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Conserved domains on  [gi|1886669751|gb|KAF6459902|]
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zinc finger ZZ-type and EF-hand domain containing 1 [Rousettus aegyptiacus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
APC10-like super family cl02148
APC10-like DOC1 domains in E3 ubiquitin ligases that mediate substrate ubiquitination; This ...
 251-355 1.44e-68

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.


The actual alignment was detected with superfamily member cd08667:

Pssm-ID: 382862  Cd Length: 131  Bit Score: 212.46  E-value: 1.44e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886669751 251 KCYAYIETSSNPADIDKMTNGETSSYWQSDGSARSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVAVGRNASDLQE 330
Cdd:cd08667     2 KCYAYIEVSSNSADIDRMTDGETSTYWQSDGSARSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVSVGRSASSLQE 81

                          90       100
                  ....*....|....*....|....*
gi 1886669751 331 VRDVHIPSNVTGYVTLLENANISQL 355
Cdd:cd08667    82 VRDVHIPSNVTGYVTLLENANISYL 106
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
95-141 8.79e-05

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG5126:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.09  E-value: 8.79e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1886669751  95 VTLEQFRELLEARGAgcTGEQFEEAFAQFDAEGDGTVDAENMLEALK 141
Cdd:COG5126    86 ISADEFRRLLTALGV--SEEEADELFARLDTDGDGKISFEEFVAAVR 130
 
Name Accession Description Interval E-value
APC10-ZZEF1 cd08667
APC10/DOC1-like domain of uncharacterized Zinc finger ZZ-type and EF-hand domain-containing ...
 251-355 1.44e-68

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: 212.46  E-value: 1.44e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886669751 251 KCYAYIETSSNPADIDKMTNGETSSYWQSDGSARSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVAVGRNASDLQE 330
Cdd:cd08667     2 KCYAYIEVSSNSADIDRMTDGETSTYWQSDGSARSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVSVGRSASSLQE 81

                          90       100
                  ....*....|....*....|....*
gi 1886669751 331 VRDVHIPSNVTGYVTLLENANISQL 355
Cdd:cd08667    82 VRDVHIPSNVTGYVTLLENANISYL 106
ANAPC10 pfam03256
Anaphase-promoting complex, subunit 10 (APC10);
265-337 2.39e-08

Anaphase-promoting complex, subunit 10 (APC10);


Pssm-ID: 367420  Cd Length: 185  Bit Score: 53.60  E-value: 2.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886669751 265 IDKMTNGETSSYWQSDGSaRSHWIRLKMKPDVVLRHLSIAV-AATDQSYMPQQVTVAVGRNASDLQEVRD---------V 334
Cdd:pfam03256  42 VDLLRDDNLDTYWQSDGS-QPHLVNIQFRKKTPVKYVAIYLdYKLDESYTPSKISVRAGTGFNDLQEVRVvdleeptgwV 120


                  ...
gi 1886669751 335 HIP 337
Cdd:pfam03256 121 HIP 123
DOC1 COG5156
Anaphase-promoting complex (APC), subunit 10 [Cell division and chromosome partitioning / ...
 257-346 1.68e-06

Anaphase-promoting complex (APC), subunit 10 [Cell division and chromosome partitioning / Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227485  Cd Length: 189  Bit Score: 48.05  E-value: 1.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886669751 257 ETSSNPadIDKMTNGETSSYWQSDGSaRSHWIRLKMKPDVVLRHLSIAVAAT-DQSYMPQQVTVAVGRNASDLQEVRDVH 335
Cdd:COG5156    37 FKRGHP--LRELLDDNMDTYWQSDGV-QPHSIQISFDKRRYIQSVQLFLSFTqDESYTPSKIGVRAGLTREDVREISSVE 113

                          90
                  ....*....|.
gi 1886669751 336 IpSNVTGYVTL 346
Cdd:COG5156   114 V-VEPEGWVTL 123
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
95-141 8.79e-05

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.09  E-value: 8.79e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1886669751  95 VTLEQFRELLEARGAgcTGEQFEEAFAQFDAEGDGTVDAENMLEALK 141
Cdd:COG5126    86 ISADEFRRLLTALGV--SEEEADELFARLDTDGDGKISFEEFVAAVR 130
EF-hand_6 pfam13405
EF-hand domain;
115-142 1.41e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 36.00  E-value: 1.41e-03
                          10        20
                  ....*....|....*....|....*...
gi 1886669751 115 QFEEAFAQFDAEGDGTVDAENMLEALKN 142
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRS 28
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 115-142 1.94e-03

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 35.43  E-value: 1.94e-03
                           10        20
                   ....*....|....*....|....*...
gi 1886669751  115 QFEEAFAQFDAEGDGTVDAENMLEALKN 142
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKA 28
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 115-157 3.49e-03

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 35.60  E-value: 3.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1886669751 115 QFEEAFAQFDAEGDGTVDAENMLEALKNSSGANLQGELSHIIR 157
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIR 43
 
Name Accession Description Interval E-value
APC10-ZZEF1 cd08667
APC10/DOC1-like domain of uncharacterized Zinc finger ZZ-type and EF-hand domain-containing ...
 251-355 1.44e-68

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: 212.46  E-value: 1.44e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886669751 251 KCYAYIETSSNPADIDKMTNGETSSYWQSDGSARSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVAVGRNASDLQE 330
Cdd:cd08667     2 KCYAYIEVSSNSADIDRMTDGETSTYWQSDGSARSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVSVGRSASSLQE 81

                          90       100
                  ....*....|....*....|....*
gi 1886669751 331 VRDVHIPSNVTGYVTLLENANISQL 355
Cdd:cd08667    82 VRDVHIPSNVTGYVTLLENANISYL 106
APC10-like1 cd08365
APC10-like DOC1 domains of E3 ubiquitin ligases that mediate substrate ubiquitination; This ...
 251-355 2.66e-55

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: 178.47  E-value: 2.66e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886669751 251 KCY-AYIETSSNPADIDKMTNGETSSYWQSDGSARSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVAVGRNASDLQ 329
Cdd:cd08365     2 KCYvESIEVSSNPADASRLTDGNTSTYWQSDGSQGSHWIRLKMKPDVLVRHLSLAVDATDSSYMPQRVVVAGGRSASNLQ 81

                          90       100
                  ....*....|....*....|....*.
gi 1886669751 330 EVRDVHIPSNVTGYVTLLENANISQL 355
Cdd:cd08365    82 ELRDVNIPPSVTGYVTLLEDATISQP 107
APC10-like cd08159
APC10-like DOC1 domains in E3 ubiquitin ligases that mediate substrate ubiquitination; This ...
 251-355 2.78e-50

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: 165.34  E-value: 2.78e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886669751 251 KCY-AYIETSSNPADIDKMTNGETSSYWQSDGSARSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVAVGRNASDLQ 329
Cdd:cd08159     1 KCYtASIEVSSNPLPVSRLTDGNYDTYWQSDGSQGSHWIRLFMKKDVLIRVLAIFVDMADSSYMPSLVVVYGGHSPSDLR 80

                          90       100
                  ....*....|....*....|....*.
gi 1886669751 330 EVRDVHIPsNVTGYVTLLENANISQL 355
Cdd:cd08159    81 ELKDVNIR-PSNGWVALLEDDTLKCP 105
APC10-HECTD3 cd08666
APC10-like DOC1 domain of HECTD3, a HECT E3 ubiquitin ligase protein that mediates substrate ...
 248-350 1.71e-23

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: 94.78  E-value: 1.71e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886669751 248 SVAKCYAYIETSSNPADIDK--MTNGETSSYWQSDGSARSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVAvGRNA 325
Cdd:cd08666     2 SVKQYVESIEVSSYTDDFNVscLTDGDPDTYWESDGSQGQHWIRLHMKKGTIIKKLLLTVDATDDNYMPKRVAVY-GGEG 80

                          90       100
                  ....*....|....*....|....*
gi 1886669751 326 SDLQEVRDVHIPSNVTGYVTLLENA 350
Cdd:cd08666    81 DNLKKLNDVSIDETLIGDVCILEDM 105
APC10-CUL7 cd08665
APC10-like DOC1 domain of CUL7, subunit of the SCF-ROC1-like E3 ubiquitin ligase complex that ...
 251-349 3.66e-22

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: 91.14  E-value: 3.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886669751 251 KCYAYIETSSNPADIDKMTNGETSSYWQSDGSARSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVAVGRNASDLQ- 329
Cdd:cd08665     2 KCWEKVEVSSNPHRANKLTDGNPKTYWESNGSTGSHYINIHMHRGVVIRQLYMLVASEDSSYMPARVVVLGGDSPSCITt 81

                          90       100
                  ....*....|....*....|
gi 1886669751 330 EVRDVHIpSNVTGYVTLLEN 349
Cdd:cd08665    82 ELNAVNV-SPTASRVVLLEN 100
APC10-HERC2 cd08664
APC10-like DOC1 domain present in HERC2 (HECT domain and RLD2); This model represents the ...
 241-350 2.47e-19

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: 83.96  E-value: 2.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886669751 241 PEMDKLKSVAKCYAYIETSSNPADIDKMTNGeTSSYWQSDGSARSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVA 320
Cdd:cd08664    16 GEGDLIDDWSRCVRSLTVSSNENQAKRLIDG-SGSYWQSSGSQGKHWIRLELHPDVLIHSLKIIVDPADSSYMPSLVVVS 94

                          90       100       110
                  ....*....|....*....|....*....|
gi 1886669751 321 VGRNASDLQEVRDVHIPSNVTgYVTLLENA 350
Cdd:cd08664    95 GGDSLNSLKELKTINVNATDT-LVTLLQDV 123
APC10 cd08366
APC10 subunit of the anaphase-promoting complex (APC) that mediates substrate ubiquitination; ...
 265-346 2.59e-09

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: 55.26  E-value: 2.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886669751 265 IDKMTNGETSSYWQSDGSArSHWIRLKMKPDVVLRHLSIAVA-ATDQSYMPQQVTVAVGRNASDLQEVRDVHIpSNVTGY 343
Cdd:cd08366    20 VDQLRDDSLDTYWQSDGPQ-PHLINIQFSKKTDISAVALYLDyKLDESYTPSKISIRAGTSPHDLQEVRTVEL-EEPNGW 97


                  ...
gi 1886669751 344 VTL 346
Cdd:cd08366    98 VHI 100
ANAPC10 pfam03256
Anaphase-promoting complex, subunit 10 (APC10);
265-337 2.39e-08

Anaphase-promoting complex, subunit 10 (APC10);


Pssm-ID: 367420  Cd Length: 185  Bit Score: 53.60  E-value: 2.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886669751 265 IDKMTNGETSSYWQSDGSaRSHWIRLKMKPDVVLRHLSIAV-AATDQSYMPQQVTVAVGRNASDLQEVRD---------V 334
Cdd:pfam03256  42 VDLLRDDNLDTYWQSDGS-QPHLVNIQFRKKTPVKYVAIYLdYKLDESYTPSKISVRAGTGFNDLQEVRVvdleeptgwV 120


                  ...
gi 1886669751 335 HIP 337
Cdd:pfam03256 121 HIP 123
DOC1 COG5156
Anaphase-promoting complex (APC), subunit 10 [Cell division and chromosome partitioning / ...
 257-346 1.68e-06

Anaphase-promoting complex (APC), subunit 10 [Cell division and chromosome partitioning / Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227485  Cd Length: 189  Bit Score: 48.05  E-value: 1.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886669751 257 ETSSNPadIDKMTNGETSSYWQSDGSaRSHWIRLKMKPDVVLRHLSIAVAAT-DQSYMPQQVTVAVGRNASDLQEVRDVH 335
Cdd:COG5156    37 FKRGHP--LRELLDDNMDTYWQSDGV-QPHSIQISFDKRRYIQSVQLFLSFTqDESYTPSKIGVRAGLTREDVREISSVE 113

                          90
                  ....*....|.
gi 1886669751 336 IpSNVTGYVTL 346
Cdd:COG5156   114 V-VEPEGWVTL 123
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
95-141 8.79e-05

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.09  E-value: 8.79e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1886669751  95 VTLEQFRELLEARGAgcTGEQFEEAFAQFDAEGDGTVDAENMLEALK 141
Cdd:COG5126    86 ISADEFRRLLTALGV--SEEEADELFARLDTDGDGKISFEEFVAAVR 130
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 256-342 1.20e-04

F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 41.66  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886669751 256 IETSSNPAD---IDKMTNGETSSYWQSDGSARSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVAVGRNASDLQEVR 332
Cdd:pfam00754   2 ITASSSYSGegpAAAALDGDPNTAWSAWSGDDPQWIQVDLGKPKKITGVVTQGRQDGSNGYVTSYKIEYSLDGENWTTVK 81

                          90
                  ....*....|
gi 1886669751 333 DVHIPSNVTG 342
Cdd:pfam00754  82 DEKIPGNNDN 91
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
76-142 5.38e-04

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.78  E-value: 5.38e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1886669751  76 HHGALLRWLEERLGR----GEESVTLEQFRELLEARGAGCTGEQFEEAFAQFDAEGDGTVDAENMLEALKN 142
Cdd:COG5126    27 FEALFRRLWATLFSEadtdGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTA 97
EF-hand_6 pfam13405
EF-hand domain;
115-142 1.41e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 36.00  E-value: 1.41e-03
                          10        20
                  ....*....|....*....|....*...
gi 1886669751 115 QFEEAFAQFDAEGDGTVDAENMLEALKN 142
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRS 28
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 115-142 1.94e-03

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 35.43  E-value: 1.94e-03
                           10        20
                   ....*....|....*....|....*...
gi 1886669751  115 QFEEAFAQFDAEGDGTVDAENMLEALKN 142
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKA 28
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 115-157 3.49e-03

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 35.60  E-value: 3.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1886669751 115 QFEEAFAQFDAEGDGTVDAENMLEALKNSSGANLQGELSHIIR 157
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIR 43
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 116-141 7.12e-03

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 33.91  E-value: 7.12e-03
                          10        20
                  ....*....|....*....|....*.
gi 1886669751 116 FEEAFAQFDAEGDGTVDAENMLEALK 141
Cdd:pfam00036   2 LKEIFRLFDKDGDGKIDFEEFKELLK 27
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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