWALTSpETPLTlkEPPRRVGIFLDYEAGDVSFYNMTDGSHIYTFPQtAFSGPLRPF 158


                   ...
gi 1907094698 3641 FAL 3643
Cdd:cd15819    159 FRL 161
SPRY_PRY_TRIM14 cd13738
PRY/SPRY domain of tripartite motif-binding protein 14 (TRIM14); This is a TRIM14 domain ...
 3500-3643 2.64e-10

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: 62.11  E-value: 2.64e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3500 ETAHPALQISANGTVISFSERRRLTEIPS--------VLGEELPACGQHYWETTVADSPA-YRLGICTSSAVRAGA---- 3566
Cdd:cd13738      6 DTLHPRLRLSDDRLTVSCGWLGTLGLCPPqrfdklwqVLSRDSFFSGRHYWEVDLQEAGAgWWVGAAYPSIGRKGDseaa 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3567 -LGQGETSWYMhcsepQRYTF----FYSGIVSEVHATERPARVGILLDYTNQRLLFINAESGQL-LFIVRHRFNEGVHPA 3640
Cdd:cd13738     86 rLGWNRQSWCL-----KRYDLeywaFHDGQRSRLRPEDDPDRLGVFLDYEAGILSFYDVTGGMThLHTFRATFQEPLYPA 160


                   ...
gi 1907094698 3641 FAL 3643
Cdd:cd13738    161 LRL 163
SPRY_PRY_RFPL cd15821
Ret finger protein-like (RFPL), includes RFP1, 2, 3, 4; This domain, consisting of the ...
 3497-3650 3.08e-10

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: 61.94  E-value: 3.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3497 LLRETAHPALQISANGTVI---SFSERR-----RLTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAGA-- 3566
Cdd:cd15821      8 LDVDTANNYLIISEDLRSVrcgCFRQNRkelaeRFDDALCVLGSPRFTSGRHYWEVDVGTSTEWDLGVCRESVNRQGPie 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3567 LGQGETSWYMHCSEPQRYtffysgIVSEVHAT-----ERPARVGILLDYTNQRLLFINAESGQLLFIVRHRFNEG-VHPA 3640
Cdd:cd15821     88 LSPEHGFWTVSLRDGSVF------FASTVPLTvlwvnPRLHRVGIFLDMEMGTISFYDVSDGSHIFTFTKISAEEpLRPF 161

                          170
                   ....*....|
gi 1907094698 3641 FAlekPGRCT 3650
Cdd:cd15821    162 FA---PANPY 168
SPRY_PRY_TRIM20 cd15813
PRY/SPRY domain in tripartite motif-binding protein 20 (TRIM20), also known as pyrin; This ...
 3500-3641 3.79e-10

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


Pssm-ID: 293985  Cd Length: 184  Bit Score: 62.08  E-value: 3.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3500 ETAHPALQISANGTVISFSERR-RLTEIP-------SVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAG--ALGQ 3569
Cdd:cd15813     16 ETAHPNLIFSDDLKSVRLGNKWdRLPDNPerfdsciIVLGSPSFTSGRHYWEVEVGDKTGWILGVCKASVSRKGsmTLSP 95

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907094698 3570 GETSW---YMHCSEPQRYTFfysgIVSEVHATERPARVGILLDYTNQRLLFINAESGQLLFIVRHRFNEG-VHPAF 3641
Cdd:cd15813     96 ENGYWvvmMTKRNEYQASTS----PPTRLWLREPPRRVGIFLDYEAGDISFYNVTAKSHIYTFTSFSSSGpLQPIF 167
SPRY_PRY_TRIM7_like cd12888
PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7)-like, including TRIM7, TRIM10, ...
 3500-3651 4.73e-10

PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7)-like, including TRIM7, TRIM10, TRIM15, TRIM26, TRIM39, TRIM41; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several tripartite motif-containing (TRIM) proteins, including TRIM7 (also referred to as glycogenin-interacting protein, RING finger protein 90 or RNF90), TRIM10, TRIM15, TRIM26, TRIM39 and TRIM41. TRIM7 or GNIP interacts with glycogenin and stimulates its self-glucosylating activity via its SPRY domain. TRIM10 (also known as hematopoietic RING finger 1 (HERF1) or TRIM10/HERF1) plays a key role in definitive erythroid development; downregulation of the Spi-1/PU.1 oncogene induces the expression of TRIM10/HERF1, a key factor required for terminal erythroid cell differentiation and survival. Antiviral activity of TRIM15 is dependent on the ability of its B-box to interact with the MLV Gag precursor protein; downregulation of TRIM15, along with TRIM11, enhances virus release suggesting that these proteins contribute to the endogenous restriction of retroviruses in cells. Tripartite motif-containing 26 (TRIM26) function is as yet unknown; however, since it is localized in the human histocompatibility complex (MHC) class I region, TRIM26 may play a role in immune response although studies show no association between TRIM26 polymorphisms and the risk of aspirin-exacerbated respiratory disease. TRIM39 is a MOAP-1 (Modulator of Apoptosis)-binding protein that stabilizes MOAP-1 through inhibition of its poly-ubiquitination process. TRIM41 (also known as RING finger-interacting protein with C kinase or RINCK) functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C.


