E3 ubiquitin-protein ligase RNF152 C-terminus; This family represents the C-terminal region of the E3 ubiquitin ligase RNF152 containing the hydrophobic transmembrane domain, responsible for the lysosomal localization of the protein as well as its ubiquitination activity. This protein polyubiquitinates several proteins and itself, which leads to proteasome degradation. It has been shown that RNF152 has also pro-apoptotic activity, dependent on its RING finger and transmembrane domains. In addition, the transmembrane domain of RNF152 is necessary for negative regulation of the mTORC1 pathway in an amino-acid-sensitive manner, as it mediates RNF152-RagA interaction and RagA ubiquitination.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309406163  67 SQLPDDPEVLAVIAIPHTSEHTPVFIKLPSNGCYMLPLPISKERALLPGDMGCRLLPGSQQKSVTVVTIPaEQQPLQGGA 146
Cdd:pfam19325   1 SQLPDDPDVLAVISVPHTSEHTPVFIRLPSNGCYMLPLPVSKEGALLPGDLGCRLLPGSQQKSVGVVTIA-EQQPLQGHD 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2309406163 147 PQEAAEEEQDRRGVVKSSTWSGVCTVILVACVLVFLLGIVLHNMSCISKRFTVISCG 203
Cdd:pfam19325  80 GLEAGEEEGERRGGVKSSTWTGVCTVILVACVLLFLLGIVLHNMSCISKRFTVISCG 136

E3 ubiquitin-protein ligase RNF152 C-terminus; This family represents the C-terminal region of the E3 ubiquitin ligase RNF152 containing the hydrophobic transmembrane domain, responsible for the lysosomal localization of the protein as well as its ubiquitination activity. This protein polyubiquitinates several proteins and itself, which leads to proteasome degradation. It has been shown that RNF152 has also pro-apoptotic activity, dependent on its RING finger and transmembrane domains. In addition, the transmembrane domain of RNF152 is necessary for negative regulation of the mTORC1 pathway in an amino-acid-sensitive manner, as it mediates RNF152-RagA interaction and RagA ubiquitination.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309406163  67 SQLPDDPEVLAVIAIPHTSEHTPVFIKLPSNGCYMLPLPISKERALLPGDMGCRLLPGSQQKSVTVVTIPaEQQPLQGGA 146
Cdd:pfam19325   1 SQLPDDPDVLAVISVPHTSEHTPVFIRLPSNGCYMLPLPVSKEGALLPGDLGCRLLPGSQQKSVGVVTIA-EQQPLQGHD 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2309406163 147 PQEAAEEEQDRRGVVKSSTWSGVCTVILVACVLVFLLGIVLHNMSCISKRFTVISCG 203
Cdd:pfam19325  80 GLEAGEEEGERRGGVKSSTWTGVCTVILVACVLLFLLGIVLHNMSCISKRFTVISCG 136

DNA repair protein rad18; All proteins in this family for which functions are known are involved in nucleotide excision repair.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2309406163   7 DSLLECQICFNYYsprRRPKLLDCKHTCCSVCLQqmRTSQKDVRCPWCR 55
Cdd:TIGR00599  24 DTSLRCHICKDFF---DVPVLTSCSHTFCSLCIR--RCLSNQPKCPLCR 67

RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2309406163   7 DSLLECQICFNYYsprRRPKLLDCKHTCCSVCLQQMRTSQKDvrCPWCR 55
Cdd:COG5432    23 DSMLRCRICDCRI---SIPCETTCGHTFCSLCIRRHLGTQPF--CPVCR 66

E3 ubiquitin-protein ligase RNF152 C-terminus; This family represents the C-terminal region of the E3 ubiquitin ligase RNF152 containing the hydrophobic transmembrane domain, responsible for the lysosomal localization of the protein as well as its ubiquitination activity. This protein polyubiquitinates several proteins and itself, which leads to proteasome degradation. It has been shown that RNF152 has also pro-apoptotic activity, dependent on its RING finger and transmembrane domains. In addition, the transmembrane domain of RNF152 is necessary for negative regulation of the mTORC1 pathway in an amino-acid-sensitive manner, as it mediates RNF152-RagA interaction and RagA ubiquitination.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309406163  67 SQLPDDPEVLAVIAIPHTSEHTPVFIKLPSNGCYMLPLPISKERALLPGDMGCRLLPGSQQKSVTVVTIPaEQQPLQGGA 146
Cdd:pfam19325   1 SQLPDDPDVLAVISVPHTSEHTPVFIRLPSNGCYMLPLPVSKEGALLPGDLGCRLLPGSQQKSVGVVTIA-EQQPLQGHD 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2309406163 147 PQEAAEEEQDRRGVVKSSTWSGVCTVILVACVLVFLLGIVLHNMSCISKRFTVISCG 203
Cdd:pfam19325  80 GLEAGEEEGERRGGVKSSTWTGVCTVILVACVLLFLLGIVLHNMSCISKRFTVISCG 136

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2309406163  10 LECQICFNYYSPR-RRPKLLDCKHTCCSVCLQQM----RTSQKDVRCPWCRGVTKLP 61
Cdd:cd16556     1 LECSICFSSYDNTfKTPKLLDCGHTFCLECLARLslasPPQAERVPCPLCRQPTVLP 57

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2309406163  10 LECQICFNYYSP-RRRPKLLDCKHTCCSVCLQQMR--TSQKDVRCPWCRGV 57
Cdd:cd16587     1 LECPICLESFDEgQLRPKLLHCGHTICEQCLEKLLasLSINGVRCPFCRKV 51

RING finger, HC subclass, found in SH3 domain-containing RING finger protein 2 (SH3RF2) and similar proteins; SH3RF2, also known as heart protein phosphatase 1-binding protein (HEPP1), plenty of SH3s (POSH)-eliminating RING protein (POSHER), protein phosphatase 1 regulatory subunit 39, or RING finger protein 158 (RNF158), is a putative E3 ubiquitin-protein ligase that acts as an anti-apoptotic regulator for the c-Jun N-terminal kinase (JNK) pathway by binding to and promoting the proteasomal degradation of SH3RF1 (or POSH), a scaffold protein that is required for pro-apoptotic JNK activation. It may also play a role in cardiac functions together with protein phosphatase 1. SH3RF2 contains an N-terminal C3HC4-type RING-HC finger responsible for the E3 ligase activity and four Src Homology 3 (SH3) domains, which are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2309406163  10 LECQICFNYYSPRrrPKLLDCKHTCCSVCLQQMRTSQKDVRCPWCR 55
Cdd:cd16749     1 LECPVCFEKLDVT--AKVLPCQHTFCKPCLQRIFKARKELRCPECR 44

RING finger, HC subclass, found in Caenorhabditis elegans RING finger protein NHL-1 and similar proteins; NHL-1 functions as an E3 ubiquitin-protein ligase in the presence of both UBC-13 and UBC-1 within the ubiquitin pathway of Caenorhabditis elegans. It acts in chemosensory neurons to promote stress resistance in distal tissues by the transcription factor DAF-16 activation but is dispensable for the activation of heat shock factor 1 (HSF-1). NHL-1 belongs to the TRIM (tripartite motif)-NHL 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 domain, as well as an 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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2309406163   7 DSLLECQICFNYYsprRRPKLLDCKHT-CCSVCLQQM-RTSQKDVRCPWCR 55
Cdd:cd16524     3 EQLLTCPICLDRY---RRPKLLPCQHTfCLSPCLEGLvDYVTRKLKCPECR 50

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

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2309406163  11 ECQIC-FNYYSPRRRPKLLDCKHTCCSVCLQQM--RTSQKDVRCPWCRGVTK 59
Cdd:cd23140     3 ECSVCsEGYNEDERVPLLLQCGHTFCKDCLSQMfiRCTDLTLKCPRCRQSVL 54

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2309406163  10 LECQICFNYYsprRRPKLLDCKHTCCSVCLQQMRTSQKdVRCPWC 54
Cdd:cd16449     1 LECPICLERL---KDPVLLPCGHVFCRECIRRLLESGS-IKCPIC 41

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2309406163  10 LECQICFNYYS-PRRRPKLLDCKHTCCSVCLQQMRT---SQKDVRCPWCRGVTKLPPG 63
Cdd:cd16565     1 LDCIICYSAYDlSTRLPRRLYCGHTFCQACLKRLDTvinEQRWIPCPQCRQNTPTPRG 58

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2309406163   8 SLLECQICFNYYSprrRPKLLDCKHTCCSVCLQQMRTSQKDVRCPWCR 55
Cdd:cd16568     3 ETQECIICHEYLY---EPMVTTCGHTYCYTCLNTWFKSNRSLSCPDCR 47

RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2309406163   7 DSLLECQICFNYYsprRRPKLLDCKHTCCSVCLQQMRTSQKDvrCPWCR 55
Cdd:COG5432    23 DSMLRCRICDCRI---SIPCETTCGHTFCSLCIRRHLGTQPF--CPVCR 66

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2309406163  10 LECQICFNYYsprRRPKLLDCKHTCCSVCLQQM--RTSQKDVRCPWCRGVTKLPPG 63
Cdd:cd16609     4 LTCSICLGLY---QDPVTLPCQHSFCRACIEDHwrQKDEGSFSCPECRAPFPEGPT 56

Ring finger domain;

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2309406163  11 ECQICFNYYSPRRRPKLLDCKHTCCSVCLQQMRTSQKdvRCPWCR 55
Cdd:pfam13639   2 ECPICLEEFEEGDKVVVLPCGHHFHRECLDKWLRSSN--TCPLCR 44

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2309406163  10 LECQICFNYYsprRRPKLLDCKHTCCSVCLQQM---RTSQKDVRCPWCR 55
Cdd:cd16579     5 LRCPGCKAEY---KCPKLLPCLHTVCSGCLEALaeqASETTEFQCPICK 50

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2309406163  10 LECQIC-FNYYSPRRRPKLLDCKHTCCSVCLQQM---RTSQKDVRCPWCRGVTKL 60
Cdd:cd16559     2 LLCPTCgHSYNFTNKRPRILSCLHSVCEECLQILyesCPKYKFISCPTCKRETVL 56

RING finger, HC subclass, found in SH3 domain-containing RING finger proteins SH3RF1, SH3RF2, SH3RF3, and similar proteins; SH3RF1, also known as plenty of SH3s (POSH), RING finger protein 142 (RNF142), or SH3 multiple domains protein 2 (SH3MD2), is a trans-Golgi network-associated pro-apoptotic scaffold protein with E3 ubiquitin-protein ligase activity. SH3RF2, also known as heart protein phosphatase 1-binding protein (HEPP1), plenty of SH3s (POSH)-eliminating RING protein (POSHER), protein phosphatase 1 regulatory subunit 39, or RING finger protein 158 (RNF158), is a putative E3 ubiquitin-protein ligase that acts as an anti-apoptotic regulator for the c-Jun N-terminal kinase (JNK) pathway by binding to and promoting the proteasomal degradation of SH3RF1 (or POSH) that is required for pro-apoptotic JNK activation. SH3RF3, also known as plenty of SH3s 2 (POSH2) or SH3 multiple domains protein 4 (SH3MD4), is a scaffold protein with E3 ubiquitin-protein ligase activity. It was identified in the screen for interacting partners of p21-activated kinase 2 (PAK2) and may play a role in regulating c-Jun N-terminal kinase (JNK) mediated apoptosis in certain conditions. Members of this subfamily contain an N-terminal C3HC4-type RING-HC finger responsible for the E3 ligase activity and four Src Homology 3 (SH3) domains, which are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2309406163  10 LECQICFNYYSprRRPKLLDCKHTCCSVCLQQMRTSQKDVRCPWCR 55
Cdd:cd16570     1 LECPVCLERLD--VSAKVLPCQHTFCKRCLQIIVASRGELRCPECR 44

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2309406163  11 ECQICFNYYspRRRPKLLDCKHTCCSVCLQQMrTSQKDVRCPWCRGVTKLP 61
Cdd:cd16564     2 ECPVCYEDF--DDAPRILSCGHSFCEDCLVKQ-LVSMTISCPICRRVTFIS 49

RING finger, HC subclass, found in tripartite motif-containing protein TRIM2, TRIM3, and similar proteins; TRIM2, also known as RING finger protein 86 (RNF86), is an E3 ubiquitin-protein ligase that ubiquitinates the neurofilament light chain, a component of the intermediate filament in axons. Loss of function of TRIM2 results in early-onset axonal neuropathy. TRIM3, also known as brain-expressed RING finger protein (BERP), RING finger protein 97 (RNF97), or RING finger protein 22 (RNF22), is an E3 ubiquitin-protein ligase involved in the pathogenesis of various cancers. It also plays an important role in the central nervous system (CNS). In addition, TRIM3 may be involved in vesicular trafficking via its association with the cytoskeleton-associated-recycling or transport (CART) complex that is necessary for efficient transferrin receptor recycling, but not for epidermal growth factor receptor (EGFR) degradation. Both TRIM2 and TRIM3 belong 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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2309406163   9 LLECQICFNYYsprRRPKLLDCKHTCCSVCLQQMRTSQK-DVRCPWCR 55
Cdd:cd16586     1 FLSCGICLERY---KNPKVLPCLHTFCERCLQNYIPAESlSLSCPVCR 45