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Conserved domains on  [gi|24642006|ref|NP_572969|]
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uncharacterized protein Dmel_CG5334 [Drosophila melanogaster]

Protein Classification

RING-HC_MKRN domain-containing protein( domain architecture ID 11613725)

RING-HC_MKRN domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RING-HC_MKRN cd16521
RING finger, HC subclass, found in the makorin (MKRN) proteins; The MKRN protein subfamily ...
81-136 5.22e-22

RING finger, HC subclass, found in the makorin (MKRN) proteins; The MKRN protein subfamily includes ribonucleoproteins that are characterized by a variety of zinc-finger motifs, including typical arrays of one to four C3H1-type zinc fingers and a C3HC4-type RING-HC finger. Another motif rich in Cys and His residues (CH), with so far unknown function, is also generally present in MKRN proteins. MKRN proteins may have E3 ubiquitin ligase activity.


:

Pssm-ID: 438184 [Multi-domain]  Cd Length: 53  Bit Score: 84.64  E-value: 5.22e-22
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24642006  81 KMCGICLETVVKKrgrECRFGILPKCKHIFCLTCIRRWRQAEYIEDNVKRGCPECR 136
Cdd:cd16521   1 IECGICMEVVLEK---ERRFGILSNCNHVFCLECIREWRSSKDFENSIVRSCPICR 53
 
Name Accession Description Interval E-value
RING-HC_MKRN cd16521
RING finger, HC subclass, found in the makorin (MKRN) proteins; The MKRN protein subfamily ...
81-136 5.22e-22

RING finger, HC subclass, found in the makorin (MKRN) proteins; The MKRN protein subfamily includes ribonucleoproteins that are characterized by a variety of zinc-finger motifs, including typical arrays of one to four C3H1-type zinc fingers and a C3HC4-type RING-HC finger. Another motif rich in Cys and His residues (CH), with so far unknown function, is also generally present in MKRN proteins. MKRN proteins may have E3 ubiquitin ligase activity.


Pssm-ID: 438184 [Multi-domain]  Cd Length: 53  Bit Score: 84.64  E-value: 5.22e-22
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24642006  81 KMCGICLETVVKKrgrECRFGILPKCKHIFCLTCIRRWRQAEYIEDNVKRGCPECR 136
Cdd:cd16521   1 IECGICMEVVLEK---ERRFGILSNCNHVFCLECIREWRSSKDFENSIVRSCPICR 53
PHA02929 PHA02929
N1R/p28-like protein; Provisional
78-142 1.68e-11

N1R/p28-like protein; Provisional


Pssm-ID: 222944 [Multi-domain]  Cd Length: 238  Bit Score: 61.33  E-value: 1.68e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24642006   78 SQDKMCGICLETVVKKRGRECRFGILPKCKHIFCLTCIRRWRQAeyiednvKRGCPECRVFSEFV 142
Cdd:PHA02929 172 SKDKECAICMEKVYDKEIKNMYFGILSNCNHVFCIECIDIWKKE-------KNTCPVCRTPFISV 229
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
83-135 6.33e-03

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: 33.64  E-value: 6.33e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 24642006     83 CGICLEtvvkkrgRECRFGILPKCKHIFCLTCIRRWRQAEYIEdnvkrgCPEC 135
Cdd:smart00184   1 CPICLE-------EYLKDPVILPCGHTFCRSCIRKWLESGNNT------CPIC 40
 
Name Accession Description Interval E-value
RING-HC_MKRN cd16521
RING finger, HC subclass, found in the makorin (MKRN) proteins; The MKRN protein subfamily ...
81-136 5.22e-22

RING finger, HC subclass, found in the makorin (MKRN) proteins; The MKRN protein subfamily includes ribonucleoproteins that are characterized by a variety of zinc-finger motifs, including typical arrays of one to four C3H1-type zinc fingers and a C3HC4-type RING-HC finger. Another motif rich in Cys and His residues (CH), with so far unknown function, is also generally present in MKRN proteins. MKRN proteins may have E3 ubiquitin ligase activity.


