Vacuolar sorting-associated protein 13, N-terminal; VPS13 is a family of eukaryotic vacuolar ...
158-422
5.82e-78
Vacuolar sorting-associated protein 13, N-terminal; VPS13 is a family of eukaryotic vacuolar sorting-associated 13 proteins that lies just downstream from Chorein_N family, pfam12624. The exact function of this domain is not known.
:
Pssm-ID: 465309 Cd Length: 234 Bit Score: 258.73 E-value: 5.82e-78
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
2662-2768
3.60e-06
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.
:
Pssm-ID: 175973 [Multi-domain] Cd Length: 102 Bit Score: 48.22 E-value: 3.60e-06
Vacuolar protein sorting-associated protein 62; Vps62 is a vacuolar protein sorting (VPS) ...
2265-2384
3.88e-06
Vacuolar protein sorting-associated protein 62; Vps62 is a vacuolar protein sorting (VPS) protein required for cytoplasm to vacuole targeting of proteins.
The actual alignment was detected with superfamily member pfam06101:
Pssm-ID: 461828 Cd Length: 539 Bit Score: 53.00 E-value: 3.88e-06
SHR-binding domain of vacuolar-sorting associated protein 13; SHR-BD is a family of eukaryotic ...
3159-3466
1.32e-05
SHR-binding domain of vacuolar-sorting associated protein 13; SHR-BD is a family of eukaryotic proteins found on vacuolar-sorting associated proteins towards the C-terminus. In plants, the domain is found to be the region which interacts with SHR or the SHORT-ROOT transcription factor, a regulator of root-growth and asymmetric cell division that separates ground tissue into endodermis and cortex. The plant protein containing the SHR-BD is named SHRUBBY or SHBY, UniProtKB:Q9FT44.
The actual alignment was detected with superfamily member pfam06650:
Pssm-ID: 461974 [Multi-domain] Cd Length: 275 Bit Score: 50.00 E-value: 1.32e-05
Vacuolar sorting-associated protein 13, N-terminal; VPS13 is a family of eukaryotic vacuolar ...
158-422
5.82e-78
Vacuolar sorting-associated protein 13, N-terminal; VPS13 is a family of eukaryotic vacuolar sorting-associated 13 proteins that lies just downstream from Chorein_N family, pfam12624. The exact function of this domain is not known.
Pssm-ID: 465309 Cd Length: 234 Bit Score: 258.73 E-value: 5.82e-78
Repeating coiled region of VPS13; This repeat is a family of repeating regions of eukaryotic ...
617-849
2.21e-47
Repeating coiled region of VPS13; This repeat is a family of repeating regions of eukaryotic vacuolar sorting-associated 13 proteins. This repeating region shares a common core element that includes a well-conserved P-x4-P-x13-17-G sequence. The exact function of this repeat is not known.
Pssm-ID: 465311 [Multi-domain] Cd Length: 236 Bit Score: 171.16 E-value: 2.21e-47
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
2662-2768
3.60e-06
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.
Pssm-ID: 175973 [Multi-domain] Cd Length: 102 Bit Score: 48.22 E-value: 3.60e-06
Vacuolar protein sorting-associated protein 62; Vps62 is a vacuolar protein sorting (VPS) ...
2265-2384
3.88e-06
Vacuolar protein sorting-associated protein 62; Vps62 is a vacuolar protein sorting (VPS) protein required for cytoplasm to vacuole targeting of proteins.
Pssm-ID: 461828 Cd Length: 539 Bit Score: 53.00 E-value: 3.88e-06
SHR-binding domain of vacuolar-sorting associated protein 13; SHR-BD is a family of eukaryotic ...
3159-3466
1.32e-05
SHR-binding domain of vacuolar-sorting associated protein 13; SHR-BD is a family of eukaryotic proteins found on vacuolar-sorting associated proteins towards the C-terminus. In plants, the domain is found to be the region which interacts with SHR or the SHORT-ROOT transcription factor, a regulator of root-growth and asymmetric cell division that separates ground tissue into endodermis and cortex. The plant protein containing the SHR-BD is named SHRUBBY or SHBY, UniProtKB:Q9FT44.
Pssm-ID: 461974 [Multi-domain] Cd Length: 275 Bit Score: 50.00 E-value: 1.32e-05
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
2661-2768
1.54e-05
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.
Pssm-ID: 214577 [Multi-domain] Cd Length: 101 Bit Score: 46.33 E-value: 1.54e-05
Vacuolar-sorting-associated 13 protein C-terminal; VPS13_C is a family of eukaryotic vacuolar ...
3715-3927
2.10e-05
Vacuolar-sorting-associated 13 protein C-terminal; VPS13_C is a family of eukaryotic vacuolar sorting-associated 13 proteins that lies at the C-terminus of the members, The exact function of this domain is not known.
Pssm-ID: 465310 [Multi-domain] Cd Length: 175 Bit Score: 47.92 E-value: 2.10e-05
Vacuolar sorting-associated protein 13, N-terminal; VPS13 is a family of eukaryotic vacuolar ...