Pssm-ID: 293946 [Multi-domain]  Cd Length: 169  Bit Score: 61.03  E-value: 4.73e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3500 ETAHPALQISANGTVISFSERR--------RLTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAGA--LGQ 3569
Cdd:cd12888      7 DTAHPRLVLSEDRKSVRWGDTRqdlpdnpeRFDTWPCVLGCEGFTSGRHYWEVEVGDGGGWAVGVARESVRRKGEisFSP 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3570 GETSWYMHCSEPQRYTFFYSGIVSEVHatERPARVGILLDYTNQRLLFINAESGQLLFIVRHRFNEG--VHPAFALEKPG 3647
Cdd:cd12888     87 EEGIWAVGQWGGQYWALTSPETPLPLS--EVPRRIRVYLDYEGGQVAFFDADNEAPIFTFPPASFAGerIFPWFWVGKGS 164


                   ....
gi 1907094698 3648 RCTL 3651
Cdd:cd12888    165 QLKL 168
SPRY_PRY_TRIM18 cd12892
PRY/SPRY domain of TRIM18/MID1, also known as FXY or RNF59; This domain, consisting of the ...
 3495-3659 5.63e-10

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: 61.18  E-value: 5.63e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3495 FLLLRETAHPALQISANGTVISFSE--------RRRLTEIPS--VLGEELPACGQHYWETTVADSPAYRLGICTSSAVRA 3564
Cdd:cd12892      2 FKLDPKSAHRKLKVSHDNLTVERDEtsskkshtPERFTSQGSygVAGNVFIDSGRHYWEVVISGSTWYAIGIAYKSAPKH 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3565 GALGQGETSWYMhCSEPQRYTFFYSGIVSEVHATERPARVGILLDYTNQRLLFINAESGQLLFIVRHRFNEGVHPAFALE 3644
Cdd:cd12892     82 EWIGKNSASWVL-CRCNNNWVVRHNSKEIPIEPSPHLRRVGILLDYDNGSLSFYDALNSIHLYTFDIAFAQPVCPTFTVW 160

                          170
                   ....*....|....*.
gi 1907094698 3645 KpgRC-TLHLGLEPPD 3659
Cdd:cd12892    161 N--KClTILTGLPIPD 174
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 3537-3654 6.89e-10

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: 59.23  E-value: 6.89e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698  3537 CGQHYWETTVADSPAYRLGICTSSAVRAGALGQGET--SWYMHCSEPQRYtffYSGIVSE--VHATERPARVGILLDYTN 3612
Cdd:smart00449    1 SGRHYFEVEIGDGGHWRVGVATKSVPRGYFALLGEDkgSWGYDGDGGKKY---HNSTGPEygLPLQEPGDVIGCFLDLEA 77

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 1907094698  3613 QRLLFINAESGQLLFIVRH-RFNEGVHPAFALEKPGRCTLHLG 3654
Cdd:smart00449   78 GTISFYKNGKYLHGLAFFDvKFSGPLYPAFSLGSGNSVRLNFG 120
SPRY_PRY_TRIM25 cd13736
PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25); This domain, consisting of ...
 3501-3641 3.30e-09

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: 58.74  E-value: 3.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3501 TAHPALQISANGTVISFSER--------RRLTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAGA---LGQ 3569
Cdd:cd13736      7 TAHNKVSLSENYTKASVSDDpqnyrehpQRFTYCSQVLGLHCFKQGIHYWEVELQKNNFCGVGICYGSMDRQGPesrLGR 86

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907094698 3570 GETSWymhCSEpqrytFFYSGI------VSEVHATERPARVGILLDYTNQRLLFIN-AESGQLLFIVRHRFNEGVHPAF 3641
Cdd:cd13736     87 NSESW---CVE-----WFNVKIsawhnnVEKTLPSTKATRVGVLLNCDHGFVIFFAvQDKVHLMYKFKVDFTEALYPAF 157
SPRY_PRY_TRIM41 cd13741
PRY/SPRY domain in tripartite motif-binding protein 41 (TRIM41); This domain, consisting of ...
 3500-3638 7.18e-09

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: 58.62  E-value: 7.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3500 ETAHPALQISANGTVISFSERRRltEIPS----------VLGEELPACGQHYWETTVADSPAYRLGICTSSAVR------ 3563
Cdd:cd13741      7 DTAHPALLLSPDRRGVRLAERRQ--EVPEhpkrfsadccVLGAQGFRSGRHYWEVEVGGRRGWAVGAARESTHHkekvgs 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3564 -AGALGQGETSWYMHCSEP----------------------QRYTFFYSGIVSEVHATERPARVGILLDYTNQRLLFINA 3620
Cdd:cd13741     85 gGSSVSSGDASSSRHHHRRrrlhlpqqpllqrevwcvgtngKRYQAQSSTEQTLLSPSEKPRRFGVYLDYEAGRLGFYNA 164

