NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|37362650|ref|NP_011274|]
View 

anaphase promoting complex subunit DOC1 [Saccharomyces cerevisiae S288C]

Protein Classification

anaphase-promoting complex subunit 10 family protein( domain architecture ID 10009106)

anaphase-promoting complex subunit 10 (APC10) family protein is a component of the APC that mediates substrate ubiquitination

CATH:  2.60.120.260
Gene Ontology:  GO:0005680|GO:0031145|GO:0007049|GO:0051301

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
DOC1 COG5156
Anaphase-promoting complex (APC), subunit 10 [Cell division and chromosome partitioning / ...
 59-248 6.69e-120

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


:

Pssm-ID: 227485  Cd Length: 189  Bit Score: 339.64  E-value: 6.69e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37362650  59 NPTPENLQHMFHQGIEILDSARMINVTHLALWKPSSFKLGNPVDFALDDNYDTFWQSDGGQPHQLDIMFSKRMDICVMAI 138
Cdd:COG5156   1 NPTPENLQHMFHQGIEILDSARMINVTHLAEWRLSSFKRGHPLRELLDDNMDTYWQSDGVQPHSIQISFDKRRYIQSVQL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37362650 139 FFSMIADESYAPSLVKVYAGHSPSDARFYKMLEVRNVNGWVALRFLDNREDDqLLKCQFIRLLFPVNHENGKDTHLRGIR 218
Cdd:COG5156  81 FLSFTQDESYTPSKIGVRAGLTREDVREISSVEVVEPEGWVTLSVADKREDD-LLKCIYILVVINSNHQEGKDSHVRHIK 159

                       170       180       190
                ....*....|....*....|....*....|
gi 37362650 219 LYVPSNEPHQDTHEWAQTLPETNNVFQDAI 248
Cdd:COG5156 160 IYEPSTEEIYYKIEWAQTLPETNNVFQDAI 189
 
Name Accession Description Interval E-value
DOC1 COG5156
Anaphase-promoting complex (APC), subunit 10 [Cell division and chromosome partitioning / ...
 59-248 6.69e-120

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


Pssm-ID: 227485  Cd Length: 189  Bit Score: 339.64  E-value: 6.69e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37362650  59 NPTPENLQHMFHQGIEILDSARMINVTHLALWKPSSFKLGNPVDFALDDNYDTFWQSDGGQPHQLDIMFSKRMDICVMAI 138
Cdd:COG5156   1 NPTPENLQHMFHQGIEILDSARMINVTHLAEWRLSSFKRGHPLRELLDDNMDTYWQSDGVQPHSIQISFDKRRYIQSVQL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37362650 139 FFSMIADESYAPSLVKVYAGHSPSDARFYKMLEVRNVNGWVALRFLDNREDDqLLKCQFIRLLFPVNHENGKDTHLRGIR 218
Cdd:COG5156  81 FLSFTQDESYTPSKIGVRAGLTREDVREISSVEVVEPEGWVTLSVADKREDD-LLKCIYILVVINSNHQEGKDSHVRHIK 159

                       170       180       190
                ....*....|....*....|....*....|
gi 37362650 219 LYVPSNEPHQDTHEWAQTLPETNNVFQDAI 248
Cdd:COG5156 160 IYEPSTEEIYYKIEWAQTLPETNNVFQDAI 189
APC10 cd08366
APC10 subunit of the anaphase-promoting complex (APC) that mediates substrate ubiquitination; ...
 83-220 8.00e-68

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: 205.87  E-value: 8.00e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37362650  83 NVTHLALWKPSSFKLGNPVDFALDDNYDTFWQSDGGQPHQLDIMFSKRMDICVMAIFFSMIADESYAPSLVKVYAGHSPS 162
Cdd:cd08366   2 EIGSLAVWSLSSAKPGNGVDQLRDDSLDTYWQSDGPQPHLINIQFSKKTDISAVALYLDYKLDESYTPSKISIRAGTSPH 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 37362650 163 DARFYKMLEVRNVNGWVALRFLDNReDDQLLKCQFIRLLFPVNHENGKDTHLRGIRLY 220
Cdd:cd08366  82 DLQEVRTVELEEPNGWVHIPLEDNR-DGKPLRTFFLQIAILSNHQNGRDTHIRQIKVY 138
ANAPC10 pfam03256
Anaphase-promoting complex, subunit 10 (APC10);
84-227 5.75e-36

