Zinc finger (C3HC4-type RING finger) family protein [Arabidopsis thaliana]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| vWA_C3HC4_type | cd01466 | VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
325-504 | 6.58e-56 | ||||
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Membes of this subgroup belong to Zinc-finger family as they are found fused to RING finger domains. The MIDAS motif is not conserved in all the members of this family. The function of vWA domains however is not known. : Pssm-ID: 238743 [Multi-domain] Cd Length: 155 Bit Score: 187.98 E-value: 6.58e-56
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| RING-H2_WAVH2 | cd23114 | RING finger, H2 subclass, found in Arabidopsis thaliana protein WAV3 homolog 2 (WAVH2) and ... |
134-189 | 3.84e-20 | ||||
RING finger, H2 subclass, found in Arabidopsis thaliana protein WAV3 homolog 2 (WAVH2) and similar proteins; WAVH2, also known as RING-type E3 ubiquitin transferase WAVH2, is a probable E3 ubiquitin-protein ligase involved in the regulation of root growth. It acts as a positive regulator of root gravitropism. WAVH2 contains a C3H2C3-type RING-H2 finger. : Pssm-ID: 438476 [Multi-domain] Cd Length: 56 Bit Score: 84.17 E-value: 3.84e-20
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| Name | Accession | Description | Interval | E-value | ||||
| vWA_C3HC4_type | cd01466 | VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
325-504 | 6.58e-56 | ||||
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Membes of this subgroup belong to Zinc-finger family as they are found fused to RING finger domains. The MIDAS motif is not conserved in all the members of this family. The function of vWA domains however is not known. Pssm-ID: 238743 [Multi-domain] Cd Length: 155 Bit Score: 187.98 E-value: 6.58e-56
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| RING-H2_WAVH2 | cd23114 | RING finger, H2 subclass, found in Arabidopsis thaliana protein WAV3 homolog 2 (WAVH2) and ... |
134-189 | 3.84e-20 | ||||
RING finger, H2 subclass, found in Arabidopsis thaliana protein WAV3 homolog 2 (WAVH2) and similar proteins; WAVH2, also known as RING-type E3 ubiquitin transferase WAVH2, is a probable E3 ubiquitin-protein ligase involved in the regulation of root growth. It acts as a positive regulator of root gravitropism. WAVH2 contains a C3H2C3-type RING-H2 finger. Pssm-ID: 438476 [Multi-domain] Cd Length: 56 Bit Score: 84.17 E-value: 3.84e-20
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| YfbK | COG2304 | Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ... |
316-436 | 1.65e-16 | ||||
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only]; Pssm-ID: 441879 [Multi-domain] Cd Length: 289 Bit Score: 80.53 E-value: 1.65e-16
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| VWA | smart00327 | von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
326-495 | 7.99e-15 | ||||
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods. Pssm-ID: 214621 [Multi-domain] Cd Length: 175 Bit Score: 72.87 E-value: 7.99e-15
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| VWA | pfam00092 | von Willebrand factor type A domain; |
326-446 | 8.19e-11 | ||||
von Willebrand factor type A domain; Pssm-ID: 459670 [Multi-domain] Cd Length: 174 Bit Score: 61.52 E-value: 8.19e-11
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| zf-RING_11 | pfam17123 | RING-like zinc finger; |
140-172 | 1.18e-05 | ||||
RING-like zinc finger; Pssm-ID: 465355 [Multi-domain] Cd Length: 29 Bit Score: 42.52 E-value: 1.18e-05
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| RING | smart00184 | Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ... |
140-183 | 1.25e-05 | ||||
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: 42.50 E-value: 1.25e-05
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| Name | Accession | Description | Interval | E-value | ||||
| vWA_C3HC4_type | cd01466 | VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
325-504 | 6.58e-56 | ||||
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Membes of this subgroup belong to Zinc-finger family as they are found fused to RING finger domains. The MIDAS motif is not conserved in all the members of this family. The function of vWA domains however is not known. Pssm-ID: 238743 [Multi-domain] Cd Length: 155 Bit Score: 187.98 E-value: 6.58e-56
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| RING-H2_WAVH2 | cd23114 | RING finger, H2 subclass, found in Arabidopsis thaliana protein WAV3 homolog 2 (WAVH2) and ... |
134-189 | 3.84e-20 | ||||
RING finger, H2 subclass, found in Arabidopsis thaliana protein WAV3 homolog 2 (WAVH2) and similar proteins; WAVH2, also known as RING-type E3 ubiquitin transferase WAVH2, is a probable E3 ubiquitin-protein ligase involved in the regulation of root growth. It acts as a positive regulator of root gravitropism. WAVH2 contains a C3H2C3-type RING-H2 finger. Pssm-ID: 438476 [Multi-domain] Cd Length: 56 Bit Score: 84.17 E-value: 3.84e-20
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| YfbK | COG2304 | Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ... |
316-436 | 1.65e-16 | ||||
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only]; Pssm-ID: 441879 [Multi-domain] Cd Length: 289 Bit Score: 80.53 E-value: 1.65e-16
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| VWA | smart00327 | von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
326-495 | 7.99e-15 | ||||
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods. Pssm-ID: 214621 [Multi-domain] Cd Length: 175 Bit Score: 72.87 E-value: 7.99e-15
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| ChlD | COG1240 | vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ... |
305-497 | 9.41e-13 | ||||
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism]; Pssm-ID: 440853 [Multi-domain] Cd Length: 262 Bit Score: 68.81 E-value: 9.41e-13
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| vWA_subgroup | cd01465 | VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
325-436 | 7.00e-11 | ||||
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Not much is known about the function of the VWA domain in these proteins. The members do have a conserved MIDAS motif. The biochemical function however is not known. Pssm-ID: 238742 [Multi-domain] Cd Length: 170 Bit Score: 61.52 E-value: 7.00e-11
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| VWA | pfam00092 | von Willebrand factor type A domain; |
326-446 | 8.19e-11 | ||||
von Willebrand factor type A domain; Pssm-ID: 459670 [Multi-domain] Cd Length: 174 Bit Score: 61.52 E-value: 8.19e-11
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| vWFA | cd00198 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
325-478 | 3.48e-10 | ||||
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Pssm-ID: 238119 [Multi-domain] Cd Length: 161 Bit Score: 59.12 E-value: 3.48e-10
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| VWA_2 | pfam13519 | von Willebrand factor type A domain; |
327-432 | 9.90e-10 | ||||
von Willebrand factor type A domain; Pssm-ID: 463909 [Multi-domain] Cd Length: 103 Bit Score: 56.15 E-value: 9.90e-10
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| vWA_interalpha_trypsin_inhibitor | cd01461 | vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ... |
326-435 | 3.45e-08 | ||||
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- two heavy chains and one light chain (bikunin). Bikunin confers the protease-inhibitor function while the heavy chains are involved in rendering stability to the extracellular matrix by binding to hyaluronic acid. The heavy chains carry the VWA domain with a conserved MIDAS motif. Although the exact role of the VWA domains remains unknown, it has been speculated to be involved in mediating protein-protein interactions with the components of the extracellular matrix. Pssm-ID: 238738 [Multi-domain] Cd Length: 171 Bit Score: 53.76 E-value: 3.45e-08
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| RING-H2_BRAP2 | cd16457 | RING finger, H2 subclass, found in BRCA1-associated protein (BRAP2) and similar proteins; ... |
140-183 | 1.05e-07 | ||||
RING finger, H2 subclass, found in BRCA1-associated protein (BRAP2) and similar proteins; BRAP2, also known as impedes mitogenic signal propagation (IMP), RING finger protein 52, or renal carcinoma antigen NY-REN-63, is a novel cytoplasmic protein interacting with the two functional nuclear localization signal (NLS) motifs of BRCA1, a nuclear protein linked to breast cancer. It also binds to the SV40 large T antigen NLS motif and the bipartite NLS motif found in mitosin. BRAP2 serves as a cytoplasmic retention protein and plays a role in the regulation of nuclear protein transport. It contains an N-terminal RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), followed by a C3H2C3-type RING-H2 finger and a UBP-type zinc finger. Pssm-ID: 438121 [Multi-domain] Cd Length: 44 Bit Score: 48.44 E-value: 1.05e-07
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| RING-H2 | cd16448 | H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type ... |
140-183 | 3.15e-06 | ||||
H2 subclass of RING (RING-H2) fingers 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 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). This family corresponds to the H2 subclass of RING (RING-H2) finger proteins that are characterized by containing C3H2C3-type canonical RING-H2 fingers or noncanonical RING-H2 finger variants, including C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type modified RING-H2 fingers. The canonical RING-H2 finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-H-X2-C-X(4-48)-C-X2-C, X is any amino acid and the number of X residues varies in different fingers. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-H2 finger 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 serves as a scaffold 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: 438112 [Multi-domain] Cd Length: 43 Bit Score: 44.31 E-value: 3.15e-06
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| zf-RING_11 | pfam17123 | RING-like zinc finger; |
140-172 | 1.18e-05 | ||||
RING-like zinc finger; Pssm-ID: 465355 [Multi-domain] Cd Length: 29 Bit Score: 42.52 E-value: 1.18e-05
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| RING | smart00184 | Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ... |
140-183 | 1.25e-05 | ||||
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: 42.50 E-value: 1.25e-05
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| vWFA_subfamily_ECM | cd01450 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
325-482 | 3.64e-05 | ||||
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains Pssm-ID: 238727 [Multi-domain] Cd Length: 161 Bit Score: 44.59 E-value: 3.64e-05
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| RING-H2_RNF43-like | cd16666 | RING finger, H2 subclass, found in RING finger proteins RNF43, ZNRF3, and similar proteins; ... |
139-183 | 2.88e-04 | ||||
RING finger, H2 subclass, found in RING finger proteins RNF43, ZNRF3, and similar proteins; RNF43 and ZNRF3 (also known as RNF203) are transmembrane E3 ubiquitin-protein ligases that belong to the PA-TM-RING ubiquitin ligase family, characterized by containing an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C3H2C3-type RING-H2 finger followed by a long C-terminal region. Both RNF43 and RNF203 function as tumor suppressors involved in the regulation of Wnt/beta-catenin signaling. They negatively regulate Wnt signaling by interacting with complexes of frizzled (FZD) receptors and low-density lipoprotein receptor-related protein (LRP) 5/6, which leads to ubiquitination of FZD and endocytosis of the Wnt receptor. Dishevelled (DVL), a positive Wnt regulator, is required for ZNRF3/RNF43-mediated ubiquitination and degradation of FZD. They also associate with R-spondin 1 (RSPO1). This interaction may block FZD ubiquitination and enhances Wnt signaling. Pssm-ID: 438328 [Multi-domain] Cd Length: 45 Bit Score: 38.98 E-value: 2.88e-04
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| RING-H2_DTX1-like | cd16459 | RING finger, H2 subclass, found in E3 ubiquitin-protein ligase Deltex1 (DTX1), Deltex2 (DTX2), ... |
140-185 | 2.90e-04 | ||||
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase Deltex1 (DTX1), Deltex2 (DTX2), Deltex4 (DTX4), and similar proteins; This subfamily contains the vertebrate homologs of Drosophila melanogaster Deltex, specifically DTX1, DTX2, and DTX4, and other similar proteins mainly from eumetazoa. The vertebrate homologs of Deltex are involved in Notch signaling and neurogenesis. Mammalian DTX1 is most closely related to the Drosophila Deltex. Both of them bind to SH3-domain containing protein Grb2 and further inhibit E2A. DTX1 functions as a Notch downstream transcription regulator. It interacts with the transcription coactivator p300 and inhibits transcription activation mediated by the neural specific transcription factor MASH1. It is also a transcription target of nuclear factor of activated T cells (NFAT) and participates in T cell anergy and Foxp3 protein level maintenance in vivo. Moreover, DTX1 promotes protein kinase C theta degradation and sustains Casitas B-lineage lymphoma expression. DTX4, also known as RING finger protein 155, shares the highest degree of sequence similarity with DTX1. So it likely interacts with the intracellular domain of Notch as well. Like DTX1 and DTX4, DTX2 is expressed in thymocytes. It interacts with the intracellular domain of Notch receptors and acts as a negative regulator of Notch signals in T cells. However, the endogenous levels of DTX1 and DTX2 is not important for regulating Notch signals during thymocyte development. In contrast to other DTXs, DTX3 does not contain two Notch-binding WWE domains at the N-terminus, but rather a short unique N-terminal domain. It does not interact with the intracellular domain of Notch. In addition, it has a different class of RING finger (C3HC4 type or RING-HC subclass), compared with the other DTXs which harbor a C3H2C3-type RING-H2 finger. Thus DTX3 is not included in this subfamily. Drosophila melanogaster Deltex also does not belong to this subfamily. Pssm-ID: 438122 [Multi-domain] Cd Length: 64 Bit Score: 39.43 E-value: 2.90e-04
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| vWA_BatA_type | cd01467 | VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
325-437 | 3.62e-04 | ||||
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses. In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Members of this subgroup are bacterial in origin. They are typified by the presence of a MIDAS motif. Pssm-ID: 238744 [Multi-domain] Cd Length: 180 Bit Score: 41.93 E-value: 3.62e-04
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| RING-H2_RNF32_rpt2 | cd16678 | second RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; ... |
140-183 | 6.19e-04 | ||||
second RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; RNF32 is mainly expressed in testis spermatogenesis, most likely in spermatocytes and/or in spermatids, suggesting a possible role in sperm formation. RNF32 contains two C3H2C3-type RING-H2 fingers separated by an IQ domain of unknown function. Although the biological function of RNF32 remains unclear, proteins with double RING-H2 fingers may act as scaffolds for binding several proteins that function in the same pathway. This model corresponds to the second RING-H2 finger. Pssm-ID: 438340 [Multi-domain] Cd Length: 61 Bit Score: 38.50 E-value: 6.19e-04
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| RING-H2_Vps41 | cd16690 | RING finger, H2 subclass, found in vacuolar protein sorting-associated protein 41 (Vps41) and ... |
140-186 | 1.54e-03 | ||||
RING finger, H2 subclass, found in vacuolar protein sorting-associated protein 41 (Vps41) and similar proteins; Vps41, also known as S53, is a protein involved in trafficking of proteins from the late Golgi to the vacuole. It interacts with caspase-8, suggesting a potential role of Vps41 beyond lysosomal trafficking. It has been identified as a potential therapeutic target for human Parkinson's disease (PD). Vps41 and the soluble N-ethylmaleimide-sensitive factor attachment protein receptors protein VAMP7 are specifically involved in the fusion of the trans-Golgi network-derived lysosome-associated membrane protein carriers with late endosomes. Vps41 is a specific subunit of the lysosomal tethering complex HOPS (homotypic vacuole fusion and protein sorting) that also includes Vps39 and a Class C Vps core complex composed of Vps11, Vps16, Vps18, and Vps33. HOPS operates at the lysosomal vacuole, controls all traffic from late endosomes into the vacuole and interacts with the Rab7/Ypt7-GTP form. The HOPS-specific Vps39 and Vps41 subunits belong to the class B Vps. They form a subcomplex that interacts with Rab7/Ypt7 and is are required for homotypic and heterotypic late endosome fusion. Vps41 contains an N-terminal WD40 repeat, one or two clathrin repeats and a C3H2C3-type RING-H2 finger domain close to its C-terminus. Pssm-ID: 438351 Cd Length: 51 Bit Score: 36.95 E-value: 1.54e-03
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| RING-H2_Dmap-like | cd16458 | RING finger, H2 subclass, found in defective in mitotic arrest proteins (Dmap) and similar ... |
140-183 | 1.62e-03 | ||||
RING finger, H2 subclass, found in defective in mitotic arrest proteins (Dmap) and similar proteins; This subfamily includes Schizosaccharomyces pombe protein Dma1 (SpDma1p), Saccharomyces cerevisiae proteins Dma1 (ScDma1p) and Dma2 (ScDma2p), and their homologs from fungi. SpDma1p was originally isolated as a multicopy suppressor of the temperature-sensitive growth phenotype caused by cdc16 mutations. It functions to prevent mitotic exit and cytokinesis during spindle checkpoint arrest by inhibiting septation initiation network (SIN) signaling. ScDma1p and ScDma2p, also known as checkpoint forkhead associated with RING domains-containing protein 1 and 2 respectively, seem to be functionally redundant. They are involved in proper septin ring positioning and cytokinesis. The simultaneous lack of Dma1 and Dma2 leads to spindle mispositioning and defects in the spindle position checkpoint. All members of this family contain a forkhead-associated (FHA) domain and a C3H2C3-type RING-H2 finger, the latter suggesting they may possess E3 ubiquitin-ligase activities. Pssm-ID: 319372 [Multi-domain] Cd Length: 47 Bit Score: 36.70 E-value: 1.62e-03
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| RING-H2_RNF215 | cd16670 | RING finger, H2 subclass, found in RING finger protein 215 (RNF215) and similar proteins; This ... |
139-183 | 2.23e-03 | ||||
RING finger, H2 subclass, found in RING finger protein 215 (RNF215) and similar proteins; This family includes uncharacterized protein RNF215 and similar proteins. Although its biological function remains unclear, RNF215 shares high sequence similarity with PA-TM-RING ubiquitin ligases, which have been characterized by containing an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger. Pssm-ID: 438332 [Multi-domain] Cd Length: 50 Bit Score: 36.66 E-value: 2.23e-03
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| RING-H2_RBX2 | cd16466 | RING finger, H2 subclass, found in RING-box protein 2 (RBX2) and similar proteins; RBX2, also ... |
140-187 | 2.48e-03 | ||||
RING finger, H2 subclass, found in RING-box protein 2 (RBX2) and similar proteins; RBX2, also known as CKII beta-binding protein 1 (CKBBP1), RING finger protein 7 (RNF7), regulator of cullins 2 (ROC2), or sensitive to apoptosis gene protein (SAG), is an E3 ubiquitin-protein ligase that protects cells from apoptosis, confers radioresistance, and plays an essential and non-redundant role in embryogenesis and vasculogenesis. It promotes ubiquitination and degradation of a number of protein substrates, including c-JUN, DEPTOR, HIF-1alpha, IkappaBalpha, NF1, NOXA, p27, and procaspase-3, thus regulating various signaling pathways and biological processes. RBX2 is necessary for ubiquitin ligation activity of the multimeric cullin (Cul)-RING E3 ligases (CRLs). RBX2-containing CRLs are involved in the NEDD8 pathway and RBX2 specifically regulates NEDD8ylation of Cul5. It can bind and activate the HIV-1 Vif-Cullin5 E3 ligase complex in vitro. It is also a substrate of NEDD4-1 E3 ubiquitin ligase and mediates NEDD4-1 induced chemosensitization. The inactivation of RBX2 E3 ubiquitin ligase activity triggers senescence and inhibits Kras-induced immortalization. Endothelial deletion of RBX2 causes embryonic lethality and blocks tumor angiogenesis, and may have potential use in anti-angiogenesis therapy of human cancers. Moreover, as a component of the Cullin 5-RING E3 ubiquitin ligase (CRL5) complex, RBX2 regulates neuronal migration through different CRL5 adaptors, such as SOCS7. RBX2 also functions as a redox inducible antioxidant protein that scavenges oxygen radicals by forming inter- and intra-molecular disulfide bonds when acting alone. It contains a C-terminal C3H2C3-type RING-H2 finger that is essential for its ligase activity. Pssm-ID: 438129 [Multi-domain] Cd Length: 60 Bit Score: 36.75 E-value: 2.48e-03
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| RING-H2_Vps | cd16484 | RING finger, H2 subclass, found in vacuolar protein sorting-associated proteins Vps8, Vps11, ... |
140-184 | 2.84e-03 | ||||
RING finger, H2 subclass, found in vacuolar protein sorting-associated proteins Vps8, Vps11, Vps18, Vps41, and similar proteins; This subfamily corresponds to a group of vacuolar protein sorting-associated proteins containing a C-terminal C3H2C3-type RING-H2 finger, which includes Vps8, Vps11, Vps18, and Vps41. Vps11 and Vps18 associate with Vps16 and Vps33 to form a Class C Vps core complex that is required for soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE)-mediated membrane fusion at the lysosome-like yeast vacuole. The core complex, together with two additional compartment-specific subunits, forms the tethering complexes HOPS (homotypic vacuole fusion and protein sorting) and CORVET (class C core vacuole/endosome transport). CORVET contains the additional Vps3 and Vps8 subunits. It operates at endosomes, controls traffic into late endosomes and interacts with the Rab5/Vps21-GTP form. HOPS contains the additional Vps39 and Vps41 subunits. It operates at the lysosomal vacuole, controls all traffic from late endosomes into the vacuole and interacts with the Rab7/Ypt7-GTP form. Pssm-ID: 438147 Cd Length: 48 Bit Score: 36.33 E-value: 2.84e-03
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| RING-H2_RNF43 | cd16798 | RING finger, H2 subclass, found in RING finger protein 43 (RNF43) and similar proteins; RNF43 ... |
135-183 | 4.01e-03 | ||||
RING finger, H2 subclass, found in RING finger protein 43 (RNF43) and similar proteins; RNF43 is a transmembrane E3 ubiquitin-protein ligase that plays an important role in frizzled (FZD)-dependent regulation of the Wnt/beta-catenin pathway. It functions as a tumor suppressor that inhibits Wnt/beta-catenin signaling by ubiquitinating FZD receptor and targeting it to the lysosomal pathway for degradation. miR-550a-5p directly targeted the 3'-UTR of gene RNF43 and regulated its expression. Moreover, RNF43 interacts with NEDD-4-like ubiquitin-protein ligase-1 (NEDL1) and regulates p53-mediated transcription. It may also be involved in cell growth control through the interaction with HAP95, a chromatin-associated protein interfacing the nuclear envelope. Mutations of RNF43 have been identified in various tumors, including colorectal cancer (CRC), endometrial cancer, mucinous ovarian tumors, gastric adenocarcinoma, pancreatic ductal adenocarcinoma, liver fluke-associated cholangiocarcinoma, hepatocellular carcinoma, and glioma. RNF43 contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C3H2C3-type RING-H2 finger followed by a long C-terminal region. Pssm-ID: 438451 [Multi-domain] Cd Length: 53 Bit Score: 35.99 E-value: 4.01e-03
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| RING-H2_RNF121-like | cd16475 | RING finger, H2 subclass, found in RING finger proteins RNF121, RNF175 and similar proteins; ... |
140-183 | 5.20e-03 | ||||
RING finger, H2 subclass, found in RING finger proteins RNF121, RNF175 and similar proteins; This subfamily includes RNF121, RNF175 and similar proteins. RNF121 is an E3-ubiquitin ligase present in the endoplasmic reticulum (ER) and cis-Golgi compartments. It is a novel regulator of apoptosis. It also facilitates the degradation and membrane localization of voltage-gated sodium (NaV) channels, and thus plays a role in the quality control of NaV channels during their synthesis and subsequent transport to the membrane. Moreover, RNF121 acts as a broad regulator of nuclear factor kappaB (NF-kappaB) signaling since its silencing also dampens NF-kappaB activation following stimulation of toll-like receptors (TLRs), nod-like receptors (NLRs), RIG-I-like Receptors (RLRs) or after DNA damage. RNF121 contains five conserved transmembrane (TM) domains and a C3H2C2-type RING-H2 finger. RNF175 is an uncharacterized RING finger protein that shows high sequence similarity with RNF121. This family also includes Arabidopsis RING finger E3 ligase RHA2A, RHA2B, and their homologs. RHA2A is a positive regulator of abscisic acid (ABA) signaling during seed germination and early seedling development. RHA2B may play a role in the ubiquitin-dependent proteolysis pathway that respond to proteasome inhibition. All subfamily members contain a C3H2C3-type RING-H2 finger, which is responsible for E3-ubiquitin ligase activity. Pssm-ID: 438138 [Multi-domain] Cd Length: 55 Bit Score: 35.73 E-value: 5.20e-03
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| RING-H2_PA-TM-RING | cd16454 | RING finger, H2 subclass, found in the PA-TM-RING ubiquitin ligase family; The PA-TM-RING ... |
140-183 | 6.97e-03 | ||||
RING finger, H2 subclass, found in the PA-TM-RING ubiquitin ligase family; The PA-TM-RING family represents a group of transmembrane-type E3 ubiquitin ligases, which has been characterized by an N-terminal transient signal peptide, a PA (protease-associated) domain, a TM (transmembrane) domain, as well as a C-terminal C3H2C3-type RING-H2 finger domain. It includes RNF13, RNF167, ZNRF4 (zinc and RING finger 4), GRAIL (gene related to anergy in lymphocytes)/RNF128, RNF130, RNF133, RNF148, RNF149 and RNF150 (which are more closely related), as well as RNF43 and ZNRF3, which have substantially longer C-terminal tail extensions compared with the others. PA-TM-RING proteins are expressed at low levels in all mammalian tissues and species, but they are not present in yeast. They play a common regulatory role in intracellular trafficking/sorting, suggesting that abrogation of their function may result in dysregulation of cellular signaling events in cancer. Pssm-ID: 438118 [Multi-domain] Cd Length: 43 Bit Score: 34.94 E-value: 6.97e-03
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| zf-rbx1 | pfam12678 | RING-H2 zinc finger domain; There are 8 cysteine/ histidine residues which are proposed to be ... |
140-183 | 8.17e-03 | ||||
RING-H2 zinc finger domain; There are 8 cysteine/ histidine residues which are proposed to be the conserved residues involved in zinc binding. The protein, of which this domain is the conserved region, participates in diverse functions relevant to chromosome metabolism and cell cycle control. Pssm-ID: 463669 [Multi-domain] Cd Length: 55 Bit Score: 34.99 E-value: 8.17e-03
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