                          170
                   ....*....|....*...
gi 1907094698 3621 ESgqLLFIvrHRFNEGVH 3638
Cdd:cd13741    165 ET--LAHV--HTFSAAFL 178
SPRY_PRY_TRIM72 cd13742
PRY/SPRY domain in tripartite motif-binding protein 72 (TRIM72); This domain, consisting of ...
 3500-3641 7.38e-09

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: 58.33  E-value: 7.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3500 ETAHPALQISANGTVISFSER---------RRLTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAGALGQG 3570
Cdd:cd13742     19 DTAHPYLVVSSDGKRVECADQkqavssddpNRFDKANCVVSHQSFSEGEHYWEVIVGDKPRWALGVISAEAGRKGRLHAL 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3571 ETS--WYMHCSEpqrytffysGIVSEVHAT----------ERPARVGILLDYTNQRLLFINA---ESGQLLFIVRHRFNE 3635
Cdd:cd13742     99 PSNgfWLLGCKE---------GKVYEAHVEhkepralrveGRPTRIGVYLSFSDGVLSFYDAsdeDNLVQLFAFHERFPG 169


                   ....*.
gi 1907094698 3636 GVHPAF 3641
Cdd:cd13742    170 PLYPFF 175
SPRY_PRY_TRIM67_9 cd12889
PRY/SPRY domain in tripartite motif-containing proteins, TRIM9 and TRIM67; This domain, ...
 3501-3658 1.26e-08

PRY/SPRY domain in tripartite motif-containing proteins, TRIM9 and TRIM67; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM9 proteins. TRIM9 protein is expressed mainly in the cerebral cortex, and functions as an E3 ubiquitin ligase. It has been shown that TRIM9 is localized to the neurons in the normal human brain and its immunoreactivity in affected brain areas in Parkinson's disease and dementia with Lewy bodies is severely decreased, possibly playing an important role in the regulation of neuronal function and participating in pathological process of Lewy body disease through its ligase. TRIM67 negatively regulates Ras activity via degradation of 80K-H, leading to neural differentiation, including neuritogenesis.


Pssm-ID: 293947  Cd Length: 172  Bit Score: 57.25  E-value: 1.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3501 TAHPALQISANGTVI---SFSERrrlteipSVLGEELPACGQHYWETTV------ADsPAYrlGICTSSAVRAGALGQ-- 3569
Cdd:cd12889     16 TSHPDIILSNDNMTVtcnSYEDR-------VVLGSVGFSRGVHYWEVTIdrydghPD-PAF--GVARIDVNKDKMLGKdd 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3570 --------GETSWYMHCSEPQRYTffYSGIvsevhatERPARVGILLDYTNQRLLF-INAESGQLlfiVRHRFNEGV-HP 3639
Cdd:cd12889     86 kgwsmyidNNRSWFLHNNEHSNRT--EGGI-------TVGSVVGVLLDLDRHTLSFyVNDEPQGP---IAFRNLPGVfYP 153

                          170
                   ....*....|....*....
gi 1907094698 3640 AFALEKPGRCTLHLGLEPP 3658
Cdd:cd12889    154 AVSLNRNVQVTLHTGLEPP 172
SPRY_PRY_TRIM27 cd15814
PRY/SPRY domain in tripartite motif-containing protein 27 (TRIM27), also known as RING finger ...
 3500-3647 3.80e-08

PRY/SPRY domain in tripartite motif-containing protein 27 (TRIM27), also known as RING finger protein 76 (RNF76); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM27, also known as RING finger protein 76 (RNF76) or RET finger protein (RFP). TRIM27 domain is composed of RING/B-box/coiled-coil core and also known as RBCC proteins. It is highly expressed in the spleen, thymus and in cells of the hematopoietic compartment. TRIM27 exhibits either nuclear or cytosolic localization depending on the cell type. TRIM27 negatively regulates nucleotide-binding oligomerization domain containing 2 (NOD2)-mediated signaling by proteasomal degradation of NOD2, suggesting that TRIM27 could be a new target for therapeutic intervention in NOD2-associated diseases such as Crohn's. High expression of TRIM27 is observed in several human cancers, including breast and endometrial cancer, where elevated TRIM27 expression predicts poor prognosis. Also, TRIM27 forms an oncogenic fusion protein with Ret proto-oncogene. It is involved in different stages of spermatogenesis and its significant expression in male germ cells and seminomas, suggests that TRIM27 may be associated with the regulation of testicular germ cell proliferation and histological-type of germ cell tumors. TRIM27 could also be a predictive marker for chemoresistance in ovarian cancer patients. In the neurotoxin model of Parkinson's disease (PD), deficiency of TRIM27 decreases apoptosis and protects dopaminergic neurons, making TRIM27 an effective potential target during the treatment of PD.


Pssm-ID: 293986 [Multi-domain]  Cd Length: 177  Bit Score: 55.85  E-value: 3.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3500 ETAHPALQISANGTVISFS--------ERRRLTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAGALGQGE 3571
Cdd:cd15814      9 DTAYPSLILSDNLRQVRYSylqqdlpdNPERFNLFPCVLGSPCFIAGRHYWEVEVGDKAKWTIGVCEDSVCRKGGVTSAP 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3572 TSWYMHCSepQRYTFFYSGIVSEVHA--TERP-ARVGILLDYTNQRLLFINAESGQLLFIVRH-RFNEGVHPAFALEKPG 3647
Cdd:cd15814     89 QNGFWAVS--LWYGKEYWALTSPMTAlpLRTPlQRVGIFLDYDAGEVSFYNVTERCHTFTFSHaTFCGPVRPYFSLSYSG 166
SPRY_PRY_TRIM38 cd15815
PRY/SPRY domain of tripartite motif-binding protein 38 (TRIM38), also known as Ring finger ...
 3500-3641 4.35e-08

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: 55.82  E-value: 4.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3500 ETAHPALQISANGTVISF--------SERRRLTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAGALGQGE 3571
Cdd:cd15815     20 DTAHPELTLSKDQRQVTYgrcqenldASPKRFTVLPCVLGCEGFTSGRHYFEVDVGEGTGWDVGVCLENVQRGFGMKQEP 99

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907094698 3572 TS--WYMHCSEPQRYTFFYSgIVSEVHATERPARVGILLDYTNQRLLFINAESGQLLFIV-RHRFNEGVHPAF 3641
Cdd:cd15815    100 EFgfWTIRLCEEDGYVALTS-PPTPLPLREKPLVVGVFLDYEAGLVSFYNMTTGSHIFTFpKASFSDTLRPYF 171
SPRY_PRY_A33L cd12905
zinc-binding protein A33-like; This domain, consisting of the distinct N-terminal PRY ...
 3500-3642 8.44e-08

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: 54.73  E-value: 8.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3500 ETAHPALQISANGTVISFSER--------RRLTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAG--ALGQ 3569
Cdd:cd12905     11 ETAHPSLILSRDLTAVTESDEmqpyprspKRFLQCVNVLASQGFQSGRHYWEVWVGSKTKWDLGVASESVDRQArvKLCP 90

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907094698 3570 GETSWYMHCSEPQRYTFFYSGIVSeVHATERPARVGILLDYTNQRLLFINAESGQLLFIVRHRFNEGVHPAFA 3642
Cdd:cd12905     91 ENGYWTLRLRNGDEYWAGTQPWTR-LRVTSRPQRIGVFLDCEERKVSFYNADDMSLLYSFHQGPRGKVFPFFS 162
SPRY_PRY_TRIM69 cd15818
PRY/SPRY domain in tripartite motif-binding protein 69 (TRIM69), also known as RING finger ...
 3501-3641 9.46e-08

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: 54.81  E-value: 9.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3501 TAHPALQISANGTVISFSERRR-LTEIP-------SVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAGA--LGQG 3570
Cdd:cd15818     21 TAHPNLILSEDLTCVWHGDTKQmLPDNPerfdssvAVLGSEGFTSGKHYWEVEVAKKTKWTLGVVRESINRKGNcpLSPE 100

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907094698 3571 ETSWYMHCSEPQRYTFFysgivsEVHA-----TERPARVGILLDYTNQRLLFINAESGQLLFIVRHRFNEGVHPAF 3641
Cdd:cd15818    101 DGFWLLRLRNQNELKAL------DVPSfsltlTSNLNKVGIYLDYEGGQVSFYNANTMSHIYTFSDTFTEKIYPYF 170
SPRY_PRY_RNF135 cd12902
PRY/SPRY domain in RING finger protein RNF135; This domain, consisting of the distinct ...
 3526-3661 3.34e-07

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: 52.90  E-value: 3.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3526 IPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAGALGQGETSWYMHCSEPQRYTFFYSGiVSEVHATERPARVG 3605
Cdd:cd12902     39 ISQVLCSQAFSSGQHYWEVDTRQCSHWAVGVASWEMSRDQMLGRTMDSWCIEWKGTGQLSAWHMN-KETVLGSDKPRVVG 117

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907094698 3606 ILLDYTNQRLLFINAESGQ-LLFIVRHRFNEGVHPAFALekpgrctlhLGLEPPDSV 3661
Cdd:cd12902    118 IWLDLEEGKLAFYSVANQErLLHECEVSASSPLHPAFWL---------YGLEPGNSL 165
SPRY_PRY_TRIM1 cd13739
PRY/SPRY domain of tripartite motif-binding protein 1 (TRIM1) or MID2; This domain, consisting ...
 3495-3643 6.57e-07

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: 52.32  E-value: 6.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3495 FLLLRETAHPALQISANGTVIS----------FSERRRLTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRA 3564
Cdd:cd13739      1 FKLDPKMAHKKLKISNDGLQMEkdesslkkshTPERFSGTGCYGAAGNIFIDSGCHYWEVVVGSSTWYAIGIAYKSAPKN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3565 GALGQGETSW-YMHCSepQRYTFFYSGIVSEVHATERPARVGILLDYTNQRLLFINAESGQLLFIVRHRFNEGVHPAFAL 3643
Cdd:cd13739     81 EWIGKNSSSWvFSRCN--NNFVVRHNNKEMLVDVPPQLKRLGVLLDYDNNMLSFYDPANSLHLHTFEVSFILPVCPTFTI 158
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 489-640 1.35e-06

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 54.79  E-value: 1.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698  489 EPIVHREEEHAPEPivhREEEHAPESivHREEEHAPESIVQREEEHAPEPESIVHREEEHAPGPvpivHREEEHVPELES 568
Cdd:PTZ00341   434 ESVEDNEEEHSGDA---NEEELSVDE--HVEEHNADDSGEQQSDDESGEHQSVNEIVEEQSVNE----HVEEPTVADIVE 504

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907094698  569 iVHRGEEHAPEPIVHRDEGHapepivHREEEHVPEPIVhrDEGHAPEPIVhREEEHVPEPESIVHREEEHAP 640
Cdd:PTZ00341   505 -QETVDEHVEEPAVDENEEQ------QTADEHVEEPTI--AEEHVEEEIS-TAEEHIEEPASDVQQDSEAAP 566
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 3540-3655 1.41e-06

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: 50.03  E-value: 1.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3540 HYWETTV--ADSPAYRLGICTSSAVRAGALGQGET--SWYMHCSEPQRYTffysgiVSEVHATERPA-----RVGILLDY 3610
Cdd:pfam00622    2 HYFEVEIfgQDGGGWRVGWATKSVPRKGERFLGDEsgSWGYDGWTGKKYW------ASTSPLTGLPLfepgdVIGCFLDY 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1907094698 3611 TNQRLLFINAEsGQLLFIVRH-RFNEGVHPAFALEKPGRCTLHLGL 3655
Cdd:pfam00622   76 EAGTISFTKNG-KSLGYAFRDvPFAGPLFPAVSLGAGEGLKFNFGL 120
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 3309-3397 1.45e-06

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: 49.03  E-value: 1.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3309 EPSSATSTTIAVYWSVNKED--VVDSFQVYCVEEPQDD-QEINELVeeyrltVKESCCIFEDLEPDRCYQVWVMAVNFTG 3385
Cdd:cd00063      8 RVTDVTSTSVTLSWTPPEDDggPITGYVVEYREKGSGDwKEVEVTP------GSETSYTLTGLKPGTEYEFRVRAVNGGG 81

                           90
                   ....*....|..
gi 1907094698 3386 CSLPSERAIFRT 3397
Cdd:cd00063     82 ESPPSESVTVTT 93
SPRY_PRY_BTN3 cd15820
PRY/SPRY domain of butyrophilin 3 (BTN3), includes BTN3A1, BTN3A2, BTN3A3 as well as BTN-like ...
 3500-3643 1.94e-06

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: 50.89  E-value: 1.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3500 ETAHPALQISANGTVISF-SERRRLTEIP-------SVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAGALGQGE 3571
Cdd:cd15820     11 DTANPILLISEDQRSLQWaDEPQNLPDNPkrfdwhyCVLGCKSFTSGRHFWEVEVGDRKEWYVGVCRENVERKLWVKMAP 90

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907094698 3572 TS--WYMHCSEPQRYTFFySGIVSEVHATERPARVGILLDYTNQRLLFINAESGQLLFIVRH-RFNEGVHPAFAL 3643
Cdd:cd15820     91 ENgfWTIGLSDGNDYQAL-TDPRTKLTIANPPQRVGVFLDYETGEVSFYNAMDGSHIYTFPHtSFSGPLYPVFRL 164
SPRY_PRY_TRIM21 cd12900
PRY/SPRY domain in tripartite motif-binding protein 21 (TRIM21) also known as 52kD ...
 3492-3641 2.93e-06

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: 50.65  E-value: 2.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3492 GTRFLLLRETAHPALQISANGTVISFSERR--------RLTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVR 3563
Cdd:cd12900      2 MVHITLDPDTANPWLILSKDRRQVRLGDTHqnvpeneeRFDNYPMVLGAQRFNSGKHYWEVDVTGKEAWDLGVCRDSVRR 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3564 AGALGQGE-----TSW-----YMHCSEPQrytffysgivSEVHATERPARVGILLDYTNQRLLFIN-AESGQLLFIVRH- 3631
Cdd:cd12900     82 KGQFLLSPengfwTIWlwnkkYEAGTSPQ----------TTLHLQVPPCQVGIFLDYEAGVVSFYNiTDHGSLIYTFSEc 151

                          170
                   ....*....|
gi 1907094698 3632 RFNEGVHPAF 3641
Cdd:cd12900    152 AFTGPLRPFF 161
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 3300-3387 3.95e-06

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: 47.61  E-value: 3.95e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698  3300 PQPPRLEPqepSSATSTTIAVYWSVNKEDVVDSFQVYCVEEpqdDQEINELVEEYRLTVKESCCIFEDLEPDRCYQVWVM 3379
Cdd:smart00060    2 SPPSNLRV---TDVTSTSVTLSWEPPPDDGITGYIVGYRVE---YREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVR 75


                    ....*...
gi 1907094698  3380 AVNFTGCS 3387
Cdd:smart00060   76 AVNGAGEG 83
rne PRK10811
ribonuclease E; Reviewed
 448-609 1.75e-05

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 51.19  E-value: 1.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698  448 QEKFEPDMEGLEPISTEKTEQASEYVTSSEPIVHREEEHAPEPIVHRE---------EEHAPEPIVHREEEHaPESIVHR 518
Cdd:PRK10811   856 EEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEpqpeevvvvETTHPEVIAAPVTEQ-PQVITES 934

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698  519 EEEHAPESIVQREEEHAPEPE-SIVHREEEHAPGPV--PIVHREEEHVPELESIVHRGEEHAPEPIVHRDEGHAPEPIVH 595
Cdd:PRK10811   935 DVAVAQEVAEHAEPVVEPQDEtADIEEAAETAEVVVaePEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVPEATVEHN 1014

                          170       180
                   ....*....|....*....|...
gi 1907094698  596 REE---------EHVPEPIVHRD 609
Cdd:PRK10811  1015 HATapmtrapapEYVPEAPRHSD 1037
rne PRK10811
ribonuclease E; Reviewed
 467-688 2.27e-05

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 50.81  E-value: 2.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698  467 EQASEYVTSSEPIVhREEEHAPEPiVHREEEHAPEPIVHREEEHAPESIVHREE--EHAPESIVQREEEHAPEPESIVHR 544
Cdd:PRK10811   835 EMASGKVWIRYPVV-RPQDVQVEE-QREAEEVQVQPVVAEVPVAAAVEPVVSAPvvEAVAEVVEEPVVVAEPQPEEVVVV 912

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698  545 EEEHAPGPVPIVHREEEHVPELESIVHRGEEHAPEPIVHRDEGHAPEPivhrEEEHVPEPIVhrdeghaPEPIVHREEEH 624
Cdd:PRK10811   913 ETTHPEVIAAPVTEQPQVITESDVAVAQEVAEHAEPVVEPQDETADIE----EAAETAEVVV-------AEPEVVAQPAA 981

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907094698  625 VPEPESIVHREEEHAPEPMVLRKAQLERGVE---TSTPITDTTEPEDSSLEEEIIELDYPESPLASK 688
Cdd:PRK10811   982 PVVAEVAAEVETVTAVEPEVAPAQVPEATVEhnhATAPMTRAPAPEYVPEAPRHSDWQRPTFAFEGK 1048
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 3404-3490 3.70e-05

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: 45.18  E-value: 3.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3404 IHVEDCTvcWNTATVRWRPANPEATE--TYTLEYCRQHSPEGEGLRSfSGIKGLQLKV-NLPPNDNYFFYVRATNASGTS 3480
Cdd:cd00063      7 LRVTDVT--STSVTLSWTPPEDDGGPitGYVVEYREKGSGDWKEVEV-TPGSETSYTLtGLKPGTEYEFRVRAVNGGGES 83

                           90
                   ....*....|
gi 1907094698 3481 EQSEAALIST 3490
Cdd:cd00063     84 PPSESVTVTT 93
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
 3141-3265 6.53e-05

B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains


Pssm-ID: 128778  Cd Length: 127  Bit Score: 45.33  E-value: 6.53e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698  3141 KVQLGEFLENLQEKSLRIEAFVSEIESFFNTIEEKCSKNEKRLEMQNEEMMKRVLAQYDEKAQSFEEVKKKKMEFLHDQM 3220
Cdd:smart00502    2 REALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQL 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 1907094698  3221 VHFLQSMDTAKDTLETIVREAEELDETVFLASFEEINERLLSAME 3265
Cdd:smart00502   82 ESLTQKQEKLSHAINFTEEALNSGDPTELLLSKKLIIERLQNLLK 126
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 461-672 1.56e-04

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 47.86  E-value: 1.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698  461 ISTEKTEQASEYVTSSEPIVHREEEHAPEPIVHREEEHAPEPIVHREEEHAPESIVHREEEHAPESIVQREEEHAPE--P 538
Cdd:PTZ00341   921 INLINKELKNQNENVPEHLKEHAEANIEEDAEENVEEDAEENVEENVEENVEENVEENVEENVEENVEENVEENVEEnvE 1000

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698  539 ESIVHREEEHAPGPVP--IVHREEEHVPELESIVHRGEEHAPEPIVHRDEGHAPEPIVHREEEHVPEPIVHRDEgHAPEP 616
Cdd:PTZ00341  1001 ENIEENVEENVEENIEenVEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEIEE-NIEEN 1079

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907094698  617 IVHREEEHVPE-PESIVHREEEHAPEPMvlrKAQLERGVETSTPITDTTEPEDSSLE 672
Cdd:PTZ00341  1080 IEENVEENVEEnVEEIEENVEENVEENA---EENAEENAEENAEEYDDENPEEHNEE 1133
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 373-560 7.16e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.85  E-value: 7.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698  373 MEPPSIPATMVLERAKEELEQNAQGKESSEDDASVLTGSADDVQQEGLVSVNHSMPWEaekeslETGPPRPAPAIQEKFE 452
Cdd:PRK10263   341 TQTPPVASVDVPPAQPTVAWQPVPGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNEPLQ------QPVQPQQPYYAPAAEQ 414

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698  453 PDMEGLEPISTEKTEQASEYVTSSEPIVHREEEHAPEPivhrEEEHAPEPiVHREEEHAPESIVHREEEHAPESIvqrEE 532
Cdd:PRK10263   415 PAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQ----QSTFAPQS-TYQTEQTYQQPAAQEPLYQQPQPV---EQ 486

                          170       180
                   ....*....|....*....|....*...
gi 1907094698  533 EHAPEPESIVhreEEHAPGPVPIVHREE 560
Cdd:PRK10263   487 QPVVEPEPVV---EETKPARPPLYYFEE 511
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 3404-3480 7.35e-04

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: 41.06  E-value: 7.35e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907094698  3404 IHVEDCTvcWNTATVRWRPANPEATETYTLEYCRQHSPEGEGLRSFSGI-KGLQLKV-NLPPNDNYFFYVRATNASGTS 3480
Cdd:smart00060    7 LRVTDVT--STSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTpSSTSYTLtGLKPGTEYEFRVRAVNGAGEG 83
PTZ00121 PTZ00121
MAEBL; Provisional
 385-676 1.23e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698  385 ERAKEELEQNAQGKESSEDDASVLTGSADDVQQEGLVSVNHSMPWEAEKESLETGPPRPAPAIQEKFE---PDMEGLEPI 461
Cdd:PTZ00121  1556 ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEelkKAEEEKKKV 1635

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698  462 STEKTEQASEYVTSSEpiVHREEEhapEPIVHREEEHAPEpivHREEEHAPESIVHREEEHAPESIVQREEEHAPEPESI 541
Cdd:PTZ00121  1636 EQLKKKEAEEKKKAEE--LKKAEE---ENKIKAAEEAKKA---EEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698  542 VHREEEHAPGPVPIVHREEEHVPELESIVHRGEEhapepivhrDEGHAPEPIVHREEEHVPEPIVHRDEGHAPEPIVHRE 621
Cdd:PTZ00121  1708 KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE---------DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907094698  622 ---EEHVPEPESIVHREEEHAPEPMVLRKAQLERGVETSTP-ITDTTEPEDSSLEEEII 676
Cdd:PTZ00121  1779 aviEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLvINDSKEMEDSAIKEVAD 1837
SPRY_PRY_TRIM34 cd15825
PRY/SPRY domain in tripartite motif-containing protein 34 (TRIM34), also known as RING finger ...
 3519-3657 1.27e-03

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: 42.90  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3519 ERRRLTEIP---------SVLGEELPACGQHYWETTVADSPAYRLGI------CTSSAVRAGALGQGETS--------WY 3575
Cdd:cd15825     20 DQRQVTSVPiwpfkcynyGILGSQYFSSGKHYWEVDVSKKTAWILGVycrkrsRTFKYVRQGKNHPNVYSryrpqygyWV 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3576 MHCSEPQRYTFFYSGIVSEVHA-----TERPARVGILLDYTNQRLLFINAES-GQLLFIVRH-RFNEGVHPAFaleKPGR 3648
Cdd:cd15825    100 IGLQNKSEYYAFEDSSTSDPKVltlsvATPPHRVGVFLDYEAGTVSFFNVTNhGSLIYKFSKcCFSQPVYPYF---NPWN 176


                   ....*....
gi 1907094698 3649 CTLHLGLEP 3657
Cdd:cd15825    177 CPAPMTLCP 185
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 1762-2126 1.53e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 44.68  E-value: 1.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 1762 KPDGLVNQHEDRKPGTGQLESSESTDLMSEKlGAAPLDTDHTSETRNQETSKAPVSGEKLSQ--EPRRVQSKAVDDS-EE 1838
Cdd:PTZ00449   548 KPGETKEGEVGKKPGPAKEHKPSKIPTLSKK-PEFPKDPKHPKDPEEPKKPKRPRSAQRPTRpkSPKLPELLDIPKSpKR 626

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 1839 GRKLASGNVEVLTQSKSVP----AVKAKATPQPPETPEVTQKPSEKSLVTEQGL-PAEKGKKGIS------SFKSWMSSL 1907
Cdd:PTZ00449   627 PESPKSPKRPPPPQRPSSPerpeGPKIIKSPKPPKSPKPPFDPKFKEKFYDDYLdAAAKSKETKTtvvldeSFESILKET 706

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 1908 LFGS---------SIPDSKVSDNEDLETRPG-PSVEKAVPAIEPKGTVPAEVNIAEKPAVHSLPEVTVKLAEEPkgvsvk 1977
Cdd:PTZ00449   707 LPETpgtpfttprPLPPKLPRDEEFPFEPIGdPDAEQPDDIEFFTPPEEERTFFHETPADTPLPDILAEEFKEE------ 780

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 1978 sSISQDLKEKltflsnEDVLKQPKSNSENygQKELPGFSEGM--------GESLATSVGDKHPGIHPCSPMGEKVGMEEA 2049
Cdd:PTZ00449   781 -DIHAETGEP------DEAMKRPDSPSEH--EDKPPGDHPSLpkkrhrldGLALSTTDLESDAGRIAKDASGKIVKLKRS 851

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 2050 QNMAPLHITESQRRQKPEVSspsmwNISARKEEPSSDHKETWLSS----SDVVDRMPQK-----PKSAQSAFTRmnseEP 2120
Cdd:PTZ00449   852 KSFDDLTTVEEAEEMGAEAR-----KIVVDDDGTEADDEDTHPPEekhkSEVRRRRPPKkpskpKKPSKPKKPK----KP 922


                   ....*.
gi 1907094698 2121 ASMILP 2126
Cdd:PTZ00449   923 DSAFIP 928
SPRY_PRY_TRIM7 cd13740
PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7); This domain, consisting of the ...
 3532-3643 1.67e-03

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: 42.25  E-value: 1.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3532 EELPACG----QHYWETTVADSPAYRLGICTSSAVRAG--ALGQGETSW--------YMHCSEPQRyTFFYSGIVSevha 3597
Cdd:cd13740     43 RVLASCGfssgRHHWEVEVGSKDGWAFGVARESVRRKGltPFTPEEGVWalqlnggqYWAVTSPER-TPLSCGHLS---- 117

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1907094698 3598 terpaRVGILLDYTNQRLLFINAESGQLLFIVRHRFNEGVHPAFAL 3643
Cdd:cd13740    118 -----RVRVALDLEVGAVSFYAAEDMRHIYTFRVNFQERVFPLFSV 158
fn3 pfam00041
Fibronectin type III domain;
3311-3390 2.27e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 39.71  E-value: 2.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3311 SSATSTTIAVYWS--VNKEDVVDSFQVYC--VEEPQDDQEINELVEEYRLTVKesccifeDLEPDRCYQVWVMAVNFTGC 3386
Cdd:pfam00041    9 TDVTSTSLTVSWTppPDGNGPITGYEVEYrpKNSGEPWNEITVPGTTTSVTLT-------GLKPGTEYEVRVQAVNGGGE 81


                   ....
gi 1907094698 3387 SLPS 3390
Cdd:pfam00041   82 GPPS 85
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 537-663 2.72e-03

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 44.01  E-value: 2.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698  537 EPESIVHREEEHAPGPVPIVHREEEHVPE--------LESIVHRGEEHAPEPIVHRDEG--HAPEPIV------HREEEH 600
Cdd:PTZ00341   432 EDESVEDNEEEHSGDANEEELSVDEHVEEhnaddsgeQQSDDESGEHQSVNEIVEEQSVneHVEEPTVadiveqETVDEH 511

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907094698  601 VPEPIVHRDEG------HAPEPIVhrEEEHVPEPESIVhreEEHAPEPMvlRKAQLERGVETSTPITDT 663
Cdd:PTZ00341   512 VEEPAVDENEEqqtadeHVEEPTI--AEEHVEEEISTA---EEHIEEPA--SDVQQDSEAAPTIEIPDT 573
SPRY_PRY_TRIM6 cd15823
PRY/SPRY domain in tripartite motif-binding protein 6 (TRIM6), also known as RING finger ...
 3528-3619 3.19e-03

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: 41.77  E-value: 3.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3528 SVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAGAL---GQGETS----------WYMHCSEPQRYTFFYSGIVSE 3594
Cdd:cd15823     45 SVLGSQHFSSGKHYWEVDVTKKTAWILGVCSHSLGPTFSFnqyAQNHNAysryqpqsgyWVIGLQHNHEYRAYEDSSTSL 124

                           90       100
                   ....*....|....*....|....*.
gi 1907094698 3595 VHA-TERPARVGILLDYTNQRLLFIN 3619
Cdd:cd15823    125 LLSmTVPPRRVGVFLDYEAGTVSFYN 150
SPRY_PRY_TRIM4 cd15809
PRY/SPRY domain in tripartite motif-binding protein 4 (TRIM4), also known as RING finger ...
 3522-3643 8.05e-03

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: 40.59  E-value: 8.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094698 3522 RLTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVraGALGQGETS-----WYMHCSePQRYTFFYSGIVSEVH 3596
Cdd:cd15809     59 RFQHLPCVLGKNVFTSGKHYWEVENRDSLEIAVGVCREDVM--GITDGSEMSphvgiWAICWS-SAGYRPLTSSPVSPTK 135

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1907094698 3597 ATERPARVGILLDYTNQRLLFINAESGQLLFIVRHRFNEGVHPAFAL 3643
Cdd:cd15809    136 QEPALHRVGVFLDHGAGEVSFYSAVDGVHLHTFSCPLVSRLRPFFWL 182
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH