E3 ubiquitin-protein ligase HERC2 isoform X1 [Taeniopygia guttata]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| HECTc | cd00078 | HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
4426-4797 | 8.91e-121 | ||||||
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains. : Pssm-ID: 238033 [Multi-domain] Cd Length: 352 Bit Score: 386.92 E-value: 8.91e-121
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| APC10-HERC2 | cd08664 | APC10-like DOC1 domain present in HERC2 (HECT domain and RLD2); This model represents the ... |
2769-2914 | 6.76e-92 | ||||||
APC10-like DOC1 domain present in HERC2 (HECT domain and RLD2); This model represents the APC10/DOC1 domain present in HERC2 (HECT domain and RLD2), a large multi-domain protein with three RCC1-like domains (RLDs), additional internal domains including a zinc finger ZZ-type and Cyt-b5 (Cytochrome b5-like Heme/Steroid binding) domains, and a C-terminal HECT (Homologous to the E6-AP Carboxyl Terminus) domain. The APC10/DOC1 domain of HERC2 is a homolog of the APC10 subunit and the DOC1 domain present in E3 ubiquitin ligases which mediate substrate ubiquitination (or ubiquitylation), a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. As suggested by structural relationships between HERC2 and other proteins such as HERC1, the proposed role for HERC2 in protein trafficking and degradation pathways is consistent with observations that mutations in HERC2 lead to neuromuscular secretory vesicle and sperm acrosome defects, other developmental abnormalities, and juvenile lethality of jdf2 mice. Recent studies have shown that the protein complex, HERC2-RNF8, coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes. : Pssm-ID: 176485 Cd Length: 152 Bit Score: 295.44 E-value: 6.76e-92
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| ATS1 | COG5184 | Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ... |
2952-3305 | 2.70e-79 | ||||||
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton]; : Pssm-ID: 444065 [Multi-domain] Cd Length: 343 Bit Score: 267.23 E-value: 2.70e-79
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| ATS1 | COG5184 | Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ... |
3949-4297 | 2.85e-77 | ||||||
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton]; : Pssm-ID: 444065 [Multi-domain] Cd Length: 343 Bit Score: 261.45 E-value: 2.85e-77
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| ATS1 | COG5184 | Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ... |
438-741 | 1.68e-60 | ||||||
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton]; : Pssm-ID: 444065 [Multi-domain] Cd Length: 343 Bit Score: 213.30 E-value: 1.68e-60
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| Cul7 | pfam11515 | Mouse development and cellular proliferation protein Cullin-7; The Cullin Ring Ligase family ... |
2558-2635 | 9.20e-47 | ||||||
Mouse development and cellular proliferation protein Cullin-7; The Cullin Ring Ligase family member, Cul7, is required for normal mouse development and cellular proliferation. Cul7 has a CPH domain which is a p53 interaction domain. The CPH domain interaction surface of P53 is present in the tetramerization domain. : Pssm-ID: 463286 Cd Length: 78 Bit Score: 163.29 E-value: 9.20e-47
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| ZZ_HERC2 | cd02344 | Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ... |
2710-2754 | 4.17e-29 | ||||||
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential E3 ubiquitin protein ligase and/or guanine nucleotide exchange factor. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. : Pssm-ID: 239084 Cd Length: 45 Bit Score: 111.91 E-value: 4.17e-29
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| MIB_HERC2 | pfam06701 | Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ... |
1872-1932 | 2.06e-27 | ||||||
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect). : Pssm-ID: 461991 Cd Length: 66 Bit Score: 107.69 E-value: 2.06e-27
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| UBA_HERC2 | cd14402 | UBA domain found in probable E3 ubiquitin-protein ligase HERC2 and similar proteins; HERC2, ... |
2462-2509 | 5.92e-23 | ||||||
UBA domain found in probable E3 ubiquitin-protein ligase HERC2 and similar proteins; HERC2, also called HECT domain and RCC1-like domain-containing protein 2, is a SUMO-regulated E3 ubiquitin ligase that plays an important role in the SUMO-dependent pathway which orchestrates the DNA double-strand break (DSB) response. Moreover, HERC2 functions as a RNF8 auxiliary factor that regulates ubiquitin-dependent retention of repair proteins on damaged chromosomes. In addition to a ubiquitin-association (UBA) domain, HERC2 contains more than one RCC1-like domains (RLDs) and a C-terminal HECT E3 ubiquitin ligase domain. : Pssm-ID: 270585 Cd Length: 45 Bit Score: 94.36 E-value: 5.92e-23
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| Cyt-b5 | pfam00173 | Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ... |
1212-1284 | 4.06e-09 | ||||||
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases. : Pssm-ID: 459698 [Multi-domain] Cd Length: 74 Bit Score: 56.09 E-value: 4.06e-09
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| SH3_15 super family | cl39691 | Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate ... |
2643-2700 | 1.79e-03 | ||||||
Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate recognition domain for a second, membrane-distal epitope of the Notch ligand (C-box). Although the first Mib repeat of REP may play a dominant role in ligand binding, the two repeats appear to cooperate in the engagement of the Jag1 tail. Mind bomb (Mib) proteins are large, multi-domain E3 ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. The structure and functional analysis, show that Mib1 contains two independent substrate recognition domains that engage two distinct epitopes from the cytoplasmic tail of the ligand Jagged1, one in the intracellular membrane proximal region and the other near the C terminus. REP domains have a five-stranded anti-parallel twisted beta sheet topology similar to that of SH3 domains. The actual alignment was detected with superfamily member pfam18346: Pssm-ID: 465720 Cd Length: 67 Bit Score: 39.53 E-value: 1.79e-03
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| Name | Accession | Description | Interval | E-value | ||||||
| HECTc | cd00078 | HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
4426-4797 | 8.91e-121 | ||||||
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains. Pssm-ID: 238033 [Multi-domain] Cd Length: 352 Bit Score: 386.92 E-value: 8.91e-121
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| APC10-HERC2 | cd08664 | APC10-like DOC1 domain present in HERC2 (HECT domain and RLD2); This model represents the ... |
2769-2914 | 6.76e-92 | ||||||
APC10-like DOC1 domain present in HERC2 (HECT domain and RLD2); This model represents the APC10/DOC1 domain present in HERC2 (HECT domain and RLD2), a large multi-domain protein with three RCC1-like domains (RLDs), additional internal domains including a zinc finger ZZ-type and Cyt-b5 (Cytochrome b5-like Heme/Steroid binding) domains, and a C-terminal HECT (Homologous to the E6-AP Carboxyl Terminus) domain. The APC10/DOC1 domain of HERC2 is a homolog of the APC10 subunit and the DOC1 domain present in E3 ubiquitin ligases which mediate substrate ubiquitination (or ubiquitylation), a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. As suggested by structural relationships between HERC2 and other proteins such as HERC1, the proposed role for HERC2 in protein trafficking and degradation pathways is consistent with observations that mutations in HERC2 lead to neuromuscular secretory vesicle and sperm acrosome defects, other developmental abnormalities, and juvenile lethality of jdf2 mice. Recent studies have shown that the protein complex, HERC2-RNF8, coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes. Pssm-ID: 176485 Cd Length: 152 Bit Score: 295.44 E-value: 6.76e-92
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| ATS1 | COG5184 | Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ... |
2952-3305 | 2.70e-79 | ||||||
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton]; Pssm-ID: 444065 [Multi-domain] Cd Length: 343 Bit Score: 267.23 E-value: 2.70e-79
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| ATS1 | COG5184 | Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ... |
3949-4297 | 2.85e-77 | ||||||
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton]; Pssm-ID: 444065 [Multi-domain] Cd Length: 343 Bit Score: 261.45 E-value: 2.85e-77
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| HECTc | smart00119 | Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
4469-4795 | 8.89e-77 | ||||||
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes. Pssm-ID: 214523 Cd Length: 328 Bit Score: 259.47 E-value: 8.89e-77
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| HECT | pfam00632 | HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
4493-4795 | 8.98e-72 | ||||||
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus. Pssm-ID: 459880 Cd Length: 304 Bit Score: 244.06 E-value: 8.98e-72
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| ATS1 | COG5184 | Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ... |
438-741 | 1.68e-60 | ||||||
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton]; Pssm-ID: 444065 [Multi-domain] Cd Length: 343 Bit Score: 213.30 E-value: 1.68e-60
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| Cul7 | pfam11515 | Mouse development and cellular proliferation protein Cullin-7; The Cullin Ring Ligase family ... |
2558-2635 | 9.20e-47 | ||||||
Mouse development and cellular proliferation protein Cullin-7; The Cullin Ring Ligase family member, Cul7, is required for normal mouse development and cellular proliferation. Cul7 has a CPH domain which is a p53 interaction domain. The CPH domain interaction surface of P53 is present in the tetramerization domain. Pssm-ID: 463286 Cd Length: 78 Bit Score: 163.29 E-value: 9.20e-47
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| HUL4 | COG5021 | Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
4534-4790 | 1.61e-43 | ||||||
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 174.57 E-value: 1.61e-43
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| ZZ_HERC2 | cd02344 | Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ... |
2710-2754 | 4.17e-29 | ||||||
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential E3 ubiquitin protein ligase and/or guanine nucleotide exchange factor. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Pssm-ID: 239084 Cd Length: 45 Bit Score: 111.91 E-value: 4.17e-29
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| MIB_HERC2 | pfam06701 | Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ... |
1872-1932 | 2.06e-27 | ||||||
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect). Pssm-ID: 461991 Cd Length: 66 Bit Score: 107.69 E-value: 2.06e-27
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| UBA_HERC2 | cd14402 | UBA domain found in probable E3 ubiquitin-protein ligase HERC2 and similar proteins; HERC2, ... |
2462-2509 | 5.92e-23 | ||||||
UBA domain found in probable E3 ubiquitin-protein ligase HERC2 and similar proteins; HERC2, also called HECT domain and RCC1-like domain-containing protein 2, is a SUMO-regulated E3 ubiquitin ligase that plays an important role in the SUMO-dependent pathway which orchestrates the DNA double-strand break (DSB) response. Moreover, HERC2 functions as a RNF8 auxiliary factor that regulates ubiquitin-dependent retention of repair proteins on damaged chromosomes. In addition to a ubiquitin-association (UBA) domain, HERC2 contains more than one RCC1-like domains (RLDs) and a C-terminal HECT E3 ubiquitin ligase domain. Pssm-ID: 270585 Cd Length: 45 Bit Score: 94.36 E-value: 5.92e-23
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| RCC1 | pfam00415 | Regulator of chromosome condensation (RCC1) repeat; |
676-725 | 3.06e-17 | ||||||
Regulator of chromosome condensation (RCC1) repeat; Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 78.33 E-value: 3.06e-17
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| RCC1 | pfam00415 | Regulator of chromosome condensation (RCC1) repeat; |
3280-3328 | 8.66e-16 | ||||||
Regulator of chromosome condensation (RCC1) repeat; Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 74.09 E-value: 8.66e-16
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| RCC1 | pfam00415 | Regulator of chromosome condensation (RCC1) repeat; |
4115-4165 | 1.78e-14 | ||||||
Regulator of chromosome condensation (RCC1) repeat; Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 70.24 E-value: 1.78e-14
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| ZnF_ZZ | smart00291 | Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ... |
2706-2749 | 1.46e-11 | ||||||
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy. Pssm-ID: 197633 [Multi-domain] Cd Length: 44 Bit Score: 62.07 E-value: 1.46e-11
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| ZZ | pfam00569 | Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ... |
2706-2745 | 3.64e-09 | ||||||
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure. Pssm-ID: 395451 Cd Length: 45 Bit Score: 55.18 E-value: 3.64e-09
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| Cyt-b5 | pfam00173 | Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ... |
1212-1284 | 4.06e-09 | ||||||
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases. Pssm-ID: 459698 [Multi-domain] Cd Length: 74 Bit Score: 56.09 E-value: 4.06e-09
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| ANAPC10 | pfam03256 | Anaphase-promoting complex, subunit 10 (APC10); |
2807-2926 | 2.99e-04 | ||||||
Anaphase-promoting complex, subunit 10 (APC10); Pssm-ID: 367420 Cd Length: 185 Bit Score: 45.13 E-value: 2.99e-04
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| SH3_15 | pfam18346 | Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate ... |
2643-2700 | 1.79e-03 | ||||||
Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate recognition domain for a second, membrane-distal epitope of the Notch ligand (C-box). Although the first Mib repeat of REP may play a dominant role in ligand binding, the two repeats appear to cooperate in the engagement of the Jag1 tail. Mind bomb (Mib) proteins are large, multi-domain E3 ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. The structure and functional analysis, show that Mib1 contains two independent substrate recognition domains that engage two distinct epitopes from the cytoplasmic tail of the ligand Jagged1, one in the intracellular membrane proximal region and the other near the C terminus. REP domains have a five-stranded anti-parallel twisted beta sheet topology similar to that of SH3 domains. Pssm-ID: 465720 Cd Length: 67 Bit Score: 39.53 E-value: 1.79e-03
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| Name | Accession | Description | Interval | E-value | ||||||
| HECTc | cd00078 | HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
4426-4797 | 8.91e-121 | ||||||
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains. Pssm-ID: 238033 [Multi-domain] Cd Length: 352 Bit Score: 386.92 E-value: 8.91e-121
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| APC10-HERC2 | cd08664 | APC10-like DOC1 domain present in HERC2 (HECT domain and RLD2); This model represents the ... |
2769-2914 | 6.76e-92 | ||||||
APC10-like DOC1 domain present in HERC2 (HECT domain and RLD2); This model represents the APC10/DOC1 domain present in HERC2 (HECT domain and RLD2), a large multi-domain protein with three RCC1-like domains (RLDs), additional internal domains including a zinc finger ZZ-type and Cyt-b5 (Cytochrome b5-like Heme/Steroid binding) domains, and a C-terminal HECT (Homologous to the E6-AP Carboxyl Terminus) domain. The APC10/DOC1 domain of HERC2 is a homolog of the APC10 subunit and the DOC1 domain present in E3 ubiquitin ligases which mediate substrate ubiquitination (or ubiquitylation), a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. As suggested by structural relationships between HERC2 and other proteins such as HERC1, the proposed role for HERC2 in protein trafficking and degradation pathways is consistent with observations that mutations in HERC2 lead to neuromuscular secretory vesicle and sperm acrosome defects, other developmental abnormalities, and juvenile lethality of jdf2 mice. Recent studies have shown that the protein complex, HERC2-RNF8, coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes. Pssm-ID: 176485 Cd Length: 152 Bit Score: 295.44 E-value: 6.76e-92
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| ATS1 | COG5184 | Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ... |
2952-3305 | 2.70e-79 | ||||||
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton]; Pssm-ID: 444065 [Multi-domain] Cd Length: 343 Bit Score: 267.23 E-value: 2.70e-79
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| ATS1 | COG5184 | Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ... |
2999-3330 | 1.11e-77 | ||||||
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton]; Pssm-ID: 444065 [Multi-domain] Cd Length: 343 Bit Score: 262.61 E-value: 1.11e-77
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| ATS1 | COG5184 | Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ... |
3949-4297 | 2.85e-77 | ||||||
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton]; Pssm-ID: 444065 [Multi-domain] Cd Length: 343 Bit Score: 261.45 E-value: 2.85e-77
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| HECTc | smart00119 | Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
4469-4795 | 8.89e-77 | ||||||
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes. Pssm-ID: 214523 Cd Length: 328 Bit Score: 259.47 E-value: 8.89e-77
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| HECT | pfam00632 | HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
4493-4795 | 8.98e-72 | ||||||
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus. Pssm-ID: 459880 Cd Length: 304 Bit Score: 244.06 E-value: 8.98e-72
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| ATS1 | COG5184 | Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ... |
3993-4324 | 1.43e-68 | ||||||
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton]; Pssm-ID: 444065 [Multi-domain] Cd Length: 343 Bit Score: 236.41 E-value: 1.43e-68
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| APC10-like1 | cd08365 | APC10-like DOC1 domains of E3 ubiquitin ligases that mediate substrate ubiquitination; This ... |
2790-2914 | 1.96e-62 | ||||||
APC10-like DOC1 domains of E3 ubiquitin ligases that mediate substrate ubiquitination; This model represens the APC10-like DOC1 domain of multi-domain proteins present in E3 ubiquitin ligases. E3 ubiquitin ligases mediate substrate ubiquitination (or ubiquitylation), a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. APC10/DOC1 domains such as those present in HECT (Homologous to the E6-AP Carboxyl Terminus) and Cullin-RING (Really Interesting New Gene) E3 ubiquitin ligase proteins, HECTD3, and CUL7, respectively, are also included here. CUL7 is a member of the Cullin-RING ligase family and functions as a molecular scaffold assembling a SCF-ROC1-like E3 ubiquitin ligase complex consisting of Skp1, CUL7, Fbx29 F-box protein, and ROC1 (RING-box protein 1) and promotes ubiquitination. CUL7 is a multi-domain protein with a C-terminal cullin domain that binds ROC1 and a centrally positioned APC10/DOC1 domain. HECTD3 contains a C-terminal HECT domain which contains the active site for ubiquitin transfer onto substrates, and an N-terminal APC10/DOC1 domain which is responsible for substrate recognition and binding. An APC10/DOC1 domain homolog is also present in HERC2 (HECT domain and RLD2), a large multi-domain protein with three RCC1-like domains (RLDs), additional internal domains including zinc finger ZZ-type and Cyt-b5 (Cytochrome b5-like Heme/Steroid binding) domains, and a C-terminal HECT domain. Recent studies have shown that the protein complex HERC2-RNF8 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes. Also included in this hierarchy is an uncharacterized APC10/DOC1-like domain found in a multi-domain protein, which also contains CUB, zinc finger ZZ-type, and EF-hand domains. The APC10/DOC1 domain forms a beta-sandwich structure that is related in architecture to the galactose-binding domain-like fold; their sequences are quite dissimilar, however, and are not included here. Pssm-ID: 176483 Cd Length: 131 Bit Score: 210.44 E-value: 1.96e-62
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| ATS1 | COG5184 | Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ... |
438-741 | 1.68e-60 | ||||||
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton]; Pssm-ID: 444065 [Multi-domain] Cd Length: 343 Bit Score: 213.30 E-value: 1.68e-60
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| ATS1 | COG5184 | Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ... |
505-776 | 2.66e-60 | ||||||
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton]; Pssm-ID: 444065 [Multi-domain] Cd Length: 343 Bit Score: 212.53 E-value: 2.66e-60
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| APC10-like | cd08159 | APC10-like DOC1 domains in E3 ubiquitin ligases that mediate substrate ubiquitination; This ... |
2790-2914 | 1.39e-59 | ||||||
APC10-like DOC1 domains in E3 ubiquitin ligases that mediate substrate ubiquitination; This family contains the single domain protein, APC10, a subunit of the anaphase-promoting complex (APC), as well as the DOC1 domain of multi-domain proteins present in E3 ubiquitin ligases. E3 ubiquitin ligases mediate substrate ubiquitination (or ubiquitylation), a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. The APC, a multi-protein complex (or cyclosome), is a cell cycle-regulated, E3 ubiquitin ligase that controls important transitions in mitosis and the G1 phase by ubiquitinating regulatory proteins, thereby targeting them for degradation. APC10-like DOC1 domains such as those present in HECT (Homologous to the E6-AP Carboxyl Terminus) and Cullin-RING (Really Interesting New Gene) E3 ubiquitin ligase proteins, HECTD3, and CUL7, respectively, are also included in this hierarchy. CUL7 is a member of the Cullin-RING ligase family and functions as a molecular scaffold assembling a SCF-ROC1-like E3 ubiquitin ligase complex consisting of Skp1, CUL7, Fbx29 F-box protein, and ROC1 (RING-box protein 1) and promotes ubiquitination. CUL7 is a multi-domain protein with a C-terminal cullin domain that binds ROC1 and a centrally positioned APC10/DOC1 domain. HECTD3 contains a C-terminal HECT domain which contains the active site for ubiquitin transfer onto substrates, and an N-terminal APC10 domain which is responsible for substrate recognition and binding. An APC10/DOC1 domain homolog is also present in HERC2 (HECT domain and RLD2), a large multi-domain protein with three RCC1-like domains (RLDs), additional internal domains including zinc finger ZZ-type and Cyt-b5 (Cytochrome b5-like Heme/Steroid binding) domains, and a C-terminal HECT domain. Recent studies have shown that the protein complex HERC2-RNF8 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes. Also included in this hierarchy is an uncharacterized APC10/DOC1-like domain found in a multi-domain protein, which also contains CUB, zinc finger ZZ-type, and EF-hand domains. The APC10/DOC1 domain forms a beta-sandwich structure that is related in architecture to the galactose-binding domain-like fold; their sequences are quite dissimilar, however, and are not included here. Pssm-ID: 176482 Cd Length: 129 Bit Score: 201.93 E-value: 1.39e-59
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| ATS1 | COG5184 | Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ... |
425-701 | 2.57e-50 | ||||||
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton]; Pssm-ID: 444065 [Multi-domain] Cd Length: 343 Bit Score: 183.64 E-value: 2.57e-50
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| ATS1 | COG5184 | Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ... |
555-776 | 1.49e-47 | ||||||
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton]; Pssm-ID: 444065 [Multi-domain] Cd Length: 343 Bit Score: 175.55 E-value: 1.49e-47
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| Cul7 | pfam11515 | Mouse development and cellular proliferation protein Cullin-7; The Cullin Ring Ligase family ... |
2558-2635 | 9.20e-47 | ||||||
Mouse development and cellular proliferation protein Cullin-7; The Cullin Ring Ligase family member, Cul7, is required for normal mouse development and cellular proliferation. Cul7 has a CPH domain which is a p53 interaction domain. The CPH domain interaction surface of P53 is present in the tetramerization domain. Pssm-ID: 463286 Cd Length: 78 Bit Score: 163.29 E-value: 9.20e-47
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| HUL4 | COG5021 | Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
4534-4790 | 1.61e-43 | ||||||
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 174.57 E-value: 1.61e-43
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| APC10-HECTD3 | cd08666 | APC10-like DOC1 domain of HECTD3, a HECT E3 ubiquitin ligase protein that mediates substrate ... |
2787-2913 | 1.42e-31 | ||||||
APC10-like DOC1 domain of HECTD3, a HECT E3 ubiquitin ligase protein that mediates substrate ubiquitination; This model represents the APC10/DOC1 domain present in HECTD3, a HECT (Homologous to the E6-AP Carboxyl Terminus) E3 ubiquitin ligase protein. HECT E3 ubiquitin ligases mediate substrate ubiquitination (or ubiquitylation), and are a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. They also regulate the trafficking of many receptors, channels, transporters and viral proteins. HECTD3 (HECT domain-containing protein3) contains a C-terminal HECT domain with the active site for ubiquitin transfer onto substrates, and an N-terminal APC10/DOC1 domain, which is responsible for substrate recognition and binding. HECTD3 specifically recognizes the Trio-binding protein, Tara (Trio-associated repeat on actin), implicated in regulating actin cytoskeletal, cell motility and cell growth. Tara also binds to TRF1 and may participate in telomere maintenance and/or mitotic regulation through interacting with TRF1. HECTD3 interacts with and promotes the ubiquitination of Syntaxin 8, an endosomal syntaxin proposed to mediate distinct steps of endosomal protein trafficking. HECTD3-mediated Syntaxin 8 degradation has been suggested to contribute to the pathophysiology of neurodegenerative diseases. Pssm-ID: 176487 Cd Length: 134 Bit Score: 122.13 E-value: 1.42e-31
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| ZZ_HERC2 | cd02344 | Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ... |
2710-2754 | 4.17e-29 | ||||||
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential E3 ubiquitin protein ligase and/or guanine nucleotide exchange factor. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Pssm-ID: 239084 Cd Length: 45 Bit Score: 111.91 E-value: 4.17e-29
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| APC10-CUL7 | cd08665 | APC10-like DOC1 domain of CUL7, subunit of the SCF-ROC1-like E3 ubiquitin ligase complex that ... |
2786-2915 | 9.96e-28 | ||||||
APC10-like DOC1 domain of CUL7, subunit of the SCF-ROC1-like E3 ubiquitin ligase complex that mediates substrate ubiquitination; This model represents the APC10/DOC1 domain present in CUL7, a subunit of the SCF-ROC1-like E3 Ubiquitin (Ub) ligase complex, which mediates substrate ubiquitination (or ubiquitylation), and is a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. CUL7 is a member of the Cullin-RING ligase family and functions as a molecular scaffold assembling the SCF-ROC1-like E3 Ub ligase complex consisting of the adapter protein Skp1, CUL7, the WD40 repeat-containing F-box Fbw8 (also known as Fbx29), and ROC1 (RING-box protein 1). CUL7 is a large protein with a C-terminal cullin domain that binds ROC1 and additional domains, including an APC10/DOC1 domain. While the Fbw8 protein is responsible for substrate protein recognition, the ROC1 RING domain recruits an Ub-charged E2 Ub-conjugating enzyme for substrate ubiquitination. It remains to be determined how CUL7 binds to the Skp1-Fbw8 heterodimer. The CUL7 E3 Ub ligase has been implicated in the proteasomal degradation of the cellular proteins, cyclin D1, an important regulator of the G1 to S-phase cell cycle progression, and insulin receptor substrate 1, a critical component of the signaling pathways downstream of the insulin and insulin-like growth factor 1 receptor. CUL7 appears to be an important regulator of placental development. Germ line mutations of CUL7 are linked to 3-M syndrome and Yakuts short stature syndrome. Pssm-ID: 176486 Cd Length: 131 Bit Score: 111.17 E-value: 9.96e-28
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| MIB_HERC2 | pfam06701 | Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ... |
1872-1932 | 2.06e-27 | ||||||
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect). Pssm-ID: 461991 Cd Length: 66 Bit Score: 107.69 E-value: 2.06e-27
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| APC10-ZZEF1 | cd08667 | APC10/DOC1-like domain of uncharacterized Zinc finger ZZ-type and EF-hand domain-containing ... |
2791-2915 | 2.01e-25 | ||||||
APC10/DOC1-like domain of uncharacterized Zinc finger ZZ-type and EF-hand domain-containing protein 1 (ZZEF1) and homologs; This model represents the APC10/DOC1-like domain present in the uncharacterized Zinc finger ZZ-type and EF-hand domain-containing protein 1 (ZZEF1) of Mus musculus. Members of this family contain EF-hand, APC10, CUB, and zinc finger ZZ-type domains. ZZEF1-like APC10 domains are homologous to the APC10 subunit/DOC1 domains present in E3 ubiquitin ligases, which mediate substrate ubiquitination (or ubiquitylation), and are components of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. Pssm-ID: 176488 Cd Length: 131 Bit Score: 104.60 E-value: 2.01e-25
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| UBA_HERC2 | cd14402 | UBA domain found in probable E3 ubiquitin-protein ligase HERC2 and similar proteins; HERC2, ... |
2462-2509 | 5.92e-23 | ||||||
UBA domain found in probable E3 ubiquitin-protein ligase HERC2 and similar proteins; HERC2, also called HECT domain and RCC1-like domain-containing protein 2, is a SUMO-regulated E3 ubiquitin ligase that plays an important role in the SUMO-dependent pathway which orchestrates the DNA double-strand break (DSB) response. Moreover, HERC2 functions as a RNF8 auxiliary factor that regulates ubiquitin-dependent retention of repair proteins on damaged chromosomes. In addition to a ubiquitin-association (UBA) domain, HERC2 contains more than one RCC1-like domains (RLDs) and a C-terminal HECT E3 ubiquitin ligase domain. Pssm-ID: 270585 Cd Length: 45 Bit Score: 94.36 E-value: 5.92e-23
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| RCC1 | pfam00415 | Regulator of chromosome condensation (RCC1) repeat; |
676-725 | 3.06e-17 | ||||||
Regulator of chromosome condensation (RCC1) repeat; Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 78.33 E-value: 3.06e-17
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| RCC1 | pfam00415 | Regulator of chromosome condensation (RCC1) repeat; |
570-621 | 6.79e-16 | ||||||
Regulator of chromosome condensation (RCC1) repeat; Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 74.48 E-value: 6.79e-16
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| RCC1 | pfam00415 | Regulator of chromosome condensation (RCC1) repeat; |
3280-3328 | 8.66e-16 | ||||||
Regulator of chromosome condensation (RCC1) repeat; Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 74.09 E-value: 8.66e-16
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| RCC1 | pfam00415 | Regulator of chromosome condensation (RCC1) repeat; |
3227-3276 | 3.82e-15 | ||||||
Regulator of chromosome condensation (RCC1) repeat; Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 72.16 E-value: 3.82e-15
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| ZZ | cd02249 | Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ... |
2710-2754 | 5.19e-15 | ||||||
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins. Pssm-ID: 239069 [Multi-domain] Cd Length: 46 Bit Score: 71.70 E-value: 5.19e-15
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| RCC1 | pfam00415 | Regulator of chromosome condensation (RCC1) repeat; |
3069-3118 | 1.56e-14 | ||||||
Regulator of chromosome condensation (RCC1) repeat; Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 70.62 E-value: 1.56e-14
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| RCC1 | pfam00415 | Regulator of chromosome condensation (RCC1) repeat; |
4115-4165 | 1.78e-14 | ||||||
Regulator of chromosome condensation (RCC1) repeat; Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 70.24 E-value: 1.78e-14
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| RCC1 | pfam00415 | Regulator of chromosome condensation (RCC1) repeat; |
4272-4321 | 2.10e-14 | ||||||
Regulator of chromosome condensation (RCC1) repeat; Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 70.24 E-value: 2.10e-14
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| RCC1 | pfam00415 | Regulator of chromosome condensation (RCC1) repeat; |
4220-4268 | 2.66e-14 | ||||||
Regulator of chromosome condensation (RCC1) repeat; Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 69.85 E-value: 2.66e-14
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| RCC1 | pfam00415 | Regulator of chromosome condensation (RCC1) repeat; |
4062-4111 | 3.93e-14 | ||||||
Regulator of chromosome condensation (RCC1) repeat; Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 69.47 E-value: 3.93e-14
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| RCC1 | pfam00415 | Regulator of chromosome condensation (RCC1) repeat; |
3121-3172 | 8.09e-14 | ||||||
Regulator of chromosome condensation (RCC1) repeat; Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 68.31 E-value: 8.09e-14
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| RCC1 | pfam00415 | Regulator of chromosome condensation (RCC1) repeat; |
4168-4217 | 2.30e-13 | ||||||
Regulator of chromosome condensation (RCC1) repeat; Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 67.16 E-value: 2.30e-13
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| RCC1 | pfam00415 | Regulator of chromosome condensation (RCC1) repeat; |
3175-3224 | 2.42e-13 | ||||||
Regulator of chromosome condensation (RCC1) repeat; Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 67.16 E-value: 2.42e-13
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| RCC1 | pfam00415 | Regulator of chromosome condensation (RCC1) repeat; |
624-673 | 7.35e-13 | ||||||
Regulator of chromosome condensation (RCC1) repeat; Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 65.62 E-value: 7.35e-13
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| RCC1 | pfam00415 | Regulator of chromosome condensation (RCC1) repeat; |
514-567 | 1.22e-12 | ||||||
Regulator of chromosome condensation (RCC1) repeat; Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 65.23 E-value: 1.22e-12
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| UBA_HERC1_2 | cd14331 | UBA domain found in probable E3 ubiquitin-protein ligase HERC1, HERC2 and similar proteins; ... |
2464-2507 | 5.06e-12 | ||||||
UBA domain found in probable E3 ubiquitin-protein ligase HERC1, HERC2 and similar proteins; HERC1, also called HECT domain and RCC1-like domain-containing protein 1, p532, or p619, is an ubiquitously expressed giant protein involved in ubiquitin-dependent intracellular membrane trafficking through its interaction with vesicle coat proteins such as clathrin and ARF. Moreover, it has been identified as a tuberous sclerosis complex TSC2-interacting protein that may play a role in TSC-mTOR (mammalian target of rapamycin) pathway. HERC2, also called HECT domain and RCC1-like domain-containing protein 2, is a SUMO-regulated E3 ubiquitin ligase that plays an important role in the SUMO-dependent pathway which orchestrates the DNA double-strand break (DSB) response. Moreover, HERC2 functions as a RNF8 auxiliary factor that regulates ubiquitin-dependent retention of repair proteins on damaged chromosomes. HERC1 and HERC2 are multi-domain proteins with different domain organizations. Both of them contain a ubiquitin-association (UBA) domain, more than one RCC1-like domains (RLDs) and a C-terminal HECT E3 ubiquitin ligase domain. Pssm-ID: 270516 Cd Length: 40 Bit Score: 63.21 E-value: 5.06e-12
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| ZZ_Mind_bomb | cd02339 | Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ... |
2710-2754 | 5.46e-12 | ||||||
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Mind bomb is an E3 ubiqitin ligase that has been shown to regulate signaling by the Notch ligand Delta in Drosophila melanogaster. Pssm-ID: 239079 Cd Length: 45 Bit Score: 63.25 E-value: 5.46e-12
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| ZZ_NBR1_like | cd02340 | Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ... |
2710-2754 | 1.13e-11 | ||||||
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain. Pssm-ID: 239080 Cd Length: 43 Bit Score: 62.28 E-value: 1.13e-11
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| ZnF_ZZ | smart00291 | Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ... |
2706-2749 | 1.46e-11 | ||||||
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy. Pssm-ID: 197633 [Multi-domain] Cd Length: 44 Bit Score: 62.07 E-value: 1.46e-11
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| ZZ_PCMF_like | cd02338 | Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ... |
2710-2752 | 3.28e-10 | ||||||
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Human potassium channel modulatory factor 1 or FIGC has been shown to possess intrinsic E3 ubiquitin ligase activity and to promote ubiquitination. Pssm-ID: 239078 Cd Length: 49 Bit Score: 58.13 E-value: 3.28e-10
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| ZZ | pfam00569 | Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ... |
2706-2745 | 3.64e-09 | ||||||
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure. Pssm-ID: 395451 Cd Length: 45 Bit Score: 55.18 E-value: 3.64e-09
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| Cyt-b5 | pfam00173 | Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ... |
1212-1284 | 4.06e-09 | ||||||
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases. Pssm-ID: 459698 [Multi-domain] Cd Length: 74 Bit Score: 56.09 E-value: 4.06e-09
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| RCC1_2 | pfam13540 | Regulator of chromosome condensation (RCC1) repeat; |
3263-3292 | 7.43e-09 | ||||||
Regulator of chromosome condensation (RCC1) repeat; Pssm-ID: 463914 [Multi-domain] Cd Length: 30 Bit Score: 53.97 E-value: 7.43e-09
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| APC10 | cd08366 | APC10 subunit of the anaphase-promoting complex (APC) that mediates substrate ubiquitination; ... |
2795-2915 | 1.17e-08 | ||||||
APC10 subunit of the anaphase-promoting complex (APC) that mediates substrate ubiquitination; This model represents the single domain protein APC10, a subunit of the anaphase-promoting complex (APC), which is a multi-subunit E3 ubiquitin ligase. E3 ubiquitin ligases mediate substrate ubiquitination (or ubiquitylation), a vital component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. The APC (also known as the cyclosome), is a cell cycle-regulated E3 ubiquitin ligase that controls important transitions in mitosis and the G1 phase by ubiquitinating regulatory proteins, thereby targeting them for degradation. In mitosis, the APC initiates sister chromatid separation by ubiquitinating the anaphase inhibitor securin and triggers exit from mitosis by ubiquitinating cyclin B. The C-terminus of APC10 binds to CDC27/APC3, an APC subunit that contains multiple tetratrico peptide repeats. APC10 domains are homologous to the DOC1 domains present in the HECT (Homologous to the E6-AP Carboxyl Terminus) E3 ubiquitin ligase protein, and the Cullin-RING (Really Interesting New Gene) E3 ubiquitin ligase complex. The APC10/DOC1 domain forms a beta-sandwich structure that is related in architecture to the galactose-binding domain-like fold; their sequences are quite dissimilar, however, and are not included here. Pssm-ID: 176484 Cd Length: 139 Bit Score: 56.80 E-value: 1.17e-08
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| RCC1 | pfam00415 | Regulator of chromosome condensation (RCC1) repeat; |
3014-3066 | 2.92e-08 | ||||||
Regulator of chromosome condensation (RCC1) repeat; Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 52.52 E-value: 2.92e-08
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| RCC1_2 | pfam13540 | Regulator of chromosome condensation (RCC1) repeat; |
4256-4285 | 1.18e-07 | ||||||
Regulator of chromosome condensation (RCC1) repeat; Pssm-ID: 463914 [Multi-domain] Cd Length: 30 Bit Score: 50.50 E-value: 1.18e-07
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| RCC1_2 | pfam13540 | Regulator of chromosome condensation (RCC1) repeat; |
3105-3134 | 1.57e-07 | ||||||
Regulator of chromosome condensation (RCC1) repeat; Pssm-ID: 463914 [Multi-domain] Cd Length: 30 Bit Score: 50.12 E-value: 1.57e-07
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| ZZ_dystrophin | cd02334 | Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ... |
2710-2749 | 4.30e-07 | ||||||
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan. Pssm-ID: 239074 Cd Length: 49 Bit Score: 49.28 E-value: 4.30e-07
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| ZZ_UBA_plant | cd02342 | Zinc finger, ZZ type. Zinc finger present in plant ubiquitin-associated (UBA) proteins. The ZZ ... |
2710-2740 | 5.50e-07 | ||||||
Zinc finger, ZZ type. Zinc finger present in plant ubiquitin-associated (UBA) proteins. The ZZ motif coordinates a zinc ion and most likely participates in ligand binding or molecular scaffolding. Pssm-ID: 239082 Cd Length: 43 Bit Score: 48.73 E-value: 5.50e-07
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| ZZ_ADA2 | cd02335 | Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ... |
2711-2751 | 2.70e-06 | ||||||
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Pssm-ID: 239075 [Multi-domain] Cd Length: 49 Bit Score: 47.29 E-value: 2.70e-06
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| RCC1_2 | pfam13540 | Regulator of chromosome condensation (RCC1) repeat; |
554-583 | 5.39e-06 | ||||||
Regulator of chromosome condensation (RCC1) repeat; Pssm-ID: 463914 [Multi-domain] Cd Length: 30 Bit Score: 45.88 E-value: 5.39e-06
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| ZZ_ZZZ3 | cd02341 | Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ... |
2710-2749 | 5.72e-06 | ||||||
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Pssm-ID: 239081 Cd Length: 48 Bit Score: 46.27 E-value: 5.72e-06
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| RCC1_2 | pfam13540 | Regulator of chromosome condensation (RCC1) repeat; |
712-738 | 5.89e-06 | ||||||
Regulator of chromosome condensation (RCC1) repeat; Pssm-ID: 463914 [Multi-domain] Cd Length: 30 Bit Score: 45.49 E-value: 5.89e-06
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| RCC1_2 | pfam13540 | Regulator of chromosome condensation (RCC1) repeat; |
660-687 | 8.06e-06 | ||||||
Regulator of chromosome condensation (RCC1) repeat; Pssm-ID: 463914 [Multi-domain] Cd Length: 30 Bit Score: 45.11 E-value: 8.06e-06
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| RCC1_2 | pfam13540 | Regulator of chromosome condensation (RCC1) repeat; |
4204-4233 | 1.54e-05 | ||||||
Regulator of chromosome condensation (RCC1) repeat; Pssm-ID: 463914 [Multi-domain] Cd Length: 30 Bit Score: 44.34 E-value: 1.54e-05
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| UBA_HERC1 | cd14401 | UBA domain found in probable E3 ubiquitin-protein ligase HERC1 and similar proteins; HERC1, ... |
2463-2508 | 2.02e-05 | ||||||
UBA domain found in probable E3 ubiquitin-protein ligase HERC1 and similar proteins; HERC1, also called HECT domain and RCC1-like domain-containing protein 1, or p532, or p619, is an ubiquitously expressed multi-domain protein involved in ubiquitin-dependent intracellular membrane trafficking through its interaction with vesicle coat proteins such as clathrin and ARF. Moreover, it has been identified as a tuberous sclerosis complex TSC2-interacting protein that may play a role in TSC-mTOR (mammalian target of rapamycin) pathway. In addition to a ubiquitin-association (UBA) domain, HERC1 contains more than one RCC1-like domains (RLDs) and a C-terminal HECT E3 ubiquitin ligase domain. At this point, it may function as both E3 ubiquitin ligases and guanine nucleotide exchange factors (GEFs). Pssm-ID: 270584 Cd Length: 44 Bit Score: 44.68 E-value: 2.02e-05
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| ATS1 | COG5184 | Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ... |
3946-4016 | 4.70e-05 | ||||||
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton]; Pssm-ID: 444065 [Multi-domain] Cd Length: 343 Bit Score: 49.20 E-value: 4.70e-05