Pssm-ID: 438184 [Multi-domain]  Cd Length: 53  Bit Score: 84.64  E-value: 5.22e-22
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24642006  81 KMCGICLETVVKKrgrECRFGILPKCKHIFCLTCIRRWRQAEYIEDNVKRGCPECR 136
Cdd:cd16521   1 IECGICMEVVLEK---ERRFGILSNCNHVFCLECIREWRSSKDFENSIVRSCPICR 53
RING-HC_MKRN1_3 cd16730
RING finger, HC subclass, found in makorin-1 (MKRN1), makorin-3 (MKRN3), and similar proteins; ...
80-139 1.76e-18

RING finger, HC subclass, found in makorin-1 (MKRN1), makorin-3 (MKRN3), and similar proteins; MKRN1, also known as makorin RING finger protein 1 or RING finger protein 61 (RNF61), is an E3 ubiquitin-protein ligase targeting the telomerase catalytic subunit (TERT) for proteasome processing. It regulates the ubiquitination and degradation of peroxisome-proliferator-activated receptor gamma (PPARgamma), a nuclear receptor that is linked to obesity and metabolic diseases. It also mediates the posttranslational regulation of p14ARF, and thus potentially regulates cellular senescence and tumorigenesis in gastric cancer. Moreover, MKRN1 functions as a differentially negative regulator of p53 and p21, and controls cell cycle arrest and apoptosis. It induces degradation of West Nile virus (WNV) capsid protein to protect cells from WNV. It is a RNA-binding protein involved in the modulation of cellular stress and apoptosis. It predominantly associates with proteins involved in mRNA metabolism including regulators of mRNA turnover, transport, and/or translation, and acts as a component of a ribonucleoprotein complex in embryonic stem cells (ESCs) that is recruited to stress granules upon exposure to environmental stress. MKRN1 interacts with poly(A)-binding protein (PABP), a key component of different ribonucleoprotein complexes, in an RNA-independent manner, and stimulates translation in nerve cells. In addition, MKRN1 is a novel SEREX (serological identification of antigens by recombinant cDNA expression cloning) antigen of esophageal squamous cell carcinoma (SCC). It may be involved in carcinogenesis of the well-differentiated type of tumors possibly via ubiquitination of filamin A interacting protein 1 (L-FILIP). Human MKRN1 contains three N-terminal C3H1-type zinc fingers, a motif rich in Cys and His residues (CH), a C3HC4-type RING-HC finger, and another C3H1-type zinc finger at the C-terminus. MKRN3, also known as makorin RING finger protein 3, RING finger protein 63 (RNF63), or zinc finger protein 127 (ZNF127), is a therian mammal-specific retrocopy of MKRN1. It acts as a putative E3 ubiquitin-protein ligase involved in ubiquitination and cell signaling. MKRN3 shows a potential inhibitory effect on hypothalamic gonadotropin-releasing hormone (GnRH) secretion. Its defects represent the most frequent known genetic cause of familial central precocious puberty (CPP). In contrast to human MKRN1, human MKRN3 lacks the second C3H1-type zinc finger at the N-terminal region. The RING-HC finger of mammalian MKRN4 shows high sequence similarity with that of MKRN3, and is also included in this model.


Pssm-ID: 319644 [Multi-domain]  Cd Length: 61  Bit Score: 75.61  E-value: 1.76e-18
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24642006  80 DKMCGICLETVVKKRG-RECRFGILPKCKHIFCLTCIRRWRQAEYIEDNVKRGCPECRVFS 139
Cdd:cd16730   1 DKVCGICMEVVYEKANpSERRFGILSNCNHTYCLKCIRKWRSAKQFESKIIKSCPECRITS 61
RING-HC_MKRN4 cd16732
RING finger, HC subclass, found in makorin-4 (MKRN4) and similar proteins; MKRN4, also known ...
80-139 2.14e-16

RING finger, HC subclass, found in makorin-4 (MKRN4) and similar proteins; MKRN4, also known as makorin RING finger protein pseudogene 4, makorin RING finger protein pseudogene 5, RING finger protein 64 (RNF64), zinc finger protein 127-Xp (ZNF127-Xp), or zinc finger protein 127-like 1, is a new divergent member of the makorin protein family in vertebrates. It may have an ancestral gonad-specific function and maternal embryonic expression before duplication in vertebrates. MKRN4 contains typical arrays of one to four C3H1-type zinc fingers, a motif rich in Cys and His residues (CH) and a C3HC4-type RING-HC finger. The RING-HC finger of mammalian MKRN4 shows high sequence similarity with that of MKRN3, and is not included in this model.


Pssm-ID: 438390 [Multi-domain]  Cd Length: 61  Bit Score: 70.22  E-value: 2.14e-16
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24642006  80 DKMCGICLETVVKKR-GRECRFGILPKCKHIFCLTCIRRWRQAEYIEDNVKRGCPECRVFS 139
Cdd:cd16732   1 DVACGICMDKVYEKAhAKERVFGILPNCNHAFCVGCIKKWRKSKDFQNEVIKACPQCRVKS 61
RING-HC_MKRN2 cd16731
RING finger, HC subclass, found in makorin-2 (MKRN2) and similar proteins; MKRN2, also known ...
80-136 1.93e-14

RING finger, HC subclass, found in makorin-2 (MKRN2) and similar proteins; MKRN2, also known as makorin RING finger protein 2, RING finger protein 62 (RNF62), or HSPC070, is a putative ribonucleoprotein that acts as a neurogenesis inhibitor acting upstream of glycogen synthase kinase-3beta (GSK-3beta) in the phosphatidylinositol 3-kinase (PI3K)/Akt pathway. It also functions in promoting cell proliferation of primary CD34+ progenitor cells and K562 cells, indicating its possible involvement in normal and malignant hematopoiesis. Mammalian MKRN2 contains three N-terminal C3H1-type zinc fingers, a motif rich in Cys and His residues (CH), a C3HC4-type RING-HC finger, and another C3H1-type zinc finger at the C-terminus. The third C3H1-type zinc finger, the CH motif, as well as the RING zinc finger are necessary for its anti-neurogenic activity.


Pssm-ID: 319645 [Multi-domain]  Cd Length: 58  Bit Score: 65.31  E-value: 1.93e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24642006  80 DKMCGICLETVVKKRG-RECRFGILPKCKHIFCLTCIRRWRQAEYIEDNVKRGCPECR 136
Cdd:cd16731   1 DKVCSICMEVVYEKASaSERRFGILSNCNHTYCLSCIRQWRCAKQFENPIIKSCPECR 58
PHA02929 PHA02929
N1R/p28-like protein; Provisional
78-142 1.68e-11

N1R/p28-like protein; Provisional


Pssm-ID: 222944 [Multi-domain]  Cd Length: 238  Bit Score: 61.33  E-value: 1.68e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24642006   78 SQDKMCGICLETVVKKRGRECRFGILPKCKHIFCLTCIRRWRQAeyiednvKRGCPECRVFSEFV 142
Cdd:PHA02929 172 SKDKECAICMEKVYDKEIKNMYFGILSNCNHVFCIECIDIWKKE-------KNTCPVCRTPFISV 229
PHA02926 PHA02926
zinc finger-like protein; Provisional
78-136 4.45e-09

zinc finger-like protein; Provisional


Pssm-ID: 165237 [Multi-domain]  Cd Length: 242  Bit Score: 54.68  E-value: 4.45e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642006   78 SQDKMCGICLETVVKKRGRECR-FGILPKCKHIFCLTCIRRWRQAEYiEDNVKRGCPECR 136
Cdd:PHA02926 168 SKEKECGICYEVVYSKRLENDRyFGLLDSCNHIFCITCINIWHRTRR-ETGASDNCPICR 226
PHA03096 PHA03096
p28-like protein; Provisional
81-162 6.35e-09

p28-like protein; Provisional


Pssm-ID: 222981 [Multi-domain]  Cd Length: 284  Bit Score: 54.43  E-value: 6.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642006   81 KMCGICLETVVKKRGRECRFGILPKCKHIFCLTCIRRWRqaeyIEDNVKRGCPECRVFSEFVC-------------PSAY 147
Cdd:PHA03096 179 KICGICLENIKAKYIIKKYYGILSEIKHEFNIFCIKIWM----TESLYKETEPENRRLNTVIVfiekinedlknniPSRY 254
                         90
                 ....*....|....*
gi 24642006  148 WVDTKEEKDKLLSEY 162
Cdd:PHA03096 255 WIDDKYDKNLLSFRY 269
RING-HC_Topors cd16574
RING finger, HC subclass, found in topoisomerase I-binding arginine/serine-rich protein ...
80-136 6.46e-06

RING finger, HC subclass, found in topoisomerase I-binding arginine/serine-rich protein (Topors) and similar proteins; Topors, also known as topoisomerase I-binding RING finger protein, tumor suppressor p53- binding protein 3, or p53-binding protein 3 (p53BP3), is a ubiquitously expressed nuclear E3 ubiquitin-protein ligase that can ligate both ubiquitin and small ubiquitin-like modifier (SUMO) to substrate proteins in the nucleus. It contains an N-terminal C3HC4-type RING-HC finger which ligates ubiquitin to its target proteins including DNA topoisomerase I, p53, NKX3.1, H2AX, and the AAV-2 Rep78/68 proteins. As a RING-dependent E3 ubiquitin ligase, Topors works with the E2 enzymes UbcH5a, UbcH5c, and UbcH6, but not with UbcH7, CDC34, or UbcH2b. Topors acts as a tumor suppressor in various malignancies. It regulates p53 modification, suggesting it may be responsible for astrocyte elevated gene-1 (AEG-1, also known as metadherin, or LYRIC) ubiquitin modification. Plk1-mediated phosphorylation of Topors inhibits Topors-mediated sumoylation of p53, whereas p53 ubiquitination is enhanced, leading to p53 degradation. It also functions as a negative regulator of the prostate tumor suppressor NKX3.1. Moreover, Topors is associated with promyelocytic leukemia nuclear bodies, and may be involved in the cellular response to camptothecin. It also plays a key role in the turnover of H2AX protein, discriminating the type of DNA damaging stress. Furthermore, Topors is a cilia-centrosomal protein associated with autosomal dominant retinal degeneration. Mutations in TOPORS cause autosomal dominant retinitis pigmentosa (adRP).


Pssm-ID: 438236 [Multi-domain]  Cd Length: 47  Bit Score: 41.89  E-value: 6.46e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24642006  80 DKMCGICLETVVKKRGrecrfgILPKCKHIFCLTCIRRWrqaeyieDNVKRGCPECR 136
Cdd:cd16574   1 DSSCPICLDRFENEKA------FLDGCFHAFCFTCILEW-------SKVKNECPLCK 44
RING-HC_DTX3-like cd16506
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3), Deltex-3-like ...
81-138 9.97e-05

RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3), Deltex-3-like (DTX3L) and similar proteins; This subfamily contains Deltex3 (DTX3) and Deltex-3-like (DTX3L), both of which are E3 ubiquitin-protein ligases belonging to the Deltex (DTX) family. DTX3, also known as RING finger protein 154 (RNF154), has a biological function that remains unclear. DTX3L, also known as B-lymphoma- and BAL-associated protein (BBAP) or Rhysin-2 (Rhysin2), regulates endosomal sorting of the G protein-coupled receptor CXCR4 from endosomes to lysosomes. It also regulates subcellular localization of its partner protein, B aggressive lymphoma (BAL), by a dynamic nucleocytoplasmic trafficking mechanism. In contrast to other DTXs, both DTX3 and DTX3L contain a C3HC4-type RING-HC finger, and a previously unidentified C-terminal domain. DTX3L can associate with DTX1 through its unique N termini and further enhance self-ubiquitination.


Pssm-ID: 438169 [Multi-domain]  Cd Length: 45  Bit Score: 38.50  E-value: 9.97e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24642006  81 KMCGICLETVVKKRgrecrfgILPKCKHIFCLTCIRRWRQaeyiednVKRGCPECRVF 138
Cdd:cd16506   1 DTCPICLDEIQNKK-------TLEKCKHSFCEDCIDRALQ-------VKPVCPVCGVV 44
RING-HC_EHV1-like cd23130
RING finger, HC subclass, found in Equid alphaherpesvirus 1 (Equine herpesvirus 1/EHV-1) ...
83-136 2.45e-04

RING finger, HC subclass, found in Equid alphaherpesvirus 1 (Equine herpesvirus 1/EHV-1) regulatory protein and similar proteins; EHV-1 regulatory protein belongs to the Vmw110 (IPC0) protein family. It contains a typical C3HC4-type RING-HC finger and binds zinc stably.


Pssm-ID: 438492 [Multi-domain]  Cd Length: 51  Bit Score: 37.72  E-value: 2.45e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 24642006  83 CGICLETVVKkrgrecrFGILPKCKHIFCLTCIRRWRQaeyiednVKRGCPECR 136
Cdd:cd23130   3 CPICLDDPED-------EAITLPCLHQFCYTCILRWLQ-------TSPTCPLCK 42
RING-HC_RNF213 cd16561
RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins; ...
80-137 3.11e-04

RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins; RNF213, also known as ALK lymphoma oligomerization partner on chromosome 17 or Moyamoya steno-occlusive disease-associated AAA+ and RING finger protein (mysterin), is an intracellular soluble protein that functions as an E3 ubiquitin-protein ligase and AAA+ ATPase, which possibly contributes to vascular development through mechanical processes in the cell. It plays a unique role in endothelial cells for proper gene expression in response to inflammatory signals from the environment. Mutations in RNF213 may be associated with Moyamoya disease (MMD), an idiopathic cerebrovascular occlusive disorder prevalent in East Asia. It also acts as a nuclear marker for acanthomorph phylogeny. RNF213 contains two tandem enzymatically active AAA+ ATPase modules and a C3HC4-type RING-HC finger. It can form a huge ring-shaped oligomeric complex.


Pssm-ID: 438223 [Multi-domain]  Cd Length: 50  Bit Score: 37.26  E-value: 3.11e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24642006  80 DKMCGICLETVvkkrgrecRFGILPKCKHIFCLTCIRRWRQAEyiednvkRGCPECRV 137
Cdd:cd16561   2 EQECSICLEDL--------NDPVKLPCDHVFCEECIRQWLPGQ-------MSCPLCRT 44
RING-HC_DTX3 cd16711
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3) and similar ...
80-138 7.95e-04

RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3) and similar proteins; DTX3, also known as RING finger protein 154 (RNF154), is an E3 ubiquitin-protein ligase that belongs to the Deltex (DTX) family. In contrast to other DTXs, DTX3 does not contain two N-terminal Notch-binding WWE domains, but a short unique N-terminal domain, suggesting it does not interact with the intracellular domain of Notch. Its C-terminal region includes a C3HC4-type RING-HC finger, and a previously unidentified C-terminal domain.


Pssm-ID: 438371 [Multi-domain]  Cd Length: 54  Bit Score: 36.24  E-value: 7.95e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 24642006  80 DKMCGICLETVVKKRgrecrfgILPKCKHIFCLTCIRRWRQaeyiednVKRGCPECRVF 138
Cdd:cd16711   1 EETCPICLGEIQNKK-------TLDKCKHSFCEDCITRALQ-------VKKACPMCGEF 45
RING-HC_RNF10 cd16536
RING finger, HC subclass, found in RING finger protein 10 (RNF10) and similar proteins; RNF10 ...
83-135 2.30e-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: 34.91  E-value: 2.30e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24642006  83 CGICLETVVKKRgrecrfgiLPKCKHIFCLTCIRRwrqaeYIEDNVK--RGCPEC 135
Cdd:cd16536   3 CPICLEPPVAPR--------ITRCGHIFCWPCILR-----YLSLSEKkwRKCPIC 44
RING-H2_ASR1 cd23120
RING finger, H2 subclass, found in Saccharomyces cerevisiae alcohol-sensitive RING finger ...
83-139 5.25e-03

RING finger, H2 subclass, found in Saccharomyces cerevisiae alcohol-sensitive RING finger protein 1 (ASR1) and similar proteins; ASR1 is required for tolerance to alcohol. It signals alcohol stress to the nucleus. ASR1 contains a C3H2C3-type RING-H2 finger.


Pssm-ID: 438482 [Multi-domain]  Cd Length: 54  Bit Score: 34.05  E-value: 5.25e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24642006  83 CGICLETVVKKRGRecrfgiLPKCKHIFCLTCIRRWRQAeyiedNVKRGCPECRVFS 139
Cdd:cd23120   4 CPICLEEMNSGTGY------LADCGHEFHLTCIREWHNK-----SGNLDCPICRVES 49
RING-HC_DTX3L cd16712
RING finger, HC subclass, found in protein Deltex-3-like (DTX3L) and similar proteins; DTX3L, ...
83-137 5.79e-03

RING finger, HC subclass, found in protein Deltex-3-like (DTX3L) and similar proteins; DTX3L, also known as B-lymphoma- and BAL-associated protein (BBAP) or Rhysin-2 (Rhysin2), is a RING-domain E3 ubiquitin-protein ligase that regulates endosomal sorting of the G protein-coupled receptor CXCR4 from endosomes to lysosomes. It also regulates subcellular localization of its partner protein, B aggressive lymphoma (BAL), by a dynamic nucleocytoplasmic trafficking mechanism. DTX3L has a unique N-terminus, but lacks the highly basic N-terminal motif and the central proline-rich motif present in other Deltex (DTX) family members, such as DTX1, DTX2, and DTX4. Moreover, its C-terminal region is highly homologous to DTX3. It includes a C3HC4-type RING-HC finger, and a previously unidentified C-terminal domain. DTX3L can associate with DTX1 through its unique N-terminus and further enhance self-ubiquitination.


Pssm-ID: 438372 [Multi-domain]  Cd Length: 56  Bit Score: 33.94  E-value: 5.79e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24642006  83 CGICLETVVKKRgrecrfgILPKCKHIFCLTCIRRwrqaeyiEDNVKRGCPECRV 137
Cdd:cd16712   6 CPICMDRISNKK-------VLPKCKHVFCAACIDK-------AMKYKPVCPVCGT 46
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
83-135 6.33e-03

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: 33.64  E-value: 6.33e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 24642006     83 CGICLEtvvkkrgRECRFGILPKCKHIFCLTCIRRWRQAEYIEdnvkrgCPEC 135
Cdd:smart00184   1 CPICLE-------EYLKDPVILPCGHTFCRSCIRKWLESGNNT------CPIC 40
RING-H2_RHA1-like cd23121
RING finger, H2 subclass, found in Arabidopsis thaliana RING-H2 finger A1a (RHA1A), A1b (RHA1B) ...
80-137 8.61e-03

RING finger, H2 subclass, found in Arabidopsis thaliana RING-H2 finger A1a (RHA1A), A1b (RHA1B) and similar proteins; This subfamily includes Arabidopsis thaliana RHA1A, RHA1B and XERICO. RHA1A is a probable E3 ubiquitin-protein ligase that may possess E3 ubiquitin ligase activity in vitro. RHA1B possesses E3 ubiquitin-protein ligase activity when associated with the E2 enzyme UBC8 in vitro. XERICO functions on abscisic acid homeostasis at post-translational level, probably through ubiquitin/proteasome-dependent substrate-specific degradation. Members of this subfamily contain a C3H2C3-type RING-H2 finger.


Pssm-ID: 438483 [Multi-domain]  Cd Length: 50  Bit Score: 33.23  E-value: 8.61e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24642006  80 DKMCGICLETVVKkrgrECRFGILPKCKHIFCLTCIRRWrqaeyIEDNvKRGCPECRV 137
Cdd:cd23121   1 DDCCAICLSDFNS----DEKLRQLPKCGHIFHHHCLDRW-----IRYN-KITCPLCRA 48
 
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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