Anaphase-promoting complex, subunit 10 (APC10);


Pssm-ID: 367420  Cd Length: 185  Bit Score: 126.02  E-value: 5.75e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37362650    84 VTHLALWKPSSFKLGNPVDFALDDNYDTFWQSDGGQPHQLDIMFSKRMDICVMAIFFSMIADESYAPSLVKVYAGHSPSD 163
Cdd:pfam03256  25 IGSQAVWSLSSCKPGFGVDLLRDDNLDTYWQSDGSQPHLVNIQFRKKTPVKYVAIYLDYKLDESYTPSKISVRAGTGFND 104

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37362650   164 ARFYKMLEVRNVNGWVALRFLDNRedDQLLKCQFIRLLFPVNHENGKDTHLRGIRLYVPSNEPH 227
Cdd:pfam03256 105 LQEVRVVDLEEPTGWVHIPLRDAN--GKPLRTFMLQIAVLSNHQNGRDTHVRQIKIYGPVEERS 166
 
Name Accession Description Interval E-value
DOC1 COG5156
Anaphase-promoting complex (APC), subunit 10 [Cell division and chromosome partitioning / ...
 59-248 6.69e-120

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


Pssm-ID: 227485  Cd Length: 189  Bit Score: 339.64  E-value: 6.69e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37362650  59 NPTPENLQHMFHQGIEILDSARMINVTHLALWKPSSFKLGNPVDFALDDNYDTFWQSDGGQPHQLDIMFSKRMDICVMAI 138
Cdd:COG5156   1 NPTPENLQHMFHQGIEILDSARMINVTHLAEWRLSSFKRGHPLRELLDDNMDTYWQSDGVQPHSIQISFDKRRYIQSVQL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37362650 139 FFSMIADESYAPSLVKVYAGHSPSDARFYKMLEVRNVNGWVALRFLDNREDDqLLKCQFIRLLFPVNHENGKDTHLRGIR 218
Cdd:COG5156  81 FLSFTQDESYTPSKIGVRAGLTREDVREISSVEVVEPEGWVTLSVADKREDD-LLKCIYILVVINSNHQEGKDSHVRHIK 159

                       170       180       190
                ....*....|....*....|....*....|
gi 37362650 219 LYVPSNEPHQDTHEWAQTLPETNNVFQDAI 248
Cdd:COG5156 160 IYEPSTEEIYYKIEWAQTLPETNNVFQDAI 189
APC10 cd08366
APC10 subunit of the anaphase-promoting complex (APC) that mediates substrate ubiquitination; ...
 83-220 8.00e-68

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: 205.87  E-value: 8.00e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37362650  83 NVTHLALWKPSSFKLGNPVDFALDDNYDTFWQSDGGQPHQLDIMFSKRMDICVMAIFFSMIADESYAPSLVKVYAGHSPS 162
Cdd:cd08366   2 EIGSLAVWSLSSAKPGNGVDQLRDDSLDTYWQSDGPQPHLINIQFSKKTDISAVALYLDYKLDESYTPSKISIRAGTSPH 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 37362650 163 DARFYKMLEVRNVNGWVALRFLDNReDDQLLKCQFIRLLFPVNHENGKDTHLRGIRLY 220
Cdd:cd08366  82 DLQEVRTVELEEPNGWVHIPLEDNR-DGKPLRTFFLQIAILSNHQNGRDTHIRQIKVY 138
APC10-like cd08159
APC10-like DOC1 domains in E3 ubiquitin ligases that mediate substrate ubiquitination; This ...
 88-220 2.06e-61

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: 189.22  E-value: 2.06e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37362650  88 ALWKPSSFKlgNPVDFALDDNYDTFWQSDGGQPHQLDIMFS-KRMDICVMAIFFSMiADESYAPSLVKVYAGHSPSDARF 166
Cdd:cd08159   5 ASIEVSSNP--LPVSRLTDGNYDTYWQSDGSQGSHWIRLFMkKDVLIRVLAIFVDM-ADSSYMPSLVVVYGGHSPSDLRE 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 37362650 167 YKMLEVRNVNGWVALRFLDNReddqllKCQFIRLLFPVNHENGKDTHLRGIRLY 220
Cdd:cd08159  82 LKDVNIRPSNGWVALLEDDTL------KCPYIEIRIKRCRSDGIDTRIRGLRLL 129
ANAPC10 pfam03256
Anaphase-promoting complex, subunit 10 (APC10);
84-227 5.75e-36

Anaphase-promoting complex, subunit 10 (APC10);


Pssm-ID: 367420  Cd Length: 185  Bit Score: 126.02  E-value: 5.75e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37362650    84 VTHLALWKPSSFKLGNPVDFALDDNYDTFWQSDGGQPHQLDIMFSKRMDICVMAIFFSMIADESYAPSLVKVYAGHSPSD 163
Cdd:pfam03256  25 IGSQAVWSLSSCKPGFGVDLLRDDNLDTYWQSDGSQPHLVNIQFRKKTPVKYVAIYLDYKLDESYTPSKISVRAGTGFND 104

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37362650   164 ARFYKMLEVRNVNGWVALRFLDNRedDQLLKCQFIRLLFPVNHENGKDTHLRGIRLYVPSNEPH 227
Cdd:pfam03256 105 LQEVRVVDLEEPTGWVHIPLRDAN--GKPLRTFMLQIAVLSNHQNGRDTHVRQIKIYGPVEERS 166
APC10-ZZEF1 cd08667
APC10/DOC1-like domain of uncharacterized Zinc finger ZZ-type and EF-hand domain-containing ...
 101-218 4.78e-06

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: 44.90  E-value: 4.78e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37362650 101 VDFALDDNYDTFWQSDG-GQPHQLDIMFSKRMDICVMAIFFSMIaDESYAPSLVKVYAGHSPSDARFYKMLEV-RNVNGW 178
Cdd:cd08667  16 IDRMTDGETSTYWQSDGsARSHWIRLKMKPDVVLRHLSIAVAAT-DQSYMPQQVTVSVGRSASSLQEVRDVHIpSNVTGY 94

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 37362650 179 VALrfLDNREDDQllkcqfirLLFPVN----HENGKDTHLRGIR 218
Cdd:cd08667  95 VTL--LENANISY--------LVVQINikrcHSDGCDTRIHGLK 128
APC10-like1 cd08365
APC10-like DOC1 domains of E3 ubiquitin ligases that mediate substrate ubiquitination; This ...
 106-219 4.60e-05

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: 42.11  E-value: 4.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37362650 106 DDNYDTFWQSDGGQPHQLdIMFSKRMDICVMAIffSMI---ADESYAPSLVKVYAGHSPSDarfykMLEVRNVN------ 176
Cdd:cd08365  22 DGNTSTYWQSDGSQGSHW-IRLKMKPDVLVRHL--SLAvdaTDSSYMPQRVVVAGGRSASN-----LQELRDVNippsvt 93

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 37362650 177 GWVALrfLDNREDDQLlkcqFIRLLFPVNHENGKDTHLRGIRL 219
Cdd:cd08365  94 GYVTL--LEDATISQP----YIEIRIKRCRSDGIDTRIHGLRI 130
APC10-HECTD3 cd08666
APC10-like DOC1 domain of HECTD3, a HECT E3 ubiquitin ligase protein that mediates substrate ...
 93-173 4.34e-03

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: 36.23  E-value: 4.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37362650  93 SSFKLGNPVDFALDDNYDTFWQSDG--GQPH-QLDI---MFSKRMDICVMAiffsmiADESYAPSLVKVYAGhsPSDaRF 166
Cdd:cd08666  13 SSYTDDFNVSCLTDGDPDTYWESDGsqGQHWiRLHMkkgTIIKKLLLTVDA------TDDNYMPKRVAVYGG--EGD-NL 83


                ....*..
gi 37362650 167 YKMLEVR 173
Cdd:cd08666  84 KKLNDVS 90
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH