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Conserved domains on  [gi|694857260|ref|XP_009470260|]
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PREDICTED: fibronectin type III and SPRY domain-containing protein 1 [Nipponia nippon]

Protein Classification

fibronectin type III domain-containing protein( domain architecture ID 13228450)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPRY_PRY_FSD1 cd12901
Fibronectin type III and SPRY containing 1 (FSD1) domain includes PRY at the N-terminus; This ...
 296-502 1.22e-153

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: 436.57  E-value: 1.22e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 296 FRLDASTCHQNLRVEELSVEWDATGGKV-QDVKAREKDGKGRTASPANSPARVvQSPKRMPSGRGGRDRFTAESYTVLGD 374
Cdd:cd12901    1 FKLDASSSHQNLKVEDLSVEWDATGGKVlQKIKGRENDGRSRTASPRNSSARC-QSPKRMPSARGGRDRFTAESYTVLGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 375 TLIDGDDHYWEVRYDRDSKAFGVGVAYRSLGKFDQLGKTSASWCLHLNNWLQVSFSAKHANKAKVLDVPVPDCIGVYCNF 454
Cdd:cd12901   80 TLIDGGQHYWEVRAQKDSKAFSVGVAYRSLGKFDQLGKTNASWCLHVNNWLQNSFAAKHNNKAKTLDVPVPDRIGVYCDF 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 694857260 455 HEGFLSFYNARTKQLLHTFKAKFTQPVLPAFTVWCGSFHVSSGLQVPS 502
Cdd:cd12901  160 DEGQLSFYNARTKQLLHTFKMKFTQPVLPAFMVWCGGLSVSTGLQVPS 207
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 191-291 8.26e-15

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: 69.83  E-value: 8.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 191 PSTPEiDLAESLVADNCVTLAWRMPDED-SKIDHYVLEYRKTNfegpprakeDQPWMVVEG--IKGTEYTLSGLKFDMKY 267
Cdd:cd00063    1 PSPPT-NLRVTDVTSTSVTLSWTPPEDDgGPITGYVVEYREKG---------SGDWKEVEVtpGSETSYTLTGLKPGTEY 70

                         90       100
                 ....*....|....*....|....
gi 694857260 268 mNFRVRACNKAVAGEFSEPVTLET 291
Cdd:cd00063   71 -EFRVRAVNGGGESPPSESVTVTT 93
CC_brat-like super family cl29238
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ...
 31-153 1.18e-08

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: 53.42  E-value: 1.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260    31 REALRKIITTLAVKNEEIQNFIYSLKQMMQNVEANSSRAQEDLEGEFQSLYALLDELKDEMLMKIKQDRASRTYELQAQL 110
Cdd:smart00502   2 REALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQL 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 694857260   111 AACAKALESSEELLEAANQALGTANHHDFPQAAKQIKDSVTMA 153
Cdd:smart00502  82 ESLTQKQEKLSHAINFTEEALNSGDPTELLLSKKLIIERLQNL 124
 
Name Accession Description Interval E-value
SPRY_PRY_FSD1 cd12901
Fibronectin type III and SPRY containing 1 (FSD1) domain includes PRY at the N-terminus; This ...
 296-502 1.22e-153

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: 436.57  E-value: 1.22e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 296 FRLDASTCHQNLRVEELSVEWDATGGKV-QDVKAREKDGKGRTASPANSPARVvQSPKRMPSGRGGRDRFTAESYTVLGD 374
Cdd:cd12901    1 FKLDASSSHQNLKVEDLSVEWDATGGKVlQKIKGRENDGRSRTASPRNSSARC-QSPKRMPSARGGRDRFTAESYTVLGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 375 TLIDGDDHYWEVRYDRDSKAFGVGVAYRSLGKFDQLGKTSASWCLHLNNWLQVSFSAKHANKAKVLDVPVPDCIGVYCNF 454
Cdd:cd12901   80 TLIDGGQHYWEVRAQKDSKAFSVGVAYRSLGKFDQLGKTNASWCLHVNNWLQNSFAAKHNNKAKTLDVPVPDRIGVYCDF 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 694857260 455 HEGFLSFYNARTKQLLHTFKAKFTQPVLPAFTVWCGSFHVSSGLQVPS 502
Cdd:cd12901  160 DEGQLSFYNARTKQLLHTFKMKFTQPVLPAFMVWCGGLSVSTGLQVPS 207
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 382-490 4.50e-16

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: 74.64  E-value: 4.50e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260   382 HYWEVRYDrDSKAFGVGVAYRS--LGKFDQLGKTSASWCLHLNNWLQVsfsakHANKAKVLDVPV---PDCIGVYCNFHE 456
Cdd:smart00449   4 HYFEVEIG-DGGHWRVGVATKSvpRGYFALLGEDKGSWGYDGDGGKKY-----HNSTGPEYGLPLqepGDVIGCFLDLEA 77

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 694857260   457 GFLSFYNARTK-QLLHTFKAKFTQPVLPAFTVWCG 490
Cdd:smart00449  78 GTISFYKNGKYlHGLAFFDVKFSGPLYPAFSLGSG 112
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 191-291 8.26e-15

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: 69.83  E-value: 8.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 191 PSTPEiDLAESLVADNCVTLAWRMPDED-SKIDHYVLEYRKTNfegpprakeDQPWMVVEG--IKGTEYTLSGLKFDMKY 267
Cdd:cd00063    1 PSPPT-NLRVTDVTSTSVTLSWTPPEDDgGPITGYVVEYREKG---------SGDWKEVEVtpGSETSYTLTGLKPGTEY 70

                         90       100
                 ....*....|....*....|....
gi 694857260 268 mNFRVRACNKAVAGEFSEPVTLET 291
Cdd:cd00063   71 -EFRVRAVNGGGESPPSESVTVTT 93
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 382-487 4.07e-11

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin.


Pssm-ID: 459877  Cd Length: 121  Bit Score: 60.43  E-value: 4.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260  382 HYWEVRYDRDSKA-FGVGVAYRS--LGKFDQLGKTSASWCLHLNNwLQVSFSAKHANKAKVLDVPvPDCIGVYCNFHEGF 458
Cdd:pfam00622   2 HYFEVEIFGQDGGgWRVGWATKSvpRKGERFLGDESGSWGYDGWT-GKKYWASTSPLTGLPLFEP-GDVIGCFLDYEAGT 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 694857260  459 LSFYNArTKQLLHTF-KAKFTQPVLPAFTV 487
Cdd:pfam00622  80 ISFTKN-GKSLGYAFrDVPFAGPLFPAVSL 108
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 191-278 2.82e-09

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: 53.77  E-value: 2.82e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260   191 PSTPEiDLAESLVADNCVTLAWRMPDEDSkIDHYVLEYRKTNfegppRAKEDQPWMVVEGIKGTEYTLSGLKFDMKYmNF 270
Cdd:smart00060   1 PSPPS-NLRVTDVTSTSVTLSWEPPPDDG-ITGYIVGYRVEY-----REEGSEWKEVNVTPSSTSYTLTGLKPGTEY-EF 72


                   ....*...
gi 694857260   271 RVRACNKA 278
Cdd:smart00060  73 RVRAVNGA 80
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
 31-153 1.18e-08

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


Pssm-ID: 128778  Cd Length: 127  Bit Score: 53.42  E-value: 1.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260    31 REALRKIITTLAVKNEEIQNFIYSLKQMMQNVEANSSRAQEDLEGEFQSLYALLDELKDEMLMKIKQDRASRTYELQAQL 110
Cdd:smart00502   2 REALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQL 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 694857260   111 AACAKALESSEELLEAANQALGTANHHDFPQAAKQIKDSVTMA 153
Cdd:smart00502  82 ESLTQKQEKLSHAINFTEEALNSGDPTELLLSKKLIIERLQNL 124
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
182-291 1.75e-07

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 53.85  E-value: 1.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 182 LQALAFLPVPSTPEiDLAESLVADNCVTLAWRmPDEDSKIDHYVLeYRKTNfegpprakEDQPWMVVEGIKGTEYTLSGL 261
Cdd:COG3401  224 VSVTTPTTPPSAPT-GLTATADTPGSVTLSWD-PVTESDATGYRV-YRSNS--------GDGPFTKVATVTTTSYTDTGL 292

                         90       100       110
                 ....*....|....*....|....*....|.
gi 694857260 262 KFDMKYmNFRVRACNKA-VAGEFSEPVTLET 291
Cdd:COG3401  293 TNGTTY-YYRVTAVDAAgNESAPSNVVSVTT 322
fn3 pfam00041
Fibronectin type III domain;
208-284 1.40e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 46.25  E-value: 1.40e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694857260  208 VTLAWRMPDE-DSKIDHYVLEYRKTNFEGPPRakedqpWMVVEGIKgTEYTLSGLKFDMKYmNFRVRACNKAVAGEFS 284
Cdd:pfam00041  16 LTVSWTPPPDgNGPITGYEVEYRPKNSGEPWN------EITVPGTT-TSVTLTGLKPGTEY-EVRVQAVNGGGEGPPS 85
CC_brat-like cd20482
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ...
 31-92 1.87e-03

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.