158-422
5.82e-78
Vacuolar sorting-associated protein 13, N-terminal; VPS13 is a family of eukaryotic vacuolar sorting-associated 13 proteins that lies just downstream from Chorein_N family, pfam12624. The exact function of this domain is not known.
Pssm-ID: 465309 Cd Length: 234 Bit Score: 258.73 E-value: 5.82e-78
Repeating coiled region of VPS13; This repeat is a family of repeating regions of eukaryotic ...
617-849
2.21e-47
Repeating coiled region of VPS13; This repeat is a family of repeating regions of eukaryotic vacuolar sorting-associated 13 proteins. This repeating region shares a common core element that includes a well-conserved P-x4-P-x13-17-G sequence. The exact function of this repeat is not known.
Pssm-ID: 465311 [Multi-domain] Cd Length: 236 Bit Score: 171.16 E-value: 2.21e-47
N-terminal region of Chorein or VPS13; Although mutations in the full-length vacuolar protein ...
25-135
3.23e-39
N-terminal region of Chorein or VPS13; Although mutations in the full-length vacuolar protein sorting 13A (VPS13A) protein in vertebrates lead to the disease of chorea-acanthocytosis, the exact function of any of the regions within the protein is not yet known. This region is the proposed leucine zipper at the N-terminus. The full-length protein is a transmembrane protein with a presumed role in vesicle-mediated sorting and intracellular protein transport.
Pssm-ID: 463646 Cd Length: 116 Bit Score: 143.09 E-value: 3.23e-39
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
2662-2768
3.60e-06
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.
Pssm-ID: 175973 [Multi-domain] Cd Length: 102 Bit Score: 48.22 E-value: 3.60e-06
Vacuolar protein sorting-associated protein 62; Vps62 is a vacuolar protein sorting (VPS) ...
2265-2384
3.88e-06
Vacuolar protein sorting-associated protein 62; Vps62 is a vacuolar protein sorting (VPS) protein required for cytoplasm to vacuole targeting of proteins.
Pssm-ID: 461828 Cd Length: 539 Bit Score: 53.00 E-value: 3.88e-06
SHR-binding domain of vacuolar-sorting associated protein 13; SHR-BD is a family of eukaryotic ...
3159-3466
1.32e-05
SHR-binding domain of vacuolar-sorting associated protein 13; SHR-BD is a family of eukaryotic proteins found on vacuolar-sorting associated proteins towards the C-terminus. In plants, the domain is found to be the region which interacts with SHR or the SHORT-ROOT transcription factor, a regulator of root-growth and asymmetric cell division that separates ground tissue into endodermis and cortex. The plant protein containing the SHR-BD is named SHRUBBY or SHBY, UniProtKB:Q9FT44.
Pssm-ID: 461974 [Multi-domain] Cd Length: 275 Bit Score: 50.00 E-value: 1.32e-05
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
2661-2768
1.54e-05
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.
Pssm-ID: 214577 [Multi-domain] Cd Length: 101 Bit Score: 46.33 E-value: 1.54e-05
Vacuolar-sorting-associated 13 protein C-terminal; VPS13_C is a family of eukaryotic vacuolar ...
3715-3927
2.10e-05
Vacuolar-sorting-associated 13 protein C-terminal; VPS13_C is a family of eukaryotic vacuolar sorting-associated 13 proteins that lies at the C-terminus of the members, The exact function of this domain is not known.
Pssm-ID: 465310 [Multi-domain] Cd Length: 175 Bit Score: 47.92 E-value: 2.10e-05
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
2663-2749
7.20e-05
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. There are several classes of Synaptotagmins. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.
Pssm-ID: 175975 [Multi-domain] Cd Length: 134 Bit Score: 45.27 E-value: 7.20e-05
C2 domain first repeat in Munc13 (mammalian uncoordinated)-like proteins; C2-like domains are ...
2662-2748
3.17e-03
C2 domain first repeat in Munc13 (mammalian uncoordinated)-like proteins; C2-like domains are thought to be involved in phospholipid binding in a Ca2+ independent manner in both Unc13 and Munc13. Caenorabditis elegans Unc13 has a central domain with sequence similarity to PKC, which includes C1 and C2-related domains. Unc13 binds phorbol esters and DAG with high affinity in a phospholipid manner. Mutations in Unc13 results in abnormal neuronal connections and impairment in cholinergic neurotransmission in the nematode. Munc13 is the mammalian homolog which are expressed in the brain. There are 3 isoforms (Munc13-1, -2, -3) and are thought to play a role in neurotransmitter release and are hypothesized to be high-affinity receptors for phorbol esters. Unc13 and Munc13 contain both C1 and C2 domains. There are two C2 related domains present, one central and one at the carboxyl end. Munc13-1 contains a third C2-like domain. Munc13 interacts with syntaxin, synaptobrevin, and synaptotagmin suggesting a role for these as scaffolding proteins. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-II topology.
Pssm-ID: 176058 [Multi-domain] Cd Length: 153 Bit Score: 41.20 E-value: 3.17e-03
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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