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Conserved domains on  [gi|1207185807|ref|XP_021334643|]
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RING finger protein 17 [Danio rerio]

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; ...
 1376-1481 1.62e-58

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: 196.48  E-value: 1.62e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807 1376 LTDFPIECLCLAEYSDGKYYRAKILGFSEVTPsVKLLVRHVDFGSDDIIPLHKLRQLPASLHHFPCAAVYVKLAGFKPTN 1455
Cdd:cd20418      1 LTDFRPEMPCLAEYSDGKWYRAKLLSILEFNP-VKILVRHVDYGSTAALPTSRLRQIPAELMQYPCQAIKVKLAGFKPPL 79

                           90       100
                   ....*....|....*....|....*.
gi 1207185807 1456 VSSDLERIPYSLDWTMKAMMEMIDLL 1481
Cdd:cd20418     80 NDSETERIPYCPEWSMKALWAMIDLL 105
Tudor_TDRD4_rpt4 cd20417
fourth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 1148-1215 6.94e-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: 136.03  E-value: 6.94e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207185807 1148 WKGVLGCAVMGTDMFWYRGQVQEVIGGHVKVRYVDQGLVESIPVCHVYPMVLCEDVPQLCVPCQINGV 1215
Cdd:cd20417      1 WKKGEGCVVRGSDTLWYRGKVLEVIGGMVRVQYVDQGYIEKIPQCHLYPMVLYPDIPQFCIPCQLYGT 68
Tudor_SF super family cl02573
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ...
 659-749 5.39e-23

Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally identified in the Tudor protein of Drosophila, that adopts a beta-barrel-like core structure containing four short beta-strands followed by an alpha-helical region. It binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. Tudor domain-containing proteins may mediate protein-protein interactions required for various DNA-templated biological processes, such as RNA metabolism, as well as histone modification and the DNA damage response. Members of this superfamily contain one or more copies of the Tudor domain.


The actual alignment was detected with superfamily member cd20415:

Pssm-ID: 470623  Cd Length: 96  Bit Score: 94.81  E-value: 5.39e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807  659 LHSKLQDCYNQPKSNNEcQVYCPSLSQACVA-FHDQEWSRVQVTGFPGGRMVEVRFVDFGYKRTLSVKDLRHIKDEFFVL 737
Cdd:cd20415      4 LTKKIQEFYKEGDDGGL-EILCPVQGQACVAlFEDGAWYRARIIGLPGHREVEVKYVDFGNTATVTIKHVRKIKDDFLSL 82

                           90
                   ....*....|..
gi 1207185807  738 PEMALWCNLNDV 749
Cdd:cd20415     83 PEKARECRLAFI 94
Tudor_SF super family cl02573
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ...
 894-965 4.96e-12

Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally identified in the Tudor protein of Drosophila, that adopts a beta-barrel-like core structure containing four short beta-strands followed by an alpha-helical region. It binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. Tudor domain-containing proteins may mediate protein-protein interactions required for various DNA-templated biological processes, such as RNA metabolism, as well as histone modification and the DNA damage response. Members of this superfamily contain one or more copies of the Tudor domain.


The actual alignment was detected with superfamily member cd20416:

Pssm-ID: 470623  Cd Length: 82  Bit Score: 62.89  E-value: 4.96e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207185807  894 IHDTLKNLFSKSEPQEMQWEAEMYCAV--NNTGVWERGQVCSVSTCGVAEVLRCDFGNTVKLHVDNLRPLHPDL 965
Cdd:cd20416      1 LQEKMIAEYENSKPEPVKWENDMHCAVqiQDKKQWRRGQIIRVVSDTLVEVFLYDFGNKEVVNIDCLRKLEENL 74
RING_Ubox super family cl17238
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger ...
 6-66 1.55e-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 cd16565:

Pssm-ID: 473075 [Multi-domain]  Cd Length: 59  Bit Score: 46.74  E-value: 1.55e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207185807    6 VTCKICGSPYTLpedeaVGNLPHVLLCGHIFCCTCLRALQSQGNV---ITCPECQMDTRTSEEG 66
Cdd:cd16565      1 LDCIICYSAYDL-----STRLPRRLYCGHTFCQACLKRLDTVINEqrwIPCPQCRQNTPTPRGG 59
TUDOR super family cl26991
Tudor domain;
394-534 8.59e-06

Tudor domain;


The actual alignment was detected with superfamily member pfam00567:

Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 46.19  E-value: 8.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807  394 VVTTHIVNPGHFYVRYMAEHKLGQKLTKKISEFC-SGERSFFTFSDEITTGSLLFIswkDDMWCRVKVTELFQKECFqsv 472
Cdd:pfam00567    5 VVVSHIESPSTFYIQPKSDSKKLEKLTEELQEYYaSKPPESLPPAVGDGCVAAFSE---DGKWYRAKITESLDDGLV--- 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207185807  473 tkclasevsrlCVYFLDYGFFKgfSIPSdgglsglnECLRRpdgITLiEMANWAPLAIKCSL 534
Cdd:pfam00567   79 -----------EVLFIDYGNTE--TVPL--------SDLRP---LPP-ELESLPPQAIKCQL 115
 
Name Accession Description Interval E-value
Tudor_TDRD4_rpt5 cd20418
fifth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 1376-1481 1.62e-58

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: 196.48  E-value: 1.62e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807 1376 LTDFPIECLCLAEYSDGKYYRAKILGFSEVTPsVKLLVRHVDFGSDDIIPLHKLRQLPASLHHFPCAAVYVKLAGFKPTN 1455
Cdd:cd20418      1 LTDFRPEMPCLAEYSDGKWYRAKLLSILEFNP-VKILVRHVDYGSTAALPTSRLRQIPAELMQYPCQAIKVKLAGFKPPL 79

                           90       100
                   ....*....|....*....|....*.
gi 1207185807 1456 VSSDLERIPYSLDWTMKAMMEMIDLL 1481
Cdd:cd20418     80 NDSETERIPYCPEWSMKALWAMIDLL 105
Tudor_TDRD4_rpt4 cd20417
fourth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 1148-1215 6.94e-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: 136.03  E-value: 6.94e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207185807 1148 WKGVLGCAVMGTDMFWYRGQVQEVIGGHVKVRYVDQGLVESIPVCHVYPMVLCEDVPQLCVPCQINGV 1215
Cdd:cd20417      1 WKKGEGCVVRGSDTLWYRGKVLEVIGGMVRVQYVDQGYIEKIPQCHLYPMVLYPDIPQFCIPCQLYGT 68
Tudor_TDRD4_rpt2 cd20415
second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 659-749 5.39e-23

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: 94.81  E-value: 5.39e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807  659 LHSKLQDCYNQPKSNNEcQVYCPSLSQACVA-FHDQEWSRVQVTGFPGGRMVEVRFVDFGYKRTLSVKDLRHIKDEFFVL 737
Cdd:cd20415      4 LTKKIQEFYKEGDDGGL-EILCPVQGQACVAlFEDGAWYRARIIGLPGHREVEVKYVDFGNTATVTIKHVRKIKDDFLSL 82

                           90
                   ....*....|..
gi 1207185807  738 PEMALWCNLNDV 749
Cdd:cd20415     83 PEKARECRLAFI 94
TUDOR pfam00567
Tudor domain;
634-746 2.80e-22

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 93.57  E-value: 2.80e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807  634 NAMVSHVNTPSDFYVQLVENTE-YPLLHSKLQDCYNQPKsnNECQVYCPSLSQACVAFHDQEWSRVQVTGFPGGRMVEVR 712
Cdd:pfam00567    4 DVVVSHIESPSTFYIQPKSDSKkLEKLTEELQEYYASKP--PESLPPAVGDGCVAAFSEDGKWYRAKITESLDDGLVEVL 81

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1207185807  713 FVDFGYKRTLSVKDLRHIKDEFFVLPEMALWCNL 746
Cdd:pfam00567   82 FIDYGNTETVPLSDLRPLPPELESLPPQAIKCQL 115
TUDOR pfam00567
Tudor domain;
1106-1214 1.43e-14

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 71.62  E-value: 1.43e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807 1106 ISAVSEQGVIYAMTHQAVCEFDRLRERLQQHIKTLPRQKNYNWKGVLGCAVMGTDMFWYRGQVQEVI-GGHVKVRYVDQG 1184
Cdd:pfam00567    7 VSHIESPSTFYIQPKSDSKKLEKLTEELQEYYASKPPESLPPAVGDGCVAAFSEDGKWYRAKITESLdDGLVEVLFIDYG 86

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1207185807 1185 LVESIPVCHVYPMVL-CEDVPQLCVPCQING 1214
Cdd:pfam00567   87 NTETVPLSDLRPLPPeLESLPPQAIKCQLAG 117
TUDOR pfam00567
Tudor domain;
1326-1450 3.26e-12

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 64.68  E-value: 3.26e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807 1326 KHFPAKVKHIRTPNEvFLCVLDKSLCKLEQdesMEETLEQVNENIENLSLLTDFPIECLCLAeYSDGKYYRAKILgfsEV 1405
Cdd:pfam00567    1 STIDVVVSHIESPST-FYIQPKSDSKKLEK---LTEELQEYYASKPPESLPPAVGDGCVAAF-SEDGKWYRAKIT---ES 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1207185807 1406 TPSVKLLVRHVDFGSDDIIPLHKLRQLPASLHHFPCAAVYVKLAG 1450
Cdd:pfam00567   73 LDDGLVEVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQLAG 117
Tudor_TDRD4_rpt3 cd20416
third Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 894-965 4.96e-12

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: 62.89  E-value: 4.96e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207185807  894 IHDTLKNLFSKSEPQEMQWEAEMYCAV--NNTGVWERGQVCSVSTCGVAEVLRCDFGNTVKLHVDNLRPLHPDL 965
Cdd:cd20416      1 LQEKMIAEYENSKPEPVKWENDMHCAVqiQDKKQWRRGQIIRVVSDTLVEVFLYDFGNKEVVNIDCLRKLEENL 74
TUDOR pfam00567
Tudor domain;
865-977 1.59e-11

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 62.76  E-value: 1.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807  865 KDIRVRVTHVTSPGNICVQLLQFDNQLKRIHDTLKNLFSKSEPQEMQ-WEAEMYCAVNNT-GVWERGQVCSVSTCGVAEV 942
Cdd:pfam00567    1 STIDVVVSHIESPSTFYIQPKSDSKKLEKLTEELQEYYASKPPESLPpAVGDGCVAAFSEdGKWYRAKITESLDDGLVEV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1207185807  943 LRCDFGNTVKLHVDNLRPL--HPDLIGSFLLECNLSG 977
Cdd:pfam00567   81 LFIDYGNTETVPLSDLRPLppELESLPPQAIKCQLAG 117
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
 679-734 1.18e-07

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: 49.58  E-value: 1.18e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207185807   679 YCPSLSQACVAFH-DQEWSRVQVTGFPGGRMVEVRFVDFGYKRTLSVKDLRHIKDEF 734
Cdd:smart00333    1 PTFKVGDKVAARWeDGEWYRARIVKVDGEQLYEVFFIDYGNEEVVPPSDLRQLPEEL 57
RING-HC_RNF224 cd16565
RING finger, HC subclass, found in RING finger protein RNF224 and similar proteins; RNF224 is ...
 6-66 1.55e-06

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: 46.74  E-value: 1.55e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207185807    6 VTCKICGSPYTLpedeaVGNLPHVLLCGHIFCCTCLRALQSQGNV---ITCPECQMDTRTSEEG 66
Cdd:cd16565      1 LDCIICYSAYDL-----STRLPRRLYCGHTFCQACLKRLDTVINEqrwIPCPQCRQNTPTPRGG 59
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
 1384-1433 5.86e-06

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: 44.96  E-value: 5.86e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1207185807  1384 LCLAEYSDGKYYRAKILgfsEVTPSVKLLVRHVDFGSDDIIPLHKLRQLP 1433
Cdd:smart00333    8 KVAARWEDGEWYRARIV---KVDGEQLYEVFFIDYGNEEVVPPSDLRQLP 54
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
 8-56 7.05e-06

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: 44.42  E-value: 7.05e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 1207185807     8 CKICGSPYTlpedeavgNLPHVLLCGHIFCCTCLRALQSQGNvITCPEC 56
Cdd:smart00184    1 CPICLEEYL--------KDPVILPCGHTFCRSCIRKWLESGN-NTCPIC 40
TUDOR pfam00567
Tudor domain;
394-534 8.59e-06

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 46.19  E-value: 8.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807  394 VVTTHIVNPGHFYVRYMAEHKLGQKLTKKISEFC-SGERSFFTFSDEITTGSLLFIswkDDMWCRVKVTELFQKECFqsv 472
Cdd:pfam00567    5 VVVSHIESPSTFYIQPKSDSKKLEKLTEELQEYYaSKPPESLPPAVGDGCVAAFSE---DGKWYRAKITESLDDGLV--- 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207185807  473 tkclasevsrlCVYFLDYGFFKgfSIPSdgglsglnECLRRpdgITLiEMANWAPLAIKCSL 534
Cdd:pfam00567   79 -----------EVLFIDYGNTE--TVPL--------SDLRP---LPP-ELESLPPQAIKCQL 115
zf-RING_UBOX pfam13445
RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.
 8-54 4.74e-05

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: 42.00  E-value: 4.74e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1207185807    8 CKICGSPYTLPedeavgnlphVLLCGHIFCCTCLRALQSQGNV-ITCP 54
Cdd:pfam13445    1 CPICLELFTDP----------VLPCGHTFCRECLEEMSQKKGGkFKCP 38
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
 915-965 2.93e-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: 37.25  E-value: 2.93e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1207185807   915 EMYCAVNNTGVWERGQVCSVSTCGVAEVLRCDFGNTVKLHVDNLRPLHPDL 965
Cdd:smart00333    7 DKVAARWEDGEWYRARIVKVDGEQLYEVFFIDYGNEEVVPPSDLRQLPEEL 57
 
Name Accession Description Interval E-value
Tudor_TDRD4_rpt5 cd20418
fifth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 1376-1481 1.62e-58

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: 196.48  E-value: 1.62e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807 1376 LTDFPIECLCLAEYSDGKYYRAKILGFSEVTPsVKLLVRHVDFGSDDIIPLHKLRQLPASLHHFPCAAVYVKLAGFKPTN 1455
Cdd:cd20418      1 LTDFRPEMPCLAEYSDGKWYRAKLLSILEFNP-VKILVRHVDYGSTAALPTSRLRQIPAELMQYPCQAIKVKLAGFKPPL 79

                           90       100
                   ....*....|....*....|....*.
gi 1207185807 1456 VSSDLERIPYSLDWTMKAMMEMIDLL 1481
Cdd:cd20418     80 NDSETERIPYCPEWSMKALWAMIDLL 105
Tudor_TDRD4_rpt4 cd20417
fourth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 1148-1215 6.94e-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: 136.03  E-value: 6.94e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207185807 1148 WKGVLGCAVMGTDMFWYRGQVQEVIGGHVKVRYVDQGLVESIPVCHVYPMVLCEDVPQLCVPCQINGV 1215
Cdd:cd20417      1 WKKGEGCVVRGSDTLWYRGKVLEVIGGMVRVQYVDQGYIEKIPQCHLYPMVLYPDIPQFCIPCQLYGT 68
Tudor_TDRD4_rpt2 cd20415
second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 659-749 5.39e-23

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: 94.81  E-value: 5.39e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807  659 LHSKLQDCYNQPKSNNEcQVYCPSLSQACVA-FHDQEWSRVQVTGFPGGRMVEVRFVDFGYKRTLSVKDLRHIKDEFFVL 737
Cdd:cd20415      4 LTKKIQEFYKEGDDGGL-EILCPVQGQACVAlFEDGAWYRARIIGLPGHREVEVKYVDFGNTATVTIKHVRKIKDDFLSL 82

                           90
                   ....*....|..
gi 1207185807  738 PEMALWCNLNDV 749
Cdd:cd20415     83 PEKARECRLAFI 94
TUDOR pfam00567
Tudor domain;
634-746 2.80e-22

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 93.57  E-value: 2.80e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807  634 NAMVSHVNTPSDFYVQLVENTE-YPLLHSKLQDCYNQPKsnNECQVYCPSLSQACVAFHDQEWSRVQVTGFPGGRMVEVR 712
Cdd:pfam00567    4 DVVVSHIESPSTFYIQPKSDSKkLEKLTEELQEYYASKP--PESLPPAVGDGCVAAFSEDGKWYRAKITESLDDGLVEVL 81

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1207185807  713 FVDFGYKRTLSVKDLRHIKDEFFVLPEMALWCNL 746
Cdd:pfam00567   82 FIDYGNTETVPLSDLRPLPPELESLPPQAIKCQL 115
TUDOR pfam00567
Tudor domain;
1106-1214 1.43e-14

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 71.62  E-value: 1.43e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807 1106 ISAVSEQGVIYAMTHQAVCEFDRLRERLQQHIKTLPRQKNYNWKGVLGCAVMGTDMFWYRGQVQEVI-GGHVKVRYVDQG 1184
Cdd:pfam00567    7 VSHIESPSTFYIQPKSDSKKLEKLTEELQEYYASKPPESLPPAVGDGCVAAFSEDGKWYRAKITESLdDGLVEVLFIDYG 86

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1207185807 1185 LVESIPVCHVYPMVL-CEDVPQLCVPCQING 1214
Cdd:pfam00567   87 NTETVPLSDLRPLPPeLESLPPQAIKCQLAG 117
Tudor_TDRD15_rpt4 cd20439
fourth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 633-749 1.95e-14

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: 71.37  E-value: 1.95e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807  633 VNAMVSHVNTPSDFYVQLVENT-EYPLLHSKLQDCYNQPKSNNE-CQVycpslsqACVAFH--DQEWSRVQVTGFPGGRM 708
Cdd:cd20439     12 VDVKCSYVNSPGDFWCQLQTKSsELKSLMKQIQSYYLIHNDPYKhGQI-------ACVAKYskDGKWYRAAVLKQVSAKE 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1207185807  709 VEVRFVDFGYKRTLSVKDLRHIKDEFFVLPEMALWCNLNDV 749
Cdd:cd20439     85 VDVIFVDYGNQERVLISDLRAIKPQFLLLEGQAFRCSLNNF 125
Tudor_TDRD1_rpt1 cd20408
first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 637-761 4.17e-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: 67.78  E-value: 4.17e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807  637 VSHVNTPSDFYVQLV--ENTEYPL-LHSKLQDCYnqpKSNNECQVYCPSLSQACVAFH--DQEWSRVQV-TGFPGGRMVE 710
Cdd:cd20408      3 VTEFKNPGEFYIQIYtlEVLESLVkLTSQLKKTY---ASVNNHKEYIPEVGEVCVAKYseDQNWYRALVqTVDVQQKKAG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207185807  711 VRFVDFGYKRTLSVKDLRHIKDEFFVLPEMALWCNLNDVISSQETWANEAC 761
Cdd:cd20408     80 VFYIDYGNEETVPLNRIQPLKKDIELFPPCAIKCCLANVKPPSGSWSEECI 130
TUDOR pfam00567
Tudor domain;
1326-1450 3.26e-12

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 64.68  E-value: 3.26e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807 1326 KHFPAKVKHIRTPNEvFLCVLDKSLCKLEQdesMEETLEQVNENIENLSLLTDFPIECLCLAeYSDGKYYRAKILgfsEV 1405
Cdd:pfam00567    1 STIDVVVSHIESPST-FYIQPKSDSKKLEK---LTEELQEYYASKPPESLPPAVGDGCVAAF-SEDGKWYRAKIT---ES 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1207185807 1406 TPSVKLLVRHVDFGSDDIIPLHKLRQLPASLHHFPCAAVYVKLAG 1450
Cdd:pfam00567   73 LDDGLVEVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQLAG 117
Tudor_TDRD4_rpt3 cd20416
third Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 894-965 4.96e-12

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: 62.89  E-value: 4.96e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207185807  894 IHDTLKNLFSKSEPQEMQWEAEMYCAV--NNTGVWERGQVCSVSTCGVAEVLRCDFGNTVKLHVDNLRPLHPDL 965
Cdd:cd20416      1 LQEKMIAEYENSKPEPVKWENDMHCAVqiQDKKQWRRGQIIRVVSDTLVEVFLYDFGNKEVVNIDCLRKLEENL 74
Tudor_TDRD6_rpt3 cd20422
third Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 634-765 1.19e-11

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: 63.68  E-value: 1.19e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807  634 NAMVSHVNTPSDFYVQLVEN-TEYPLLHSKLQDCYNQpKSNNECQVYCPSLSQACVA-FHDQEWSRVQVTGFPGgRMVEV 711
Cdd:cd20422      3 DAQVEFVKDPSEFWIRLGEHaVPFSKLMRSMTAFYSQ-ASKLDGVVLKPQPGQLCCAkWKEDRYYRAIVTAVKG-KMVEV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207185807  712 RFVDFGYKRTLSVKDLRHIKDEFFVLPEMALWCNLNDVISSQETWANEACESFK 765
Cdd:cd20422     81 FLVDRGNTEMVDWYDVKKLLPQFRELPALALKCCLADICPLGERWSPEAISAFK 134
TUDOR pfam00567
Tudor domain;
865-977 1.59e-11

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 62.76  E-value: 1.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807  865 KDIRVRVTHVTSPGNICVQLLQFDNQLKRIHDTLKNLFSKSEPQEMQ-WEAEMYCAVNNT-GVWERGQVCSVSTCGVAEV 942
Cdd:pfam00567    1 STIDVVVSHIESPSTFYIQPKSDSKKLEKLTEELQEYYASKPPESLPpAVGDGCVAAFSEdGKWYRAKITESLDDGLVEV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1207185807  943 LRCDFGNTVKLHVDNLRPL--HPDLIGSFLLECNLSG 977
Cdd:pfam00567   81 LFIDYGNTETVPLSDLRPLppELESLPPQAIKCQLAG 117
Tudor_TDRD6_rpt7 cd20426
seventh Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 633-773 9.27e-11

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: 61.36  E-value: 9.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807  633 VNAMVSHVNTPSDFYVQL-VENTEYplLHSKLQDCYNQPKSNNECqVYCPSLSQACVAFH--DQEWSRVQVTGFpGGRMV 709
Cdd:cd20426      1 IEAYATAVDSPEYFWCQFaTEKIQC--LAVKVQEAGEQVADRGNF-IPSIYVGDPCIVKYseDNHWYRALVTKI-NDNLV 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207185807  710 EVRFVDFGYKRTLSVKDLRHIKDEFFVLPEMALWCNLNDVISSQETWANEACESFKELVEGKLM 773
Cdd:cd20426     77 SVRFVDYGNEEDVVREQVRALPSELLKIPVQAFPCCLSGFNLSEGLWSDEANDYFYEIVTEDLL 140
Tudor_TDRD6_rpt6 cd20425
sixth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 633-746 5.94e-10

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: 58.24  E-value: 5.94e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807  633 VNAMVSHVNTPSDFYVQLVENTEyplLHSKLQDCYNQPKSNNEcQVYCPSLSQA---CVAF-HDQEWSRVQVTGFPGGRM 708
Cdd:cd20425      2 TEVYVSHVNSPSDFYVQLAQDED---ELSMISEKLNASKANDE-EVECESLQLGdliCAEYpEDGLWYRAVVKEKIPNNL 77

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1207185807  709 VEVRFVDFGYKRTLSVKDLRHIKDEFFVLPEMALWCNL 746
Cdd:cd20425     78 VSVQFIDYGNTSVVQPSKIHRLPKELLSIPALSIHCFL 115
Tudor_TDRD15_rpt3 cd20438
third Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 635-766 1.80e-09

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: 57.48  E-value: 1.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807  635 AMVSHVNTPSDFYVQLVE-NTEYPLLHSKLQDCYNqPKSNNECQVYCPSLSQACVAFH--DQEWSRVQVTGFPGGRmVEV 711
Cdd:cd20438      9 AFVEYVLNPSNFWIRTDEyNNEFQALMKNIADIYN-LCGNDEELLKKPEPGLLCCARYskDRHYYRAVITEVLDLK-VSV 86

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1207185807  712 RFVDFGYKRTLSVKDLRHIKDEFFVLPEMALWCNLNDVISSQETWANEACESFKE 766
Cdd:cd20438     87 YFLDFGNTDTVPFYDVKTLLPEFSELPALAMCCSLAHVFPVEEVWTKNANDFFKK 141
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 1384-1453 9.47e-09

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: 55.33  E-value: 9.47e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207185807 1384 LCLAEYSDGKYYRAKILGFSEVTPS---VKLLVRHVDFGSDDIIPLHKLRQLPASLHHFPCAAVYVKLAGFKP 1453
Cdd:cd20435     55 LCAVEDENNLYHRVKVLEITEKDDKtkpREVLVKFIDEGRVETVVVSQLLELPEELKSLPPQAVEVFLCNVKP 127
Tudor_TDRD15_rpt5 cd20440
fifth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 622-746 1.08e-08

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: 55.15  E-value: 1.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807  622 YPSVQPSLNVEVNAMVSHVNTPSDFYVQLVENTE-YPLLHSKLQDCYNQPKSnnecQVYCPSLSQACVA--FHDQEWSRV 698
Cdd:cd20440      1 YSSFNIKVGSEEEVYITHVYSPAKFYCQLDRNTEiLEALMEKIAEISKLFNS----QILDNCKTRLCLAkyFEDGQWYRA 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207185807  699 QVTGFPGGRMVEVRFVDFGYKRTLSVKDLRHIKDEFFVL---PEMALWCNL 746
Cdd:cd20440     77 LAHPVESSSHLSVYFVDYGNKQIVEKNEVLPIPDTAVDLlltPMQAIKCCL 127
Tudor_TDRD6_rpt2 cd20421
second Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 621-746 2.37e-08

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: 53.97  E-value: 2.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807  621 FYPSVQpsLNVEVNAMVSHVNTPSDFYVQL-VENTEYPLLHSKLQDCYNQpKSNNECQVYCPSLSQACVAF-HDQEWSR- 697
Cdd:cd20421      3 FYPQLQ--VGVTETVVVTEVTDPHRIFCQLrSLSQELKRLSESMHQYYEG-RVGSGYETRPEKLGSPCAARgSDGRWYRa 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207185807  698 -VQVTgFPGGRMVEVRFVDFGYKRTLSVKDLRHIKDEFFVLPEMALWCNL 746
Cdd:cd20421     80 vLQQV-FSANRVVEVLHVDYGRKEVVSVSNLRYLAPEYFRMPVVTYPCAL 128
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
 685-730 2.56e-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: 2.56e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1207185807  685 QACVAFH--DQEWSRVQVTGFPGGRMVEVRFVDFGYKRTLSVKDLRHI 730
Cdd:cd20379      3 DLCAAKYeeDGKWYRARVLEVLSNDKVEVFFVDYGNTETVPLSDLRPL 50
Tudor_TDRD11 cd20433
Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, ...
 1384-1437 3.21e-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: 52.30  E-value: 3.21e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1207185807 1384 LCLAEYS-DGKYYRAKILgfsEVTPSVKLLVRHVDFGSDDIIPLHKLRQLPASLH 1437
Cdd:cd20433     33 LCAAKFVeDGEWYRAKVE---KVEGDKKVHVLYIDYGNREVLPSTRLAALPPAFS 84
Tudor_TDRD15_rpt2 cd20437
second Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 631-748 6.23e-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: 52.42  E-value: 6.23e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807  631 VEVNAMVShvntPSDFYVQLVE-NTEYPLLHSKLQDCYNqpKSNNECQVYCPSLSQACVA-FHDQEWSRVQVTGFPGGRM 708
Cdd:cd20437      7 VKITAAVS----PSKFYCQLLSwEPELSKLTTQMTLHYE--SVSKELNPSCENFGLLCAAkGKDGQWHRGFLQQLLPPSQ 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1207185807  709 VEVRFVDFGYKRTLSVKDLRHIKDEFFVLPEMALWCNLND 748
Cdd:cd20437     81 VKVWFIDYGNSEAVSSHSVLKLPPDFFSLPLMSFPCSLSC 120
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
 1384-1432 1.05e-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: 49.82  E-value: 1.05e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207185807 1384 LCLAEYS-DGKYYRAKILgfsEVTPSVKLLVRHVDFGSDDIIPLHKLRQL 1432
Cdd:cd20379      4 LCAAKYEeDGKWYRARVL---EVLSNDKVEVFFVDYGNTETVPLSDLRPL 50
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
 679-734 1.18e-07

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: 49.58  E-value: 1.18e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207185807   679 YCPSLSQACVAFH-DQEWSRVQVTGFPGGRMVEVRFVDFGYKRTLSVKDLRHIKDEF 734
Cdd:smart00333    1 PTFKVGDKVAARWeDGEWYRARIVKVDGEQLYEVFFIDYGNEEVVPPSDLRQLPEEL 57
Tudor_TDRD7_rpt2 cd20428
second Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; ...
 634-760 1.37e-07

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: 52.06  E-value: 1.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807  634 NAMVSHVNTPSDFYVQLVENTEYPL--LHSKLQDCYNQPKSNNECQVYCPSLSQACVAFHDQEWSRVQVTGFPGGRMVEV 711
Cdd:cd20428      3 NVRVTNVCSDGTLYCQVPSKGLSKLneILDKIEYYFHSRQMTSEYFVSLPFCGKICLARYKGKWARVEITNVHSSRALDV 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207185807  712 RFVDFGYKRTLSVKDLRHIKDEFF----VLPEMALWCNLNDVISSQETWANEA 760
Cdd:cd20428     83 HFLDTGTVASVKVSELREIPPPFLreliSIPPQALKCCLADLPLNIGMWTPDA 135
Tudor_TDRD6_rpt4 cd20423
fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 686-750 6.94e-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: 48.25  E-value: 6.94e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207185807  686 ACVAFH--DQEWSRVQVTG-FPGGRMVEVRFVDFGYKRTLSVKDLRHIKDEFFVLPEMALWCNLNDVI 750
Cdd:cd20423      8 VCLAKYseDGKWCRALIDNvYEPVEMVEVTYVDYGNKELVSLKNLRSISEEFLKLKAQAFRCSLYNLI 75
RING-HC_RNF224 cd16565
RING finger, HC subclass, found in RING finger protein RNF224 and similar proteins; RNF224 is ...
 6-66 1.55e-06

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: 46.74  E-value: 1.55e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207185807    6 VTCKICGSPYTLpedeaVGNLPHVLLCGHIFCCTCLRALQSQGNV---ITCPECQMDTRTSEEG 66
Cdd:cd16565      1 LDCIICYSAYDL-----STRLPRRLYCGHTFCQACLKRLDTVINEqrwIPCPQCRQNTPTPRGG 59
Tudor_TDRD1_rpt2 cd20409
second Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 1357-1436 1.60e-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: 47.45  E-value: 1.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807 1357 ESMEETLEQVNENIENLSLLTDF--PIECLCLAEYS-DGKYYRAKILGfseVTPSVKLLVRHVDFGSDDIIPLHKLRQLP 1433
Cdd:cd20409      2 RQLAELQESLSAYCKVAPASSDFspAVGEVCCAQFTeDNQWYRASVLA---YSSEDSVLVGYIDFGNSEEVALSRLRPIP 78


                   ...
gi 1207185807 1434 ASL 1436
Cdd:cd20409     79 PSL 81
Tudor_TDRD4_rpt2 cd20415
second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 1385-1453 1.75e-06

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: 47.81  E-value: 1.75e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207185807 1385 CLAEYSDGKYYRAKILGFsevTPSVKLLVRHVDFGSDDIIPLHKLRQLPASLHHFPCAAVYVKLAGFKP 1453
Cdd:cd20415     31 CVALFEDGAWYRARIIGL---PGHREVEVKYVDFGNTATVTIKHVRKIKDDFLSLPEKARECRLAFIEP 96
Tudor_TDRD9 cd20431
Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is ...
 1356-1436 1.95e-06

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: 47.77  E-value: 1.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807 1356 DESMEETLEQVNENIeNLSLLTDFPIEC----LCLAEYSDG---KYYRAKILGFSEVTpsvkLLVRHVDFGSDDIIPLHK 1428
Cdd:cd20431     15 DENSSEILQQLTAEI-NQRQLVPLTTKPvpnlLCLAPFTDAdmkKYYRAKILYVSGSS----AEVFFVDYGNTSQVPSSL 89


                   ....*...
gi 1207185807 1429 LRQLPASL 1436
Cdd:cd20431     90 LREIPETL 97
Tudor_AtTudor1-like cd20443
Tudor domain found in Arabidopsis thaliana ribonuclease Tudor 1 (AtTudor1), ribonuclease Tudor ...
 1384-1453 2.74e-06

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: 47.85  E-value: 2.74e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207185807 1384 LCLAEYS-DGKYYRAKILGF---SEVTPSVKLLVRHVDFGSDDIIPLHKLRQLPASLHHFPCAAVYVKLAGFKP 1453
Cdd:cd20443     43 LVLAQFSaDNSWNRAMVVNAprqGTQSPKDEYEVFYIDYGNQETVPLSALRPLDPSVSSAPGLAQLCSLAHIKV 116
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
 1384-1433 5.86e-06

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: 44.96  E-value: 5.86e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1207185807  1384 LCLAEYSDGKYYRAKILgfsEVTPSVKLLVRHVDFGSDDIIPLHKLRQLP 1433
Cdd:smart00333    8 KVAARWEDGEWYRARIV---KVDGEQLYEVFFIDYGNEEVVPPSDLRQLP 54
Tudor_vreteno-like_rpt1 cd20444
first Tudor domain found in Drosophila melanogaster protein vreteno and similar proteins; ...
 1384-1436 6.50e-06

first Tudor domain found in Drosophila melanogaster protein vreteno and similar proteins; Vreteno is a gonad-specific protein essential for germline development to repress transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process in both germline and somatic gonadal tissues by mediating the repression of transposable elements during meiosis. Vreteno contains two 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: 410515  Cd Length: 55  Bit Score: 44.60  E-value: 6.50e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207185807 1384 LCLAEYsDGKYYRAKILGFSevTPSVKLLVRHVDFGSDDIIPLHKLRQLPASL 1436
Cdd:cd20444      6 MVIAKF-DGNHYRAIVLRVL--NPDLKILVRFVDFGNVEVMKLENLYECPEYL 55
Tudor_TDRD6_rpt7 cd20426
seventh Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 1351-1451 6.54e-06

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: 47.49  E-value: 6.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807 1351 CKLEQD--ESMEETLEQVNEN-IENLSLLTDFPIECLCLAEYS-DGKYYRAKILGfsevTPSVKLLVRHVDFGSDDIIPL 1426
Cdd:cd20426     16 CQFATEkiQCLAVKVQEAGEQvADRGNFIPSIYVGDPCIVKYSeDNHWYRALVTK----INDNLVSVRFVDYGNEEDVVR 91

                           90       100
                   ....*....|....*....|....*
gi 1207185807 1427 HKLRQLPASLHHFPCAAVYVKLAGF 1451
Cdd:cd20426     92 EQVRALPSELLKIPVQAFPCCLSGF 116
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
 8-56 7.05e-06

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: 44.42  E-value: 7.05e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 1207185807     8 CKICGSPYTlpedeavgNLPHVLLCGHIFCCTCLRALQSQGNvITCPEC 56
Cdd:smart00184    1 CPICLEEYL--------KDPVILPCGHTFCRSCIRKWLESGN-NTCPIC 40
Tudor_TDRD5 cd20419
Tudor domain found in Tudor domain-containing protein 5 (TDRD5) and similar proteins; TDRD5 is ...
 637-746 7.18e-06

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: 46.67  E-value: 7.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807  637 VSHVNTPSDFYVQLVENTEYPLLHS---KLQDCYNQPKSNNECQV--YCPSLSQACVAFH--DQEWSRVQVTGFPGGRMV 709
Cdd:cd20419      2 VEYIESPSQFYVRFYSKDTSEMLEDmmiEMRRCYSNEHVSERYVMpeAFIQPGQVCCVRIpeDVWWYRVIIHQVLNKQEV 81

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1207185807  710 EVRFVDFGYKRTLSVKDLRHIKDEFFVLPEMALWCNL 746
Cdd:cd20419     82 EVFYPDFGDIGTVQKSRLRFLKCCYSKLPAQAIPASL 118
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
 916-961 7.49e-06

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: 44.43  E-value: 7.49e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1207185807  916 MYCAV--NNTGVWERGQVCSVSTCGVAEVLRCDFGNTVKLHVDNLRPL 961
Cdd:cd20379      3 DLCAAkyEEDGKWYRARVLEVLSNDKVEVFFVDYGNTETVPLSDLRPL 50
Tudor_AKAP1 cd20407
Tudor domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; ...
 687-750 8.07e-06

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: 45.28  E-value: 8.07e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207185807  687 CVAFHDQEWSRVQVTG-FPGGRMVEVRFVDFG-YKRtLSVKDLRHIKDEFFVLPEMALWCNLNDVI 750
Cdd:cd20407     11 CAAPVMNAWYRAQVVGvFEETDEVEIKYLDYGgYER-VPVDDLRQIRSDFMTLPFQATECYLANIE 75
TUDOR pfam00567
Tudor domain;
394-534 8.59e-06

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 46.19  E-value: 8.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807  394 VVTTHIVNPGHFYVRYMAEHKLGQKLTKKISEFC-SGERSFFTFSDEITTGSLLFIswkDDMWCRVKVTELFQKECFqsv 472
Cdd:pfam00567    5 VVVSHIESPSTFYIQPKSDSKKLEKLTEELQEYYaSKPPESLPPAVGDGCVAAFSE---DGKWYRAKITESLDDGLV--- 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207185807  473 tkclasevsrlCVYFLDYGFFKgfSIPSdgglsglnECLRRpdgITLiEMANWAPLAIKCSL 534
Cdd:pfam00567   79 -----------EVLFIDYGNTE--TVPL--------SDLRP---LPP-ELESLPPQAIKCQL 115
Tudor_TDRD1_rpt3 cd20410
third Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 1154-1194 1.59e-05

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: 43.87  E-value: 1.59e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1207185807 1154 CAVMGTDMFWYRGQVQEVI-GGHVKVRYVDQGLVESIPVCHV 1194
Cdd:cd20410     10 CAFFSGDGNWYRAMVKEILpGGAVKVHFVDYGNVEEVTLDKL 51
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type ...
 7-56 1.81e-05

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: 43.24  E-value: 1.81e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207185807    7 TCKICGSPYtlpedeavgNLPHVLLCGHIFCCTCLRALQSQGNvITCPEC 56
Cdd:cd16449      2 ECPICLERL---------KDPVLLPCGHVFCRECIRRLLESGS-IKCPIC 41
mRING-HC-C3HC3D_TRIM23_C-IX cd16645
Modified RING finger, HC subclass (C3HC3D-type), found in tripartite motif-containing protein ...
 8-54 2.16e-05

Modified RING finger, HC subclass (C3HC3D-type), found in tripartite motif-containing protein 23 (TRIM23) and similar proteins; TRIM23, also known as ADP-ribosylation factor domain-containing protein 1, GTP-binding protein ARD-1, or RING finger protein 46 (RNF46), is an E3 ubiquitin-protein ligase belonging to the C-IX subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a modified C3HC3D-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as C-terminal ADP ribosylation factor (ARF) domains. TRIM23 is involved in nuclear factor (NF)-kappaB activation. It mediates atypical lysine 27 (K27)-linked polyubiquitin conjugation to NF-kappaB essential modulator NEMO, also known as IKKgamma, which plays an important role in the NF-kappaB pathway, and this conjugation is essential for TLR3- and RIG-I/MDA5-mediated antiviral innate and inflammatory responses. It also regulates adipocyte differentiation via stabilization of the adipogenic activator peroxisome proliferator-activated receptor gamma (PPARgamma) through atypical ubiquitin conjugation to PPARgamma. Moreover, TRIM23 interacts with and polyubiquitinates yellow fever virus (YFV) NS5 to promote its binding to STAT2 and trigger type I interferon (IFN-I) signaling inhibition.


Pssm-ID: 438307 [Multi-domain]  Cd Length: 50  Bit Score: 43.20  E-value: 2.16e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1207185807    8 CKICGSPYTLPEDEavgnLPHVLLCGHIFCCTCLRALQSQGNVITCP 54
Cdd:cd16645      4 CGVCEDVFSLQGDK----VPRLLLCGHTVCHDCLTRLPLHGRAVRCP 46
Tudor_TDRD6_rpt4 cd20423
fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 1385-1455 2.35e-05

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: 44.01  E-value: 2.35e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207185807 1385 CLAEYS-DGKYYRAKILGFSEVTPSVKllVRHVDFGSDDIIPLHKLRQLPASLHHFPCAAVYVKLAGFKPTN 1455
Cdd:cd20423      9 CLAKYSeDGKWCRALIDNVYEPVEMVE--VTYVDYGNKELVSLKNLRSISEEFLKLKAQAFRCSLYNLIQPS 78
zf-RING_UBOX pfam13445
RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.
 8-54 4.74e-05

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: 42.00  E-value: 4.74e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1207185807    8 CKICGSPYTLPedeavgnlphVLLCGHIFCCTCLRALQSQGNV-ITCP 54
Cdd:pfam13445    1 CPICLELFTDP----------VLPCGHTFCRECLEEMSQKKGGkFKCP 38
Tudor_TDRD15_rpt3 cd20438
third Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 1150-1222 4.89e-05

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: 44.77  E-value: 4.89e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207185807 1150 GVLGCAVMGTDMFWYRGQVQEVIGGHVKVRYVDQGLVESIPVCHVYPMV-LCEDVPQLCVPCQINGVLPIGKGW 1222
Cdd:cd20438     58 GLLCCARYSKDRHYYRAVITEVLDLKVSVYFLDFGNTDTVPFYDVKTLLpEFSELPALAMCCSLAHVFPVEEVW 131
Tudor_TDRD15_rpt2 cd20437
second Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 1118-1194 5.01e-05

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: 44.33  E-value: 5.01e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207185807 1118 MTHQAVCEFDRlrerlqQHIKTLPRQKNYnwkGVLgCAVMGTDMFWYRGQVQEV-IGGHVKVRYVDQGLVESIPVCHV 1194
Cdd:cd20437     32 LTTQMTLHYES------VSKELNPSCENF---GLL-CAAKGKDGQWHRGFLQQLlPPSQVKVWFIDYGNSEAVSSHSV 99
Tudor_TDRD1_rpt4 cd20411
fourth Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 1154-1197 6.26e-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: 43.97  E-value: 6.26e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1207185807 1154 CAVMGTDMFWYRGQVQEVIGGHVKVRYVDQGLVESIPVCHVYPM 1197
Cdd:cd20411     55 CARFTGDKNWYRAVVLETSDSEVKVLYADYGNTETLPLSRILPI 98
Tudor_TDRD6_rpt2 cd20421
second Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 869-964 8.14e-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: 43.95  E-value: 8.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807  869 VRVTHVTSPGNICVQLLQFDNQLKRIHDTLKNLFSKSEPQEMQWEAEMY---CAV-NNTGVWERGQVCSV-STCGVAEVL 943
Cdd:cd20421     15 VVVTEVTDPHRIFCQLRSLSQELKRLSESMHQYYEGRVGSGYETRPEKLgspCAArGSDGRWYRAVLQQVfSANRVVEVL 94

                           90       100
                   ....*....|....*....|.
gi 1207185807  944 RCDFGNTVKLHVDNLRPLHPD 964
Cdd:cd20421     95 HVDYGRKEVVSVSNLRYLAPE 115
zf-C3HC4 pfam00097
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a ...
 8-56 8.70e-05

Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a cysteine-rich domain of 40 to 60 residues that coordinates two zinc ions, and has the consensus sequence: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C where X is any amino acid. Many proteins containing a RING finger play a key role in the ubiquitination pathway.


Pssm-ID: 395049 [Multi-domain]  Cd Length: 40  Bit Score: 41.19  E-value: 8.70e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1207185807    8 CKICGSPYTlpedeavgNLPHVLLCGHIFCCTCLRALQSQGNViTCPEC 56
Cdd:pfam00097    1 CPICLEEPK--------DPVTLLPCGHLFCSKCIRSWLESGNV-TCPLC 40
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
 1163-1197 9.92e-05

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: 41.35  E-value: 9.92e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1207185807 1163 WYRGQVQEVI-GGHVKVRYVDQGLVESIPVCHVYPM 1197
Cdd:cd20379     15 WYRARVLEVLsNDKVEVFFVDYGNTETVPLSDLRPL 50
Tudor_TDRD1_rpt1 cd20408
first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 1125-1222 1.16e-04

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: 43.51  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807 1125 EFDRLRERLQQHIKTLPRQKNYN-WKGVLGCAVMGTDMFWYRGQVQEV--IGGHVKVRYVDQGLVESIPVCHVYPM-VLC 1200
Cdd:cd20408     24 SLVKLTSQLKKTYASVNNHKEYIpEVGEVCVAKYSEDQNWYRALVQTVdvQQKKAGVFYIDYGNEETVPLNRIQPLkKDI 103

                           90       100
                   ....*....|....*....|..
gi 1207185807 1201 EDVPQLCVPCQINGVLPIGKGW 1222
Cdd:cd20408    104 ELFPPCAIKCCLANVKPPSGSW 125
Tudor_TDRD7_rpt1 cd20427
first Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; ...
 658-746 1.23e-04

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: 42.42  E-value: 1.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807  658 LLHSKLQDCYNqpKSNNECQVYCPSLSQaCVAFHDQE--WSRVQVTGFPGGRmVEVRFVDFGYKRTLSVKDLRHIKDEFF 735
Cdd:cd20427      2 QMEDEMKEFYS--KSSTAMCLRSPSVGQ-LVAVKAEEdaWLRAQVIEVEEDK-VKVYYVDHGFSEVVERSKLFKLNKQFY 77

                           90
                   ....*....|.
gi 1207185807  736 VLPEMALWCNL 746
Cdd:cd20427     78 SLPFQATKCKL 88
Tudor_TDRD6_rpt5 cd20424
fifth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 1335-1448 1.28e-04

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: 43.26  E-value: 1.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807 1335 IRTPNEVFLCVLDKSL---CKLEQDEsmeETLEQVNENIENLSLlTDFPIEC------LCLAEYSDGKYYRAKILgfsEV 1405
Cdd:cd20424     10 IGSEEEVYITYVNDPWtfyCQLARNA---GVLDQLASAISRLSS-EIRKLELsvnpgtLCLAKYSDQHWYRGIII---TN 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1207185807 1406 TPSVKllVRHVDFGSDDIIPLHKLRQLPA---SLHHFPCAAVYVKL 1448
Cdd:cd20424     83 KNSTE--VFFVDYGNTEKVEKEDMLPIPSdayELLLLPMQAIKCSL 126
Tudor_TDRD1_rpt1 cd20408
first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 1332-1457 1.29e-04

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: 43.51  E-value: 1.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807 1332 VKHIRTPNEVFLCVLD----KSLCKLEQDesMEETLEQVNENIENLslltdfPIE-CLCLAEYS-DGKYYRAKIlgfSEV 1405
Cdd:cd20408      3 VTEFKNPGEFYIQIYTlevlESLVKLTSQ--LKKTYASVNNHKEYI------PEVgEVCVAKYSeDQNWYRALV---QTV 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207185807 1406 TPSVKLL-VRHVDFGSDDIIPLHKLRQLPASLHHFPCAAVYVKLAGFKPTNVS 1457
Cdd:cd20408     72 DVQQKKAgVFYIDYGNEETVPLNRIQPLKKDIELFPPCAIKCCLANVKPPSGS 124
Tudor_AKAP1 cd20407
Tudor domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; ...
 1380-1453 1.36e-04

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: 41.81  E-value: 1.36e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207185807 1380 PIE--CLCLAeYSDGKYYRAKILGFSEVTPSVklLVRHVDFGSDDIIPLHKLRQLPASLHHFPCAAVYVKLAGFKP 1453
Cdd:cd20407      4 PIEvgVICAA-PVMNAWYRAQVVGVFEETDEV--EIKYLDYGGYERVPVDDLRQIRSDFMTLPFQATECYLANIEP 76
Tudor_TDRD2 cd20412
Tudor domain found in Tudor domain-containing protein 2 (TDRD2) and similar proteins; TDRD2, ...
 691-745 1.64e-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: 41.90  E-value: 1.64e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1207185807  691 HDQEWSRVQVTGFPGGRMVEVRFVDFGYKRTLSVKDLRHIKDEFFVLPEMALWCN 745
Cdd:cd20412     41 HDGSWYRARVLGFLENGNLDLYFVDYGDSGYVPLEDLRALRSDFLSLPFQAIECS 95
zf-RING_5 pfam14634
zinc-RING finger domain;
8-57 2.59e-04

zinc-RING finger domain;


Pssm-ID: 434085 [Multi-domain]  Cd Length: 43  Bit Score: 40.10  E-value: 2.59e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207185807    8 CKICGSPYTLPEDeavgnlPHVLLCGHIFCCTCLRALQSQgnvITCPECQ 57
Cdd:pfam14634    2 CNKCFKELSKTRP------FYLTSCGHIFCEECLTRLLQE---RQCPICK 42
Tudor_ERCC6L2 cd20400
Tudor domain found in DNA excision repair protein ERCC-6-like 2 (ERCC6L2) and similar proteins; ...
 1384-1433 2.69e-04

Tudor domain found in DNA excision repair protein ERCC-6-like 2 (ERCC6L2) and similar 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. ERCC6L2 gene mutations have been associated with bone marrow failure that includes developmental delay and microcephaly. It contains an N-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: 410471  Cd Length: 59  Bit Score: 40.39  E-value: 2.69e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207185807 1384 LCLAEYS-DGKYYRAKILGFSEVTPSVKL-LVRHVDFGSDD--IIPLHKLRQLP 1433
Cdd:cd20400      6 RCLAPYSgDGKLYEAVIKSISTDENGKSFaVVKFLGYESDEdeKVPVSKLQKVK 59
RING-HC_RNF182 cd16555
RING finger, HC subclass, found in RING finger protein 182 (RNF182) and similar proteins; ...
 8-60 2.82e-04

RING finger, HC subclass, found in RING finger protein 182 (RNF182) and similar proteins; RNF182 is a brain-enriched E3 ubiquitin-protein ligase that stimulates E2-dependent polyubiquitination in vitro. It is upregulated in Alzheimer"s disease (AD) brains and neuronal cells exposed to injurious insults. It interacts with ATP6V0C and promotes its degradation by the ubiquitin-proteosome pathway, suggesting a very specific role in controlling the turnover of an essential component of the neurotransmitter release machinery. RNF182 contains an N-terminal C3HC4-type RING-HC finger, and a C-terminal transmembrane domain.


Pssm-ID: 438217 [Multi-domain]  Cd Length: 55  Bit Score: 40.11  E-value: 2.82e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207185807    8 CKICGSPYTLPEDEavgnlPHVLLCGHIFCCTCLRALQSQG----NVITCPECQMDT 60
Cdd:cd16555      4 CKICYNRYDLRQRR-----PKVLECCHRVCAKCLYKIVDLGdsspSVLVCPFCRFET 55
Tudor_TDRD1_rpt1 cd20408
first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 871-992 3.16e-04

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: 42.36  E-value: 3.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807  871 VTHVTSPGNICVQLLQFDN--QLKRIHDTLKNLFSKSEPQ-EMQWEAEMYCAVNNT--GVWERGQVCSVSTC-GVAEVLR 944
Cdd:cd20408      3 VTEFKNPGEFYIQIYTLEVleSLVKLTSQLKKTYASVNNHkEYIPEVGEVCVAKYSedQNWYRALVQTVDVQqKKAGVFY 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207185807  945 CDFGNTVKLHVDNLRPLHPD--LIGSFLLECNLSGVRPAGGrsTWTATAC 992
Cdd:cd20408     83 IDYGNEETVPLNRIQPLKKDieLFPPCAIKCCLANVKPPSG--SWSEECI 130
Tudor_TDRD11 cd20433
Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, ...
 687-735 3.22e-04

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: 40.75  E-value: 3.22e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207185807  687 CVA-F-HDQEWSRVQVTGFPGGRMVEVRFVDFGYKRTLSVKDLRHIKDEFF 735
Cdd:cd20433     34 CAAkFvEDGEWYRAKVEKVEGDKKVHVLYIDYGNREVLPSTRLAALPPAFS 84
Tudor_AKAP1 cd20407
Tudor domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; ...
 918-980 3.25e-04

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: 40.65  E-value: 3.25e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207185807  918 CAVNNTGVWERGQVCSVS-TCGVAEVLRCDFGNTVKLHVDNLRPLHPDLIGSFL--LECNLSGVRP 980
Cdd:cd20407     11 CAAPVMNAWYRAQVVGVFeETDEVEIKYLDYGGYERVPVDDLRQIRSDFMTLPFqaTECYLANIEP 76
Tudor_TDRD6_rpt6 cd20425
sixth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 869-966 3.31e-04

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: 41.67  E-value: 3.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807  869 VRVTHVTSPGNICVQLLQFDNQLKRIHDTLKNLFSKSEPQEMQW--EAEMYCAV-NNTGVWERGQVCSVSTCGVAEVLRC 945
Cdd:cd20425      4 VYVSHVNSPSDFYVQLAQDEDELSMISEKLNASKANDEEVECESlqLGDLICAEyPEDGLWYRAVVKEKIPNNLVSVQFI 83

                           90       100
                   ....*....|....*....|.
gi 1207185807  946 DFGNTVKLHVDNLRPLHPDLI 966
Cdd:cd20425     84 DYGNTSVVQPSKIHRLPKELL 104
RING-HC_RNF183-like cd16556
RING finger, HC subclass, found in RING finger protein RNF183, RNF223, RNF225 and similar ...
 8-61 4.75e-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: 39.66  E-value: 4.75e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207185807    8 CKICGSPYTlpedeAVGNLPHVLLCGHIFCCTCL----RALQSQGNVITCPECQMDTR 61
Cdd:cd16556      3 CSICFSSYD-----NTFKTPKLLDCGHTFCLECLarlsLASPPQAERVPCPLCRQPTV 55
Tudor_TDRD4_rpt2 cd20415
second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 1154-1197 6.39e-04

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: 40.50  E-value: 6.39e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1207185807 1154 CAVMGTDMFWYRGQVQEVIGG-HVKVRYVDQGLVESIPVCHVYPM 1197
Cdd:cd20415     31 CVALFEDGAWYRARIIGLPGHrEVEVKYVDFGNTATVTIKHVRKI 75
Tudor_TDRD6_rpt2 cd20421
second Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 1125-1214 7.36e-04

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: 41.26  E-value: 7.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807 1125 EFDRLRERLQQHIKTLPRQKNYNWKGVLG--CAVMGTDMFWYRGQVQEVIGGH--VKVRYVDQGLVESIPVCHVYPM-VL 1199
Cdd:cd20421     36 ELKRLSESMHQYYEGRVGSGYETRPEKLGspCAARGSDGRWYRAVLQQVFSANrvVEVLHVDYGRKEVVSVSNLRYLaPE 115

                           90
                   ....*....|....*
gi 1207185807 1200 CEDVPQLCVPCQING 1214
Cdd:cd20421    116 YFRMPVVTYPCALFG 130
Tudor_TDRD2 cd20412
Tudor domain found in Tudor domain-containing protein 2 (TDRD2) and similar proteins; TDRD2, ...
 1390-1444 7.50e-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: 40.36  E-value: 7.50e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1207185807 1390 SDGKYYRAKILGFsevTPSVKLLVRHVDFGSDDIIPLHKLRQLPASLHHFPCAAV 1444
Cdd:cd20412     41 HDGSWYRARVLGF---LENGNLDLYFVDYGDSGYVPLEDLRALRSDFLSLPFQAI 92
Tudor_TDRD1_rpt3 cd20410
third Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 1385-1436 7.79e-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: 39.25  E-value: 7.79e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207185807 1385 CLAEYS-DGKYYRAKILgfsEVTPSVKLLVRHVDFGSDDIIPLHKLRQLPASL 1436
Cdd:cd20410      9 CCAFFSgDGNWYRAMVK---EILPGGAVKVHFVDYGNVEEVTLDKLRKITSTF 58
RING-HC_RNF4 cd16533
RING finger, HC subclass, found in RING finger protein 4 (RNF4) and similar proteins; RNF4, ...
 5-57 9.14e-04

RING finger, HC subclass, found in RING finger protein 4 (RNF4) and similar proteins; RNF4, also known as small nuclear ring finger protein (SNURF), is a SUMO-targeted E3 ubiquitin-protein ligase with a pivotal function in the DNA damage response (DDR) by interacting with the deubiquitinating enzyme ubiquitin-specific protease 11 (USP11), a known DDR-component, and further facilitating DNA repair. It plays a novel role in preventing the loss of intact chromosomes and ensures the maintenance of chromosome integrity. Moreover, RNF4 is responsible for the UbcH5A-catalyzed formation of K48 chains that target SUMO-modified promyelocytic leukemia (PML) protein for proteasomal degradation in response to arsenic treatment. It also interacts with telomeric repeat binding factor 2 (TRF2) in a small ubiquitin-like modifier (SUMO)-dependent manner and preferentially targets SUMO-conjugated TRF2 for ubiquitination through SUMO-interacting motifs (SIMs). Furthermore, RNF4 can form a complex with a Ubc13-ubiquitin conjugate and Ube2V2. It catalyzes K63-linked polyubiquitination by the Ube2V2-Ubc13 (ubiquitin-loaded) complex. Meanwhile, RNF4 negatively regulates nuclear factor kappa B (NF-kappaB) signaling by down-regulating transforming growth factor beta (TGF-beta)-activated kinase 1 (TAK1)-TAK1-binding protein2 (TAB2). RNF4 contains four SIMs followed by a C3HC4-type RING-HC finger at the C-terminus.


Pssm-ID: 438195 [Multi-domain]  Cd Length: 57  Bit Score: 38.72  E-value: 9.14e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207185807    5 AVTCKICGSPYTlpEDEAVGNLPHVLLCGHIFCCTCLRalQSQGNVITCPECQ 57
Cdd:cd16533      3 TVSCPICMDGYS--EIVQSGRLIVSTECGHVFCSQCLR--DSLKNANTCPTCR 51
RING-HC_TRIM32_C-VII cd16587
RING finger, HC subclass, found in tripartite motif-containing protein 32 (TRIM32) and similar ...
 6-56 9.86e-04

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: 38.54  E-value: 9.86e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207185807    6 VTCKICGSPYTlpeDEAvgNLPHVLLCGHIFCCTCLRAL--QSQGNVITCPEC 56
Cdd:cd16587      1 LECPICLESFD---EGQ--LRPKLLHCGHTICEQCLEKLlaSLSINGVRCPFC 48
Tudor_TDRD6_rpt6 cd20425
sixth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 1150-1212 1.08e-03

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: 40.52  E-value: 1.08e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207185807 1150 GVLGCAVMGTDMFWYRGQVQEVIG-GHVKVRYVDQGLVESIPVCHVY--PMVLCEdVPQLCVPCQI 1212
Cdd:cd20425     51 GDLICAEYPEDGLWYRAVVKEKIPnNLVSVQFIDYGNTSVVQPSKIHrlPKELLS-IPALSIHCFL 115
zf-RING_2 pfam13639
Ring finger domain;
7-56 1.11e-03

Ring finger domain;


Pssm-ID: 433370 [Multi-domain]  Cd Length: 44  Bit Score: 38.16  E-value: 1.11e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207185807    7 TCKICGSPYTLPEDeavgnlPHVLLCGHIFCCTCLRALQSQGNviTCPEC 56
Cdd:pfam13639    2 ECPICLEEFEEGDK------VVVLPCGHHFHRECLDKWLRSSN--TCPLC 43
RING-HC_TRIM59_C-V cd16763
RING finger, HC subclass, found in tripartite motif-containing protein 59 (TRIM59) and similar ...
 3-57 1.22e-03

RING finger, HC subclass, found in tripartite motif-containing protein 59 (TRIM59) and similar proteins; TRIM59, also known as RING finger protein 104 (RNF104) or tumor suppressor TSBF-1, is a putative E3 ubiquitin-protein ligase that functions as a novel multiple cancer biomarker for immunohistochemical detection of early tumorigenesis. It is upregulated in gastric cancer and promotes gastric carcinogenesis by interacting with and targeting the P53 tumor suppressor for its ubiquitination and degradation. It also acts as a novel accessory molecule involved in cytotoxicity of BCG-activated macrophages (BAM). Moreover, TRIM59 may serve as a multifunctional regulator for innate immune signaling pathways. It interacts with ECSIT and negatively regulates nuclear factor-kappaB (NF- kappa B) and interferon regulatory factor (IRF)-3/7-mediated signal pathways. TRIM59 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. In addition, TRIM59 contains a C-terminal transmembrane domain.


Pssm-ID: 438419 [Multi-domain]  Cd Length: 56  Bit Score: 38.35  E-value: 1.22e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207185807    3 ETAVTCKICgspYTLPEDeavgnlPHVLLCGHIFCCTCLR-ALQSQGNV---------ITCPECQ 57
Cdd:cd16763      1 EEDLTCSVC---YSLFED------PRVLPCSHTFCRNCLEnILQVSGNFsiwrplrppLKCPNCR 56
Tudor_TDRD15_rpt7 cd20442
seventh Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 1152-1259 1.32e-03

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: 41.18  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807 1152 LGCAVMGTDMF-WYRGQVQEVIGGHVK--VRYVDQGLVESIPVCHVypMVLCEDV---PQLCVPCQINGVLPIGKgwqwD 1225
Cdd:cd20442     54 LECLAKSKKNLkWYRAVVEHLYPETEKmlVFFVDHGITEVVSMGNI--KQLSNDLlqiPRQAVLCRWNWPESSKE----L 127

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1207185807 1226 AVVLMKELLLGRSVNVQIMEHPKDpCGCVTVEIM 1259
Cdd:cd20442    128 SFEILWKSLAGKEVKLLFLSYSEA-DQLWEVEIL 160
RING-HC_RNF222 cd16564
RING finger, HC subclass, found in RING finger protein 222 (RNF222) and similar proteins; ...
 7-56 1.33e-03

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: 38.15  E-value: 1.33e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207185807    7 TCKICGSPYTLPedeavgnlPHVLLCGHIFCCTCLRAlQSQGNVITCPEC 56
Cdd:cd16564      2 ECPVCYEDFDDA--------PRILSCGHSFCEDCLVK-QLVSMTISCPIC 42
Tudor_TDRD15_rpt6 cd20441
sixth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 643-749 1.34e-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: 39.72  E-value: 1.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807  643 PSDFYVQLVENtEYPLLHskLQDCYNQPKSNNECQVYCPSLSQACVAFH---DQEWSRVQVTGFPGGRMVEVRFVDFGYK 719
Cdd:cd20441      2 PSRFFIQLSED-EKVILQ--LAEELNETSEKSRENAAVKLKVGDLVAAEydeDLALYRAVITAVLPGKSFKVEFIDYGNT 78

                           90       100       110
                   ....*....|....*....|....*....|
gi 1207185807  720 RTLSVKDLRHIKDEFFVLPEMALWCNLNDV 749
Cdd:cd20441     79 AVVDKSNIYTLQEKFLSLPRLSIPCSLSGV 108
RING-HC_TRIM65_C-IV cd16609
RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar ...
 3-66 1.47e-03

RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar proteins; TRIM65 is an E3 ubiquitin-protein ligase that interacts with the innate immune receptor MDA5, enhancing its ability to stimulate interferon-beta signaling. It functions as a potential oncogenic protein that negatively regulates p53 through ubiquitination, providing insight into the development of novel approaches targeting TRIM65 for non-small cell lung carcinoma (NSCLC) treatment, and also overcoming chemotherapy resistance. Moreover, TRIM65 negatively regulates microRNA-driven suppression of mRNA translation by targeting TNRC6 proteins for ubiquitination and degradation. TRIM65 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438271 [Multi-domain]  Cd Length: 58  Bit Score: 38.12  E-value: 1.47e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207185807    3 ETAVTCKICGSPYTLPEdeavgnlphVLLCGHIFCCTCLR--ALQSQGNVITCPECQMDTRTSEEG 66
Cdd:cd16609      1 EEELTCSICLGLYQDPV---------TLPCQHSFCRACIEdhWRQKDEGSFSCPECRAPFPEGPTL 57
Tudor_vreteno-like_rpt2 cd20445
second Tudor domain found in Drosophila melanogaster protein vreteno and similar proteins; ...
 918-966 1.68e-03

second Tudor domain found in Drosophila melanogaster protein vreteno and similar proteins; Vreteno is a gonad-specific protein essential for germline development to repress transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process in both germline and somatic gonadal tissues by mediating the repression of transposable elements during meiosis. Vreteno contains two 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: 410516  Cd Length: 56  Bit Score: 38.17  E-value: 1.68e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207185807  918 CAVNNTGVWERGqVCSVSTC-GVAEVLRCDFGNTVKLHVDNLRPLHPDLI 966
Cdd:cd20445      5 CIAKYMDKWYRA-VCLESVGdGRPTVLFCDYGNILMARLTDIRPFPPTFA 53
RING-HC_TRIM71_C-VII cd16589
RING finger, HC subclass, found in tripartite motif-containing protein 71 (TRIM71) and similar ...
 8-64 1.70e-03

RING finger, HC subclass, found in tripartite motif-containing protein 71 (TRIM71) and similar proteins; TRIM71, also known as protein lineage variant 41 (lin-41), is an E3 ubiquitin-protein ligase that may play essential roles in embryonic stem cells, cellular reprogramming and the timing of embryonic neurogenesis. It was first identified in the nematode Caenorhabditis elegans as a target of the differentiation-associated microRNA (miRNA) let-7 (lethal 7) and is therefore part of a heterochronic gene network that controls larval development. In humans, it regulates let-7 microRNA biogenesis via modulation of Lin28B protein polyubiquitination. TRIM71 localizes to cytoplasmic P-bodies and directly interacts with the miRNA pathway proteins Argonaute 2 (AGO2) and DICER. It represses miRNA activity by promoting degradative ubiquitination of AGO2. Moreover, TRIM71 associates with SHCBP1, a novel component of the fibroblast growth factor (FGF) signaling pathway, and regulates its non-degradative polyubiquitination. It is also involved in the post-transcriptional regulation of the CDKN1A, RBL1 and RBL2 or EGR1 mRNAs by mediating RNA-binding in embryonic stem cells. TRIM71 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.


Pssm-ID: 438251 [Multi-domain]  Cd Length: 91  Bit Score: 39.32  E-value: 1.70e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207185807    8 CK-ICGSPYTLPEDEAVGNL---------------PHVLLCGHIFCCTCLRALQSQGNV----ITCPECQMDTRTSE 64
Cdd:cd16589     15 CKeMCGSPAPLSSNSSTSSTssgggggsagaatrrLHVLPCLHAFCRQCLEAQRSPGAGpalkLRCPVCDQKVVLSE 91
RING-HC_SHPRH-like cd16569
RING finger, HC subclass, found in SNF2 histone-linker PHD finger RING finger helicase (SHPRH) ...
 7-60 2.17e-03

RING finger, HC subclass, found in SNF2 histone-linker PHD finger RING finger helicase (SHPRH) and similar proteins; SHPRH is a yeast RAD5 homolog found in mammals. It functions as an E3 ubiquitin-protein ligase that associates with proliferating cell nuclear antigen (PCNA), RAD18, and the ubiquitin-conjugating enzyme UBC13 (E2), and suppresses genomic instability by proliferating methyl methanesulfonate (MMS)-induced PCNA polyubiquitination. SHPRH contains a SWI/SNF helicase domain that is divided into N- and C-terminal parts by an insertion of a linker histone domain (H15), a PHD-finger, and a C3HC4-type RING-HC finger involved in the poly-ubiquitination of PCNA. This subfamily also includes tripartite motif-containing protein 15 (TRIM15). TRIM15, also known as RING finger protein 93 (RNF93), zinc finger protein 178 (ZNF178), or zinc finger protein B7 (ZNFB7), is a focal adhesion protein that regulates focal adhesion disassembly. It localizes to focal contacts in a myosin-II-independent manner by an interaction between its coiled-coil domain and the LD2 motif of paxillin. TRIM15 can also associate with coronin 1B, cortactin, filamin binding LIM protein1, and vasodilator-stimulated phosphoprotein, which are involved in actin cytoskeleton dynamics. As an additional component of the integrin adhesome, it regulates focal adhesion turnover and cell migration. TRIM15 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438231 [Multi-domain]  Cd Length: 53  Bit Score: 37.71  E-value: 2.17e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207185807    7 TCKICGSPYtlpEDEAVgnlphVLLCGHIFCCTCLRAL-----QSQGNVITCPECQMDT 60
Cdd:cd16569      3 PCPICARPL---GKQWS-----VLPCGHCFCLECIAILidqyaQSRRRSLKCPICRETT 53
RING-HC_PEX2 cd16526
RING finger, HC subclass, found in peroxin-2 (PEX2) and similar proteins; PEX2, also known as ...
 7-56 2.33e-03

RING finger, HC subclass, found in peroxin-2 (PEX2) and similar proteins; PEX2, also known as peroxisome biogenesis factor 2, 35 kDa peroxisomal membrane protein, peroxisomal membrane protein 3, peroxisome assembly factor 1 (PAF-1), or RING finger protein 72 (RNF72), is an integral peroxisomal membrane protein with two transmembrane regions and a C3HC4-type RING-HC finger within its cytoplasmically exposed C-terminus. It may be involved in the biogenesis of peroxisomes, as well as in peroxisomal matrix protein import. Mutations in the PEX2 gene are the primary defect in a subset of patients with Zellweger syndrome and related peroxisome biogenesis disorders. Moreover, PEX2 functions as an E3-ubiquitin ligase that mediates the UBC4-dependent polyubiquitination of PEX5, a key player in peroxisomal matrix protein import, to control PEX5 receptor recycling or degradation.


Pssm-ID: 438189 [Multi-domain]  Cd Length: 49  Bit Score: 37.36  E-value: 2.33e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207185807    7 TCKICGspytlpEDEAvgNLPHVLLCGHIFCCTCLRALQSQGNVITCPEC 56
Cdd:cd16526      3 ECAICG------EWPT--NNPYSTGCGHVYCYYCIKSNLLADDSFTCPRC 44
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
 915-965 2.93e-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: 37.25  E-value: 2.93e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1207185807   915 EMYCAVNNTGVWERGQVCSVSTCGVAEVLRCDFGNTVKLHVDNLRPLHPDL 965
Cdd:smart00333    7 DKVAARWEDGEWYRARIVKVDGEQLYEVFFIDYGNEEVVPPSDLRQLPEEL 57
mRING-HC-C3HC3D_arc-1-like cd23124
Modified RING finger, HC subclass (C3HC3D-type), found in Caenorhabditis elegans putative ...
 7-55 3.17e-03

Modified RING finger, HC subclass (C3HC3D-type), found in Caenorhabditis elegans putative GTP-binding protein trim-23 homolog (arc-1) and similar proteins; arc-1, also called RING-type E3 ubiquitin transferase arc-1, is an E3 ubiquitin-protein ligase that mediates E2-dependent protein ubiquitination. arc-1 contains a modified C3HC3D-type RING-HC finger.


Pssm-ID: 438486 [Multi-domain]  Cd Length: 55  Bit Score: 37.09  E-value: 3.17e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207185807    7 TCKICGSPYTLPEDEAVgnlPHVLL-CGHIFCCTCLRALQSQGNV-ITCPE 55
Cdd:cd23124      3 ECGICQQEYSADDPLLI---PRILTeCGHTICTNCAGTILGQSSGsIFCPF 50
Tudor_TDRD11 cd20433
Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, ...
 1125-1197 3.34e-03

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: 38.05  E-value: 3.34e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207185807 1125 EFDRLRERLQQHIK-TLPRQKNYNWK-GVLGCAVMGTDMFWYRGQVQEVIGGH-VKVRYVDQGLVESIPVCHVYPM 1197
Cdd:cd20433      4 QLEKLMEKLRFEIAsNPPLPGSYTPRkGDLCAAKFVEDGEWYRAKVEKVEGDKkVHVLYIDYGNREVLPSTRLAAL 79
RING-HC_TRIM69_C-IV cd16611
RING finger, HC subclass, found in tripartite motif-containing protein 69 (TRIM69) and similar ...
 27-58 3.49e-03

RING finger, HC subclass, found in tripartite motif-containing protein 69 (TRIM69) and similar proteins; TRIM69, also known as RFP-like domain-containing protein trimless or RING finger protein 36 (RNF36), is a testis E3 ubiquitin-protein ligase that plays a specific role in apoptosis and may also play an important role in germ cell homeostasis during spermatogenesis. TRIM69 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438273 [Multi-domain]  Cd Length: 59  Bit Score: 37.43  E-value: 3.49e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1207185807   27 PHVLLCGHIFCCTCLRAL--QSQGNViTCPECQM 58
Cdd:cd16611     17 PVMLSCGHNFCQSCITGFweLQAEDT-TCPECRE 49
Tudor_TDRD15_rpt3 cd20438
third Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 1384-1449 3.78e-03

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: 39.38  E-value: 3.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807 1384 LCLAEYS-DGKYYRAKIlgfSEVTpSVKLLVRHVDFGSDDIIPLHKLR-------QLPA-----SLHH-FPCAAVYVKLA 1449
Cdd:cd20438     60 LCCARYSkDRHYYRAVI---TEVL-DLKVSVYFLDFGNTDTVPFYDVKtllpefsELPAlamccSLAHvFPVEEVWTKNA 135
RING-HC_TRIM13_like_C-V cd16581
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM13, TRIM59 and ...
 6-56 4.19e-03

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM13, TRIM59 and similar proteins; TRIM13 and TRIM59, two closely related tripartite motif-containing proteins, belong 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, followed by a C-terminal transmembrane domain. TRIM13, also known as B-cell chronic lymphocytic leukemia tumor suppressor Leu5, leukemia-associated protein 5, putative tumor suppressor RFP2, RING finger protein 77 (RNF77), or Ret finger protein 2, is an endoplasmic reticulum (ER) membrane anchored E3 ubiquitin-protein ligase that interacts with proteins localized to the ER, including valosin-containing protein (VCP), a protein indispensable for ER-associated degradation (ERAD). TRIM59, also known as RING finger protein 104 (RNF104) or tumor suppressor TSBF-1, is a putative E3 ubiquitin-protein ligase that functions as a novel multiple cancer biomarker for immunohistochemical detection of early tumorigenesis.


Pssm-ID: 438243 [Multi-domain]  Cd Length: 50  Bit Score: 36.72  E-value: 4.19e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207185807    6 VTCKICGSpytlpedeaVGNLPHVLLCGHIFCCTCLRAL-QSQGNV----ITCPEC 56
Cdd:cd16581      3 LTCSICYN---------IFDDPKILPCSHTFCKNCLEKLlAASGYYllasLKCPTC 49
Tudor_SpSPF30-like cd20446
Tudor domain found in Schizosaccharomyces pombe splicing factor spf30 (SpSPF30) and similar ...
 1384-1432 4.81e-03

Tudor domain found in Schizosaccharomyces pombe splicing factor spf30 (SpSPF30) and similar proteins; SpSPF30, also called survival of motor neuron-related-splicing factor 30, is necessary for spliceosome assembly. It contains 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: 410517  Cd Length: 56  Bit Score: 36.70  E-value: 4.81e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207185807 1384 LCLAEY--SDGKYYRAKILGFSEVTPSVKLLVRHVDFGSDDIIPLHKLRQL 1432
Cdd:cd20446      6 VVMARWksGDGKFYPARITSITGSSINPIYTVKFLDYGEIDTVYLKDIRPL 56
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 642-738 5.52e-03

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: 38.77  E-value: 5.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807  642 TPSDFYVQLVE------------NTEYPLLHSKLQDCYnqPKSNNECQVYCPSLSQACVAFHDQ-EWSRVQVTGFP---- 704
Cdd:cd20435      1 DATHYSARILEhrssdgevtksmSSTYLKLSMKLNMYY--SDPSNRILHGKVKVGDLCAVEDENnLYHRVKVLEITekdd 78

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1207185807  705 --GGRMVEVRFVDFGYKRTLSVKDLRHIKDEFFVLP 738
Cdd:cd20435     79 ktKPREVLVKFIDEGRVETVVVSQLLELPEELKSLP 114
mRING-C3HGC3_RFWD3 cd16450
Modified RING finger, C3HGC3-type, found in RING finger and WD repeat domain-containing ...
 5-57 6.34e-03

Modified RING finger, C3HGC3-type, found in RING finger and WD repeat domain-containing protein 3 (RFWD3) and similar proteins; RFWD3, also known as RING finger protein 201 (RNF201) or FLJ10520, is an E3 ubiquitin-protein ligase that forms a complex with Mdm2 and p53 to synergistically ubiquitinate p53 and acts as a positive regulator of p53 stability in response to DNA damage. It is phosphorylated by checkpoint kinase ATM/ATR and the phosphorylation mutant fails to stimulate p53 ubiquitination. RFWD3 also functions as a novel replication protein A (RPA)-associated protein involved in DNA replication checkpoint control. RFWD3 contains an N-terminal SQ-rich region followed by a RING finger domain that exhibits robust E3 ubiquitin ligase activity toward p53, a coiled-coil domain and three WD40 repeats in the C-terminus, the latter two of which may be responsible for protein-protein interaction. The RING finger in this family is a modified C3HGC3-type RING finger, but not a canonical C3H2C3-type RING-H2 finger or C3HC4-type RING-HC finger.


Pssm-ID: 438114 [Multi-domain]  Cd Length: 61  Bit Score: 36.44  E-value: 6.34e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207185807    5 AVTCKICGSPYTLPEDEAVGNLPhvllCGHIFCCTCL-RALQSQGNviTCPECQ 57
Cdd:cd16450      2 GNTCPICFEPWTSSGEHRLVSLK----CGHLFGYSCIeKWLKGKGK--KCPQCN 49
RING-HC_ScPSH1-like cd16568
RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated ...
 26-64 7.07e-03

RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated protein 1 (ScPSH1) and similar proteins; ScPSH1 is a Cse4-specific E3 ubiquitin ligase that interacts with the kinetochore protein Pat1 and targets the degradation of budding yeast centromeric histone H3 variant, CENP-ACse4, which is essential for faithful chromosome segregation. ScPSH1 contains a C3HC4-type RING-HC finger and a DNA directed RNA polymerase domain.


Pssm-ID: 438230 [Multi-domain]  Cd Length: 54  Bit Score: 36.19  E-value: 7.07e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1207185807   26 LPHVLLCGHIFCCTCLRALQSQGNVITCPECQMDTRTSE 64
Cdd:cd16568     16 EPMVTTCGHTYCYTCLNTWFKSNRSLSCPDCRTKITTQP 54
Tudor_TDRD4_rpt3 cd20416
third Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 659-742 7.53e-03

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: 37.08  E-value: 7.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807  659 LHSKLQDCYNqpKSNNECQVYCPSLSQACVAFHDQEWSRVQVTGFPGGRMVEVRFVDFGYKRTLSVKDLRHIKDEFFVLP 738
Cdd:cd20416      1 LQEKMIAEYE--NSKPEPVKWENDMHCAVQIQDKKQWRRGQIIRVVSDTLVEVFLYDFGNKEVVNIDCLRKLEENLKTIG 78


                   ....
gi 1207185807  739 EMAL 742
Cdd:cd20416     79 KLAL 82
Tudor_SPF30 cd20399
Tudor domain found in survival of motor neuron-related-splicing factor 30 (SPF30) and similar ...
 1385-1435 7.65e-03

Tudor domain found in survival of motor neuron-related-splicing factor 30 (SPF30) and similar proteins; 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. Overexpression of SPF30 causes apoptosis. It contains 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: 410470 [Multi-domain]  Cd Length: 55  Bit Score: 36.13  E-value: 7.65e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207185807 1385 CLAEYS-DGKYYRAKILGFSEvtpSVKLLVRHVDFGSDDIIPLHKLRQLPAS 1435
Cdd:cd20399      7 CMAVWSeDGQYYEATIEEISE---DGTCTVTFDGYGNTEVTPLSQLKPREEG 55
Tudor_SMN_SPF30-like cd21182
Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing ...
 1385-1432 8.20e-03

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: 36.08  E-value: 8.20e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1207185807 1385 CLAEYS-DGKYYRAKILgfSEVTPSVKLLVRHVDFGSDDIIPLHKLRQL 1432
Cdd:cd21182      4 CLAPYSdDGKYYEATIE--EITEESDTATVVFDGYGNSEEVPLSDLKPL 50
Tudor_TDRD6_rpt2 cd20421
second Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 1329-1442 8.42e-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: 38.17  E-value: 8.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185807 1329 PAKVKHIRTPNEVFlCVLdKSLCklEQDESMEETLEQVNENIENLSLLTDFPI-ECLCLAEYSDGKYYRAKILgfsEVTP 1407
Cdd:cd20421     14 TVVVTEVTDPHRIF-CQL-RSLS--QELKRLSESMHQYYEGRVGSGYETRPEKlGSPCAARGSDGRWYRAVLQ---QVFS 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1207185807 1408 SVKL-LVRHVDFGSDDIIPLHKLRQLPASLHH-----FPCA 1442
Cdd:cd20421     87 ANRVvEVLHVDYGRKEVVSVSNLRYLAPEYFRmpvvtYPCA 127
RING-HC_RNF208 cd16559
RING finger, HC subclass, found in RING finger protein 208 (RNF208) and similar proteins; ...
 8-60 8.63e-03

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: 36.06  E-value: 8.63e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207185807    8 CKICGSPYTLpedeaVGNLPHVLLCGHIFCCTCLRALQS---QGNVITCPECQMDT 60
Cdd:cd16559      4 CPTCGHSYNF-----TNKRPRILSCLHSVCEECLQILYEscpKYKFISCPTCKRET 54
Tudor_ZGPAT cd20384
Tudor domain found in zinc finger CCCH-type with G patch domain-containing protein (ZGPAT) and ...
 1372-1426 9.03e-03

Tudor domain found in zinc finger CCCH-type with G patch domain-containing protein (ZGPAT) and similar proteins; ZGPAT, also called ZIP, G patch domain-containing protein 6 (GPATC6), GPATCH6, zinc finger CCCH domain-containing protein 9 (ZC3HDC9), ZC3H9, or zinc finger and G patch domain-containing protein, is a transcription repressor that specifically binds the 5'-GGAG[GA]A[GA]A-3' consensus sequence. It represses transcription by recruiting the chromatin multiprotein complex NuRD to target promoters. It contains 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: 410455  Cd Length: 55  Bit Score: 36.05  E-value: 9.03e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207185807 1372 NLSLLTdfpIECLCLAEYSDGKYYRAKILGFSEV-TPSVKLLVR--HVDFGSDDIIPL 1426
Cdd:cd20384      1 DFSSLK---EGSRCLAKYDDGLWYPATVTDIDEDgKYTVKFDSYgeVAVVELDDILPL 55
 
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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