Pssm-ID: 467844 [Multi-domain]  Cd Length: 122  Bit Score: 38.29  E-value: 1.87e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694857260  31 REALRKIIttlavknEEIQNFIYSLKQMMQNVEANSSR-------AQEDLEGEFQSLYALLDELKDEML 92
Cdd:cd20482    2 KESLQQLL-------EEARAKIPELRDALKNVEHALSRlqmqyhkAQNEINETFQFYRSMLEERKDELL 63
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
28-148 6.21e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 6.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260  28 AQAREALRKIITTLAVKNEEIQNFIYSLKQM---MQNVEANSSRAQEDLE---GEFQSLYALLDELKDEmLMKIKQDRAS 101
Cdd:COG4372   69 EQARSELEQLEEELEELNEQLQAAQAELAQAqeeLESLQEEAEELQEELEelqKERQDLEQQRKQLEAQ-IAELQSEIAE 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 694857260 102 RtyelQAQLAACAKALESSEELLEAANQALGTANHHDFPQAAKQIKD 148
Cdd:COG4372  148 R----EEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
 
Name Accession Description Interval E-value
SPRY_PRY_FSD1 cd12901
Fibronectin type III and SPRY containing 1 (FSD1) domain includes PRY at the N-terminus; This ...
 296-502 1.22e-153

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: 436.57  E-value: 1.22e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 296 FRLDASTCHQNLRVEELSVEWDATGGKV-QDVKAREKDGKGRTASPANSPARVvQSPKRMPSGRGGRDRFTAESYTVLGD 374
Cdd:cd12901    1 FKLDASSSHQNLKVEDLSVEWDATGGKVlQKIKGRENDGRSRTASPRNSSARC-QSPKRMPSARGGRDRFTAESYTVLGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 375 TLIDGDDHYWEVRYDRDSKAFGVGVAYRSLGKFDQLGKTSASWCLHLNNWLQVSFSAKHANKAKVLDVPVPDCIGVYCNF 454
Cdd:cd12901   80 TLIDGGQHYWEVRAQKDSKAFSVGVAYRSLGKFDQLGKTNASWCLHVNNWLQNSFAAKHNNKAKTLDVPVPDRIGVYCDF 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 694857260 455 HEGFLSFYNARTKQLLHTFKAKFTQPVLPAFTVWCGSFHVSSGLQVPS 502
Cdd:cd12901  160 DEGQLSFYNARTKQLLHTFKMKFTQPVLPAFMVWCGGLSVSTGLQVPS 207
SPRY_PRY_C-II cd13734
PRY/SPRY domain in tripartite motif-containing proteins 1, 9, 18, 36, 46, 67,76 (TRIM1, TRIM9, ...
 296-494 1.47e-46

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: 159.75  E-value: 1.47e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 296 FRLDASTCHQNLRVEE--LSVEWDATGGKVQDVKarekdgkgrtaspansparvvqspkrmpsgrggRDRFTAESYTVLG 373
Cdd:cd13734    1 FKLDPKTAHRKLRLSNdnLTVEYDPEGSKDQAAV---------------------------------LPRRFTGSPAVLG 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 374 DTLIDGDDHYWEVRYDRdSKAFGVGVAYRSLGKFDQLGKTSASWCLHLNNwlqVSFSAKHANKAKVLDVPV-PDCIGVYC 452
Cdd:cd13734   48 DVAISSGRHYWEVSVSR-STSYRVGVAYKSAPRDEDLGKNSTSWCLSRDN---NRYTARHDGKVVDLRVTGhPARIGVLL 123

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 694857260 453 NFHEGFLSFYNARTKQLLHTFKAKFTQPVLPAFTVWCGSFHV 494
Cdd:cd13734  124 DYDNGTLSFYDAESKQHLYTFHVDFEGPVCPAFAVWNGSLTL 165
SPRY_PRY cd12874
PRY/SPRY domain, also known as B30.2; This domain contains residues in the N-terminus that ...
 298-491 2.90e-37

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: 135.13  E-value: 2.90e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 298 LDASTCHQNLRVEE--LSVEWDATGGKvqdvkarekdgkgrtaspansparvvqspkrmpsgRGGRDRFTAESYTVLGDT 375
Cdd:cd12874    3 FDPDTAHLNLILSDdlRSVRVGDISQH-----------------------------------PPEPPPRFFECWQVLGSQ 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 376 LIDGDDHYWEVRYdRDSKAFGVGVAYRSL---GKFDQLGKTSASWCLHlnnWLQVSFSAKHANKAKVLDVPVPDCIGVYC 452
Cdd:cd12874   48 SFSSGRHYWEVDV-QDDSSWYVGVTYKSLprkGKMSNLGRNNGSWCLE---WRENEFSAWHNNPETRLPVTPPRRLGVFL 123

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 694857260 453 NFHEGFLSFYN-ARTKQLLHTFKAKFTQPVLPAFTVWCGS 491
Cdd:cd12874  124 DCDGGSLSFYGvTDGVQLLYTFKAKFTEPLYPAFWLGEGS 163
SPRY_PRY_TRIM18 cd12892
PRY/SPRY domain of TRIM18/MID1, also known as FXY or RNF59; This domain, consisting of the ...
 296-501 4.96e-28

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: 110.10  E-value: 4.96e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 296 FRLDASTCHQNLRV--EELSVEWDATGGKvqdvkarekdgkgRTASPansparvvqspkrmpsgrggrDRFTAE-SYTVL 372
Cdd:cd12892    2 FKLDPKSAHRKLKVshDNLTVERDETSSK-------------KSHTP---------------------ERFTSQgSYGVA 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 373 GDTLIDGDDHYWEVRYDrDSKAFGVGVAYRSLGKFDQLGKTSASW--CLHLNNWLqvsfsAKHANKAKVLDvPVPDC--I 448
Cdd:cd12892   48 GNVFIDSGRHYWEVVIS-GSTWYAIGIAYKSAPKHEWIGKNSASWvlCRCNNNWV-----VRHNSKEIPIE-PSPHLrrV 120

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 694857260 449 GVYCNFHEGFLSFYNARTKQLLHTFKAKFTQPVLPAFTVWCGSFHVSSGLQVP 501
Cdd:cd12892  121 GILLDYDNGSLSFYDALNSIHLYTFDIAFAQPVCPTFTVWNKCLTILTGLPIP 173
SPRY_PRY_C-I_2 cd12891
PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM14-like, ...
 356-493 4.23e-27

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: 107.33  E-value: 4.23e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 356 SGRGGRDRFTAESytVLGDTLIDGDDHYWEVRYdRDSKAFGVGVAYRSL---GKFDQLGKTSASWCLHlnnWLQVSFSAK 432
Cdd:cd12891   29 HYPDSPERFTHSQ--VLSTQSFSSGRHYWEVEV-SESGGWSVGVAYPSIerkGDESRIGRNDKSWCLE---WQDKSFSAW 102

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694857260 433 HANKAKVLDVPVPDCIGVYCNFHEGFLSFYNAR-TKQLLHTFKAKFTQPVLPAFTVWCGSFH 493
Cdd:cd12891  103 HNNEETPLPSVSSRRLGVYLDYEAGRLSFYELSdPIRHLHTFTATFTEPLHPAFWVLEGGWI 164
SPRY_PRY_SNTX cd16040
Stonustoxin subunit alpha or SNTX subunit alpha; This domain, consisting of the distinct ...
 382-491 9.60e-26

Stonustoxin subunit alpha or SNTX subunit alpha; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of Stonustoxin alpha proteins. Stonustoxin (SNTX) is a multifunctional lethal protein isolated from venom elaborated by the stonefish. It comprises two subunits, termed alpha and beta. SNTX elicits an array of biological responses, particularly a potent hypotension and respiratory difficulties.


Pssm-ID: 294002 [Multi-domain]  Cd Length: 180  Bit Score: 103.72  E-value: 9.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 382 HYWEVryDRDSKAFGVGVAYRSL---GKFDQ--LGKTSASWCLhlnNWLQVSFSAKHANKAKVLDVPVPDC--IGVYCNF 454
Cdd:cd16040   63 CYWEV--EWSGGGVDIAVAYKGIsrkGDGDDsrFGYNDKSWSL---ECSPSGYSFWHNNKKTEISVPSSSSsrVGVYLDH 137

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 694857260 455 HEGFLSFYN-ARTKQLLHTFKAKFTQPVLPAFTVWCGS 491
Cdd:cd16040  138 SAGTLSFYSvSDTMTLLHTVQTTFTEPLYPGFGVGYGS 175
SPRY_PRY_TRIM1 cd13739
PRY/SPRY domain of tripartite motif-binding protein 1 (TRIM1) or MID2; This domain, consisting ...
 296-498 1.57e-23

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: 97.39  E-value: 1.57e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 296 FRLDASTCHQNLRVEelsvewdatggkvQDVKAREKDgkgrtaspaNSPARVVQSPKRMpSGRGgrdrftaeSYTVLGDT 375
Cdd:cd13739    1 FKLDPKMAHKKLKIS-------------NDGLQMEKD---------ESSLKKSHTPERF-SGTG--------CYGAAGNI 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 376 LIDGDDHYWEVRYDrDSKAFGVGVAYRSLGKFDQLGKTSASWCL-HLNNwlqvSFSAKHANKAKVLDVPvPDC--IGVYC 452
Cdd:cd13739   50 FIDSGCHYWEVVVG-SSTWYAIGIAYKSAPKNEWIGKNSSSWVFsRCNN----NFVVRHNNKEMLVDVP-PQLkrLGVLL 123

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 694857260 453 NFHEGFLSFYNARTKQLLHTFKAKFTQPVLPAFTVWCGSFHVSSGL 498
Cdd:cd13739  124 DYDNNMLSFYDPANSLHLHTFEVSFILPVCPTFTIWNKSLMILSGL 169
SPRY_PRY_RNF135 cd12902
PRY/SPRY domain in RING finger protein RNF135; This domain, consisting of the distinct ...
 362-501 6.36e-18

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: 81.41  E-value: 6.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 362 DRFTAESytVLGDTLIDGDDHYWEVRyDRDSKAFGVGVAYRSLGKFDQLGKTSASWCLHLNNWLQvsFSAKHANKAKVLD 441
Cdd:cd12902   35 DRFSISQ--VLCSQAFSSGQHYWEVD-TRQCSHWAVGVASWEMSRDQMLGRTMDSWCIEWKGTGQ--LSAWHMNKETVLG 109

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 694857260 442 VPVPDCIGVYCNFHEGFLSFYN-ARTKQLLHTFKAKFTQPVLPAFtvWCGSFHVSSGLQVP 501
Cdd:cd12902  110 SDKPRVVGIWLDLEEGKLAFYSvANQERLLHECEVSASSPLHPAF--WLYGLEPGNSLIIK 168
SPRY_PRY_TRIM25 cd13736
PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25); This domain, consisting of ...
 339-495 7.23e-18

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: 81.08  E-value: 7.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 339 SPANSPARVVQSPKRMPSGRggrDRFTAESyTVLGDTLIDGDDHYWEVRYDRDSKAfGVGVAYRSL---GKFDQLGKTSA 415
Cdd:cd13736   15 SENYTKASVSDDPQNYREHP---QRFTYCS-QVLGLHCFKQGIHYWEVELQKNNFC-GVGICYGSMdrqGPESRLGRNSE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 416 SWCLHlnnWLQVSFSAKHANKAKVLDVPVPDCIGVYCNFHEGFLSFYNARTK-QLLHTFKAKFTQPVLPAFTVWCGSFHV 494
Cdd:cd13736   90 SWCVE---WFNVKISAWHNNVEKTLPSTKATRVGVLLNCDHGFVIFFAVQDKvHLMYKFKVDFTEALYPAFWVFSAGTTL 166


                 .
gi 694857260 495 S 495
Cdd:cd13736  167 S 167
SPRY_PRY_TRIM14 cd13738
PRY/SPRY domain of tripartite motif-binding protein 14 (TRIM14); This is a TRIM14 domain ...
 371-495 7.94e-18

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: 80.99  E-value: 7.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 371 VLGDTLIDGDDHYWEVRYDRDSKAFGVGVAYRSLGK-----FDQLGKTSASWCLH---LNNWlqvsfsAKH-ANKAKVLD 441
Cdd:cd13738   43 VLSRDSFFSGRHYWEVDLQEAGAGWWVGAAYPSIGRkgdseAARLGWNRQSWCLKrydLEYW------AFHdGQRSRLRP 116

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 694857260 442 VPVPDCIGVYCNFHEGFLSFYNARTKQL-LHTFKAKFTQPVLPAFTVWCGSFHVS 495
Cdd:cd13738  117 EDDPDRLGVFLDYEAGILSFYDVTGGMThLHTFRATFQEPLYPALRLWEGSISIC 171
SPRY_PRY_TRIM76 cd12898
PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76), also called ...
 335-485 9.66e-17

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: 78.05  E-value: 9.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 335 GRTASPA---NSPARVVQSPKRMPSGRGGrdrfTAESYTVLGDTLIDGDDHYWEVRYDRdSKAFGVGVAYRSLGKFDQLG 411
Cdd:cd12898    8 RETAHPAlhiSSDRGTVIYFHERRRKMSS----LTECPSVLGEELPSCGQYYWETTVTR-CPAYRLGICSSSASQAGALG 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694857260 412 KTSASWCLH-LNNWLQVSFSAKHAN-KAKVLDVPVPDCIGVYCNFHEGFLSFYNARTKQLLHTFKAKFTQPVLPAF 485
Cdd:cd12898   83 EGSTSWCLHcVPTSEPCRYTLLHSGiVSDVFVTERPARVGTLLDYNNGRLIFINAESGQLLGIFRHRFAQPCHPAF 158
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 382-490 4.50e-16

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: 74.64  E-value: 4.50e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260   382 HYWEVRYDrDSKAFGVGVAYRS--LGKFDQLGKTSASWCLHLNNWLQVsfsakHANKAKVLDVPV---PDCIGVYCNFHE 456
Cdd:smart00449   4 HYFEVEIG-DGGHWRVGVATKSvpRGYFALLGEDKGSWGYDGDGGKKY-----HNSTGPEYGLPLqepGDVIGCFLDLEA 77

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 694857260   457 GFLSFYNARTK-QLLHTFKAKFTQPVLPAFTVWCG 490
Cdd:smart00449  78 GTISFYKNGKYlHGLAFFDVKFSGPLYPAFSLGSG 112
SPRY_PRY_SPRYD4 cd12903
PRY/SPRY domain containing protein 4 (SPRYD4); This domain, consisting of the distinct ...
 344-497 6.36e-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: 72.48  E-value: 6.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 344 PARVVQSPKRMpsgrggRDRftaesYTVLGDTLIDGDDHYWEVRYDRdSKAFGVGVAYRSLGKFDQLGKTSASWCLhlnN 423
Cdd:cd12903   30 PTKVPQNPERF------RDW-----AVVLGDTPVTSGRHYWEVTVKR-SQEFRIGVADVDMSRDECIGTNESSWVF---A 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694857260 424 WLQVSFSAKHANKAkvldVPV-----PDCIGVYCNFHEGFLSFYNARTKQLLHTFKAKFTQPVLPAFTVWCGSFHVSSG 497
Cdd:cd12903   95 YAQRKWYAMVANET----VPVplvgkPDRVGLLLDYEAGKLSLVDVEKNSVVHTMSAEFRGPVVPAFALWDGELLTHSG 169
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 191-291 8.26e-15

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: 69.83  E-value: 8.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 191 PSTPEiDLAESLVADNCVTLAWRMPDED-SKIDHYVLEYRKTNfegpprakeDQPWMVVEG--IKGTEYTLSGLKFDMKY 267
Cdd:cd00063    1 PSPPT-NLRVTDVTSTSVTLSWTPPEDDgGPITGYVVEYREKG---------SGDWKEVEVtpGSETSYTLTGLKPGTEY 70

                         90       100
                 ....*....|....*....|....
gi 694857260 268 mNFRVRACNKAVAGEFSEPVTLET 291
Cdd:cd00063   71 -EFRVRAVNGGGESPPSESVTVTT 93
SPRY_PRY_TRIM65 cd12896
PRY/SPRY domain in tripartite motif-containing domain 65 (TRIM65); This domain, consisting of ...
 382-490 2.71e-14

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


Pssm-ID: 293953 [Multi-domain]  Cd Length: 182  Bit Score: 71.33  E-value: 2.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 382 HYWEVRYDRDSKAfgVGVAYRSL------GKFDQLGKTSASWCLHLNnwlQVSFSAKHANKAKVLDVPVPDCIGVYCNFH 455
Cdd:cd12896   65 HYWEVEVSSHSVT--LGVTYPGLprhkqgGHKDNIGRNPCSWGLQIQ---EDSLQAWHNGRAQKLQGVSYRLLGVDLDLE 139

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 694857260 456 EGFLSFYNARTK-QLLHTFKAKFTQPVLPAFtvWCG 490
Cdd:cd12896  140 AGTLTFYGLEPGtQRLHTFHAIFTQPLYPVF--WLL 173
SPRY_PRY_TRIM75 cd15829
PRY/SPRY domain of tripartite motif-binding protein 75 (TRIM75); This domain, consisting of ...
 279-491 5.24e-13

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: 67.70  E-value: 5.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 279 VAGEFSEPVTLetrafmfrlDASTCHQNLRVEElsvewDATggKVQDVKAREkdgkgrtaspanspaRVVQSPKRmpsgr 358
Cdd:cd15829   13 IIKKFRVDVTL---------DPETAHPNLLVSE-----DKK--CVTFTKKKQ---------------RVPDSPKR----- 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 359 ggrdrFTAESyTVLGDTLIDGDDHYWEVRYDRDSK-AFGVGVAYRSLGKFDQLGKTSASWCLHLNNwlqvsfSAKHANKA 437
Cdd:cd15829   57 -----FTVNP-VVLGFPGFHSGRHFWEVEVGDKPEwAVGVCKDSLSTKARRPPSGQQGCWRIQLQG------GDYDAPGA 124

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 694857260 438 KVLDVPV---PDCIGVYCNFHEGFLSFYNARTKQLLHTFKAKFTQPVLPAFTVWCGS 491
Cdd:cd15829  125 VPPPLLLevkPRGIGVFLDYELGEISFYNMPEKSHIHTFTDTFSGPLRPYFYVGPDS 181
SPRY_PRY_TRIM16 cd12890
PRY/SPRY domain in tripartite motif-containing protein 16 (TRIM16); This domain, consisting of ...
 382-485 1.06e-12

PRY/SPRY domain in tripartite motif-containing protein 16 (TRIM16); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM16 and TRIM-like proteins. TRIM16 (also known as estrogen-responsive B box protein or EBBP) does not possess a RING domain like the other TRIM proteins, but contains two B-box domains and can heterodimerize with other TRIM proteins such as TRIM24, Promyelocytic leukemia (PML) protein and Midline-1 (MID1 or TRIM18). It is a regulator of keratinocyte differentiation and a tumor suppressor in retinoid-sensitive neuroblastoma. It has been shown that loss of TRIM16 expression plays an important role in the development of cutaneous squamous cell carcinoma (SCC) and is a determinant of retinoid sensitivity. TRIM16 also has E3 ubiquitin ligase activity.


Pssm-ID: 293948  Cd Length: 182  Bit Score: 66.72  E-value: 1.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 382 HYWEVrydrDSKAFG--VGVAYRSLgkfDQLGKTS--------ASWCLHlnnWLQVSFSAKHANKAKVLDVPVPDCIGVY 451
Cdd:cd12890   65 YYFEV----EISGEGtyVGLTYKSI---DRKGSESnscisgnnFSWCLQ---WNGKEFSAWHSDVETPLKKGPFTRLGIY 134

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 694857260 452 CNFHEGFLSFY--NARTKQLLHTFKAKFTQPVLPAF 485
Cdd:cd12890  135 LDYPGGTLSFYgvEDDGMTLLHKFQCKFTEPLYPAF 170
SPRY_PRY_TRIM25-like cd13737
PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25)-like; This domain, ...
 382-491 4.36e-12

PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25)-like; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of proteins similar to TRIM25 (composed of RING/B-box/coiled-coil core and also known as RBCC proteins). TRIM25 (also called Efp) ubiquitinates the N terminus of the viral RNA receptor retinoic acid-inducible gene-I (RIG-I) in response to viral infection, leading to activation of the RIG-I signaling pathway, thus resulting in type I interferon production to limit viral replication. It has been shown that the influenza A virus targets TRIM25 and disables its antiviral function.


Pssm-ID: 293972  Cd Length: 172  Bit Score: 64.51  E-value: 4.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 382 HYWEVRYDRDSKAFGVGVAYR-SLGK---FDQLGKTSASWCLHlnnWLQVSFSAKHANKAKVLDVPVPDCIGVYCNFHEG 457
Cdd:cd13737   55 HYWEAEVSNSWVCLGVTYSYShPTGKsciFYLIGRNPYSWCLE---WDSLKFSVWHNNIQTVVHGSYYKTIGVLLDYAAG 131

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 694857260 458 FLSFYN-ARTKQLLHTFKAKFTQPVLPAFTVWCGS 491
Cdd:cd13737  132 SLTFYGvANTMNLIYRFLTTFTEPLYPAVMVSSGA 166
SPRY_PRY_TRIM76_like cd12899
PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76)-like; This domain is ...
 371-487 5.91e-12

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: 64.42  E-value: 5.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 371 VLGDTLIDGDDHYWEVRYDRDSKaFGVGVAYRSLGKFDQLGKTSASWCL-HLNNWLQVSFSAKHANKAKVLDVPV-PDCI 448
Cdd:cd12899   47 VMGSLIPVRGKHYWEVEVDEQTE-YRVGVAFEDTQRNGYLGANNTSWCMrHIITPSRHKYEFLHNGWTPDIRITVpPKKI 125

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 694857260 449 GVYCNFHEGFLSFYNARTKQLLHTFKAKFTQPVLPAFTV 487
Cdd:cd12899  126 GILLDYDSGRLSFFNVDLAQHLYTFSCQFQHFVHPCFSL 164
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 382-487 4.07e-11

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin.


Pssm-ID: 459877  Cd Length: 121  Bit Score: 60.43  E-value: 4.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260  382 HYWEVRYDRDSKA-FGVGVAYRS--LGKFDQLGKTSASWCLHLNNwLQVSFSAKHANKAKVLDVPvPDCIGVYCNFHEGF 458
Cdd:pfam00622   2 HYFEVEIFGQDGGgWRVGWATKSvpRKGERFLGDESGSWGYDGWT-GKKYWASTSPLTGLPLFEP-GDVIGCFLDYEAGT 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 694857260  459 LSFYNArTKQLLHTF-KAKFTQPVLPAFTV 487
Cdd:pfam00622  80 ISFTKN-GKSLGYAFrDVPFAGPLFPAVSL 108
SPRY_PRY_C-I_1 cd13733
PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM5, TRIM6, TRIM7, ...
 363-485 7.43e-10

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: 57.87  E-value: 7.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 363 RFTaESYTVLGDTLIDGDDHYWEVRYdRDSKAFGVGVAYRSLgkfDQLGKTSAS-----WCLHLNNWLQVSFSAKHANKA 437
Cdd:cd13733   37 RFD-TCVCVLGSEGFSSGRHYWEVEV-GGKTDWDLGVARESV---NRKGKITLSpengyWTVGLRNGNEYKALTSPSTPL 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 694857260 438 KvLDVPvPDCIGVYCNFHEGFLSFYNARTKQLLHTFKAKFTQPVLPAF 485
Cdd:cd13733  112 S-LREK-PQKVGVFLDYEEGQVSFYNVDDGSHIYTFTDCFTEKLYPYF 157
SPRY_PRY_TRIM35 cd12893
PRY/SPRY domain in tripartite motif-containing protein 35 (TRIM35); This PRY/SPRY domain is ...
 363-492 8.74e-10

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: 57.64  E-value: 8.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 363 RFTaESYTVLGDTLIDGDDHYWEVRYdRDSKAFGVGVAYRSL---GKFDqLGKTSASWCL-HLNNwlqvSFSAKHANKAK 438
Cdd:cd12893   37 RFD-PYPCVLGSEGFTSGKHSWDVEV-GDNTSWMLGVAKESVqrkGKFT-LSPESGFWTIgFSEG----KYSARTSPEPR 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 694857260 439 VLdVPV---PDCIGVYCNFHEGFLSFYNARTKQLLHTFKAKFTQPVLPAFTVWCGSF 492
Cdd:cd12893  110 TP-LRVkqkPQRIRVQLDWDRGKVSFSDPDTNTHIHTFTHTFTERVFPYFYTGCKSE 165
SPRY_PRY_TRIM69 cd15818
PRY/SPRY domain in tripartite motif-binding protein 69 (TRIM69), also known as RING finger ...
 362-485 1.77e-09

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: 57.12  E-value: 1.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 362 DRFTAeSYTVLGDTLIDGDDHYWEVRYDRDSKaFGVGVAYRSLGKFDQ--LGKTSASWCLHLNNwlqvsfsakhANKAKV 439
Cdd:cd15818   49 ERFDS-SVAVLGSEGFTSGKHYWEVEVAKKTK-WTLGVVRESINRKGNcpLSPEDGFWLLRLRN----------QNELKA 116

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 694857260 440 LDVPV--------PDCIGVYCNFHEGFLSFYNARTKQLLHTFKAKFTQPVLPAF 485
Cdd:cd15818  117 LDVPSfsltltsnLNKVGIYLDYEGGQVSFYNANTMSHIYTFSDTFTEKIYPYF 170
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 191-278 2.82e-09

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: 53.77  E-value: 2.82e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260   191 PSTPEiDLAESLVADNCVTLAWRMPDEDSkIDHYVLEYRKTNfegppRAKEDQPWMVVEGIKGTEYTLSGLKFDMKYmNF 270
Cdd:smart00060   1 PSPPS-NLRVTDVTSTSVTLSWEPPPDDG-ITGYIVGYRVEY-----REEGSEWKEVNVTPSSTSYTLTGLKPGTEY-EF 72


                   ....*...
gi 694857260   271 RVRACNKA 278
Cdd:smart00060  73 RVRAVNGA 80
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
 31-153 1.18e-08

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


Pssm-ID: 128778  Cd Length: 127  Bit Score: 53.42  E-value: 1.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260    31 REALRKIITTLAVKNEEIQNFIYSLKQMMQNVEANSSRAQEDLEGEFQSLYALLDELKDEMLMKIKQDRASRTYELQAQL 110
Cdd:smart00502   2 REALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQL 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 694857260   111 AACAKALESSEELLEAANQALGTANHHDFPQAAKQIKDSVTMA 153
Cdd:smart00502  82 ESLTQKQEKLSHAINFTEEALNSGDPTELLLSKKLIIERLQNL 124
SPRY_BSPRY cd12904
SPRY domain in Ro-Ret family; This domain, named BSPRY, has been identified in the Ro-Ret ...
 371-487 2.06e-08

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: 53.96  E-value: 2.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 371 VLGDTLIDGDDHYWEVRYDRdSKAFGVGVAYRSL-----GKFDQLGKTSASWCL-HLNNwlqvSFSAKHANKAKVLD-VP 443
Cdd:cd12904   45 ALASLSFSSGTHAWVVDVGK-SCAYKVGVCYGSLerkgsGNEARLGYNAFSWVFsRYDG----EFSFSHNGQHVPLElLK 119

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 694857260 444 VPDCIGVYCNFHEGFLSFYNARTKQLLHTFKAKFTQPVLPAFTV 487
Cdd:cd12904  120 CPARVGVLLDWPSQELLFYDPDSCTVLHSHREAFAAPLLPVFAV 163
SPRY_PRY_TRIM62 cd13744
PRY/SPRY domain in tripartite motif-binding protein 62 (TRIM62); This domain, consisting of ...
 363-486 2.18e-08

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


Pssm-ID: 293978  Cd Length: 188  Bit Score: 54.24  E-value: 2.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 363 RFTAEsYTVLGDTLIDGDDHYWEVRYDrDSKAFGVGVAYRSLGKFD--QLGKTSASWCLHLNNWLQVSFSAKHANKAKVL 440
Cdd:cd13744   50 RFDVE-VSVLGSEGFSGGVHYWEVVVS-EKTQWMIGLAHEAVSRKGsiQIQPGRGFYCIVMHDGNQYSACTEPWTRLNVK 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 694857260 441 DVPvpDCIGVYCNFHEGFLSFYNARTKQLLHTFKAKFTQPVLPAFT 486
Cdd:cd13744  128 SKL--EKVGVYLDYDKGLLIFYNADDMSWLYTFREKFPGKLCSYFS 171
SPRY_PRY_TRIM60_75 cd15817
PRY/SPRY domain of tripartite motif-binding protein 60 and 75 (TRIM60 and TRIM75); This domain, ...
 363-487 3.77e-08

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: 52.94  E-value: 3.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 363 RFTAESyTVLGDTLIDGDDHYWEVRYdRDSKAFGVGVAYRSLGKFDQLGKTSASWCLHLNNWLQvSFSAKHANKAKVLDV 442
Cdd:cd15817   37 RFTVYP-AVLGSEGFDSGRHFWEVEV-GGKGEWILGVCKDSLPRNAQDPPSPLGGCWQIGRYMS-GYVASGPKTTQLLPV 113

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 694857260 443 PVPDCIGVYCNFHEGFLSFYNARTKQLLHTFKAKFTQPVLPAFTV 487
Cdd:cd15817  114 VKPSRIGIFLDYELGEVSFYNMNDRSHLYTFTDTFTGKLIPYFYV 158
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
182-291 1.75e-07

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 53.85  E-value: 1.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 182 LQALAFLPVPSTPEiDLAESLVADNCVTLAWRmPDEDSKIDHYVLeYRKTNfegpprakEDQPWMVVEGIKGTEYTLSGL 261
Cdd:COG3401  224 VSVTTPTTPPSAPT-GLTATADTPGSVTLSWD-PVTESDATGYRV-YRSNS--------GDGPFTKVATVTTTSYTDTGL 292

                         90       100       110
                 ....*....|....*....|....*....|.
gi 694857260 262 KFDMKYmNFRVRACNKA-VAGEFSEPVTLET 291
Cdd:COG3401  293 TNGTTY-YYRVTAVDAAgNESAPSNVVSVTT 322
SPRY_PRY_TRIM72 cd13742
PRY/SPRY domain in tripartite motif-binding protein 72 (TRIM72); This domain, consisting of ...
 363-487 4.62e-07

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: 50.24  E-value: 4.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 363 RFTAESYTVLGDTLIDGDdHYWEVRYDrDSKAFGVGVAYRSLGKFDQLGKTSAS--WCLHLNNWLQVSFSAKHaNKAKVL 440
Cdd:cd13742   50 RFDKANCVVSHQSFSEGE-HYWEVIVG-DKPRWALGVISAEAGRKGRLHALPSNgfWLLGCKEGKVYEAHVEH-KEPRAL 126

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 694857260 441 DVPV-PDCIGVYCNFHEGFLSFYNARTKQ---LLHTFKAKFTQPVLPAFTV 487
Cdd:cd13742  127 RVEGrPTRIGVYLSFSDGVLSFYDASDEDnlvQLFAFHERFPGPLYPFFDV 177
SPRY_PRY_TRIM34 cd15825
PRY/SPRY domain in tripartite motif-containing protein 34 (TRIM34), also known as RING finger ...
 364-488 7.06e-07

PRY/SPRY domain in tripartite motif-containing protein 34 (TRIM34), also known as RING finger protein 21 (RNF21) or interferon-responsive finger protein (IFP1); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM34, also known as RING finger protein 21 (RNF21) or interferon-responsive finger protein (IFP1). TRIM34 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. The TRIM21 cDNA possesses at least three kinds of isoforms, due to alternative splicing, of which only the long and medium forms contain the SPRY domain. It is an interferon-induced protein, predominantly expressed in the testis, kidney, and ovary. The SPRY domain provides the capsid recognition motif that dictates specificity to retroviral restriction. While the PRY-SPRY domain provides specificity and the capsid recognition motif to retroviral restriction, TRIM34 binds HIV-1 capsid but does not restrict HIV-1 infection.


Pssm-ID: 293997  Cd Length: 185  Bit Score: 49.45  E-value: 7.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 364 FTAESYTVLGDTLIDGDDHYWEVRYDRdSKAFGVGVAYRSLG---KFDQLGKTSAS-----------WCLHLNNWLQVS- 428
Cdd:cd15825   32 FKCYNYGILGSQYFSSGKHYWEVDVSK-KTAWILGVYCRKRSrtfKYVRQGKNHPNvysryrpqygyWVIGLQNKSEYYa 110

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694857260 429 FSAKHANKAKVLD--VPVPDC-IGVYCNFHEGFLSFYNARTK-QLLHTF-KAKFTQPVLPAFTVW 488
Cdd:cd15825  111 FEDSSTSDPKVLTlsVATPPHrVGVFLDYEAGTVSFFNVTNHgSLIYKFsKCCFSQPVYPYFNPW 175
SPRY_PRY_TRIM41 cd13741
PRY/SPRY domain in tripartite motif-binding protein 41 (TRIM41); This domain, consisting of ...
 337-487 7.10e-07

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: 49.76  E-value: 7.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 337 TASPANSPARVVQSPKRMPSGRGGR--------DRFTAEsYTVLGDTLIDGDDHYWEVRYDrDSKAFGVGVAYRSLGKFD 408
Cdd:cd13741    3 TLDPDTAHPALLLSPDRRGVRLAERrqevpehpKRFSAD-CCVLGAQGFRSGRHYWEVEVG-GRRGWAVGAARESTHHKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 409 QLGKTSAS------------------------------WCLHLNNwlqVSFSAKHANKAKVLD-VPVPDCIGVYCNFHEG 457
Cdd:cd13741   81 KVGSGGSSvssgdasssrhhhrrrrlhlpqqpllqrevWCVGTNG---KRYQAQSSTEQTLLSpSEKPRRFGVYLDYEAG 157

                        170       180       190
                 ....*....|....*....|....*....|.
gi 694857260 458 FLSFYNARTKQLLHTFKAKF-TQPVLPAFTV 487
Cdd:cd13741  158 RLGFYNAETLAHVHTFSAAFlGERVFPFFRV 188
fn3 pfam00041
Fibronectin type III domain;
208-284 1.40e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 46.25  E-value: 1.40e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694857260  208 VTLAWRMPDE-DSKIDHYVLEYRKTNFEGPPRakedqpWMVVEGIKgTEYTLSGLKFDMKYmNFRVRACNKAVAGEFS 284
Cdd:pfam00041  16 LTVSWTPPPDgNGPITGYEVEYRPKNSGEPWN------EITVPGTT-TSVTLTGLKPGTEY-EVRVQAVNGGGEGPPS 85
SPRY_PRY_TRIM7_like cd12888
PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7)-like, including TRIM7, TRIM10, ...
 363-491 3.51e-06

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: 47.17  E-value: 3.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 363 RFTAEsYTVLGDTLIDGDDHYWEVRYDrDSKAFGVGVAYRSLGKFDQLGKTSAS--WCLHLNNWLqvsFSAKHANKAKVL 440
Cdd:cd12888   37 RFDTW-PCVLGCEGFTSGRHYWEVEVG-DGGGWAVGVARESVRRKGEISFSPEEgiWAVGQWGGQ---YWALTSPETPLP 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 694857260 441 DVPVPDCIGVYCNFHEGFLSFYNARTKQLLHTFKAKF--TQPVLPAFTVWCGS 491
Cdd:cd12888  112 LSEVPRRIRVYLDYEGGQVAFFDADNEAPIFTFPPASfaGERIFPWFWVGKGS 164
SPRY_PRY_TRIM21 cd12900
PRY/SPRY domain in tripartite motif-binding protein 21 (TRIM21) also known as 52kD ...
 346-487 5.41e-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: 46.80  E-value: 5.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 346 RVVQSPKRMPsgrGGRDRFtaESY-TVLGDTLIDGDDHYWEVryDRDSK-AFGVGVAYRSL---GKFdQLGKTSASWCLh 420
Cdd:cd12900   26 RLGDTHQNVP---ENEERF--DNYpMVLGAQRFNSGKHYWEV--DVTGKeAWDLGVCRDSVrrkGQF-LLSPENGFWTI- 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 421 lnnWLQVSFSAKHANKAKVLDVPVPDC-IGVYCNFHEGFLSFYN-ARTKQLLHTF-KAKFTQPVLPAFTV 487
Cdd:cd12900   97 ---WLWNKKYEAGTSPQTTLHLQVPPCqVGIFLDYEAGVVSFYNiTDHGSLIYTFsECAFTGPLRPFFNP 163
SPRY_PRY_TRIM60 cd15828
PRY/SPRY domain of tripartite motif-binding protein 60 (TRIM60) also known as RING finger ...
 371-485 5.63e-06

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: 46.90  E-value: 5.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 371 VLGDTLIDGDDHYWEVRYDRDSKAFgVGVAYRSL--GKFDQLGKTSASWCLHLnnWLQVSFSAKHANKAKVLDVPVPDCI 448
Cdd:cd15828   54 VLGSEGFHSGRQYWEVEVGDKPEWT-LGVCQDCLprNWSNQPSVQDGLWAIGR--YSESNYVALGPKKIQLLPKVRPSKI 130

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 694857260 449 GVYCNFHEGFLSFYNARTKQLLHTFKAKFTQPVLPAF 485
Cdd:cd15828  131 GIFLDYELGEVSFYNMNDRSLLYTFSDSFTGTLWPYF 167
SPRY_PRY_TRIM7 cd13740
PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7); This domain, consisting of the ...
 363-487 9.98e-06

PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of tripartite motif-containing protein 7 (TRIM7), also referred to as glycogenin-interacting protein (GNIP) or RING finger protein 90 (RNF90). TRIM7 or GNIP interacts with glycogenin and stimulates its self-glucosylating activity via its SPRY domain. The GNIP gene encodes at least four distinct isoforms of GNIP, of which three (GNIP1, GNIP2, and GNIP3) have the B30.2 domain.


