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Conserved domains on  [gi|2065618660|ref|XP_007903793|]
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RING finger protein 17 isoform X1 [Callorhinchus milii]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tudor_TDRD4_rpt5 cd20418
fifth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
1555-1659 2.06e-65

fifth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the fifth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


:

Pssm-ID: 410489  Cd Length: 105  Bit Score: 216.51  E-value: 2.06e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1555 LTDFRSEMPCLAEYDDGRWYRAKVLSVDNLHPLKILVQHVDFGSSASLPESRLRQLPIGLMQYPARAIRVKLMGFKPPAS 1634
Cdd:cd20418      1 LTDFRPEMPCLAEYSDGKWYRAKLLSILEFNPVKILVRHVDYGSTAALPTSRLRQIPAELMQYPCQAIKVKLAGFKPPLN 80
                           90       100
                   ....*....|....*....|....*
gi 2065618660 1635 MNNLHQLVYCPEWSMEALWTMIDIV 1659
Cdd:cd20418     81 DSETERIPYCPEWSMKALWAMIDLL 105
Tudor_TDRD4_rpt2 cd20415
second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
799-893 5.90e-48

second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the second one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


:

Pssm-ID: 410486  Cd Length: 96  Bit Score: 166.07  E-value: 5.90e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  799 LIILTKKMFEVYTEKNV-RMEILCPVVGQACAAMFEDGGWYRCQINSLTGHREVDVKYVDFGNTARIPITAVRKIKGDFL 877
Cdd:cd20415      1 FLILTKKIQEFYKEGDDgGLEILCPVQGQACVALFEDGAWYRARIIGLPGHREVEVKYVDFGNTATVTIKHVRKIKDDFL 80
                           90
                   ....*....|....*.
gi 2065618660  878 TLPIQALQCRLADVEP 893
Cdd:cd20415     81 SLPEKARECRLAFIEP 96
Tudor_TDRD4_rpt3 cd20416
third Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
1048-1128 4.79e-40

third Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the third one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


:

Pssm-ID: 410487  Cd Length: 82  Bit Score: 143.01  E-value: 4.79e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1048 LQEKIKSEYSSSEAD-IEWEESMHCALLVFENKEWRRGKVTKVNLNKTAEVFCYDFGNKELVNICMLKKLKEDIQTIRPL 1126
Cdd:cd20416      1 LQEKMIAEYENSKPEpVKWENDMHCAVQIQDKKQWRRGQIIRVVSDTLVEVFLYDFGNKEVVNIDCLRKLEENLKTIGKL 80

                   ..
gi 2065618660 1127 AM 1128
Cdd:cd20416     81 AL 82
Tudor_TDRD4_rpt4 cd20417
fourth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
1309-1376 1.45e-38

fourth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the fourth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


:

Pssm-ID: 410488  Cd Length: 68  Bit Score: 138.34  E-value: 1.45e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2065618660 1309 YSKGEGCVVKGSDTLWYRGKILEVIGVCVKVYYVDNGYIETIPHVHVYPMVMYPEIPELCLPFQLYGV 1376
Cdd:cd20417      1 WKKGEGCVVRGSDTLWYRGKVLEVIGGMVRVQYVDQGYIEKIPQCHLYPMVLYPDIPQFCIPCQLYGT 68
Tudor_TDRD4_rpt1 cd20414
first Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
562-637 1.03e-34

first Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the first one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


:

Pssm-ID: 410485  Cd Length: 77  Bit Score: 127.71  E-value: 1.03e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2065618660  562 ELGERIIVKSNLFCTWCRGIITELVPSEE-NEEKPNGPTRYRITEVAVMQVFLLDIGHSEIFVVTGFNNLVKKLQDG 637
Cdd:cd20414      1 ELGERIAVKSKKNGMWCRGTITELIPLENkNKGKPCGPTRYKIHDVAVMQVFLLDYGHSEVFVVTGVGVLVVRPEDV 77
TUDOR super family cl26991
Tudor domain;
515-674 2.74e-06

Tudor domain;


The actual alignment was detected with superfamily member pfam00567:

Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 48.12  E-value: 2.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  515 VSVSHVINPCHFYIQKSSEKKKASLLASEATNFCNNvesQKIPIPALELGERIIVKSNLFCTWCRGIITELVPSEEneek 594
Cdd:pfam00567    5 VVVSHIESPSTFYIQPKSDSKKLEKLTEELQEYYAS---KPPESLPPAVGDGCVAAFSEDGKWYRAKITESLDDGL---- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  595 pngptryritevavMQVFLLDIGHSEIfvvtgfnnlVKklqdgidaysyVNDLSQCVRKLGPevkgvintTPPLAIKCSL 674
Cdd:pfam00567   78 --------------VEVLFIDYGNTET---------VP-----------LSDLRPLPPELES--------LPPQAIKCQL 115
RING_Ubox super family cl17238
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger ...
13-70 3.92e-06

RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type RING fingers are closely related to RING-HC fingers. In contrast, C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type RING fingers are more closely related to RING-H2 fingers. However, not all RING finger-containing proteins display regular RING finger features, and the RING finger family has turned out to be multifarious. The degenerate RING fingers of the Siz/PIAS RING (SP-RING) family proteins and sporulation protein RMD5, are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues. They bind only one Zn2+ ion. On the other hand, the RING fingers of the human APC11 and RBX1 proteins can bind a third Zn atom since they harbor four additional Zn ligands. U-box is a modified form of the RING finger domain that lacks metal chelating Cys and His residues. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms. RING finger/U-box-containing proteins are a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enable efficient transfer of ubiquitin from E2 to the substrates.


The actual alignment was detected with superfamily member cd16559:

Pssm-ID: 473075 [Multi-domain]  Cd Length: 56  Bit Score: 45.69  E-value: 3.92e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660   13 CPRCQTPFQLpesfsdaTEHLPRLLDCEHVFCDQCLLTIH--CTESNFIICPSCQVSTPV 70
Cdd:cd16559      4 CPTCGHSYNF-------TNKRPRILSCLHSVCEECLQILYesCPKYKFISCPTCKRETVL 56
CC_brat-like super family cl29238
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ...
222-295 4.56e-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.


The actual alignment was detected with superfamily member smart00502:

Pssm-ID: 475168  Cd Length: 127  Bit Score: 38.79  E-value: 4.56e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2065618660   222 IQRLEDSSSSIENNCNKIRKELHKEFEKIVRAVQNRKAILLKEIETISQHHLDGIANVRKILEEKTSVLDSAID 295
Cdd:smart00502   23 LKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQLESLTQKQEKLSHAIN 96
 
Name Accession Description Interval E-value
Tudor_TDRD4_rpt5 cd20418
fifth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
1555-1659 2.06e-65

fifth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the fifth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410489  Cd Length: 105  Bit Score: 216.51  E-value: 2.06e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1555 LTDFRSEMPCLAEYDDGRWYRAKVLSVDNLHPLKILVQHVDFGSSASLPESRLRQLPIGLMQYPARAIRVKLMGFKPPAS 1634
Cdd:cd20418      1 LTDFRPEMPCLAEYSDGKWYRAKLLSILEFNPVKILVRHVDYGSTAALPTSRLRQIPAELMQYPCQAIKVKLAGFKPPLN 80
                           90       100
                   ....*....|....*....|....*
gi 2065618660 1635 MNNLHQLVYCPEWSMEALWTMIDIV 1659
Cdd:cd20418     81 DSETERIPYCPEWSMKALWAMIDLL 105
Tudor_TDRD4_rpt2 cd20415
second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
799-893 5.90e-48

second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the second one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410486  Cd Length: 96  Bit Score: 166.07  E-value: 5.90e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  799 LIILTKKMFEVYTEKNV-RMEILCPVVGQACAAMFEDGGWYRCQINSLTGHREVDVKYVDFGNTARIPITAVRKIKGDFL 877
Cdd:cd20415      1 FLILTKKIQEFYKEGDDgGLEILCPVQGQACVALFEDGAWYRARIIGLPGHREVEVKYVDFGNTATVTIKHVRKIKDDFL 80
                           90
                   ....*....|....*.
gi 2065618660  878 TLPIQALQCRLADVEP 893
Cdd:cd20415     81 SLPEKARECRLAFIEP 96
Tudor_TDRD4_rpt3 cd20416
third Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
1048-1128 4.79e-40

third Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the third one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410487  Cd Length: 82  Bit Score: 143.01  E-value: 4.79e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1048 LQEKIKSEYSSSEAD-IEWEESMHCALLVFENKEWRRGKVTKVNLNKTAEVFCYDFGNKELVNICMLKKLKEDIQTIRPL 1126
Cdd:cd20416      1 LQEKMIAEYENSKPEpVKWENDMHCAVQIQDKKQWRRGQIIRVVSDTLVEVFLYDFGNKEVVNIDCLRKLEENLKTIGKL 80

                   ..
gi 2065618660 1127 AM 1128
Cdd:cd20416     81 AL 82
Tudor_TDRD4_rpt4 cd20417
fourth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
1309-1376 1.45e-38

fourth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the fourth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410488  Cd Length: 68  Bit Score: 138.34  E-value: 1.45e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2065618660 1309 YSKGEGCVVKGSDTLWYRGKILEVIGVCVKVYYVDNGYIETIPHVHVYPMVMYPEIPELCLPFQLYGV 1376
Cdd:cd20417      1 WKKGEGCVVRGSDTLWYRGKVLEVIGGMVRVQYVDQGYIEKIPQCHLYPMVLYPDIPQFCIPCQLYGT 68
Tudor_TDRD4_rpt1 cd20414
first Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
562-637 1.03e-34

first Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the first one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410485  Cd Length: 77  Bit Score: 127.71  E-value: 1.03e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2065618660  562 ELGERIIVKSNLFCTWCRGIITELVPSEE-NEEKPNGPTRYRITEVAVMQVFLLDIGHSEIFVVTGFNNLVKKLQDG 637
Cdd:cd20414      1 ELGERIAVKSKKNGMWCRGTITELIPLENkNKGKPCGPTRYKIHDVAVMQVFLLDYGHSEVFVVTGVGVLVVRPEDV 77
TUDOR pfam00567
Tudor domain;
774-890 3.37e-27

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 107.83  E-value: 3.37e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  774 ENIQVMITHVNDPSDFYIQL-ADTVKLIILTKKMFEVYTEKnvRMEILCPVVGQACAAMF-EDGGWYRCQINSLTGHREV 851
Cdd:pfam00567    1 STIDVVVSHIESPSTFYIQPkSDSKKLEKLTEELQEYYASK--PPESLPPAVGDGCVAAFsEDGKWYRAKITESLDDGLV 78
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2065618660  852 DVKYVDFGNTARIPITAVRKIKGDFLTLPIQALQCRLAD 890
Cdd:pfam00567   79 EVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQLAG 117
TUDOR pfam00567
Tudor domain;
1019-1133 1.42e-17

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 80.09  E-value: 1.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1019 KHVEVKITYVASPSSIFVQLLSSQSLVTDLQEKIKSEYSSSEADIEweESMH---CALLVFENKEWRRGKVTKVNLNKTA 1095
Cdd:pfam00567    1 STIDVVVSHIESPSTFYIQPKSDSKKLEKLTEELQEYYASKPPESL--PPAVgdgCVAAFSEDGKWYRAKITESLDDGLV 78
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2065618660 1096 EVFCYDFGNKELVNICMLKKLKEDIQTIRPLAMECSLS 1133
Cdd:pfam00567   79 EVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQLA 116
TUDOR pfam00567
Tudor domain;
1261-1375 5.94e-12

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 64.30  E-value: 5.94e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1261 NIFEVEVTGVGDDGVIYGIRKSLQEEFTMLTSAIQASFKiLPLLKPYCYSKGEGCVVK-GSDTLWYRGKILEVI-GVCVK 1338
Cdd:pfam00567    1 STIDVVVSHIESPSTFYIQPKSDSKKLEKLTEELQEYYA-SKPPESLPPAVGDGCVAAfSEDGKWYRAKITESLdDGLVE 79
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2065618660 1339 VYYVDNGYIETIPHVHVYPMVMYPE-IPELCLPFQLYG 1375
Cdd:pfam00567   80 VLFIDYGNTETVPLSDLRPLPPELEsLPPQAIKCQLAG 117
TUDOR pfam00567
Tudor domain;
1494-1626 8.58e-11

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 60.83  E-value: 8.58e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1494 KVFPVTVKHLETPNWVYIcidqrRDSESDSDMDRglkyepeddnLDKALRDLNPSAERlPLLTDFRSEMPCLAEYDDGRW 1573
Cdd:pfam00567    1 STIDVVVSHIESPSTFYI-----QPKSDSKKLEK----------LTEELQEYYASKPP-ESLPPAVGDGCVAAFSEDGKW 64
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2065618660 1574 YRAKVLSVDNlhPLKILVQHVDFGSSASLPESRLRQLPIGLMQYPARAIRVKL 1626
Cdd:pfam00567   65 YRAKITESLD--DGLVEVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQL 115
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
822-876 1.20e-09

Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in the Drosophila Tudor protein. Initial proposal that the survival motor neuron gene product contain a Tudor domain are corroborated by more recent database search techniques such as PSI-BLAST (unpublished).


Pssm-ID: 197660  Cd Length: 57  Bit Score: 55.36  E-value: 1.20e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 2065618660   822 PVVGQACAAMFEDGGWYRCQINSLTGHREVDVKYVDFGNTARIPITAVRKIKGDF 876
Cdd:smart00333    3 FKVGDKVAARWEDGEWYRARIVKVDGEQLYEVFFIDYGNEEVVPPSDLRQLPEEL 57
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
1562-1611 1.39e-08

Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in the Drosophila Tudor protein. Initial proposal that the survival motor neuron gene product contain a Tudor domain are corroborated by more recent database search techniques such as PSI-BLAST (unpublished).


Pssm-ID: 197660  Cd Length: 57  Bit Score: 52.66  E-value: 1.39e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 2065618660  1562 MPCLAEYDDGRWYRAKVLSVDNLHplKILVQHVDFGSSASLPESRLRQLP 1611
Cdd:smart00333    7 DKVAARWEDGEWYRARIVKVDGEQ--LYEVFFIDYGNEEVVPPSDLRQLP 54
TUDOR pfam00567
Tudor domain;
515-674 2.74e-06

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 48.12  E-value: 2.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  515 VSVSHVINPCHFYIQKSSEKKKASLLASEATNFCNNvesQKIPIPALELGERIIVKSNLFCTWCRGIITELVPSEEneek 594
Cdd:pfam00567    5 VVVSHIESPSTFYIQPKSDSKKLEKLTEELQEYYAS---KPPESLPPAVGDGCVAAFSEDGKWYRAKITESLDDGL---- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  595 pngptryritevavMQVFLLDIGHSEIfvvtgfnnlVKklqdgidaysyVNDLSQCVRKLGPevkgvintTPPLAIKCSL 674
Cdd:pfam00567   78 --------------VEVLFIDYGNTET---------VP-----------LSDLRPLPPELES--------LPPQAIKCQL 115
RING-HC_RNF208 cd16559
RING finger, HC subclass, found in RING finger protein 208 (RNF208) and similar proteins; ...
13-70 3.92e-06

RING finger, HC subclass, found in RING finger protein 208 (RNF208) and similar proteins; RNF208 is an E3 ubiquitin-protein ligase whose activity can be modulated by S-nitrosylation. It contains a C3HC4-type RING-HC finger.


Pssm-ID: 438221 [Multi-domain]  Cd Length: 56  Bit Score: 45.69  E-value: 3.92e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660   13 CPRCQTPFQLpesfsdaTEHLPRLLDCEHVFCDQCLLTIH--CTESNFIICPSCQVSTPV 70
Cdd:cd16559      4 CPTCGHSYNF-------TNKRPRILSCLHSVCEECLQILYesCPKYKFISCPTCKRETVL 56
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
13-64 5.55e-04

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 39.03  E-value: 5.55e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 2065618660    13 CPRCQTPFqlpesfsdatEHLPRLLDCEHVFCDQCLLTihCTESNFIICPSC 64
Cdd:smart00184    1 CPICLEEY----------LKDPVILPCGHTFCRSCIRK--WLESGNNTCPIC 40
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
1307-1358 1.03e-03

Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in the Drosophila Tudor protein. Initial proposal that the survival motor neuron gene product contain a Tudor domain are corroborated by more recent database search techniques such as PSI-BLAST (unpublished).


Pssm-ID: 197660  Cd Length: 57  Bit Score: 38.79  E-value: 1.03e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2065618660  1307 YCYSKGEGCVVKGSDTLWYRGKILEVIGV-CVKVYYVDNGYIETIPHVHVYPM 1358
Cdd:smart00333    1 PTFKVGDKVAARWEDGEWYRARIVKVDGEqLYEVFFIDYGNEEVVPPSDLRQL 53
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
1075-1120 1.03e-03

Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in the Drosophila Tudor protein. Initial proposal that the survival motor neuron gene product contain a Tudor domain are corroborated by more recent database search techniques such as PSI-BLAST (unpublished).


Pssm-ID: 197660  Cd Length: 57  Bit Score: 38.79  E-value: 1.03e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 2065618660  1075 VFENKEWRRGKVTKVNLNKTAEVFCYDFGNKELVNICMLKKLKEDI 1120
Cdd:smart00333   12 RWEDGEWYRARIVKVDGEQLYEVFFIDYGNEEVVPPSDLRQLPEEL 57
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
222-295 4.56e-03

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


Pssm-ID: 128778  Cd Length: 127  Bit Score: 38.79  E-value: 4.56e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2065618660   222 IQRLEDSSSSIENNCNKIRKELHKEFEKIVRAVQNRKAILLKEIETISQHHLDGIANVRKILEEKTSVLDSAID 295
Cdd:smart00502   23 LKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQLESLTQKQEKLSHAIN 96
zf-RING_UBOX pfam13445
RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.
13-62 5.30e-03

RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.


Pssm-ID: 463881 [Multi-domain]  Cd Length: 38  Bit Score: 36.22  E-value: 5.30e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2065618660   13 CPRCQTPFQLPesfsdatehlprLLDCEHVFCDQCLLTIHCTESNFIICP 62
Cdd:pfam13445    1 CPICLELFTDP------------VLPCGHTFCRECLEEMSQKKGGKFKCP 38
 
Name Accession Description Interval E-value
Tudor_TDRD4_rpt5 cd20418
fifth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
1555-1659 2.06e-65

fifth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the fifth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410489  Cd Length: 105  Bit Score: 216.51  E-value: 2.06e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1555 LTDFRSEMPCLAEYDDGRWYRAKVLSVDNLHPLKILVQHVDFGSSASLPESRLRQLPIGLMQYPARAIRVKLMGFKPPAS 1634
Cdd:cd20418      1 LTDFRPEMPCLAEYSDGKWYRAKLLSILEFNPVKILVRHVDYGSTAALPTSRLRQIPAELMQYPCQAIKVKLAGFKPPLN 80
                           90       100
                   ....*....|....*....|....*
gi 2065618660 1635 MNNLHQLVYCPEWSMEALWTMIDIV 1659
Cdd:cd20418     81 DSETERIPYCPEWSMKALWAMIDLL 105
Tudor_TDRD4_rpt2 cd20415
second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
799-893 5.90e-48

second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the second one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410486  Cd Length: 96  Bit Score: 166.07  E-value: 5.90e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  799 LIILTKKMFEVYTEKNV-RMEILCPVVGQACAAMFEDGGWYRCQINSLTGHREVDVKYVDFGNTARIPITAVRKIKGDFL 877
Cdd:cd20415      1 FLILTKKIQEFYKEGDDgGLEILCPVQGQACVALFEDGAWYRARIIGLPGHREVEVKYVDFGNTATVTIKHVRKIKDDFL 80
                           90
                   ....*....|....*.
gi 2065618660  878 TLPIQALQCRLADVEP 893
Cdd:cd20415     81 SLPEKARECRLAFIEP 96
Tudor_TDRD4_rpt3 cd20416
third Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
1048-1128 4.79e-40

third Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the third one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410487  Cd Length: 82  Bit Score: 143.01  E-value: 4.79e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1048 LQEKIKSEYSSSEAD-IEWEESMHCALLVFENKEWRRGKVTKVNLNKTAEVFCYDFGNKELVNICMLKKLKEDIQTIRPL 1126
Cdd:cd20416      1 LQEKMIAEYENSKPEpVKWENDMHCAVQIQDKKQWRRGQIIRVVSDTLVEVFLYDFGNKEVVNIDCLRKLEENLKTIGKL 80

                   ..
gi 2065618660 1127 AM 1128
Cdd:cd20416     81 AL 82
Tudor_TDRD4_rpt4 cd20417
fourth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
1309-1376 1.45e-38

fourth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the fourth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410488  Cd Length: 68  Bit Score: 138.34  E-value: 1.45e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2065618660 1309 YSKGEGCVVKGSDTLWYRGKILEVIGVCVKVYYVDNGYIETIPHVHVYPMVMYPEIPELCLPFQLYGV 1376
Cdd:cd20417      1 WKKGEGCVVRGSDTLWYRGKVLEVIGGMVRVQYVDQGYIEKIPQCHLYPMVLYPDIPQFCIPCQLYGT 68
Tudor_TDRD4_rpt1 cd20414
first Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
562-637 1.03e-34

first Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the first one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410485  Cd Length: 77  Bit Score: 127.71  E-value: 1.03e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2065618660  562 ELGERIIVKSNLFCTWCRGIITELVPSEE-NEEKPNGPTRYRITEVAVMQVFLLDIGHSEIFVVTGFNNLVKKLQDG 637
Cdd:cd20414      1 ELGERIAVKSKKNGMWCRGTITELIPLENkNKGKPCGPTRYKIHDVAVMQVFLLDYGHSEVFVVTGVGVLVVRPEDV 77
TUDOR pfam00567
Tudor domain;
774-890 3.37e-27

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 107.83  E-value: 3.37e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  774 ENIQVMITHVNDPSDFYIQL-ADTVKLIILTKKMFEVYTEKnvRMEILCPVVGQACAAMF-EDGGWYRCQINSLTGHREV 851
Cdd:pfam00567    1 STIDVVVSHIESPSTFYIQPkSDSKKLEKLTEELQEYYASK--PPESLPPAVGDGCVAAFsEDGKWYRAKITESLDDGLV 78
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2065618660  852 DVKYVDFGNTARIPITAVRKIKGDFLTLPIQALQCRLAD 890
Cdd:pfam00567   79 EVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQLAG 117
TUDOR pfam00567
Tudor domain;
1019-1133 1.42e-17

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 80.09  E-value: 1.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1019 KHVEVKITYVASPSSIFVQLLSSQSLVTDLQEKIKSEYSSSEADIEweESMH---CALLVFENKEWRRGKVTKVNLNKTA 1095
Cdd:pfam00567    1 STIDVVVSHIESPSTFYIQPKSDSKKLEKLTEELQEYYASKPPESL--PPAVgdgCVAAFSEDGKWYRAKITESLDDGLV 78
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2065618660 1096 EVFCYDFGNKELVNICMLKKLKEDIQTIRPLAMECSLS 1133
Cdd:pfam00567   79 EVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQLA 116
Tudor_AKAP1 cd20407
Tudor domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; ...
822-893 2.79e-17

Tudor domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; AKAP1, also called A-kinase anchor protein 149 kDa (AKAP 149), dual specificity A-kinase-anchoring protein 1 (D-AKAP-1), protein kinase A-anchoring protein 1 (PRKA1), or Spermatid A-kinase anchor protein 84 (S-AKAP84), is found in mitochondria and in the endoplasmic reticulum-nuclear envelope, where it anchors protein kinases, phosphatases, and a phosphodiesterase. It regulates multiple cellular processes governing mitochondrial homeostasis and cell viability. AKAP1 binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane. It contains a C-terminal Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410478  Cd Length: 76  Bit Score: 78.02  E-value: 2.79e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2065618660  822 PVVGQACAAMFEdGGWYRCQINSLTGHR-EVDVKYVDFGNTARIPITAVRKIKGDFLTLPIQALQCRLADVEP 893
Cdd:cd20407      5 IEVGVICAAPVM-NAWYRAQVVGVFEETdEVEIKYLDYGGYERVPVDDLRQIRSDFMTLPFQATECYLANIEP 76
Tudor_TDRD1_rpt1 cd20408
first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
778-902 1.18e-16

first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four Tudor domains. This model corresponds to the first one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410479  Cd Length: 130  Bit Score: 78.18  E-value: 1.18e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  778 VMITHVNDPSDFYIQLADTV---KLIILTKKMFEVYTEKNVRMEILcPVVGQACAAMF-EDGGWYRCQINSLTGHRE-VD 852
Cdd:cd20408      1 GTVTEFKNPGEFYIQIYTLEvleSLVKLTSQLKKTYASVNNHKEYI-PEVGEVCVAKYsEDQNWYRALVQTVDVQQKkAG 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2065618660  853 VKYVDFGNTARIPITAVRKIKGDFLTLPIQALQCRLADVEPTNrtEGWDD 902
Cdd:cd20408     80 VFYIDYGNEETVPLNRIQPLKKDIELFPPCAIKCCLANVKPPS--GSWSE 127
Tudor_TDRD2 cd20412
Tudor domain found in Tudor domain-containing protein 2 (TDRD2) and similar proteins; TDRD2, ...
802-886 1.90e-16

Tudor domain found in Tudor domain-containing protein 2 (TDRD2) and similar proteins; TDRD2, also called Tudor and KH domain-containing protein (TDRKH), participates in the primary piwi-interacting RNA (piRNA) biogenesis pathway and is required during spermatogenesis to repress transposable elements and prevent their mobilization, which is essential for germline integrity. The family also includes the TDRD2 homolog found in Drosophila melanogaster (dTDRKH), which is also called partner of PIWIs protein, or PAPI, and is involved in Zucchini-mediated piRNA 3'-end maturation. TDRD2 contains two KH domains and one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410483  Cd Length: 95  Bit Score: 76.18  E-value: 1.90e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  802 LTKKMFEVYTEKNVRMEILCPVVGQACAAMFE-DGGWYRCQINSLTGHREVDVKYVDFGNTARIPITAVRKIKGDFLTLP 880
Cdd:cd20412      9 LVQEMTQYYESEENRHTLLTVQVGDIVAAPFRhDGSWYRARVLGFLENGNLDLYFVDYGDSGYVPLEDLRALRSDFLSLP 88

                   ....*.
gi 2065618660  881 IQALQC 886
Cdd:cd20412     89 FQAIEC 94
Tudor_TDRD15_rpt4 cd20439
fourth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
776-888 2.68e-16

fourth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the fourth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410510  Cd Length: 125  Bit Score: 76.76  E-value: 2.68e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  776 IQVMITHVNDPSDFYIQL-ADTVKLIILTKKMFEVYTEKNVRMEIlcpvvGQ-ACAAMF-EDGGWYRCQINSLTGHREVD 852
Cdd:cd20439     12 VDVKCSYVNSPGDFWCQLqTKSSELKSLMKQIQSYYLIHNDPYKH-----GQiACVAKYsKDGKWYRAAVLKQVSAKEVD 86
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2065618660  853 VKYVDFGNTARIPITAVRKIKGDFLTLPIQALQCRL 888
Cdd:cd20439     87 VIFVDYGNQERVLISDLRAIKPQFLLLEGQAFRCSL 122
Tudor_TDRD15_rpt2 cd20437
second Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
777-890 1.38e-15

second Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the second one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410508  Cd Length: 120  Bit Score: 74.76  E-value: 1.38e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  777 QVMITHVNDPSDFYIQLADTVK-LIILTKKMFEVYTEKNVRMEILCPVVGQACAAMFEDGGWYRCQINSLTGHREVDVKY 855
Cdd:cd20437      6 KVKITAAVSPSKFYCQLLSWEPeLSKLTTQMTLHYESVSKELNPSCENFGLLCAAKGKDGQWHRGFLQQLLPPSQVKVWF 85
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2065618660  856 VDFGNTARIPITAVRKIKGDFLTLPIQALQCRLAD 890
Cdd:cd20437     86 IDYGNSEAVSSHSVLKLPPDFFSLPLMSFPCSLSC 120
Tudor_TDRD6_rpt7 cd20426
seventh Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
776-911 1.08e-14

seventh Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the seventh one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410497  Cd Length: 140  Bit Score: 72.92  E-value: 1.08e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  776 IQVMITHVNDPSDFYIQLAdTVKLIILTKKMFEV-YTEKNVRMEILCPVVGQACAAMF-EDGGWYRCQINSLTGHReVDV 853
Cdd:cd20426      1 IEAYATAVDSPEYFWCQFA-TEKIQCLAVKVQEAgEQVADRGNFIPSIYVGDPCIVKYsEDNHWYRALVTKINDNL-VSV 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2065618660  854 KYVDFGNTARIPITAVRKIKGDFLTLPIQALQCRLADVeptNRTEG-WDDFAKERLKEL 911
Cdd:cd20426     79 RFVDYGNEEDVVREQVRALPSELLKIPVQAFPCCLSGF---NLSEGlWSDEANDYFYEI 134
Tudor_TDRD6_rpt3 cd20422
third Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
778-893 1.46e-14

third Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the third one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410493  Cd Length: 135  Bit Score: 72.16  E-value: 1.46e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  778 VMITHVNDPSDFYIQLAD-TVKLIILTKKMFEVYTEKNvRME--ILCPVVGQACAAMFEDGGWYRCQINSLTGhREVDVK 854
Cdd:cd20422      4 AQVEFVKDPSEFWIRLGEhAVPFSKLMRSMTAFYSQAS-KLDgvVLKPQPGQLCCAKWKEDRYYRAIVTAVKG-KMVEVF 81
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2065618660  855 YVDFGNTARIPITAVRKIKGDFLTLPIQALQCRLADVEP 893
Cdd:cd20422     82 LVDRGNTEMVDWYDVKKLLPQFRELPALALKCCLADICP 120
Tudor_TDRD6_rpt6 cd20425
sixth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
777-888 1.74e-14

sixth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the sixth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410496  Cd Length: 115  Bit Score: 71.33  E-value: 1.74e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  777 QVMITHVNDPSDFYIQLA-DTVKLIILTKKMFEVYTEKNvrmEILCPVVGQA---CAAMFEDGGWYRCQINSLTGHREVD 852
Cdd:cd20425      3 EVYVSHVNSPSDFYVQLAqDEDELSMISEKLNASKANDE---EVECESLQLGdliCAEYPEDGLWYRAVVKEKIPNNLVS 79
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2065618660  853 VKYVDFGNTARIPITAVRKIKGDFLTLPIQALQCRL 888
Cdd:cd20425     80 VQFIDYGNTSVVQPSKIHRLPKELLSIPALSIHCFL 115
Tudor_TDRD7_rpt1 cd20427
first Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; ...
805-893 6.67e-14

first Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; TDRD7, also called PCTAIRE2-binding protein, or Tudor repeat associator with PCTAIRE-2 (Trap), is a component of specific cytoplasmic RNA granules involved in post-transcriptional regulation of specific genes: probably acts by binding to specific mRNAs and regulating their translation. It is required for lens transparency during lens development, by regulating translation of genes such as CRYBB3 and HSPB1 in the developing lens. It is also essential for dynamic ribonucleoprotein (RNP) remodeling of chromatoid bodies during spermatogenesis. TDRD7 contains three Tudor domains. The model corresponds to the first one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410498  Cd Length: 98  Bit Score: 68.99  E-value: 6.67e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  805 KMFEVYTEKNVRMEILCPVVGQACAAMFEDGGWYRCQINSLTGHReVDVKYVDFGNTARIPITAVRKIKGDFLTLPIQAL 884
Cdd:cd20427      6 EMKEFYSKSSTAMCLRSPSVGQLVAVKAEEDAWLRAQVIEVEEDK-VKVYYVDHGFSEVVERSKLFKLNKQFYSLPFQAT 84

                   ....*....
gi 2065618660  885 QCRLADVEP 893
Cdd:cd20427     85 KCKLAGLEP 93
Tudor_TDRD1_rpt1 cd20408
first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
1030-1141 3.12e-13

first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four Tudor domains. This model corresponds to the first one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410479  Cd Length: 130  Bit Score: 68.17  E-value: 3.12e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1030 SPSSIFVQLLSSQSL--VTDLQEKIKSEYSSSEADIEW--EESMHCALLVFENKEWRRGKVTKVN-LNKTAEVFCYDFGN 1104
Cdd:cd20408      8 NPGEFYIQIYTLEVLesLVKLTSQLKKTYASVNNHKEYipEVGEVCVAKYSEDQNWYRALVQTVDvQQKKAGVFYIDYGN 87
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2065618660 1105 KELVNICMLKKLKEDIQTIRPLAMECSLSEIKPAGGS 1141
Cdd:cd20408     88 EETVPLNRIQPLKKDIELFPPCAIKCCLANVKPPSGS 124
Tudor_TDRD6_rpt5 cd20424
fifth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
777-888 2.22e-12

fifth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the fifth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410495  Cd Length: 126  Bit Score: 65.60  E-value: 2.22e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  777 QVMITHVNDPSDFYIQLADTVKLIILTKKMFEVYTEKNVRMEilCPVV-GQACAAMFEDGGWYRCQINSLTghREVDVKY 855
Cdd:cd20424     15 EVYITYVNDPWTFYCQLARNAGVLDQLASAISRLSSEIRKLE--LSVNpGTLCLAKYSDQHWYRGIIITNK--NSTEVFF 90
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2065618660  856 VDFGNTARIPITAVRKIKGD---FLTLPIQALQCRL 888
Cdd:cd20424     91 VDYGNTEKVEKEDMLPIPSDayeLLLLPMQAIKCSL 126
Tudor_TDRD15_rpt5 cd20440
fifth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
777-888 3.98e-12

fifth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the fifth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410511  Cd Length: 127  Bit Score: 64.78  E-value: 3.98e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  777 QVMITHVNDPSDFYIQLA-DTVKLIILTKKMFEVytEKNVRMEILCPVVGQAC-AAMFEDGGWYRCQINSLTGHREVDVK 854
Cdd:cd20440     13 EVYITHVYSPAKFYCQLDrNTEILEALMEKIAEI--SKLFNSQILDNCKTRLClAKYFEDGQWYRALAHPVESSSHLSVY 90
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2065618660  855 YVDFGNTARIPITAVRKIKG---DFLTLPIQALQCRL 888
Cdd:cd20440     91 FVDYGNKQIVEKNEVLPIPDtavDLLLTPMQAIKCCL 127
TUDOR pfam00567
Tudor domain;
1261-1375 5.94e-12

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 64.30  E-value: 5.94e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1261 NIFEVEVTGVGDDGVIYGIRKSLQEEFTMLTSAIQASFKiLPLLKPYCYSKGEGCVVK-GSDTLWYRGKILEVI-GVCVK 1338
Cdd:pfam00567    1 STIDVVVSHIESPSTFYIQPKSDSKKLEKLTEELQEYYA-SKPPESLPPAVGDGCVAAfSEDGKWYRAKITESLdDGLVE 79
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2065618660 1339 VYYVDNGYIETIPHVHVYPMVMYPE-IPELCLPFQLYG 1375
Cdd:pfam00567   80 VLFIDYGNTETVPLSDLRPLPPELEsLPPQAIKCQLAG 117
Tudor_TDRD1_rpt3 cd20410
third Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
822-877 1.47e-11

third Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four Tudor domains. This model corresponds to the third one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410481 [Multi-domain]  Cd Length: 59  Bit Score: 61.20  E-value: 1.47e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2065618660  822 PVVGQACAAMF-EDGGWYRCQINSLTGHREVDVKYVDFGNTARIPITAVRKIKGDFL 877
Cdd:cd20410      3 PIVGEPCCAFFsGDGNWYRAMVKEILPGGAVKVHFVDYGNVEEVTLDKLRKITSTFL 59
Tudor_TDRD1_rpt4 cd20411
fourth Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
778-889 2.47e-11

fourth Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four Tudor domains. This model corresponds to the fourth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410482  Cd Length: 116  Bit Score: 62.46  E-value: 2.47e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  778 VMITHVNDPSDFYI----QLADTVKLIILTKKMFEvYTEKNVRMEILCPVVGQACAAMFE-DGGWYRCQINSlTGHREVD 852
Cdd:cd20411      1 ALVLEVISPDLFYAlpktGQVNVEKLKALMTELAE-YCSKQSVPQQFRPRIGDACCARFTgDKNWYRAVVLE-TSDSEVK 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2065618660  853 VKYVDFGNTARIPITAVRKIKGDFLTLPIQALQCRLA 889
Cdd:cd20411     79 VLYADYGNTETLPLSRILPITKSHLELPFQIIRCSLA 115
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
824-872 2.60e-11

Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar proteins; dTUD is required during oogenesis for the formation of primordial germ cells and for normal abdominal segmentation. It contains 11 Tudor domains. The family also includes mitochondrial A-kinase anchor protein 1 (AKAP1) and Tudor domain-containing proteins (TDRDs). AKAP1, also called A-kinase anchor protein 149 kDa (AKAP 149), or dual specificity A-kinase-anchoring protein 1 (D-AKAP-1), or protein kinase A-anchoring protein 1 (PRKA1), or Spermatid A-kinase anchor protein 84 (S-AKAP84), is found in mitochondria and in the endoplasmic reticulum-nuclear envelope where it anchors protein kinases, phosphatases, and a phosphodiesterase. It regulates multiple cellular processes governing mitochondrial homeostasis and cell viability. AKAP1 binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane. TDRDs have diverse biological functions and may contain one or more copies of the Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410450  Cd Length: 50  Bit Score: 59.84  E-value: 2.60e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2065618660  824 VGQACAAMFE-DGGWYRCQINSLTGHREVDVKYVDFGNTARIPITAVRKI 872
Cdd:cd20379      1 VGDLCAAKYEeDGKWYRARVLEVLSNDKVEVFFVDYGNTETVPLSDLRPL 50
Tudor_TDRD5 cd20419
Tudor domain found in Tudor domain-containing protein 5 (TDRD5) and similar proteins; TDRD5 is ...
780-888 4.35e-11

Tudor domain found in Tudor domain-containing protein 5 (TDRD5) and similar proteins; TDRD5 is an RNA-binding protein directly associated with piRNA precursors. It is required for retrotransposon silencing, chromatoid body assembly, and spermiogenesis. TDRD5 participates in the repression of transposable elements and prevents their mobilization, which is essential for germline integrity. TDRD5 contains three LOTUS domains and one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410490  Cd Length: 118  Bit Score: 61.70  E-value: 4.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  780 ITHVNDPSDFYIQLA--DTV-KLIILTKKMFEVYTEKNVRMEILCP----VVGQACAAMF-EDGGWYRCQINSLTGHREV 851
Cdd:cd20419      2 VEYIESPSQFYVRFYskDTSeMLEDMMIEMRRCYSNEHVSERYVMPeafiQPGQVCCVRIpEDVWWYRVIIHQVLNKQEV 81
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2065618660  852 DVKYVDFGNTARIPITAVRKIKGDFLTLPIQALQCRL 888
Cdd:cd20419     82 EVFYPDFGDIGTVQKSRLRFLKCCYSKLPAQAIPASL 118
Tudor_TDRD15_rpt6 cd20441
sixth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
785-891 7.94e-11

sixth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the sixth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410512  Cd Length: 108  Bit Score: 60.52  E-value: 7.94e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  785 DPSDFYIQLADTVKLIIltkKMFEVYTEKNVRMEILC---PVVGQACAAMF-EDGGWYRCQINSLTGHREVDVKYVDFGN 860
Cdd:cd20441      1 SPSRFFIQLSEDEKVIL---QLAEELNETSEKSRENAavkLKVGDLVAAEYdEDLALYRAVITAVLPGKSFKVEFIDYGN 77
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2065618660  861 TARIPITAVRKIKGDFLTLPIQALQCRLADV 891
Cdd:cd20441     78 TAVVDKSNIYTLQEKFLSLPRLSIPCSLSGV 108
TUDOR pfam00567
Tudor domain;
1494-1626 8.58e-11

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 60.83  E-value: 8.58e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1494 KVFPVTVKHLETPNWVYIcidqrRDSESDSDMDRglkyepeddnLDKALRDLNPSAERlPLLTDFRSEMPCLAEYDDGRW 1573
Cdd:pfam00567    1 STIDVVVSHIESPSTFYI-----QPKSDSKKLEK----------LTEELQEYYASKPP-ESLPPAVGDGCVAAFSEDGKW 64
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2065618660 1574 YRAKVLSVDNlhPLKILVQHVDFGSSASLPESRLRQLPIGLMQYPARAIRVKL 1626
Cdd:pfam00567   65 YRAKITESLD--DGLVEVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQL 115
Tudor_TDRD6_rpt2 cd20421
second Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
778-888 6.31e-10

second Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the second one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410492  Cd Length: 130  Bit Score: 58.59  E-value: 6.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  778 VMITHVNDPSDFYIQL-ADTVKLIILTKKMFEVYTEKNV-RMEILCPVVGQACAAMFEDGGWYRCQI-NSLTGHREVDVK 854
Cdd:cd20421     15 VVVTEVTDPHRIFCQLrSLSQELKRLSESMHQYYEGRVGsGYETRPEKLGSPCAARGSDGRWYRAVLqQVFSANRVVEVL 94
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2065618660  855 YVDFGNTARIPITAVRKIKGDFLTLPIQALQCRL 888
Cdd:cd20421     95 HVDYGRKEVVSVSNLRYLAPEYFRMPVVTYPCAL 128
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
822-876 1.20e-09

Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in the Drosophila Tudor protein. Initial proposal that the survival motor neuron gene product contain a Tudor domain are corroborated by more recent database search techniques such as PSI-BLAST (unpublished).


Pssm-ID: 197660  Cd Length: 57  Bit Score: 55.36  E-value: 1.20e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 2065618660   822 PVVGQACAAMFEDGGWYRCQINSLTGHREVDVKYVDFGNTARIPITAVRKIKGDF 876
Cdd:smart00333    3 FKVGDKVAARWEDGEWYRARIVKVDGEQLYEVFFIDYGNEEVVPPSDLRQLPEEL 57
Tudor_TDRD11 cd20433
Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, ...
1536-1615 1.60e-09

Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, also called Staphylococcal nuclease domain-containing protein 1 (SND1), 100 kDa coactivator, EBNA2 coactivator p100, or p100 co-activator, is a multifunctional protein that is reportedly associated with different types of RNA molecules, including mRNA, miRNA, pre-miRNA, and dsRNA. It has been implicated in a number of biological processes in eukaryotic cells, including the cell cycle, DNA damage repair, proliferation, and apoptosis. TDRD11 is overexpressed in multiple cancers and functions as an oncogene. It contains multiple Staphylococcal nuclease (SN) domains and a C-terminal Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410504 [Multi-domain]  Cd Length: 84  Bit Score: 56.15  E-value: 1.60e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1536 DNLDKALRDLNPSAERLPLLT---DFRSEMPCLAEY-DDGRWYRAKVLSVDNlhPLKILVQHVDFGSSASLPESRLRQLP 1611
Cdd:cd20433      3 PQLEKLMEKLRFEIASNPPLPgsyTPRKGDLCAAKFvEDGEWYRAKVEKVEG--DKKVHVLYIDYGNREVLPSTRLAALP 80

                   ....
gi 2065618660 1612 IGLM 1615
Cdd:cd20433     81 PAFS 84
Tudor_TDRD4_rpt5 cd20418
fifth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
828-908 3.04e-09

fifth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the fifth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410489  Cd Length: 105  Bit Score: 55.88  E-value: 3.04e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  828 CAAMFEDGGWYRCQINSLTGHREVD--VKYVDFGNTARIPITAVRKIKGDFLTLPIQALQCRLADVEPTNRtegwdDFAK 905
Cdd:cd20418     10 CLAEYSDGKWYRAKLLSILEFNPVKilVRHVDYGSTAALPTSRLRQIPAELMQYPCQAIKVKLAGFKPPLN-----DSET 84

                   ...
gi 2065618660  906 ERL 908
Cdd:cd20418     85 ERI 87
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
1069-1116 6.93e-09

Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar proteins; dTUD is required during oogenesis for the formation of primordial germ cells and for normal abdominal segmentation. It contains 11 Tudor domains. The family also includes mitochondrial A-kinase anchor protein 1 (AKAP1) and Tudor domain-containing proteins (TDRDs). AKAP1, also called A-kinase anchor protein 149 kDa (AKAP 149), or dual specificity A-kinase-anchoring protein 1 (D-AKAP-1), or protein kinase A-anchoring protein 1 (PRKA1), or Spermatid A-kinase anchor protein 84 (S-AKAP84), is found in mitochondria and in the endoplasmic reticulum-nuclear envelope where it anchors protein kinases, phosphatases, and a phosphodiesterase. It regulates multiple cellular processes governing mitochondrial homeostasis and cell viability. AKAP1 binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane. TDRDs have diverse biological functions and may contain one or more copies of the Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410450  Cd Length: 50  Bit Score: 53.29  E-value: 6.93e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2065618660 1069 MHCALLVFENKEWRRGKVTKVNLNKTAEVFCYDFGNKELVNICMLKKL 1116
Cdd:cd20379      3 DLCAAKYEEDGKWYRARVLEVLSNDKVEVFFVDYGNTETVPLSDLRPL 50
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
1562-1611 1.39e-08

Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in the Drosophila Tudor protein. Initial proposal that the survival motor neuron gene product contain a Tudor domain are corroborated by more recent database search techniques such as PSI-BLAST (unpublished).


Pssm-ID: 197660  Cd Length: 57  Bit Score: 52.66  E-value: 1.39e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 2065618660  1562 MPCLAEYDDGRWYRAKVLSVDNLHplKILVQHVDFGSSASLPESRLRQLP 1611
Cdd:smart00333    7 DKVAARWEDGEWYRARIVKVDGEQ--LYEVFFIDYGNEEVVPPSDLRQLP 54
Tudor_TDRD15_rpt3 cd20438
third Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
780-906 1.44e-08

third Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the third one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410509  Cd Length: 141  Bit Score: 55.17  E-value: 1.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  780 ITHVNDPSDFYIQLAD-TVKLIILTKKMFEVYTEKNVRMEIL-CPVVGQACAAMF-EDGGWYRCQINSLTGHrEVDVKYV 856
Cdd:cd20438     11 VEYVLNPSNFWIRTDEyNNEFQALMKNIADIYNLCGNDEELLkKPEPGLLCCARYsKDRHYYRAVITEVLDL-KVSVYFL 89
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2065618660  857 DFGNTARIPITAVRKIKGDFLTLPIQALQCRLADVEPTNR--TEGWDDFAKE 906
Cdd:cd20438     90 DFGNTDTVPFYDVKTLLPEFSELPALAMCCSLAHVFPVEEvwTKNANDFFKK 141
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
785-900 1.98e-08

second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; TDRD12, also called ES cell-associated transcript 8 protein (ECAT8), is a putative ATP-dependent DEAD-like RNA helicase that is essential for germ cell development and maintenance. It acts as a unique piRNA biogenesis factor essential for secondary PIWI interacting RNA (piRNA) biogenesis. TDRD12 contains two Tudor domains, one at the N-terminus and the other at the C-terminal end. The model corresponds to the second/C-terminal one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410506  Cd Length: 134  Bit Score: 54.56  E-value: 1.98e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  785 DPSDFYIQL------------ADTVKLIILTKKMFEVYTEKNVRMEILCPVVGQACAAMFEDGGWYRCQI------NSLT 846
Cdd:cd20435      1 DATHYSARIlehrssdgevtkSMSSTYLKLSMKLNMYYSDPSNRILHGKVKVGDLCAVEDENNLYHRVKVleitekDDKT 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2065618660  847 GHREVDVKYVDFGNTARIPITAVRKIKGDFLTLPIQALQCRLADVEPTNRTEGW 900
Cdd:cd20435     81 KPREVLVKFIDEGRVETVVVSQLLELPEELKSLPPQAVEVFLCNVKPVDNDTEW 134
Tudor_TDRD7_rpt2 cd20428
second Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; ...
822-895 2.22e-08

second Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; TDRD7, also called PCTAIRE2-binding protein, or Tudor repeat associator with PCTAIRE-2 (Trap), is a component of specific cytoplasmic RNA granules involved in post-transcriptional regulation of specific genes: probably acts by binding to specific mRNAs and regulating their translation. It is required for lens transparency during lens development, by regulating translation of genes such as CRYBB3 and HSPB1 in the developing lens. It is also essential for dynamic ribonucleoprotein (RNP) remodeling of chromatoid bodies during spermatogenesis. TDRD7 contains three Tudor domains. The model corresponds to the second one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410499  Cd Length: 140  Bit Score: 54.76  E-value: 2.22e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2065618660  822 PVVGQACAAMFEdGGWYRCQINSLTGHREVDVKYVDFGNTARIPITAVRKIKGDFL----TLPIQALQCRLADVEPTN 895
Cdd:cd20428     52 PFCGKICLARYK-GKWARVEITNVHSSRALDVHFLDTGTVASVKVSELREIPPPFLreliSIPPQALKCCLADLPLNI 128
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
1562-1610 2.68e-08

Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar proteins; dTUD is required during oogenesis for the formation of primordial germ cells and for normal abdominal segmentation. It contains 11 Tudor domains. The family also includes mitochondrial A-kinase anchor protein 1 (AKAP1) and Tudor domain-containing proteins (TDRDs). AKAP1, also called A-kinase anchor protein 149 kDa (AKAP 149), or dual specificity A-kinase-anchoring protein 1 (D-AKAP-1), or protein kinase A-anchoring protein 1 (PRKA1), or Spermatid A-kinase anchor protein 84 (S-AKAP84), is found in mitochondria and in the endoplasmic reticulum-nuclear envelope where it anchors protein kinases, phosphatases, and a phosphodiesterase. It regulates multiple cellular processes governing mitochondrial homeostasis and cell viability. AKAP1 binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane. TDRDs have diverse biological functions and may contain one or more copies of the Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410450  Cd Length: 50  Bit Score: 51.36  E-value: 2.68e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1562 MPCLAEY-DDGRWYRAKVLSVDNlhPLKILVQHVDFGSSASLPESRLRQL 1610
Cdd:cd20379      3 DLCAAKYeEDGKWYRARVLEVLS--NDKVEVFFVDYGNTETVPLSDLRPL 50
Tudor_TDRD1_rpt1 cd20408
first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
1285-1388 2.71e-08

first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four Tudor domains. This model corresponds to the first one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410479  Cd Length: 130  Bit Score: 53.91  E-value: 2.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1285 EEFTMLTSAIQASFKILPLLKPYCYSKGEGCVVKGS-DTLWYRGKILEVIGV--CVKVYYVDNGYIETIPHVHVYPM-VM 1360
Cdd:cd20408     23 ESLVKLTSQLKKTYASVNNHKEYIPEVGEVCVAKYSeDQNWYRALVQTVDVQqkKAGVFYIDYGNEETVPLNRIQPLkKD 102
                           90       100
                   ....*....|....*....|....*...
gi 2065618660 1361 YPEIPELCLPFQLYGVEPVGNKWQEDAV 1388
Cdd:cd20408    103 IELFPPCAIKCCLANVKPPSGSWSEECI 130
Tudor_TDRD4_rpt2 cd20415
second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
1550-1631 2.88e-08

second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the second one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410486  Cd Length: 96  Bit Score: 52.82  E-value: 2.88e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1550 ERLPLLTDFRSEMpCLAEYDDGRWYRAKVLSVDNlHPlKILVQHVDFGSSASLPESRLRQLPIGLMQYPARAIRVKLMGF 1629
Cdd:cd20415     18 GGLEILCPVQGQA-CVALFEDGAWYRARIIGLPG-HR-EVEVKYVDFGNTATVTIKHVRKIKDDFLSLPEKARECRLAFI 94

                   ..
gi 2065618660 1630 KP 1631
Cdd:cd20415     95 EP 96
Tudor_TDRD15_rpt2 cd20437
second Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
1021-1133 5.55e-08

second Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the second one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410508  Cd Length: 120  Bit Score: 52.81  E-value: 5.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1021 VEVKITYVASPSSIFVQLLSSQSlvtDLQEKIKSEYSSSEADIEWEESM--HCALLVF---ENKEWRRGKVTKVNLNKTA 1095
Cdd:cd20437      5 EKVKITAAVSPSKFYCQLLSWEP---ELSKLTTQMTLHYESVSKELNPSceNFGLLCAakgKDGQWHRGFLQQLLPPSQV 81
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2065618660 1096 EVFCYDFGNKELVNICMLKKLKEDIQTIRPLAMECSLS 1133
Cdd:cd20437     82 KVWFIDYGNSEAVSSHSVLKLPPDFFSLPLMSFPCSLS 119
Tudor_TDRD11 cd20433
Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, ...
825-876 5.70e-08

Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, also called Staphylococcal nuclease domain-containing protein 1 (SND1), 100 kDa coactivator, EBNA2 coactivator p100, or p100 co-activator, is a multifunctional protein that is reportedly associated with different types of RNA molecules, including mRNA, miRNA, pre-miRNA, and dsRNA. It has been implicated in a number of biological processes in eukaryotic cells, including the cell cycle, DNA damage repair, proliferation, and apoptosis. TDRD11 is overexpressed in multiple cancers and functions as an oncogene. It contains multiple Staphylococcal nuclease (SN) domains and a C-terminal Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410504 [Multi-domain]  Cd Length: 84  Bit Score: 51.53  E-value: 5.70e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2065618660  825 GQACAAMF-EDGGWYRCQINSLTGHREVDVKYVDFGNTARIPITAVRKIKGDF 876
Cdd:cd20433     31 GDLCAAKFvEDGEWYRAKVEKVEGDKKVHVLYIDYGNREVLPSTRLAALPPAF 83
Tudor_TDRD1_rpt1 cd20408
first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
515-690 9.90e-08

first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four Tudor domains. This model corresponds to the first one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410479  Cd Length: 130  Bit Score: 52.37  E-value: 9.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  515 VSVSHVINPCHFYIQKSSEKKKASL--LASEATNFCNNVESQKIPIPalELGERIIVKSNLFCTWCRGIITELVPSEENE 592
Cdd:cd20408      1 GTVTEFKNPGEFYIQIYTLEVLESLvkLTSQLKKTYASVNNHKEYIP--EVGEVCVAKYSEDQNWYRALVQTVDVQQKKA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  593 ekpngptryritevavmQVFLLDIGHSEIFVVtgfnNLVKKLQDGIDAYsyvndlsqcvrklgpevkgvinttPPLAIKC 672
Cdd:cd20408     79 -----------------GVFYIDYGNEETVPL----NRIQPLKKDIELF------------------------PPCAIKC 113
                          170
                   ....*....|....*...
gi 2065618660  673 SLKDIVPPNfkNRWSVEA 690
Cdd:cd20408    114 CLANVKPPS--GSWSEEC 129
Tudor_TDRD6_rpt4 cd20423
fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
827-895 1.27e-07

fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the fourth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410494  Cd Length: 80  Bit Score: 50.56  E-value: 1.27e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2065618660  827 ACAAMF-EDGGWYRCQINSLTGHRE-VDVKYVDFGNTARIPITAVRKIKGDFLTLPIQALQCRLADVEPTN 895
Cdd:cd20423      8 VCLAKYsEDGKWCRALIDNVYEPVEmVEVTYVDYGNKELVSLKNLRSISEEFLKLKAQAFRCSLYNLIQPS 78
Tudor_TDRD15_rpt2 cd20437
second Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
1264-1355 1.49e-07

second Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the second one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410508  Cd Length: 120  Bit Score: 51.65  E-value: 1.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1264 EVEVTGVGDDGVIYGIRKSLQEEFTMLTSAIQASFK-ILPLLKPYCYSKGEGCVVKGSDTLWYRGKILEV-IGVCVKVYY 1341
Cdd:cd20437      6 KVKITAAVSPSKFYCQLLSWEPELSKLTTQMTLHYEsVSKELNPSCENFGLLCAAKGKDGQWHRGFLQQLlPPSQVKVWF 85
                           90
                   ....*....|....
gi 2065618660 1342 VDNGYIETIPHVHV 1355
Cdd:cd20437     86 IDYGNSEAVSSHSV 99
Tudor_TDRD6_rpt4 cd20423
fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
1557-1634 1.56e-07

fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the fourth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410494  Cd Length: 80  Bit Score: 50.17  E-value: 1.56e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2065618660 1557 DFRSEMPCLAEY-DDGRWYRAKVLSVDnLHPLKILVQHVDFGSSASLPESRLRQLPIGLMQYPARAIRVKLMGFKPPAS 1634
Cdd:cd20423      2 HSLPNPVCLAKYsEDGKWCRALIDNVY-EPVEMVEVTYVDYGNKELVSLKNLRSISEEFLKLKAQAFRCSLYNLIQPSG 79
Tudor_TDRD1_rpt2 cd20409
second Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
821-877 1.63e-07

second Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four Tudor domains. This model corresponds to the second one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410480  Cd Length: 82  Bit Score: 50.53  E-value: 1.63e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2065618660  821 CPVVGQACAAMF-EDGGWYRCQINSLTGHREVDVKYVDFGNTARIPITAVRKIKGDFL 877
Cdd:cd20409     25 SPAVGEVCCAQFtEDNQWYRASVLAYSSEDSVLVGYIDFGNSEEVALSRLRPIPPSLL 82
Tudor_AtTudor1-like cd20443
Tudor domain found in Arabidopsis thaliana ribonuclease Tudor 1 (AtTudor1), ribonuclease Tudor ...
822-893 1.78e-07

Tudor domain found in Arabidopsis thaliana ribonuclease Tudor 1 (AtTudor1), ribonuclease Tudor 2 (AtTudor2), and similar proteins; The family includes AtTudor1 (also called Tudor-SN protein 1) and AtTudor2 (also called Tudor-SN protein 2 or 100 kDa coactivator-like protein). They are cytoprotective ribonucleases (RNases) required for resistance to abiotic stresses, acting as positive regulators of mRNA decapping during stress. Members of this family contain one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410514 [Multi-domain]  Cd Length: 117  Bit Score: 51.31  E-value: 1.78e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2065618660  822 PVVGQACAAMFE-DGGWYRCQI------NSLTGHREVDVKYVDFGNTARIPITAVRKIKGDFLTLPIQALQCRLADVEP 893
Cdd:cd20443     38 PKKGELVLAQFSaDNSWNRAMVvnaprqGTQSPKDEYEVFYIDYGNQETVPLSALRPLDPSVSSAPGLAQLCSLAHIKV 116
Tudor_TDRD15_rpt3 cd20438
third Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
1025-1154 2.22e-07

third Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the third one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410509  Cd Length: 141  Bit Score: 51.71  E-value: 2.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1025 ITYVASPSSIFVQLLSSQSLVTDLQEKIKSEYSSSEADIEW----EESMHCALLVFENKEWRRGKVTKVNLNKTAeVFCY 1100
Cdd:cd20438     11 VEYVLNPSNFWIRTDEYNNEFQALMKNIADIYNLCGNDEELlkkpEPGLLCCARYSKDRHYYRAVITEVLDLKVS-VYFL 89
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2065618660 1101 DFGNKELVNICMLKKLKEDIQTIRPLAMECSLSEIKPAggSSKWAATSCDFLKE 1154
Cdd:cd20438     90 DFGNTDTVPFYDVKTLLPEFSELPALAMCCSLAHVFPV--EEVWTKNANDFFKK 141
Tudor_TDRD15_rpt4 cd20439
fourth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
1021-1135 3.43e-07

fourth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the fourth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410510  Cd Length: 125  Bit Score: 50.95  E-value: 3.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1021 VEVKITYVASPSSIFVQLLSSQSLVTDLQEKIKSEYSSSeADIEWEESMHCALLVFENKEWRRGKVTKVNLNKTAEVFCY 1100
Cdd:cd20439     12 VDVKCSYVNSPGDFWCQLQTKSSELKSLMKQIQSYYLIH-NDPYKHGQIACVAKYSKDGKWYRAAVLKQVSAKEVDVIFV 90
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2065618660 1101 DFGNKELVNICMLKKLKEDIQTIRPLAMECSLSEI 1135
Cdd:cd20439     91 DYGNQERVLISDLRAIKPQFLLLEGQAFRCSLNNF 125
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
1311-1358 4.55e-07

Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar proteins; dTUD is required during oogenesis for the formation of primordial germ cells and for normal abdominal segmentation. It contains 11 Tudor domains. The family also includes mitochondrial A-kinase anchor protein 1 (AKAP1) and Tudor domain-containing proteins (TDRDs). AKAP1, also called A-kinase anchor protein 149 kDa (AKAP 149), or dual specificity A-kinase-anchoring protein 1 (D-AKAP-1), or protein kinase A-anchoring protein 1 (PRKA1), or Spermatid A-kinase anchor protein 84 (S-AKAP84), is found in mitochondria and in the endoplasmic reticulum-nuclear envelope where it anchors protein kinases, phosphatases, and a phosphodiesterase. It regulates multiple cellular processes governing mitochondrial homeostasis and cell viability. AKAP1 binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane. TDRDs have diverse biological functions and may contain one or more copies of the Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410450  Cd Length: 50  Bit Score: 47.90  E-value: 4.55e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1311 KGEGCVVKGSDT-LWYRGKILEVI-GVCVKVYYVDNGYIETIPHVHVYPM 1358
Cdd:cd20379      1 VGDLCAAKYEEDgKWYRARVLEVLsNDKVEVFFVDYGNTETVPLSDLRPL 50
Tudor_TDRD15_rpt7 cd20442
seventh Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
1022-1143 4.77e-07

seventh Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the seventh one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410513  Cd Length: 160  Bit Score: 51.19  E-value: 4.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1022 EVKITYVASPSSIFVQLLSSQSLVTDL----QEKIKSEYSSSEADIEweESMHCALLVFENKEWRRGKVTKVNLNK-TAE 1096
Cdd:cd20442      5 KGTLLSVSKNGTFYVRLLRNSEQLTDLesliAKEAKKCKFVPVEDIK--EGLECLAKSKKNLKWYRAVVEHLYPETeKML 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2065618660 1097 VFCYDFGNKELVNICMLKKLKEDIQTIRPLAMECSLSEIKPAGGSSK 1143
Cdd:cd20442     83 VFFVDHGITEVVSMGNIKQLSNDLLQIPRQAVLCRWNWPESSKELSF 129
Tudor_TDRD9 cd20431
Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is ...
781-880 7.57e-07

Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is an ATP-dependent DEAD-like RNA helicase required during spermatogenesis. It is involved in the biosynthesis of PIWI-interacting RNAs (piRNAs). A recessive deleterious mutation mutation in TDRD9 causes non-obstructive azoospermia in infertile men. TDRD9 contains an N-terminal HrpA-like RNA helicase module and a Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410502  Cd Length: 101  Bit Score: 48.92  E-value: 7.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  781 THVNDPSDFYIQLADTVKLIILTKKMFEVYTEKNVRMEILCPVVGqACAAMFEDGG---WYRCQINSLTGHrEVDVKYVD 857
Cdd:cd20431      1 TEVVEVGHFWGYRIDENSSEILQQLTAEINQRQLVPLTTKPVPNL-LCLAPFTDADmkkYYRAKILYVSGS-SAEVFFVD 78
                           90       100
                   ....*....|....*....|...
gi 2065618660  858 FGNTARIPITAVRKIKGDFLTLP 880
Cdd:cd20431     79 YGNTSQVPSSLLREIPETLLTLP 101
Tudor_TDRD8 cd20430
Tudor domain found in Tudor domain-containing protein 8 (TDRD8) and similar proteins; TDRD8, ...
822-861 9.45e-07

Tudor domain found in Tudor domain-containing protein 8 (TDRD8) and similar proteins; TDRD8, also called serine/threonine-protein kinase (EC 2.7.11.1) 31 (STK31), serine/threonine-protein kinase NYD-SPK, or Sugen kinase 396 (SgK396), is a germ cell-specific factor expressed in embryonic gonocytes of both sexes, and in postnatal spermatocytes and round spermatids in males. It acts as a cell-cycle regulated protein that contributes to the tumorigenicity of epithelial cancer cells. TDRD8 contains a Tudor domain and a serine/threonine kinase domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410501 [Multi-domain]  Cd Length: 75  Bit Score: 48.06  E-value: 9.45e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2065618660  822 PVVGQACAAMF-EDGGWYRCQINSLTGHREVDVKYVDFGNT 861
Cdd:cd20430     19 PDPNKIYGGKFsEDNCWYRCKVKSILSDEKCTVQYIDYGNT 59
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
1564-1632 1.52e-06

second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; TDRD12, also called ES cell-associated transcript 8 protein (ECAT8), is a putative ATP-dependent DEAD-like RNA helicase that is essential for germ cell development and maintenance. It acts as a unique piRNA biogenesis factor essential for secondary PIWI interacting RNA (piRNA) biogenesis. TDRD12 contains two Tudor domains, one at the N-terminus and the other at the C-terminal end. The model corresponds to the second/C-terminal one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410506  Cd Length: 134  Bit Score: 49.17  E-value: 1.52e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2065618660 1564 CLAEYDDGRWYRAKVLSV----DNLHPLKILVQHVDFGSSASLPESRLRQLPIGLMQYPARAIRVKLMGFKPP 1632
Cdd:cd20435     56 CAVEDENNLYHRVKVLEItekdDKTKPREVLVKFIDEGRVETVVVSQLLELPEELKSLPPQAVEVFLCNVKPV 128
Tudor_TDRD6_rpt6 cd20425
sixth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
1021-1132 1.91e-06

sixth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the sixth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410496  Cd Length: 115  Bit Score: 48.22  E-value: 1.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1021 VEVKITYVASPSSIFVQLLSSQSLVTDLQEKIKSEYSSSEaDIEWEE----SMHCAllVF-ENKEWRRGKVTKVNLNKTA 1095
Cdd:cd20425      2 TEVYVSHVNSPSDFYVQLAQDEDELSMISEKLNASKANDE-EVECESlqlgDLICA--EYpEDGLWYRAVVKEKIPNNLV 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2065618660 1096 EVFCYDFGNKELVNICMLKKLKEDIQTIRPLAMECSL 1132
Cdd:cd20425     79 SVQFIDYGNTSVVQPSKIHRLPKELLSIPALSIHCFL 115
TUDOR pfam00567
Tudor domain;
515-674 2.74e-06

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 48.12  E-value: 2.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  515 VSVSHVINPCHFYIQKSSEKKKASLLASEATNFCNNvesQKIPIPALELGERIIVKSNLFCTWCRGIITELVPSEEneek 594
Cdd:pfam00567    5 VVVSHIESPSTFYIQPKSDSKKLEKLTEELQEYYAS---KPPESLPPAVGDGCVAAFSEDGKWYRAKITESLDDGL---- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660  595 pngptryritevavMQVFLLDIGHSEIfvvtgfnnlVKklqdgidaysyVNDLSQCVRKLGPevkgvintTPPLAIKCSL 674
Cdd:pfam00567   78 --------------VEVLFIDYGNTET---------VP-----------LSDLRPLPPELES--------LPPQAIKCQL 115
Tudor_TDRD1_rpt2 cd20409
second Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
1538-1611 3.31e-06

second Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four Tudor domains. This model corresponds to the second one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410480  Cd Length: 82  Bit Score: 46.68  E-value: 3.31e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2065618660 1538 LDKALRDLNPSAERLPLLTDFRSEM--PCLAEY-DDGRWYRAKVLSVDNlhPLKILVQHVDFGSSASLPESRLRQLP 1611
Cdd:cd20409      4 LAELQESLSAYCKVAPASSDFSPAVgeVCCAQFtEDNQWYRASVLAYSS--EDSVLVGYIDFGNSEEVALSRLRPIP 78
RING-HC_RNF208 cd16559
RING finger, HC subclass, found in RING finger protein 208 (RNF208) and similar proteins; ...
13-70 3.92e-06

RING finger, HC subclass, found in RING finger protein 208 (RNF208) and similar proteins; RNF208 is an E3 ubiquitin-protein ligase whose activity can be modulated by S-nitrosylation. It contains a C3HC4-type RING-HC finger.


Pssm-ID: 438221 [Multi-domain]  Cd Length: 56  Bit Score: 45.69  E-value: 3.92e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660   13 CPRCQTPFQLpesfsdaTEHLPRLLDCEHVFCDQCLLTIH--CTESNFIICPSCQVSTPV 70
Cdd:cd16559      4 CPTCGHSYNF-------TNKRPRILSCLHSVCEECLQILYesCPKYKFISCPTCKRETVL 56
Tudor_TDRD6_rpt2 cd20421
second Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
1484-1618 6.47e-06

second Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the second one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410492  Cd Length: 130  Bit Score: 47.42  E-value: 6.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1484 YDYPLLPLpGKVFPVTVKHLETPNWVY-----ICIDQRRDSESDSDMdrglkYEpeddnldkaLRDLNPSAERLPLLTDf 1558
Cdd:cd20421      2 YFYPQLQV-GVTETVVVTEVTDPHRIFcqlrsLSQELKRLSESMHQY-----YE---------GRVGSGYETRPEKLGS- 65
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2065618660 1559 rsemPCLAEYDDGRWYRA---KVLSVDNLhplkILVQHVDFGSSASLPESRLRQLPIGLMQYP 1618
Cdd:cd20421     66 ----PCAARGSDGRWYRAvlqQVFSANRV----VEVLHVDYGRKEVVSVSNLRYLAPEYFRMP 120
RING-HC_RNF224 cd16565
RING finger, HC subclass, found in RING finger protein RNF224 and similar proteins; RNF224 is ...
28-70 1.04e-05

RING finger, HC subclass, found in RING finger protein RNF224 and similar proteins; RNF224 is uncharacterized C3HC4-type RING-HC finger-containing proteins. It may function as an E3 ubiquitin-protein ligase.


Pssm-ID: 438227 [Multi-domain]  Cd Length: 59  Bit Score: 44.43  E-value: 1.04e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2065618660   28 DATEHLPRLLDCEHVFCDQCL--LTIHCTESNFIICPSCQVSTPV 70
Cdd:cd16565     11 DLSTRLPRRLYCGHTFCQACLkrLDTVINEQRWIPCPQCRQNTPT 55
Tudor_TDRD1_rpt1 cd20408
first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
1564-1632 1.54e-05

first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four Tudor domains. This model corresponds to the first one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410479  Cd Length: 130  Bit Score: 46.21  E-value: 1.54e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1564 CLAEY-DDGRWYRAKVLSVDNLHPlKILVQHVDFGSSASLPESRLRQLPIGLMQYPARAIRVKLMGFKPP 1632
Cdd:cd20408     53 CVAKYsEDQNWYRALVQTVDVQQK-KAGVFYIDYGNEETVPLNRIQPLKKDIELFPPCAIKCCLANVKPP 121
Tudor_TDRD9 cd20431
Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is ...
1552-1618 2.04e-05

Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is an ATP-dependent DEAD-like RNA helicase required during spermatogenesis. It is involved in the biosynthesis of PIWI-interacting RNAs (piRNAs). A recessive deleterious mutation mutation in TDRD9 causes non-obstructive azoospermia in infertile men. TDRD9 contains an N-terminal HrpA-like RNA helicase module and a Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410502  Cd Length: 101  Bit Score: 45.07  E-value: 2.04e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2065618660 1552 LPLLTDFRSEMPCLAEYDDG---RWYRAKVLSV--DNlhplkILVQHVDFGSSASLPESRLRQLPIGLMQYP 1618
Cdd:cd20431     35 VPLTTKPVPNLLCLAPFTDAdmkKYYRAKILYVsgSS-----AEVFFVDYGNTSQVPSSLLREIPETLLTLP 101
Tudor_TDRD6_rpt3 cd20422
third Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
1022-1153 2.76e-05

third Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the third one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410493  Cd Length: 135  Bit Score: 45.58  E-value: 2.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1022 EVKITYVASPSSIFVQLLSSQSLVTDLQEKIKSEYSSS---EADIEWEE--SMHCAllVFENKEWRRGKVTKVnLNKTAE 1096
Cdd:cd20422      3 DAQVEFVKDPSEFWIRLGEHAVPFSKLMRSMTAFYSQAsklDGVVLKPQpgQLCCA--KWKEDRYYRAIVTAV-KGKMVE 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2065618660 1097 VFCYDFGNKELVNICMLKKLKEDIQTIRPLAMECSLSEIKPAGgsSKWAATSCDFLK 1153
Cdd:cd20422     80 VFLVDRGNTEMVDWYDVKKLLPQFRELPALALKCCLADICPLG--ERWSPEAISAFK 134
Tudor_TDRD4_rpt2 cd20415
second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
1304-1369 3.35e-05

second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the second one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410486  Cd Length: 96  Bit Score: 44.35  E-value: 3.35e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2065618660 1304 LKPYCYSKGEGCVVKGSDTLWYRGKILEVIGV-CVKVYYVDNGYIETIPHVHVYPM----VMYPEIPELCL 1369
Cdd:cd20415     20 LEILCPVQGQACVALFEDGAWYRARIIGLPGHrEVEVKYVDFGNTATVTIKHVRKIkddfLSLPEKARECR 90
Tudor_TDRD5 cd20419
Tudor domain found in Tudor domain-containing protein 5 (TDRD5) and similar proteins; TDRD5 is ...
1500-1626 3.80e-05

Tudor domain found in Tudor domain-containing protein 5 (TDRD5) and similar proteins; TDRD5 is an RNA-binding protein directly associated with piRNA precursors. It is required for retrotransposon silencing, chromatoid body assembly, and spermiogenesis. TDRD5 participates in the repression of transposable elements and prevents their mobilization, which is essential for germline integrity. TDRD5 contains three LOTUS domains and one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410490  Cd Length: 118  Bit Score: 44.75  E-value: 3.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1500 VKHLETPNWVYICIDQRRDSESDSDMDRGLK--YEPEDdnldkalrdlnpSAERLPLLTDFRSE--MPCLAEYDDGRWYR 1575
Cdd:cd20419      2 VEYIESPSQFYVRFYSKDTSEMLEDMMIEMRrcYSNEH------------VSERYVMPEAFIQPgqVCCVRIPEDVWWYR 69
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2065618660 1576 AKVLSVDNLHPLKilVQHVDFGSSASLPESRLRQLPIGLMQYPARAIRVKL 1626
Cdd:cd20419     70 VIIHQVLNKQEVE--VFYPDFGDIGTVQKSRLRFLKCCYSKLPAQAIPASL 118
Tudor_TDRD6_rpt7 cd20426
seventh Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
1021-1158 4.09e-05

seventh Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the seventh one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410497  Cd Length: 140  Bit Score: 45.18  E-value: 4.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1021 VEVKITYVASPSSIFVQLLSS--QSLVTDLQEKIKSEYSSSEADIEWEESMHCALLVFENKEWRRGKVTKVNLNKTAEVF 1098
Cdd:cd20426      1 IEAYATAVDSPEYFWCQFATEkiQCLAVKVQEAGEQVADRGNFIPSIYVGDPCIVKYSEDNHWYRALVTKINDNLVSVRF 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1099 CyDFGNKELVNICMLKKLKEDIQTIRPLAMECSLSEIKPAGGSskWAATSCDFLKEILVD 1158
Cdd:cd20426     81 V-DYGNEEDVVREQVRALPSELLKIPVQAFPCCLSGFNLSEGL--WSDEANDYFYEIVTE 137
Tudor_TDRD6_rpt3 cd20422
third Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
1303-1388 4.50e-05

third Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the third one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410493  Cd Length: 135  Bit Score: 44.81  E-value: 4.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1303 LLKPycySKGEGCVVKGSDTLWYRGKILEVIGVCVKVYYVDNGYIETIPHVHVYPMV-MYPEIPELCLPFQLYGVEPVGN 1381
Cdd:cd20422     47 VLKP---QPGQLCCAKWKEDRYYRAIVTAVKGKMVEVFLVDRGNTEMVDWYDVKKLLpQFRELPALALKCCLADICPLGE 123

                   ....*..
gi 2065618660 1382 KWQEDAV 1388
Cdd:cd20422    124 RWSPEAI 130
Tudor_TDRD1_rpt4 cd20411
fourth Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
1312-1373 4.96e-05

fourth Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four Tudor domains. This model corresponds to the fourth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410482  Cd Length: 116  Bit Score: 44.36  E-value: 4.96e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2065618660 1312 GEGCVVK-GSDTLWYRGKILEVIGVCVKVYYVDNGYIETIPHVHVYPMVMYpeipELCLPFQL 1373
Cdd:cd20411     51 GDACCARfTGDKNWYRAVVLETSDSEVKVLYADYGNTETLPLSRILPITKS----HLELPFQI 109
Tudor_TDRD11 cd20433
Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, ...
1048-1118 5.14e-05

Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, also called Staphylococcal nuclease domain-containing protein 1 (SND1), 100 kDa coactivator, EBNA2 coactivator p100, or p100 co-activator, is a multifunctional protein that is reportedly associated with different types of RNA molecules, including mRNA, miRNA, pre-miRNA, and dsRNA. It has been implicated in a number of biological processes in eukaryotic cells, including the cell cycle, DNA damage repair, proliferation, and apoptosis. TDRD11 is overexpressed in multiple cancers and functions as an oncogene. It contains multiple Staphylococcal nuclease (SN) domains and a C-terminal Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410504 [Multi-domain]  Cd Length: 84  Bit Score: 43.44  E-value: 5.14e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2065618660 1048 LQEKIKSEYSSS---EADIEWEESMHCALLVFENKEWRRGKVTKVNLNKTAEVFCYDFGNKELVNICMLKKLKE 1118
Cdd:cd20433      8 LMEKLRFEIASNpplPGSYTPRKGDLCAAKFVEDGEWYRAKVEKVEGDKKVHVLYIDYGNREVLPSTRLAALPP 81
Tudor_TDRD6_rpt7 cd20426
seventh Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
1563-1629 5.73e-05

seventh Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the seventh one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410497  Cd Length: 140  Bit Score: 44.80  E-value: 5.73e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2065618660 1563 PCLAEY-DDGRWYRAKVLSV-DNLhplkILVQHVDFGSSASLPESRLRQLPIGLMQYPARAIRVKLMGF 1629
Cdd:cd20426     52 PCIVKYsEDNHWYRALVTKInDNL----VSVRFVDYGNEEDVVREQVRALPSELLKIPVQAFPCCLSGF 116
RING-HC_TRIM32_C-VII cd16587
RING finger, HC subclass, found in tripartite motif-containing protein 32 (TRIM32) and similar ...
13-64 5.88e-05

RING finger, HC subclass, found in tripartite motif-containing protein 32 (TRIM32) and similar proteins; TRIM32, also known as 72 kDa Tat-interacting protein, zinc finger protein HT2A, or BBS11, is an E3 ubiquitin-protein ligase that promotes degradation of several targets, including actin, PIASgamma, Abl interactor 2, dysbindin, X-linked inhibitor of apoptosis (XIAP), p73 transcription factor, thin filaments and Z-bands during fasting. It plays important roles in neuronal differentiation of neural progenitor cells, as well as in controlling cell fate in skeletal muscle progenitor cells. It reduces PI3K-Akt-FoxO signaling in muscle atrophy by promoting plakoglobin-PI3K dissociation. It also functions as a pluripotency-reprogramming roadblock that facilitates cellular transition towards differentiation by modulating the levels of Oct4 and cMyc. Moreover, TRIM32 is an intrinsic influenza A virus (IAV) restriction factor which senses and targets the polymerase basic protein 1 (PB1) for ubiquitination and protein degradation. It also plays a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo, binds specifically to the activation domain of HIV-1 Tat, and can also interact with the HIV-2 and EIAV Tat proteins in vivo. Furthermore, TRIM32 regulates myoblast proliferation by controlling turnover of NDRG2 (N-myc downstream-regulated gene). It negatively regulates tumor suppressor p53 to promote tumorigenesis. It also facilitates degradation of MYCN on spindle poles and induces asymmetric cell division in human neuroblastoma cells. In addition, TRIM32 plays important roles in regulation of hyperactivities and positively regulates the development of anxiety and depression disorders induced by chronic stress. It also plays a role in regeneration by affecting satellite cell cycle progression via modulation of the SUMO ligase PIASy (PIAS4). Defects in TRIM32 leads to limb-girdle muscular dystrophy type 2H (LGMD2H), sarcotubular myopathies (STM) and Bardet-Biedl syndrome. TRIM32 belongs to the C-VII subclass of the TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain. The NHL domain mediates the interaction with Argonaute proteins and consequently allows TRIM32 to modulate the activity of certain miRNAs.


Pssm-ID: 438249 [Multi-domain]  Cd Length: 51  Bit Score: 42.00  E-value: 5.88e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2065618660   13 CPRCQTPFqlpesfsDATEHLPRLLDCEHVFCDQCLLTIHCTES-NFIICPSC 64
Cdd:cd16587      3 CPICLESF-------DEGQLRPKLLHCGHTICEQCLEKLLASLSiNGVRCPFC 48
Tudor_TDRD15_rpt5 cd20440
fifth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
1022-1132 6.43e-05

fifth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the fifth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410511  Cd Length: 127  Bit Score: 44.37  E-value: 6.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1022 EVKITYVASPSSIFVQLLSSQSLVTDLQEKIKSE---YSSSEADIEweESMHCALLVFENKEWRRGKVTKVNLNKTAEVF 1098
Cdd:cd20440     13 EVYITHVYSPAKFYCQLDRNTEILEALMEKIAEIsklFNSQILDNC--KTRLCLAKYFEDGQWYRALAHPVESSSHLSVY 90
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2065618660 1099 CYDFGNKELVNICMLKKLKE---DIQTIRPLAMECSL 1132
Cdd:cd20440     91 FVDYGNKQIVEKNEVLPIPDtavDLLLTPMQAIKCCL 127
Tudor_TDRD6_rpt2 cd20421
second Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
1023-1116 6.47e-05

second Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the second one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410492  Cd Length: 130  Bit Score: 44.34  E-value: 6.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1023 VKITYVASPSSIFVQLLSSQSLVTDLQEKIKSEYSSSEA--DIEWEESMH--CALLVFENKeWRRGKVTKV-NLNKTAEV 1097
Cdd:cd20421     15 VVVTEVTDPHRIFCQLRSLSQELKRLSESMHQYYEGRVGsgYETRPEKLGspCAARGSDGR-WYRAVLQQVfSANRVVEV 93
                           90
                   ....*....|....*....
gi 2065618660 1098 FCYDFGNKELVNICMLKKL 1116
Cdd:cd20421     94 LHVDYGRKEVVSVSNLRYL 112
Tudor_TDRD11 cd20433
Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, ...
1302-1358 8.47e-05

Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, also called Staphylococcal nuclease domain-containing protein 1 (SND1), 100 kDa coactivator, EBNA2 coactivator p100, or p100 co-activator, is a multifunctional protein that is reportedly associated with different types of RNA molecules, including mRNA, miRNA, pre-miRNA, and dsRNA. It has been implicated in a number of biological processes in eukaryotic cells, including the cell cycle, DNA damage repair, proliferation, and apoptosis. TDRD11 is overexpressed in multiple cancers and functions as an oncogene. It contains multiple Staphylococcal nuclease (SN) domains and a C-terminal Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410504 [Multi-domain]  Cd Length: 84  Bit Score: 42.67  E-value: 8.47e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2065618660 1302 PLLKPYCYSKGEGCVVKGS-DTLWYRGKILEVIGVC-VKVYYVDNGYIETIPHVHVYPM 1358
Cdd:cd20433     21 PLPGSYTPRKGDLCAAKFVeDGEWYRAKVEKVEGDKkVHVLYIDYGNREVLPSTRLAAL 79
RING-HC_RNF39 cd16592
RING finger, HC subclass, found in RING finger protein 39 (RNF39) and similar proteins; RNF39, ...
9-69 9.70e-05

RING finger, HC subclass, found in RING finger protein 39 (RNF39) and similar proteins; RNF39, also called protein HZFw, may play a role in prolonged long term-potentiation (LTP) maintenance. It is involved in the etiology of Behcet's disease (BD). It may also be involved in HIV-1 replication. RNF39 acts as an E3 ubiquitin ligase that inhibits retinoic acid-inducible gene-I (RIG-I)-like receptor (RLR) pathways by mediating K48-linked ubiquitination and proteasomal degradation of DDX3X (DEAD-box RNA helicase 3, X-linked). RNF39 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438254 [Multi-domain]  Cd Length: 58  Bit Score: 41.67  E-value: 9.70e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2065618660    9 RVSACPRCQTPFQlpesfsDatehlPRLLDCEHVFCDQCLL------TIHCTESNFIICPSCQVSTP 69
Cdd:cd16592      3 EETTCPICLGYFK------D-----PVILDCEHSFCRACIArhwgqeAMEGNGAEGVFCPQCGEPCP 58
Tudor_TDRD1_rpt3 cd20410
third Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
1310-1351 1.00e-04

third Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four Tudor domains. This model corresponds to the third one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410481 [Multi-domain]  Cd Length: 59  Bit Score: 41.56  E-value: 1.00e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2065618660 1310 SKGEGCVVKGS-DTLWYRGKILEVI-GVCVKVYYVDNGYIETIP 1351
Cdd:cd20410      4 IVGEPCCAFFSgDGNWYRAMVKEILpGGAVKVHFVDYGNVEEVT 47
Tudor_TDRD6_rpt4 cd20423
fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
1077-1140 1.45e-04

fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the fourth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410494  Cd Length: 80  Bit Score: 42.08  E-value: 1.45e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2065618660 1077 ENKEWRRGKVTKVNLNK-TAEVFCYDFGNKELVNICMLKKLKEDIQTIRPLAMECSLSEIKPAGG 1140
Cdd:cd20423     15 EDGKWCRALIDNVYEPVeMVEVTYVDYGNKELVSLKNLRSISEEFLKLKAQAFRCSLYNLIQPSG 79
Tudor_AtTudor1-like cd20443
Tudor domain found in Arabidopsis thaliana ribonuclease Tudor 1 (AtTudor1), ribonuclease Tudor ...
1565-1632 1.49e-04

Tudor domain found in Arabidopsis thaliana ribonuclease Tudor 1 (AtTudor1), ribonuclease Tudor 2 (AtTudor2), and similar proteins; The family includes AtTudor1 (also called Tudor-SN protein 1) and AtTudor2 (also called Tudor-SN protein 2 or 100 kDa coactivator-like protein). They are cytoprotective ribonucleases (RNases) required for resistance to abiotic stresses, acting as positive regulators of mRNA decapping during stress. Members of this family contain one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410514 [Multi-domain]  Cd Length: 117  Bit Score: 42.84  E-value: 1.49e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2065618660 1565 LAEYD-DGRWYRAKVLSVDNLHPL----KILVQHVDFGSSASLPESRLRQLPIGLMQYPARAIRVKLMGFKPP 1632
Cdd:cd20443     45 LAQFSaDNSWNRAMVVNAPRQGTQspkdEYEVFYIDYGNQETVPLSALRPLDPSVSSAPGLAQLCSLAHIKVP 117
Tudor_TDRD1_rpt4 cd20411
fourth Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
1564-1628 1.63e-04

fourth Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four Tudor domains. This model corresponds to the fourth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410482  Cd Length: 116  Bit Score: 42.82  E-value: 1.63e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2065618660 1564 CLAEYD-DGRWYRAKVLSVDNLHplkILVQHVDFGSSASLPESRLrqLPI--GLMQYPARAIRVKLMG 1628
Cdd:cd20411     54 CCARFTgDKNWYRAVVLETSDSE---VKVLYADYGNTETLPLSRI--LPItkSHLELPFQIIRCSLAG 116
Tudor_AtTudor1-like cd20443
Tudor domain found in Arabidopsis thaliana ribonuclease Tudor 1 (AtTudor1), ribonuclease Tudor ...
1081-1137 1.88e-04

Tudor domain found in Arabidopsis thaliana ribonuclease Tudor 1 (AtTudor1), ribonuclease Tudor 2 (AtTudor2), and similar proteins; The family includes AtTudor1 (also called Tudor-SN protein 1) and AtTudor2 (also called Tudor-SN protein 2 or 100 kDa coactivator-like protein). They are cytoprotective ribonucleases (RNases) required for resistance to abiotic stresses, acting as positive regulators of mRNA decapping during stress. Members of this family contain one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410514 [Multi-domain]  Cd Length: 117  Bit Score: 42.84  E-value: 1.88e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2065618660 1081 WRRGKVtkVNLNKTA--------EVFCYDFGNKELVNICMLKKLKEDIQTIRPLAMECSLSEIKP 1137
Cdd:cd20443     54 WNRAMV--VNAPRQGtqspkdeyEVFYIDYGNQETVPLSALRPLDPSVSSAPGLAQLCSLAHIKV 116
Tudor_TDRD15_rpt3 cd20438
third Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
1315-1393 2.69e-04

third Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the third one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410509  Cd Length: 141  Bit Score: 42.85  E-value: 2.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1315 CVVKGSDTLWYRGKILEVIGVCVKVYYVDNGYIETIPHVHVYPMV-MYPEIPELCLPFQLYGVEPVGNKWQEDAVDLLRE 1393
Cdd:cd20438     62 CARYSKDRHYYRAVITEVLDLKVSVYFLDFGNTDTVPFYDVKTLLpEFSELPALAMCCSLAHVFPVEEVWTKNANDFFKK 141
RING-HC_RNF183-like cd16556
RING finger, HC subclass, found in RING finger protein RNF183, RNF223, RNF225 and similar ...
13-64 4.04e-04

RING finger, HC subclass, found in RING finger protein RNF183, RNF223, RNF225 and similar proteins; RNF183 is an E3 ubiquitin-protein ligase that is upregulated during intestinal inflammation and is negatively regulated by miR-7. It promotes intestinal inflammation by increasing the ubiquitination and degradation of inhibitor of kappa B, thereby resulting in secondary activation of the Nuclear factor-kappaB (NF-kB) pathway. The interaction between RNF183-mediated ubiquitination and miRNA may be an important novel epigenetic mechanism in the pathogenesis of inflammatory bowel disease (IBD). The biological function of RNF223 and RNF225 remains unclear. Members of this family contain an N-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438218 [Multi-domain]  Cd Length: 57  Bit Score: 40.04  E-value: 4.04e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2065618660   13 CPRCQTPFqlpesfsDATEHLPRLLDCEHVFCDQCL----LTIHCTEsNFIICPSC 64
Cdd:cd16556      3 CSICFSSY-------DNTFKTPKLLDCGHTFCLECLarlsLASPPQA-ERVPCPLC 50
Tudor_TDRD10 cd20432
Tudor domain found in Tudor domain-containing protein 10 (TDRD10) and similar proteins; TDRD10 ...
825-880 4.76e-04

Tudor domain found in Tudor domain-containing protein 10 (TDRD10) and similar proteins; TDRD10 is widely expressed and localized both to the nucleus and cytoplasm, and may play general roles like regulation of RNA metabolism. It contains a Tudor domain and an RNA recognition motif (RRM). The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410503  Cd Length: 139  Bit Score: 42.03  E-value: 4.76e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2065618660  825 GQACAAMF----EDGGWYRCQINSLTGHREVdVKYVDFGNTARIPITAVRKIKGD-FLTLP 880
Cdd:cd20432     74 GRRCLAECplgeEGGAWNRCWVLDVVEDFAV-VFFVDFGSTANIPLPSLRSLDEDeFWQIP 133
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
13-64 5.55e-04

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 39.03  E-value: 5.55e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 2065618660    13 CPRCQTPFqlpesfsdatEHLPRLLDCEHVFCDQCLLTihCTESNFIICPSC 64
Cdd:smart00184    1 CPICLEEY----------LKDPVILPCGHTFCRSCIRK--WLESGNNTCPIC 40
Tudor_TDRD1_rpt3 cd20410
third Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
1563-1615 5.82e-04

third Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four Tudor domains. This model corresponds to the third one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410481 [Multi-domain]  Cd Length: 59  Bit Score: 39.63  E-value: 5.82e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2065618660 1563 PCLAEY-DDGRWYRAKVLSVdnLHPLKILVQHVDFGSSASLPESRLRQLPIGLM 1615
Cdd:cd20410      8 PCCAFFsGDGNWYRAMVKEI--LPGGAVKVHFVDYGNVEEVTLDKLRKITSTFL 59
Tudor_TDRD2 cd20412
Tudor domain found in Tudor domain-containing protein 2 (TDRD2) and similar proteins; TDRD2, ...
1569-1622 6.28e-04

Tudor domain found in Tudor domain-containing protein 2 (TDRD2) and similar proteins; TDRD2, also called Tudor and KH domain-containing protein (TDRKH), participates in the primary piwi-interacting RNA (piRNA) biogenesis pathway and is required during spermatogenesis to repress transposable elements and prevent their mobilization, which is essential for germline integrity. The family also includes the TDRD2 homolog found in Drosophila melanogaster (dTDRKH), which is also called partner of PIWIs protein, or PAPI, and is involved in Zucchini-mediated piRNA 3'-end maturation. TDRD2 contains two KH domains and one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410483  Cd Length: 95  Bit Score: 40.74  E-value: 6.28e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2065618660 1569 DDGRWYRAKVLSVdnLHPLKILVQHVDFGSSASLPESRLRQLPIGLMQYPARAI 1622
Cdd:cd20412     41 HDGSWYRARVLGF--LENGNLDLYFVDYGDSGYVPLEDLRALRSDFLSLPFQAI 92
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type ...
13-64 6.44e-04

HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers. Some have a different Cys/His pattern. Some lack a single Cys or His residue at typical Zn ligand positions, especially, the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can chelate Zn in a RING finger as well. This family corresponds to the HC subclass of RING (RING-HC) fingers that are characterized by containing C3HC4-type canonical RING-HC fingers or noncanonical RING-HC finger variants, including C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type modified RING-HC fingers. The canonical RING-HC finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-HC fingers can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle, and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 438113 [Multi-domain]  Cd Length: 41  Bit Score: 39.01  E-value: 6.44e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2065618660   13 CPRCQTPFqlpesfsdateHLPRLLDCEHVFCDQCLLtiHCTESNFIICPSC 64
Cdd:cd16449      3 CPICLERL-----------KDPVLLPCGHVFCRECIR--RLLESGSIKCPIC 41
RING-HC_RNF222 cd16564
RING finger, HC subclass, found in RING finger protein 222 (RNF222) and similar proteins; ...
13-64 6.84e-04

RING finger, HC subclass, found in RING finger protein 222 (RNF222) and similar proteins; RNF222 is an uncharacterized C3HC4-type RING-HC finger-containing protein. It may function as an E3 ubiquitin-protein ligase.


Pssm-ID: 438226 [Multi-domain]  Cd Length: 50  Bit Score: 38.92  E-value: 6.84e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2065618660   13 CPRCQtpfqlpESFSDAtehlPRLLDCEHVFCDQCLltIHCTESNFIICPSC 64
Cdd:cd16564      3 CPVCY------EDFDDA----PRILSCGHSFCEDCL--VKQLVSMTISCPIC 42
Tudor_TDRD4_rpt3 cd20416
third Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
828-884 7.50e-04

third Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the third one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410487  Cd Length: 82  Bit Score: 40.16  E-value: 7.50e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2065618660  828 CAA-MFEDGGWYRCQINSLTGHREVDVKYVDFGNTARIPITAVRKIKGDFLTLPIQAL 884
Cdd:cd20416     25 CAVqIQDKKQWRRGQIIRVVSDTLVEVFLYDFGNKEVVNIDCLRKLEENLKTIGKLAL 82
Tudor_SMN_SPF30-like cd21182
Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing ...
825-872 8.54e-04

Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing factor 30 (SPF30), and similar proteins; This group contains SMN, SPF30, Tudor domain-containing protein 3 (TDRD3), DNA excision repair protein ERCC-6-like 2 (ERCC6L2), and similar proteins. SMN, also called component of gems 1, or Gemin-1, is part of a multimeric SMN complex that includes spliceosomal Sm core proteins and plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. SPF30, also called 30 kDa splicing factor SMNrp, SMN-related protein, or survival motor neuron domain-containing protein 1 (SMNDC1), is an essential pre-mRNA splicing factor required for assembly of the U4/U5/U6 tri-small nuclear ribonucleoprotein into the spliceosome. TDRD3 is a scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. ERCC6L2, also called DNA repair and recombination protein RAD26-like (RAD26L), may be involved in early DNA damage response. It regulates RNA Pol II-mediated transcription via its interaction with DNA-dependent protein kinase (DNA-PK) to resolve R loops and minimize transcription-associated genome instability. Members of this group contain a single Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410549  Cd Length: 50  Bit Score: 38.77  E-value: 8.54e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2065618660  825 GQACAAMF-EDGGWYRCQINSLTGHRE-VDVKYVDFGNTARIPITAVRKI 872
Cdd:cd21182      1 GDKCLAPYsDDGKYYEATIEEITEESDtATVVFDGYGNSEEVPLSDLKPL 50
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
1307-1358 1.03e-03

Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in the Drosophila Tudor protein. Initial proposal that the survival motor neuron gene product contain a Tudor domain are corroborated by more recent database search techniques such as PSI-BLAST (unpublished).


Pssm-ID: 197660  Cd Length: 57  Bit Score: 38.79  E-value: 1.03e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2065618660  1307 YCYSKGEGCVVKGSDTLWYRGKILEVIGV-CVKVYYVDNGYIETIPHVHVYPM 1358
Cdd:smart00333    1 PTFKVGDKVAARWEDGEWYRARIVKVDGEqLYEVFFIDYGNEEVVPPSDLRQL 53
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
1075-1120 1.03e-03

Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in the Drosophila Tudor protein. Initial proposal that the survival motor neuron gene product contain a Tudor domain are corroborated by more recent database search techniques such as PSI-BLAST (unpublished).


Pssm-ID: 197660  Cd Length: 57  Bit Score: 38.79  E-value: 1.03e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 2065618660  1075 VFENKEWRRGKVTKVNLNKTAEVFCYDFGNKELVNICMLKKLKEDI 1120
Cdd:smart00333   12 RWEDGEWYRARIVKVDGEQLYEVFFIDYGNEEVVPPSDLRQLPEEL 57
RING-HC_malin cd16516
RING finger, HC subclass, found in malin and similar proteins; Malin ("mal" for seizure in ...
14-65 1.33e-03

RING finger, HC subclass, found in malin and similar proteins; Malin ("mal" for seizure in French), also known as NHL repeat-containing protein 1 (NHLRC1), or EPM2B, is a nuclear E3 ubiquitin-protein ligase that ubiquitinates and promotes the degradation of laforin (EPM2A encoding protein phosphatase). Malin and laforin operate as a functional complex that play key roles in regulating cellular functions such as glycogen metabolism, unfolded cellular stress response, and proteolytic processes. They act as pro-survival factors that negatively regulate the Hipk2-p53 cell death pathway. They also negatively regulate cellular glucose uptake by preventing plasma membrane targeting of glucose transporters. Moreover, they degrade polyglucosan bodies in concert with glycogen debranching enzyme and brain isoform glycogen phosphorylase. Furthermore, they, together with Hsp70, form a new functional complex that suppress the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system. Defects in either malin or laforin may cause Lafora disease (LD), a fatal form of teenage-onset autosomal recessive progressive myoclonus epilepsy. In addition, malin may have function, independent of laforin, in lysosomal biogenesis and/or lysosomal glycogen disposal. Malin contains six NHL-repeat protein-protein interaction domains and a C3HC4-type RING-HC finger.


Pssm-ID: 438179 [Multi-domain]  Cd Length: 52  Bit Score: 38.26  E-value: 1.33e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2065618660   14 PRCQTPFqlpESFSDATEHLPRLLDCEHVFCDQCLLTIHCTESNFIICPSCQ 65
Cdd:cd16516      1 LECKVCF---EKYSHQQEHRPRNLPCGHVLCRECVTALAHPRRSKLECPFCR 49
Tudor_TDRD6_rpt5 cd20424
fifth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
1264-1358 1.35e-03

fifth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the fifth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410495  Cd Length: 126  Bit Score: 40.57  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1264 EVEVTGVGDDGVIYGIRKSLQEEFTMLTSAI-QASFKILPLLKPYcySKGEGCVVKGSDTLWYRGKILEVIGvCVKVYYV 1342
Cdd:cd20424     15 EVYITYVNDPWTFYCQLARNAGVLDQLASAIsRLSSEIRKLELSV--NPGTLCLAKYSDQHWYRGIIITNKN-STEVFFV 91
                           90
                   ....*....|....*.
gi 2065618660 1343 DNGYIETIPHVHVYPM 1358
Cdd:cd20424     92 DYGNTEKVEKEDMLPI 107
Tudor_TDRD7_rpt1 cd20427
first Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; ...
1299-1378 1.44e-03

first Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; TDRD7, also called PCTAIRE2-binding protein, or Tudor repeat associator with PCTAIRE-2 (Trap), is a component of specific cytoplasmic RNA granules involved in post-transcriptional regulation of specific genes: probably acts by binding to specific mRNAs and regulating their translation. It is required for lens transparency during lens development, by regulating translation of genes such as CRYBB3 and HSPB1 in the developing lens. It is also essential for dynamic ribonucleoprotein (RNP) remodeling of chromatoid bodies during spermatogenesis. TDRD7 contains three Tudor domains. The model corresponds to the first one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410498  Cd Length: 98  Bit Score: 39.72  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1299 KILPLLKPycySKGEGCVVKGSDTLWYRGKILEVIGVCVKVYYVDNGYIETIPHVHVYPMVmypeiPELC-LPFQ----- 1372
Cdd:cd20427     16 TAMCLRSP---SVGQLVAVKAEEDAWLRAQVIEVEEDKVKVYYVDHGFSEVVERSKLFKLN-----KQFYsLPFQatkck 87

                   ....*.
gi 2065618660 1373 LYGVEP 1378
Cdd:cd20427     88 LAGLEP 93
RING-HC_RNFT1-like cd16532
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein ...
11-50 1.66e-03

RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein RNFT1, RNFT2, and similar proteins; Both RNFT1 and RNFT2 are multi-pass membrane proteins containing a C3HC4-type RING-HC finger. Their biological roles remain unclear.


Pssm-ID: 438194 [Multi-domain]  Cd Length: 41  Bit Score: 37.67  E-value: 1.66e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2065618660   11 SACPRCQTPFqlpesfsdateHLPRLLDCEHVFCDQCLLT 50
Cdd:cd16532      1 DICPICQDEF-----------KDPVVLRCKHIFCEDCVSE 29
Tudor_TDRD6_rpt2 cd20421
second Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
1312-1375 1.70e-03

second Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the second one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410492  Cd Length: 130  Bit Score: 40.10  E-value: 1.70e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2065618660 1312 GEGCVVKGSDTLWYRGKILEVIGV--CVKVYYVDNGYIETIPHVHVYPM-VMYPEIPELCLPFQLYG 1375
Cdd:cd20421     64 GSPCAARGSDGRWYRAVLQQVFSAnrVVEVLHVDYGRKEVVSVSNLRYLaPEYFRMPVVTYPCALFG 130
Tudor_TDRD6_rpt5 cd20424
fifth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
1548-1626 2.46e-03

fifth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the fifth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410495  Cd Length: 126  Bit Score: 39.80  E-value: 2.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1548 SAERLPLLTDFRSEMPCLAEYDDGRWYRAKVLSVDNlhplKILVQHVDFGSSASLPESRLRQLP---IGLMQYPARAIRV 1624
Cdd:cd20424     49 SSEIRKLELSVNPGTLCLAKYSDQHWYRGIIITNKN----STEVFFVDYGNTEKVEKEDMLPIPsdaYELLLLPMQAIKC 124

                   ..
gi 2065618660 1625 KL 1626
Cdd:cd20424    125 SL 126
Tudor_TDRD4_rpt2 cd20415
second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
1048-1137 3.22e-03

second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the second one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410486  Cd Length: 96  Bit Score: 38.57  E-value: 3.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1048 LQEKIKSEYSssEADIEWEESM------HCALLvFENKEWRRGKVTKVNLNKTAEVFCYDFGNKELVNICMLKKLKEDIQ 1121
Cdd:cd20415      4 LTKKIQEFYK--EGDDGGLEILcpvqgqACVAL-FEDGAWYRARIIGLPGHREVEVKYVDFGNTATVTIKHVRKIKDDFL 80
                           90
                   ....*....|....*.
gi 2065618660 1122 TIRPLAMECSLSEIKP 1137
Cdd:cd20415     81 SLPEKARECRLAFIEP 96
RING-HC_RBR_RNF19 cd16629
RING finger, HC subclass, found in the family of RING finger proteins RNF19A, RNF19B and ...
12-65 4.11e-03

RING finger, HC subclass, found in the family of RING finger proteins RNF19A, RNF19B and similar proteins; The family includes RING finger protein RNF19A and RNF19B, both of which are transmembrane (TM) domain-containing RBR-type E3 ubiquitin-protein ligases. RNF19A, also known as double ring-finger protein (Dorfin) or p38, localizes to the ubiquitylated inclusions in Parkinson's disease (PD), dementia with Lewy bodies, multiple system atrophy, and amyotrophic lateral sclerosis (ALS). It interacts with Psmc3, a protein component of the 19S regulatory cap of the 26S proteasome, and further participates in the ubiquitin-proteasome system in acrosome biogenesis, spermatid head shaping, and development of the head-tail coupling apparatus and tail. It modulates the ubiquitination and degradation of calcium-sensing receptor (CaR), which may contribute to a general mechanism for CaR quality control during biosynthesis. Moreover, RNF19A can also ubiquitylate mutant superoxide dismutase 1 (SOD1), the causative gene of familial ALS. It may associate with endoplasmic reticulum-associated degradation (ERAD) pathway, which is related to the pathogenesis of neurodegenerative disorders, such as PD or Alzheimer's disease. RNF19B, also known as IBR domain-containing protein 3 or natural killer lytic-associated molecule (NKLAM), plays a role in controlling tumor dissemination and metastasis. It is involved in the cytolytic function of natural killer (NK) cells and cytotoxic T lymphocytes (CTLs). It interacts with ubiquitin conjugates UbcH7 and UbcH8, and ubiquitinates uridine kinase like-1 (URKL-1) protein, targeting it for degradation. Moreover, RNF19B is a novel component of macrophage phagosomes and plays a role in macrophage anti-bacterial activity. It functions as a novel modulator of macrophage inducible nitric oxide synthase (iNOS) expression. Both RNF19A and RNF19B contain an RBR domain followed by three TMs. The RBR domain was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction. This model corresponds to the RING domain, a C3HC4-type RING-HC finger required for RBR-mediated ubiquitination.


Pssm-ID: 438291 [Multi-domain]  Cd Length: 56  Bit Score: 37.04  E-value: 4.11e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2065618660   12 ACPRCQTPfqLPESFsdatehLPRLLDCEHVFCDQCL---LTIHCTESNF-IICPSCQ 65
Cdd:cd16629      2 ECPLCLDD--LSPEF------FPILLSCEHRSCRDCLrqyLTIEISESRVnISCPECS 51
Tudor_TDRD15_rpt1 cd20436
first Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
1308-1394 4.38e-03

first Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the first one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410507  Cd Length: 147  Bit Score: 39.33  E-value: 4.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1308 CYSKGEGCVVKGSDT-LWYRGKILEVIGVCVKVYYVDNGYIETI--PHVHVYPMVMYpEIPELCLPFQLYGVEPVGNKWQ 1384
Cdd:cd20436     46 SWGVGEFCLVEDTTSgEWYRGRVLEKIDEKYEVFLIDRGEVLNVhaTNMASASGELF-QLPPKAVCGIFANILPIGEKWS 124
                           90
                   ....*....|
gi 2065618660 1385 EDAVDLLREL 1394
Cdd:cd20436    125 STAVNYFSSL 134
RING-HC_KEG-like cd23140
RING finger, HC subclass, found in Arabidopsis thaliana protein KEEP ON GOING (KEG) and ...
10-70 4.54e-03

RING finger, HC subclass, found in Arabidopsis thaliana protein KEEP ON GOING (KEG) and similar proteins; KEG, also called RING-type E3 ubiquitin transferase KEG, is a RING E3 ubiquitin-protein ligase that mediates E2-dependent protein ubiquitination. It is essential for Arabidopsis growth and development. It acts as a negative regulator of abscisic acid signaling. It is required for ABSCISIC ACID-INSENSITIVE5 (ABI5) degradation, by mediating its ubiquitination. Together with EDR1, KEG may regulate endocytic trafficking and/or the formation of signaling complexes on trans-Golgi network (TGN)/ early endosome (EE) vesicles during stress responses. KEG is a multidomain protein that includes a C3HC4-type RING-HC finger, a kinase domain, ankyrin repeats, and 12 HERC2-like (for HECT and RCC1-like) repeats.


Pssm-ID: 438502 [Multi-domain]  Cd Length: 57  Bit Score: 36.85  E-value: 4.54e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2065618660   10 VSACPRCQTPFqlpesfsDATEHLPRLLDCEHVFCDQCL--LTIHCTESNfIICPSCQVSTPV 70
Cdd:cd23140      1 VPECSVCSEGY-------NEDERVPLLLQCGHTFCKDCLsqMFIRCTDLT-LKCPRCRQSVLV 55
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
222-295 4.56e-03

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


Pssm-ID: 128778  Cd Length: 127  Bit Score: 38.79  E-value: 4.56e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2065618660   222 IQRLEDSSSSIENNCNKIRKELHKEFEKIVRAVQNRKAILLKEIETISQHHLDGIANVRKILEEKTSVLDSAID 295
Cdd:smart00502   23 LKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQLESLTQKQEKLSHAIN 96
Tudor_TDRD15_rpt6 cd20441
sixth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
1030-1135 4.86e-03

sixth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the sixth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410512  Cd Length: 108  Bit Score: 38.57  E-value: 4.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1030 SPSSIFVQLLSSQSLVTDLQEKIKSEYSSSEADIEwEESMHCALLVFENKE---WRRGKVTKVNLNKTAEVFCYDFGNKE 1106
Cdd:cd20441      1 SPSRFFIQLSEDEKVILQLAEELNETSEKSRENAA-VKLKVGDLVAAEYDEdlaLYRAVITAVLPGKSFKVEFIDYGNTA 79
                           90       100
                   ....*....|....*....|....*....
gi 2065618660 1107 LVNICMLKKLKEDIQTIRPLAMECSLSEI 1135
Cdd:cd20441     80 VVDKSNIYTLQEKFLSLPRLSIPCSLSGV 108
zf-RING_UBOX pfam13445
RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.
13-62 5.30e-03

RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.


Pssm-ID: 463881 [Multi-domain]  Cd Length: 38  Bit Score: 36.22  E-value: 5.30e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2065618660   13 CPRCQTPFQLPesfsdatehlprLLDCEHVFCDQCLLTIHCTESNFIICP 62
Cdd:pfam13445    1 CPICLELFTDP------------VLPCGHTFCRECLEEMSQKKGGKFKCP 38
RING-HC_RNF138 cd16544
RING finger, HC subclass, found in RING finger protein 138 (RNF138) and similar proteins; ...
13-65 5.34e-03

RING finger, HC subclass, found in RING finger protein 138 (RNF138) and similar proteins; RNF138, also known as Nemo-like kinase-associated RING finger protein (NARF) or NLK-associated RING finger protein, is an E3 ubiquitin-protein ligase that plays an important role in glioma cell proliferation, apoptosis, and cell cycle. It specifically cooperates with the E2 conjugating enzyme E2-25K (Hip-2/UbcH1), regulates the ubiquitylation and degradation of T cell factor/lymphoid enhancer factor (TCF/LEF), and further suppresses Wnt-beta-catenin signaling. RNF138, together with three closely related proteins: RNF114, RNF125 and RNF166, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM).


Pssm-ID: 438206 [Multi-domain]  Cd Length: 53  Bit Score: 36.61  E-value: 5.34e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2065618660   13 CPRCQTPFQLPesfsdatehlPRLLDCEHVFCDQCLLtiHCTESNFIICPSCQ 65
Cdd:cd16544      5 CPVCQEVLKDP----------VELPPCRHIFCKACIL--LALRSSGARCPLCR 45
RING-HC_RNF186 cd16557
RING finger, HC subclass, found in RING finger protein 186 (RNF186) and similar proteins; ...
13-65 5.57e-03

RING finger, HC subclass, found in RING finger protein 186 (RNF186) and similar proteins; RNF186 is an E3 ubiquitin-protein ligase with an N-terminal C3HC4-type RING-HC finger and two putative C-terminal transmembrane domains which enable it to localize in a certain organelle. It regulates RING-dependent self-ubiquitination, as well as endoplasmic reticulum (ER) stress-mediated apoptosis through interaction with the Bcl-2 family protein BNip1.


Pssm-ID: 438219 [Multi-domain]  Cd Length: 52  Bit Score: 36.76  E-value: 5.57e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2065618660   13 CPRCQTPFqlpesfsDATEHLPRLLDCEHVFCDQCLLTIHCTESN--FIICPSCQ 65
Cdd:cd16557      4 CLVCRNPY-------SCFVRKPKLLACQHAFCAICLKLILCEQDGtwSVTCPLCR 51
RING-HC_PML_C-V cd16579
RING finger, HC subclass, found in promyelocytic leukemia protein (PML) and similar proteins; ...
13-65 5.93e-03

RING finger, HC subclass, found in promyelocytic leukemia protein (PML) and similar proteins; Protein PML, also known as RING finger protein 71 (RNF71) or tripartite motif-containing protein 19 (TRIM19), is predominantly a nuclear protein with a broad intrinsic antiviral activity. It is the eponymous component of PML nuclear bodies (PML NBs) and has been implicated in a wide variety of cell processes, including DNA damage signaling, apoptosis, and transcription. PML interferes with the replication of many unrelated viruses, including human immunodeficiency virus 1 (HIV-1), human foamy virus (HFV), poliovirus, influenza virus, rabies virus, EMCV, adeno-associated virus (AAV), and vesicular stomatitis virus (VSV). It also selectively interacts with misfolded proteins through distinct substrate recognition sites and conjugates these proteins with the small ubiquitin-like modifiers (SUMOs) through its SUMO ligase activity. PML belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain.


Pssm-ID: 438241 [Multi-domain]  Cd Length: 52  Bit Score: 36.38  E-value: 5.93e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2065618660   13 CPRCQTPFqlpesfsdateHLPRLLDCEHVFCDQCL--LTIHCTESNFIICPSCQ 65
Cdd:cd16579      7 CPGCKAEY-----------KCPKLLPCLHTVCSGCLeaLAEQASETTEFQCPICK 50
Tudor_TDRD15_rpt5 cd20440
fifth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
1564-1626 7.37e-03

fifth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the fifth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410511  Cd Length: 127  Bit Score: 38.21  E-value: 7.37e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2065618660 1564 CLAEY-DDGRWYRAKVLSVDNlhPLKILVQHVDFGSSASLPESRLRQLP---IGLMQYPARAIRVKL 1626
Cdd:cd20440     63 CLAKYfEDGQWYRALAHPVES--SSHLSVYFVDYGNKQIVEKNEVLPIPdtaVDLLLTPMQAIKCCL 127
Tudor_TDRD8 cd20430
Tudor domain found in Tudor domain-containing protein 8 (TDRD8) and similar proteins; TDRD8, ...
1570-1611 7.44e-03

Tudor domain found in Tudor domain-containing protein 8 (TDRD8) and similar proteins; TDRD8, also called serine/threonine-protein kinase (EC 2.7.11.1) 31 (STK31), serine/threonine-protein kinase NYD-SPK, or Sugen kinase 396 (SgK396), is a germ cell-specific factor expressed in embryonic gonocytes of both sexes, and in postnatal spermatocytes and round spermatids in males. It acts as a cell-cycle regulated protein that contributes to the tumorigenicity of epithelial cancer cells. TDRD8 contains a Tudor domain and a serine/threonine kinase domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410501 [Multi-domain]  Cd Length: 75  Bit Score: 36.89  E-value: 7.44e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2065618660 1570 DGRWYRAKVLSVDNLHplKILVQHVDFGSSASLPESRLRQLP 1611
Cdd:cd20430     32 DNCWYRCKVKSILSDE--KCTVQYIDYGNTETVSRSSIVELP 71
Tudor_TDRD6_rpt5 cd20424
fifth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
1022-1132 9.61e-03

fifth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the fifth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410495  Cd Length: 126  Bit Score: 37.87  E-value: 9.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065618660 1022 EVKITYVASPSSIFVQLLSSQSLVTDLQEKIkSEYSSSEADIEWE-ESMHCALLVFENKEWRRGKVTKvNLNKTaEVFCY 1100
Cdd:cd20424     15 EVYITYVNDPWTFYCQLARNAGVLDQLASAI-SRLSSEIRKLELSvNPGTLCLAKYSDQHWYRGIIIT-NKNST-EVFFV 91
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2065618660 1101 DFGNKELVNICMLKKLKEDIQTIRPLAME---CSL 1132
Cdd:cd20424     92 DYGNTEKVEKEDMLPIPSDAYELLLLPMQaikCSL 126
 
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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