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| RCC1_2 | pfam13540 | Regulator of chromosome condensation (RCC1) repeat; |
4098-4127 | 1.68e-04 | ||||||
Regulator of chromosome condensation (RCC1) repeat; Pssm-ID: 463914 [Multi-domain] Cd Length: 30 Bit Score: 41.64 E-value: 1.68e-04
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| RCC1_2 | pfam13540 | Regulator of chromosome condensation (RCC1) repeat; |
3211-3238 | 1.80e-04 | ||||||
Regulator of chromosome condensation (RCC1) repeat; Pssm-ID: 463914 [Multi-domain] Cd Length: 30 Bit Score: 41.26 E-value: 1.80e-04
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| ANAPC10 | pfam03256 | Anaphase-promoting complex, subunit 10 (APC10); |
2807-2926 | 2.99e-04 | ||||||
Anaphase-promoting complex, subunit 10 (APC10); Pssm-ID: 367420 Cd Length: 185 Bit Score: 45.13 E-value: 2.99e-04
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| RCC1_2 | pfam13540 | Regulator of chromosome condensation (RCC1) repeat; |
3157-3187 | 4.11e-04 | ||||||
Regulator of chromosome condensation (RCC1) repeat; Pssm-ID: 463914 [Multi-domain] Cd Length: 30 Bit Score: 40.49 E-value: 4.11e-04
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| UBA_UBXN1 | cd14302 | UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also ... |
2466-2509 | 4.89e-04 | ||||||
UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also called SAPK substrate protein 1 (SAKS1) or UBA/UBX 33.3 kDa protein, is a widely expressed protein containing an N-terminal ubiquitin-associated (UBA) domain, a coiled-coil region, and a C-terminal ubiquitin-like (UBX) domain. It binds polyubiquitin and valosin-containing protein (VCP), and has been identified as a substrate for stress-activated protein kinases (SAPKs). Moreover, UBXN1 specifically binds to Homer2b. It may also interact with ubiquitin (Ub) and may be involved in the Ub-proteasome proteolytic pathways. In addition, UBXN1 can associate with autoubiquitinated BRCA1 tumor suppressor and inhibit its enzymatic function through its UBA domain. Pssm-ID: 270487 [Multi-domain] Cd Length: 41 Bit Score: 40.35 E-value: 4.89e-04
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| ZZ_dah | cd02345 | Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ... |
2711-2754 | 5.03e-04 | ||||||
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dah (discontinuous actin hexagon) is a membrane associated protein essential for cortical furrow formation in Drosophila. Pssm-ID: 239085 Cd Length: 49 Bit Score: 40.65 E-value: 5.03e-04
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| ZZ_CBP | cd02337 | Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ... |
2711-2745 | 5.12e-04 | ||||||
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. CREB-binding protein (CBP) is a large multidomain protein that provides binding sites for transcriptional coactivators, the role of the ZZ domain in CBP/p300 is unclear. Pssm-ID: 239077 Cd Length: 41 Bit Score: 40.62 E-value: 5.12e-04
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| RCC1_2 | pfam13540 | Regulator of chromosome condensation (RCC1) repeat; |
3051-3081 | 7.79e-04 | ||||||
Regulator of chromosome condensation (RCC1) repeat; Pssm-ID: 463914 [Multi-domain] Cd Length: 30 Bit Score: 39.71 E-value: 7.79e-04
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| UBA1_atUBP14 | cd14295 | UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) ... |
2463-2509 | 9.36e-04 | ||||||
UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) and similar proteins; atUBP14, also called deubiquitinating enzyme 14, TITAN-6 protein, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is related to the isopeptidase T class of deubiquitinating enzymes that recycle polyubiquitin chains following protein degradation. atUBP14 is essential for early plant development. It can disassemble multi-ubiquitin chains linked internally via epsilon-amino isopeptide bonds using Lys48 and can process some, but not all, translational fusions of ubiquitin linked via alpha-amino peptide bonds. atUBP14 contains two ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain. Pssm-ID: 270481 [Multi-domain] Cd Length: 45 Bit Score: 39.66 E-value: 9.36e-04
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| SH3_15 | pfam18346 | Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate ... |
2643-2700 | 1.79e-03 | ||||||
Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate recognition domain for a second, membrane-distal epitope of the Notch ligand (C-box). Although the first Mib repeat of REP may play a dominant role in ligand binding, the two repeats appear to cooperate in the engagement of the Jag1 tail. Mind bomb (Mib) proteins are large, multi-domain E3 ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. The structure and functional analysis, show that Mib1 contains two independent substrate recognition domains that engage two distinct epitopes from the cytoplasmic tail of the ligand Jagged1, one in the intracellular membrane proximal region and the other near the C terminus. REP domains have a five-stranded anti-parallel twisted beta sheet topology similar to that of SH3 domains. Pssm-ID: 465720 Cd Length: 67 Bit Score: 39.53 E-value: 1.79e-03
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| RCC1 | pfam00415 | Regulator of chromosome condensation (RCC1) repeat; |
2964-3011 | 2.15e-03 | ||||||
Regulator of chromosome condensation (RCC1) repeat; Pssm-ID: 395335 [Multi-domain] Cd Length: 50 Bit Score: 39.04 E-value: 2.15e-03
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| ZZ_EF | cd02343 | Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif ... |
2710-2740 | 2.80e-03 | ||||||
Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Pssm-ID: 239083 Cd Length: 48 Bit Score: 38.45 E-value: 2.80e-03
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| UBA2_spUBP14_like | cd14297 | UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ... |
2462-2508 | 8.57e-03 | ||||||
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 (spUBP14) and similar proteins; spUBP14, also called deubiquitinating enzyme 14, UBA domain-containing protein 2, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, functions as a deubiquitinating enzyme that is involved in protein degradation in fission yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA2 domain. Pssm-ID: 270483 [Multi-domain] Cd Length: 39 Bit Score: 37.07 E-value: 8.57e-03
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