Pssm-ID: 293975 [Multi-domain]  Cd Length: 169  Bit Score: 46.10  E-value: 9.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 363 RFTAESyTVLGDTLIDGDDHYWEVRY-DRDSKAFGVGVAYRSLGKFDQLGKTSASWCLHLNN---WLQVS-----FSAKH 433
Cdd:cd13740   37 RFDTNT-RVLASCGFSSGRHHWEVEVgSKDGWAFGVARESVRRKGLTPFTPEEGVWALQLNGgqyWAVTSpertpLSCGH 115

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 694857260 434 ANKAKVldvpvpdcigvYCNFHEGFLSFYNARTKQLLHTFKAKFTQPVLPAFTV 487
Cdd:cd13740  116 LSRVRV-----------ALDLEVGAVSFYAAEDMRHIYTFRVNFQERVFPLFSV 158
SPRY_PRY_TRIM17 cd15812
PRY/SPRY domain of tripartite motif-binding protein 17 (TRIM17), also known as testis RING ...
 360-504 1.61e-05

PRY/SPRY domain of tripartite motif-binding protein 17 (TRIM17), also known as testis RING finger protein (terf); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM17, also known as RING finger protein 16 (RNF16) or testis RING finger protein (terf). TRIM17 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein, expressed almost exclusively in the testis. It exhibits E3 ligase activity, causing protein degradation of ZW10 interacting protein (ZWINT), a known component of the kinetochore complex required for the mitotic spindle checkpoint, and negatively regulates proliferation of breast cancer cells. TRIM17 undergoes ubiquitination in COS7 fibroblast-like cells but is inhibited and stabilized by TRIM44.


Pssm-ID: 293984 [Multi-domain]  Cd Length: 176  Bit Score: 45.65  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 360 GRDRFTAESYTVlGDTLIDGDDHYWEVRYDRDSKA-FGVGVAYRSLGKFDQLGKtsaswCLHLNNWL-QVSFSAKHAN-- 435
Cdd:cd15812   34 SKDRFLAYPCAV-GQETFSSGRHYWEVGMNLTGDAlWALGVCRDNVSRKDRVPK-----SPENGFWVvQLSKGKKYLSam 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694857260 436 --KAKVLDVPVPDCIGVYCNFHEGFLSFYNARTKQLLHTF-KAKFTQPVLPAFTVWCGsfhvSSGLQVPSAV 504
Cdd:cd15812  108 saLTPVTLTEPPSHMGIFLDFEAGEVSFYSVNDGSHLHTYsQAAFPGPLQPFFCLGAP----KSGQMVISTV 175
SPRY_PRY_TRIM4 cd15809
PRY/SPRY domain in tripartite motif-binding protein 4 (TRIM4), also known as RING finger ...
 371-485 1.74e-05

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: 45.59  E-value: 1.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 371 VLGDTLIDGDDHYWEVRyDRDSKAFGVGVAyrslgKFDQLGKTSAS--------WCLHLNN---WLQVSFSAKHANKAkv 439
Cdd:cd15809   66 VLGKNVFTSGKHYWEVE-NRDSLEIAVGVC-----REDVMGITDGSemsphvgiWAICWSSagyRPLTSSPVSPTKQE-- 137

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 694857260 440 ldvPVPDCIGVYCNFHEGFLSFYNARTKQLLHTFKAKFTQPVLPAF 485
Cdd:cd15809  138 ---PALHRVGVFLDHGAGEVSFYSAVDGVHLHTFSCPLVSRLRPFF 180
SPRY_PRY_TRIM10 cd15827
PRY/SPRY domain of tripartite motif-binding protein 10 (TRIM10) also known as hematopoietic ...
 445-488 1.95e-05

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


Pssm-ID: 293999 [Multi-domain]  Cd Length: 172  Bit Score: 45.21  E-value: 1.95e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 694857260 445 PDCIGVYCNFHEGFLSFYNARTKQLLHTFKAKFTQPVLPAFTVW 488
Cdd:cd15827  120 PRQVRVSLDYEVGWVTFVNAVTQEPIYTFTASFTQKVFPFFGLW 163
SPRY_PRY_TRIM5_6_22_34 cd15810
PRY/SPRY domain of tripartite motif-binding protein 5, 6, 22 and 34 (TRIM5, TRIM6, TRIM22 and ...
 345-488 2.71e-05

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


Pssm-ID: 293982 [Multi-domain]  Cd Length: 189  Bit Score: 45.16  E-value: 2.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 345 ARVVQSPkrmPSGRGGRDRFTAesYTVLGDTLIDGDDHYWEVRYDRDSkAFGVGVAYRS---LGKFDQLGKTSAS----- 416
Cdd:cd15810   22 VRIVPPQ---TSGQALTNNNYD--FGVLGSQYFSSGKHYWEVDVSKKS-AWILGVCSHKrsdAMTKSNANQINHQnvysr 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 417 -------WCLHLNNWLQVS---FSAKHANKAKVLDVPV-PDCIGVYCNFHEGFLSFYNArTKQ--LLHTF-KAKFTQPVL 482
Cdd:cd15810   96 yqpqygyWVIGLQNESEYNafeDSSSFNPHVLTLSVTVpPHRVGVFLDYEAGTVSFFNV-TNHgsLIYKFsKCCFSTTVC 174


                 ....*.
gi 694857260 483 PAFTVW 488
Cdd:cd15810  175 PYFNPW 180
SPRY_PRY_TRIM50_72 cd12897
PRY/SPRY domain in tripartite motif-binding (TRIM) proteins TRIM50 and TRIM72; This domain, ...
 381-487 5.15e-05

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: 44.14  E-value: 5.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 381 DHYWEVRY-DRDSKAFGV--GVAYRSlgkfdqlGKTSAS-----WCLHLNNWlQVSFSAKHANKAKVLDVP-VPDCIGVY 451
Cdd:cd12897   66 EHYWEVVVgDKPRWALGVikGTASRK-------GKLHASpshgvWLIGLKEG-KVYEAHGEPKEPRPLRVAgRPHRIGVY 137

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 694857260 452 CNFHEGFLSFYNARTK---QLLHTFKAKFTQPVLPAFTV 487
Cdd:cd12897  138 LSFEDGVLSFFDASDPddlRTLYTFQERFQGKLYPFFDV 176
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 382-462 7.08e-05

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


Pssm-ID: 293931  Cd Length: 118  Bit Score: 42.42  E-value: 7.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 382 HYWEVRYDRDSK---AFGVGVAYRSLGKFDQLGKTSASWCLHLNNWLQVSfsaKHANKAKVLDVPVPDCIGVYCNFHEGF 458
Cdd:cd11709    3 WYWEVRVDSGNGgliQVGWATKSFSLDGEGGVGDDEESWGYDGSRLRKGH---GGSSGPGGRPWKSGDVVGCLLDLDEGT 79


                 ....
gi 694857260 459 LSFY 462
Cdd:cd11709   80 LSFS 83
SPRY_PRY_TRIM11 cd15811
PRY/SPRY domain of tripartite motif-binding protein 11 (TRIM11), also known as RING finger ...
 371-486 1.01e-04

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: 43.02  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 371 VLGDTLIDGDDHYWEVRY-DRDSKAFGVGVAYRSLGKFDQLGKTSASWCLhlnNWLQVSFSAKHANKAKVLDVPVPdcIG 449
Cdd:cd15811   44 VLGRERFTSGRHYWEVEVgDRTSWALGVCKENVNRKEKGELSAGNGFWIL---VFLGNYYSSERRTFAPLRDPPRR--VG 118

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 694857260 450 VYCNFHEGFLSFYNARTKQLLHTF-KAKFTQPVLPAFT 486
Cdd:cd15811  119 IFLDYEAGHLSFYSATDGSLLFIFpETPFSGTLRPLFS 156
SPRY_PRY_TRIM67_9 cd12889
PRY/SPRY domain in tripartite motif-containing proteins, TRIM9 and TRIM67; This domain, ...
 365-462 1.33e-04

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: 42.61  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 365 TAESY---TVLGDTLIDGDDHYWEV---RYDRDSK-AFGVgvAYRSLGKFDQLGKTSASWCLHLNN---WLQvsFSAKHA 434
Cdd:cd12889   31 TCNSYedrVVLGSVGFSRGVHYWEVtidRYDGHPDpAFGV--ARIDVNKDKMLGKDDKGWSMYIDNnrsWFL--HNNEHS 106

                         90       100
                 ....*....|....*....|....*...
gi 694857260 435 NKAKVlDVPVPDCIGVYCNFHEGFLSFY 462
Cdd:cd12889  107 NRTEG-GITVGSVVGVLLDLDRHTLSFY 133
SPRY_PRY_A33L cd12905
zinc-binding protein A33-like; This domain, consisting of the distinct N-terminal PRY ...
 298-486 1.38e-03

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: 39.70  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 298 LDASTCHQNLRVEElsvewDATggkvqdvKAREKDgkgrtaspanSPARVVQSPKRMpsgrggrdrftAESYTVLGDTLI 377
Cdd:cd12905    8 FDPETAHPSLILSR-----DLT-------AVTESD----------EMQPYPRSPKRF-----------LQCVNVLASQGF 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 378 DGDDHYWEVRYDRDSKaFGVGVAYRSLGKFD--QLGKTSASWCLHLNNWLQVSFSAKHANKAKVLDVPVPdcIGVYCNFH 455
Cdd:cd12905   55 QSGRHYWEVWVGSKTK-WDLGVASESVDRQArvKLCPENGYWTLRLRNGDEYWAGTQPWTRLRVTSRPQR--IGVFLDCE 131

                        170       180       190
                 ....*....|....*....|....*....|.
gi 694857260 456 EGFLSFYNARTKQLLHTFKAKFTQPVLPAFT 486
Cdd:cd12905  132 ERKVSFYNADDMSLLYSFHQGPRGKVFPFFS 162
CC_brat-like cd20482
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ...
 31-92 1.87e-03

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.


Pssm-ID: 467844 [Multi-domain]  Cd Length: 122  Bit Score: 38.29  E-value: 1.87e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694857260  31 REALRKIIttlavknEEIQNFIYSLKQMMQNVEANSSR-------AQEDLEGEFQSLYALLDELKDEML 92
Cdd:cd20482    2 KESLQQLL-------EEARAKIPELRDALKNVEHALSRlqmqyhkAQNEINETFQFYRSMLEERKDELL 63
SPRY_PRY_BTN3 cd15820
PRY/SPRY domain of butyrophilin 3 (BTN3), includes BTN3A1, BTN3A2, BTN3A3 as well as BTN-like ...
 298-493 2.65e-03

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: 38.95  E-value: 2.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 298 LDASTCHQNLRVEE--LSVEWdatggkvqdvkarekdgkgrtaspANSPARVVQSPKRMpsgrggrDRFtaesYTVLGDT 375
Cdd:cd15820    8 LDPDTANPILLISEdqRSLQW------------------------ADEPQNLPDNPKRF-------DWH----YCVLGCK 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 376 LIDGDDHYWEVRYDrDSKAFGVGVAYRSLGKFDQLGKTSAS--WCLHLNNwlQVSFSAKHANKAKVLDVPVPDCIGVYCN 453
Cdd:cd15820   53 SFTSGRHFWEVEVG-DRKEWYVGVCRENVERKLWVKMAPENgfWTIGLSD--GNDYQALTDPRTKLTIANPPQRVGVFLD 129

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 694857260 454 FHEGFLSFYNARTKQLLHTF-KAKFTQPVLPAFTVwCGSFH 493
Cdd:cd15820  130 YETGEVSFYNAMDGSHIYTFpHTSFSGPLYPVFRL-LSWDP 169
SPRY_PRY_BTN1_2 cd15819
butyrophilin subfamily member A1 and A2 (BTN1A and BTN2A); This domain, consisting of the ...
 371-488 2.92e-03

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: 38.75  E-value: 2.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 371 VLGDTLIDGDDHYWEVRYdRDSKAFGVGVAYRSLGKfdqLGKTSAS-----WCLHLNN---W----LQVSFSAKHAnkak 438
Cdd:cd15819   46 VLGQEGFTSGRHYWEVEV-GDRTSWDLGVCRDNVMR---KGRVTLSpengfWAIRLYGneyWaltsPETPLTLKEP---- 117

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 694857260 439 vldvpvPDCIGVYCNFHEGFLSFYNARTKQLLHTF-KAKFTQPVLPAFTVW 488
Cdd:cd15819  118 ------PRRVGIFLDYEAGDVSFYNMTDGSHIYTFpQTAFSGPLRPFFRLW 162
SPRY_PRY_TRIM22 cd15824
PRY/SPRY domain in tripartite motif-containing protein 22 (TRIM22), also known as RING finger ...
 417-488 4.16e-03

PRY/SPRY domain in tripartite motif-containing protein 22 (TRIM22), also known as RING finger protein 94 (RNF94) or Stimulated trans-acting factor of 50 kDa (STAF50); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM22, also known as RING finger protein 94 (RNF94) or STAF50 (Stimulated trans-acting factor of 50 kDa). TRIM6 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. TRIM22 is an interferon-induced protein, predominantly expressed in peripheral blood leukocytes, in lymphoid tissue such as spleen and thymus, and in the ovary.TRIM22 plays an integral role in the host innate immune response to viruses; it has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. TRIM22 inhibits influenza A virus (IAV) infection by targeting the viral nucleoprotein for degradation; it represents a novel restriction factor up-regulated upon IAV infection that curtails its replicative capacity in epithelial cells. Altered TRIM22 expression has also been associated with multiple sclerosis, cancer, and autoimmune disease. A large number of high-risk non-synonymous (ns)SNPs have been identified in the highly polymorphic TRIM22 gene, most of which are located in the SPRY domain and could possibly alter critical regions of the SPRY structural and functional residues, including several sites that undergo post-translational modification. TRIM22 is a direct p53 target gene and inhibits the clonogenic growth of leukemic cells. Its expression in Wilms tumors is negatively associated with disease relapse. It is greatly under-expressed in breast cancer cells as compared to non-malignant cell lines; p53 dysfunction may be one of the mechanisms for its down-regulation.


Pssm-ID: 293996 [Multi-domain]  Cd Length: 198  Bit Score: 38.67  E-value: 4.16e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694857260 417 WCLHLNNWLQV-SFSAKHANKAKVLDV--PVPDC-IGVYCNFHEGFLSFYNARTK-QLLHTF-KAKFTQPVLPAFTVW 488
Cdd:cd15824  110 WVIGLQNESEYnAFEDSSSSDPKVLTLsmAVPPHrVGVFLDYEAGTVSFFNVTNHgSLIYKFsKCCFSQPVYPYFNPW 187
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
28-148 6.21e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 6.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260  28 AQAREALRKIITTLAVKNEEIQNFIYSLKQM---MQNVEANSSRAQEDLE---GEFQSLYALLDELKDEmLMKIKQDRAS 101
Cdd:COG4372   69 EQARSELEQLEEELEELNEQLQAAQAELAQAqeeLESLQEEAEELQEELEelqKERQDLEQQRKQLEAQ-IAELQSEIAE 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 694857260 102 RtyelQAQLAACAKALESSEELLEAANQALGTANHHDFPQAAKQIKD 148
Cdd:COG4372  148 R----EEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
SPRY_PRY_TRIM47 cd15808
PRY/SPRY domain in tripartite motif-containing protein 47 (TRIM47), also known as RING finger ...
 363-475 6.30e-03

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


Pssm-ID: 293980  Cd Length: 206  Bit Score: 38.33  E-value: 6.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694857260 363 RFTaESYTVLGDTLIDGDDHYWEVRYDRDSKAFGVGVA-YRSLGKFD--QLGKTSASWCLHlnnWLQVSFSAKHANKAKV 439
Cdd:cd15808   44 RFT-HCEQVLGEGALDRGTYYWEVEIIEGWVSVGVMAEdFSPREPYDrgRLGRNAHSCCLQ---WNGRNFSVWFHGLEAP 119

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 694857260 440 LDVPVPDCIGVYCNFHEGFLSFYNARTK--QLLHTFKA 475
Cdd:cd15808  120 LPHPFSPTVGVCLEYADRALAFYAVRDGkvSLLRRLKA 157
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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