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Conserved domains on  [gi|9506663|ref|NP_061935|]
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E3 ubiquitin-protein ligase RNF186 [Homo sapiens]

Protein Classification

RING finger protein( domain architecture ID 13010596)

RING finger protein such as E3 ubiquitin protein ligase, which mediates through its RING domain the ubiquitination of target proteins by bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RING-HC_RNF186 cd16557
RING finger, HC subclass, found in RING finger protein 186 (RNF186) and similar proteins; ...
37-87 1.50e-21

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


:

Pssm-ID: 438219 [Multi-domain]  Cd Length: 52  Bit Score: 83.75  E-value: 1.50e-21
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 9506663   37 DLECLVCREPYSC-PRLPKLLACQHAFCAICLKLLLCVQDNTWSITCPLCRK 87
Cdd:cd16557   1 DLECLVCRNPYSCfVRKPKLLACQHAFCAICLKLILCEQDGTWSVTCPLCRR 52
RAD18 super family cl35000
RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];
38-148 1.86e-05

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


The actual alignment was detected with superfamily member COG5432:

Pssm-ID: 227719 [Multi-domain]  Cd Length: 391  Bit Score: 44.69  E-value: 1.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506663   38 LECLVCREPYscpRLPKLLACQHAFCAICLKLLLCVQDNtwsitCPLCR---KVTAVPGGLIC------------SLRDH 102
Cdd:COG5432  26 LRCRICDCRI---SIPCETTCGHTFCSLCIRRHLGTQPF-----CPVCRedpCESRLRGSSGSreinesharnrdLLRKV 97
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 9506663  103 EAVVGQLAQPCTEVSLCPQGLVDPADLAAGHpslvGEDGQDEVSAN 148
Cdd:COG5432  98 LESLCRLPRPIKEERPCRWETVIAQDSASGD----EEWEDDLASNS 139
 
Name Accession Description Interval E-value
RING-HC_RNF186 cd16557
RING finger, HC subclass, found in RING finger protein 186 (RNF186) and similar proteins; ...
37-87 1.50e-21

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


Pssm-ID: 438219 [Multi-domain]  Cd Length: 52  Bit Score: 83.75  E-value: 1.50e-21
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 9506663   37 DLECLVCREPYSC-PRLPKLLACQHAFCAICLKLLLCVQDNTWSITCPLCRK 87
Cdd:cd16557   1 DLECLVCRNPYSCfVRKPKLLACQHAFCAICLKLILCEQDGTWSVTCPLCRR 52
rad18 TIGR00599
DNA repair protein rad18; All proteins in this family for which functions are known are ...
35-86 1.18e-05

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]


Pssm-ID: 273165 [Multi-domain]  Cd Length: 397  Bit Score: 45.38  E-value: 1.18e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 9506663     35 ECDLECLVCREPYscpRLPKLLACQHAFCAICLKLLLCVQDNtwsitCPLCR 86
Cdd:TIGR00599  24 DTSLRCHICKDFF---DVPVLTSCSHTFCSLCIRRCLSNQPK-----CPLCR 67
RAD18 COG5432
RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];
38-148 1.86e-05

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


Pssm-ID: 227719 [Multi-domain]  Cd Length: 391  Bit Score: 44.69  E-value: 1.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506663   38 LECLVCREPYscpRLPKLLACQHAFCAICLKLLLCVQDNtwsitCPLCR---KVTAVPGGLIC------------SLRDH 102
Cdd:COG5432  26 LRCRICDCRI---SIPCETTCGHTFCSLCIRRHLGTQPF-----CPVCRedpCESRLRGSSGSreinesharnrdLLRKV 97
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 9506663  103 EAVVGQLAQPCTEVSLCPQGLVDPADLAAGHpslvGEDGQDEVSAN 148
Cdd:COG5432  98 LESLCRLPRPIKEERPCRWETVIAQDSASGD----EEWEDDLASNS 139
zf-RING_5 pfam14634
zinc-RING finger domain;
39-87 1.76e-03

zinc-RING finger domain;


Pssm-ID: 434085 [Multi-domain]  Cd Length: 43  Bit Score: 35.10  E-value: 1.76e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 9506663     39 ECLVCREPYSCPRLPKLLACQHAFCAICLKLLLCvqdntwSITCPLCRK 87
Cdd:pfam14634   1 HCNKCFKELSKTRPFYLTSCGHIFCEECLTRLLQ------ERQCPICKK 43
PEX10 COG5574
RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
35-86 9.12e-03

RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227861 [Multi-domain]  Cd Length: 271  Bit Score: 36.41  E-value: 9.12e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 9506663   35 ECDLECLVCREPYSCPrlpKLLACQHAFCAICLKLLLCVQDntwSITCPLCR 86
Cdd:COG5574 213 LADYKCFLCLEEPEVP---SCTPCGHLFCLSCLLISWTKKK---YEFCPLCR 258
 
Name Accession Description Interval E-value
RING-HC_RNF186 cd16557
RING finger, HC subclass, found in RING finger protein 186 (RNF186) and similar proteins; ...
37-87 1.50e-21

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


Pssm-ID: 438219 [Multi-domain]  Cd Length: 52  Bit Score: 83.75  E-value: 1.50e-21
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 9506663   37 DLECLVCREPYSC-PRLPKLLACQHAFCAICLKLLLCVQDNTWSITCPLCRK 87
Cdd:cd16557   1 DLECLVCRNPYSCfVRKPKLLACQHAFCAICLKLILCEQDGTWSVTCPLCRR 52
RING-HC_RNF224 cd16565
RING finger, HC subclass, found in RING finger protein RNF224 and similar proteins; RNF224 is ...
38-94 5.41e-07

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: 45.58  E-value: 5.41e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 9506663   38 LECLVCREPYS-CPRLPKLLACQHAFCAICLKLLLCVQDNTWSITCPLCRKVTAVPGG 94
Cdd:cd16565   1 LDCIICYSAYDlSTRLPRRLYCGHTFCQACLKRLDTVINEQRWIPCPQCRQNTPTPRG 58
RING-HC_RNF183-like cd16556
RING finger, HC subclass, found in RING finger protein RNF183, RNF223, RNF225 and similar ...
38-92 9.80e-06

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: 41.97  E-value: 9.80e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 9506663   38 LECLVCREPYSCP-RLPKLLACQHAFCAICL-KLLLCVQDNTWSITCPLCRKVTAVP 92
Cdd:cd16556   1 LECSICFSSYDNTfKTPKLLDCGHTFCLECLaRLSLASPPQAERVPCPLCRQPTVLP 57
rad18 TIGR00599
DNA repair protein rad18; All proteins in this family for which functions are known are ...
35-86 1.18e-05

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]


Pssm-ID: 273165 [Multi-domain]  Cd Length: 397  Bit Score: 45.38  E-value: 1.18e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 9506663     35 ECDLECLVCREPYscpRLPKLLACQHAFCAICLKLLLCVQDNtwsitCPLCR 86
Cdd:TIGR00599  24 DTSLRCHICKDFF---DVPVLTSCSHTFCSLCIRRCLSNQPK-----CPLCR 67
RING-HC_TRIM32_C-VII cd16587
RING finger, HC subclass, found in tripartite motif-containing protein 32 (TRIM32) and similar ...
38-88 1.30e-05

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


Pssm-ID: 438249 [Multi-domain]  Cd Length: 51  Bit Score: 41.23  E-value: 1.30e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 9506663   38 LECLVCREPYSC-PRLPKLLACQHAFCAICLKLLLcVQDNTWSITCPLCRKV 88
Cdd:cd16587   1 LECPICLESFDEgQLRPKLLHCGHTICEQCLEKLL-ASLSINGVRCPFCRKV 51
RAD18 COG5432
RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];
38-148 1.86e-05

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


Pssm-ID: 227719 [Multi-domain]  Cd Length: 391  Bit Score: 44.69  E-value: 1.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506663   38 LECLVCREPYscpRLPKLLACQHAFCAICLKLLLCVQDNtwsitCPLCR---KVTAVPGGLIC------------SLRDH 102
Cdd:COG5432  26 LRCRICDCRI---SIPCETTCGHTFCSLCIRRHLGTQPF-----CPVCRedpCESRLRGSSGSreinesharnrdLLRKV 97
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 9506663  103 EAVVGQLAQPCTEVSLCPQGLVDPADLAAGHpslvGEDGQDEVSAN 148
Cdd:COG5432  98 LESLCRLPRPIKEERPCRWETVIAQDSASGD----EEWEDDLASNS 139
RING-HC_RNF152 cd16548
RING finger, HC subclass, found in RING finger protein 152 (RNF152) and similar proteins; ...
38-86 1.39e-04

RING finger, HC subclass, found in RING finger protein 152 (RNF152) and similar proteins; RNF152 is a lysosome-anchored E3 ubiquitin-protein ligase involved in apoptosis. It is polyubiquitinated through K48 linkage. It negatively regulates the activation of the mTORC1 pathway by targeting RagA GTPase for K63-linked ubiquitination. It interacts with and ubiquitinates RagA in an amino-acid-sensitive manner. The ubiquitination of RagA recruits its inhibitor GATOR1, a GAP complex for Rag GTPases, to the Rag complex, thereby inactivating mTORC1 signaling. RNF152 contains an N-terminal C3HC4-type RING-HC finger and a C-terminal transmembrane domain, both of which are responsible for its E3 ligase activity.


Pssm-ID: 438210 [Multi-domain]  Cd Length: 46  Bit Score: 38.44  E-value: 1.39e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 9506663   38 LECLVCREPYSCPRLPKLLACQHAFCAICLKLLLCVQDNtwsITCPLCR 86
Cdd:cd16548   1 LECQICFNYYSPRRRPKLLDCKHTCCSVCLQQMRTSQKD---LRCPWCR 46
RING-HC_PML_C-V cd16579
RING finger, HC subclass, found in promyelocytic leukemia protein (PML) and similar proteins; ...
34-86 7.35e-04

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


Pssm-ID: 438241 [Multi-domain]  Cd Length: 52  Bit Score: 36.38  E-value: 7.35e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 9506663   34 TECDLECLVCREPYSCPrlpKLLACQHAFCAICLKLLLCVQDNTWSITCPLCR 86
Cdd:cd16579   1 EFKFLRCPGCKAEYKCP---KLLPCLHTVCSGCLEALAEQASETTEFQCPICK 50
RING-HC_NHL-1-like cd16524
RING finger, HC subclass, found in Caenorhabditis elegans RING finger protein NHL-1 and ...
38-88 1.45e-03

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.


Pssm-ID: 438187 [Multi-domain]  Cd Length: 53  Bit Score: 35.86  E-value: 1.45e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 9506663   38 LECLVCREPYscpRLPKLLACQHAFC-AICLKllLCVQDNTWSITCPLCRKV 88
Cdd:cd16524   6 LTCPICLDRY---RRPKLLPCQHTFClSPCLE--GLVDYVTRKLKCPECRAE 52
zf-RING_5 pfam14634
zinc-RING finger domain;
39-87 1.76e-03

zinc-RING finger domain;


Pssm-ID: 434085 [Multi-domain]  Cd Length: 43  Bit Score: 35.10  E-value: 1.76e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 9506663     39 ECLVCREPYSCPRLPKLLACQHAFCAICLKLLLCvqdntwSITCPLCRK 87
Cdd:pfam14634   1 HCNKCFKELSKTRPFYLTSCGHIFCEECLTRLLQ------ERQCPICKK 43
RING-HC_RNF138 cd16544
RING finger, HC subclass, found in RING finger protein 138 (RNF138) and similar proteins; ...
37-88 2.41e-03

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


Pssm-ID: 438206 [Multi-domain]  Cd Length: 53  Bit Score: 35.07  E-value: 2.41e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 9506663   37 DLECLVCREPYSCPrlPKLLACQHAFCAICLKLLLCVQdntwSITCPLCRKV 88
Cdd:cd16544   2 ELTCPVCQEVLKDP--VELPPCRHIFCKACILLALRSS----GARCPLCRGP 47
RING-HC_RNF208 cd16559
RING finger, HC subclass, found in RING finger protein 208 (RNF208) and similar proteins; ...
37-89 3.13e-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: 34.91  E-value: 3.13e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 9506663   37 DLECLVCREPYS-CPRLPKLLACQHAFCAICLKLLLCVQDNTWSITCPLCRKVT 89
Cdd:cd16559   1 PLLCPTCGHSYNfTNKRPRILSCLHSVCEECLQILYESCPKYKFISCPTCKRET 54
RING-H2_RNF115 cd16800
RING finger, H2 subclass, found in RING finger protein 115 (RNF115) and similar proteins; ...
38-87 3.51e-03

RING finger, H2 subclass, found in RING finger protein 115 (RNF115) and similar proteins; RNF115, also known as Rab7-interacting ring finger protein (Rabring 7), or zinc finger protein 364 (ZNF364), or breast cancer-associated gene 2 (BCA2), is an E3 ubiquitin-protein ligase that is an endogenous inhibitor of adenosine monophosphate-activated protein kinase (AMPK) activation and its inhibition increases the efficacy of metformin in breast cancer cells. It also functions as a co-factor in the restriction imposed by tetherin on HIV-1, and targets HIV-1 Gag for lysosomal degradation, impairing virus assembly and release, in a tetherin-independent manner. Moreover, RNF115 is a Rab7-binding protein that stimulates c-Myc degradation through mono-ubiquitination of MM-1. It also plays crucial roles as a Rab7 target protein in vesicle traffic to late endosome/lysosome and lysosome biogenesis. Furthermore, RNF115 and the related protein, RNF126 associate with the epidermal growth factor receptor (EGFR) and promote ubiquitylation of EGFR, suggesting they play a role in the ubiquitin-dependent sorting and downregulation of membrane receptors. RNF115 contains an N-terminal BCA2 Zinc-finger domain (BZF), the AKT-phosphorylation sites, and the C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 438452 [Multi-domain]  Cd Length: 50  Bit Score: 34.54  E-value: 3.51e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 9506663   38 LECLVCREPYSCPRLPKLLACQHAFCAICLKLLLCVQDntwsiTCPLCRK 87
Cdd:cd16800   1 LECPVCKEDYTVGEQVRQLPCNHFFHSDCIVPWLELHD-----TCPVCRK 45
RING-HC_RNF222 cd16564
RING finger, HC subclass, found in RING finger protein 222 (RNF222) and similar proteins; ...
39-93 3.64e-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: 34.68  E-value: 3.64e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 9506663   39 ECLVCREPYSCPrlPKLLACQHAFCAICLKLLLcvqdNTWSITCPLCRKVTAVPG 93
Cdd:cd16564   2 ECPVCYEDFDDA--PRILSCGHSFCEDCLVKQL----VSMTISCPICRRVTFISK 50
zf-RING_UBOX pfam13445
RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.
40-83 4.68e-03

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


Pssm-ID: 463881 [Multi-domain]  Cd Length: 38  Bit Score: 33.91  E-value: 4.68e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 9506663     40 CLVCREPYSCPRLPkllaCQHAFCAICLKLLLcvQDNTWSITCP 83
Cdd:pfam13445   1 CPICLELFTDPVLP----CGHTFCRECLEEMS--QKKGGKFKCP 38
RING-HC_TRIM65_C-IV cd16609
RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar ...
35-96 4.75e-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: 34.27  E-value: 4.75e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9506663   35 ECDLECLVCREPYscpRLPKLLACQHAFCAICLKLLLCVQDNTwSITCPLCRKVTAVPGGLI 96
Cdd:cd16609   1 EEELTCSICLGLY---QDPVTLPCQHSFCRACIEDHWRQKDEG-SFSCPECRAPFPEGPTLE 58
RING-HC_RNF182 cd16555
RING finger, HC subclass, found in RING finger protein 182 (RNF182) and similar proteins; ...
37-89 5.61e-03

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: 34.33  E-value: 5.61e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 9506663   37 DLECLVCREPYSC-PRLPKLLACQHAFCAICL-KLLLCVQDNTWSITCPLCRKVT 89
Cdd:cd16555   1 ELECKICYNRYDLrQRRPKVLECCHRVCAKCLyKIVDLGDSSPSVLVCPFCRFET 55
RING-HC_RFPL4B cd16623
RING finger, HC subclass, found in Ret finger protein-like 4B (RFPL4B) and similar proteins; ...
35-92 5.89e-03

RING finger, HC subclass, found in Ret finger protein-like 4B (RFPL4B) and similar proteins; RFPL4B, also called RING finger protein 211 (RNF211), is an uncharacterized RING finger protein containing a typical C3HC4-type RING-HC finger.


Pssm-ID: 438285 [Multi-domain]  Cd Length: 63  Bit Score: 34.40  E-value: 5.89e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 9506663   35 ECDLECLVCREPYSCPrlpKLLACQHAFCAICLKLLLCVQDNTwSITCPLCRKVTAVP 92
Cdd:cd16623   6 EMEATCPICLDFFSHP---ISLSCAHIFCFDCIQKWMTKREDS-ILTCPLCRKEQKKP 59
RING-HC_RBR_RNF19 cd16629
RING finger, HC subclass, found in the family of RING finger proteins RNF19A, RNF19B and ...
38-85 6.66e-03

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


Pssm-ID: 438291 [Multi-domain]  Cd Length: 56  Bit Score: 33.96  E-value: 6.66e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 9506663   38 LECLVCREPYSCPRLPKLLACQHAFCAICLK--LLLCVQDNTWSITCPLC 85
Cdd:cd16629   1 LECPLCLDDLSPEFFPILLSCEHRSCRDCLRqyLTIEISESRVNISCPEC 50
PEX10 COG5574
RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
35-86 9.12e-03

RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227861 [Multi-domain]  Cd Length: 271  Bit Score: 36.41  E-value: 9.12e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 9506663   35 ECDLECLVCREPYSCPrlpKLLACQHAFCAICLKLLLCVQDntwSITCPLCR 86
Cdd:COG5574 213 LADYKCFLCLEEPEVP---SCTPCGHLFCLSCLLISWTKKK---YEFCPLCR 258
RING-HC_RNF10 cd16536
RING finger, HC subclass, found in RING finger protein 10 (RNF10) and similar proteins; RNF10 ...
39-85 9.63e-03

RING finger, HC subclass, found in RING finger protein 10 (RNF10) and similar proteins; RNF10 is an E3 ubiquitin-protein ligase that interacts with mesenchyme Homeobox 2 (MEOX2) transcription factor, a regulator of the proliferation, differentiation and migration of vascular smooth muscle cells and cardiomyocytes; it enhances Meox2 activation of the p21 promoter. It also regulates the expression of myelin-associated glycoprotein (MAG) genes and is required for myelin production in Schwann cells of the peripheral nervous system. Moreover, RNF10 regulates retinoic acid-induced neuronal differentiation and the cell cycle exit of P19 embryonic carcinoma cells. RNF10 contains a C3HC4-type RING-HC finger and three putative nuclear localization signals.


Pssm-ID: 438198 [Multi-domain]  Cd Length: 54  Bit Score: 33.37  E-value: 9.63e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 9506663   39 ECLVCREPYSCPRLPKllaCQHAFCAICLKLLLCVQDNTWSiTCPLC 85
Cdd:cd16536   2 QCPICLEPPVAPRITR---CGHIFCWPCILRYLSLSEKKWR-KCPIC 44
zf-RING_2 pfam13639
Ring finger domain;
39-86 9.83e-03

Ring finger domain;


Pssm-ID: 433370 [Multi-domain]  Cd Length: 44  Bit Score: 33.15  E-value: 9.83e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 9506663     39 ECLVCREPYSCPRLPKLLACQHAFCAICLKLLLcvqdnTWSITCPLCR 86
Cdd:pfam13639   2 ECPICLEEFEEGDKVVVLPCGHHFHRECLDKWL-----RSSNTCPLCR 44
 
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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