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Conserved domains on  [gi|530410150|ref|XP_005256618|]
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zinc finger ZZ-type and EF-hand domain-containing protein 1 isoform X3 [Homo sapiens]

Protein Classification

ZZ-type zinc finger protein( domain architecture ID 13418930)

ZZ-type zinc finger protein may function as a molecular serve as scaffold in various cell signaling pathways

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
APC10-ZZEF1 cd08667
APC10/DOC1-like domain of uncharacterized Zinc finger ZZ-type and EF-hand domain-containing ...
 251-380 6.05e-83

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: 268.31  E-value: 6.05e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410150  251 KCYAYIETSSNSADIDKMTNGETSSYWQSDGSACSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVAVGRNASDLQE 330
Cdd:cd08667     2 KCYAYIEVSSNSADIDRMTDGETSTYWQSDGSARSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVSVGRSASSLQE 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 530410150  331 VRDVHIPSNVTGYVTLLENANVSQLYVQINIKRCLSDGCDTRIHGLRAVG 380
Cdd:cd08667    82 VRDVHIPSNVTGYVTLLENANISYLVVQINIKRCHSDGCDTRIHGLKTIG 131
ZZ_EF cd02343
Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif ...
 1782-1829 1.13e-30

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: 115.88  E-value: 1.13e-30
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 530410150 1782 ISCDGCDEIAPWHRYRCLQCSDMDLCKTCFLGGVKPEGHGDDHEMVNM 1829
Cdd:cd02343     1 ISCDGCDEIAPWHRYRCLQCTDMDLCKTCFLGGVKPEGHEDDHEMVNM 48
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 1831-1878 5.77e-17

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: 76.70  E-value: 5.77e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 530410150 1831 FTCDHCQGLIIGRRMNCNVCDDFDLCYGCYAAKKysYGHLPTHSITAH 1878
Cdd:cd02249     1 YSCDGCLKPIVGVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
95-141 3.50e-04

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: 43.24  E-value: 3.50e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 530410150   95 VTLEQFRELLEARGAgcSSEQFEEAFAQFDAEGDGTVDAENMLEALK 141
Cdd:COG5126    86 ISADEFRRLLTALGV--SEEEADELFARLDTDGDGKISFEEFVAAVR 130
CUB super family cl00049
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 1120-1190 4.18e-04

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


The actual alignment was detected with superfamily member smart00042:

Pssm-ID: 412131 [Multi-domain]  Cd Length: 102  Bit Score: 41.99  E-value: 4.18e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530410150   1120 TYFEVEFDDRCetekRYDYLEFTDARGRKTRYDTKVGTDKWPKKVTFKAGPRLQFLFHSDSSHNEWGYKFT 1190
Cdd:smart00042   35 TDFDLESSDNC----EYDYVEIYDGPSASSPLLGRFCGSEAPPPVISSSSNSLTLTFVSDSSVQKRGFSAR 101
 
Name Accession Description Interval E-value
APC10-ZZEF1 cd08667
APC10/DOC1-like domain of uncharacterized Zinc finger ZZ-type and EF-hand domain-containing ...
 251-380 6.05e-83

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: 268.31  E-value: 6.05e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410150  251 KCYAYIETSSNSADIDKMTNGETSSYWQSDGSACSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVAVGRNASDLQE 330
Cdd:cd08667     2 KCYAYIEVSSNSADIDRMTDGETSTYWQSDGSARSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVSVGRSASSLQE 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 530410150  331 VRDVHIPSNVTGYVTLLENANVSQLYVQINIKRCLSDGCDTRIHGLRAVG 380
Cdd:cd08667    82 VRDVHIPSNVTGYVTLLENANISYLVVQINIKRCHSDGCDTRIHGLKTIG 131
ZZ_EF cd02343
Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif ...
 1782-1829 1.13e-30

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: 115.88  E-value: 1.13e-30
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 530410150 1782 ISCDGCDEIAPWHRYRCLQCSDMDLCKTCFLGGVKPEGHGDDHEMVNM 1829
Cdd:cd02343     1 ISCDGCDEIAPWHRYRCLQCTDMDLCKTCFLGGVKPEGHEDDHEMVNM 48
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 1831-1878 5.77e-17

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: 76.70  E-value: 5.77e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 530410150 1831 FTCDHCQGLIIGRRMNCNVCDDFDLCYGCYAAKKysYGHLPTHSITAH 1878
Cdd:cd02249     1 YSCDGCLKPIVGVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 1829-1869 2.38e-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: 60.53  E-value: 2.38e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 530410150   1829 MEFTCDHCQGLIIGRRMNCNVCDDFDLCYGCYAAKKYSYGH 1869
Cdd:smart00291    3 HSYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEH 43
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 1781-1820 7.62e-08

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: 50.90  E-value: 7.62e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 530410150   1781 DISCDGCDEIAPWHRYRCLQCSDMDLCKTCFLGGVKPEGH 1820
Cdd:smart00291    4 SYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEH 43
ANAPC10 pfam03256
Anaphase-promoting complex, subunit 10 (APC10);
265-375 1.67e-07

Anaphase-promoting complex, subunit 10 (APC10);


Pssm-ID: 367420  Cd Length: 185  Bit Score: 53.99  E-value: 1.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410150   265 IDKMTNGETSSYWQSDGSAcSHWIRLKMKPDVVLRHLSIAV-AATDQSYMPQQVTVAVGRNASDLQEVRDVHIpSNVTGY 343
Cdd:pfam03256   42 VDLLRDDNLDTYWQSDGSQ-PHLVNIQFRKKTPVKYVAIYLdYKLDESYTPSKISVRAGTGFNDLQEVRVVDL-EEPTGW 119

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 530410150   344 VTL-LENANVSQLYV---QINIKRCLSDGCDT-----RIHG 375
Cdd:pfam03256  120 VHIpLRDANGKPLRTfmlQIAVLSNHQNGRDThvrqiKIYG 160
DOC1 COG5156
Anaphase-promoting complex (APC), subunit 10 [Cell division and chromosome partitioning / ...
 265-377 8.67e-07

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


Pssm-ID: 227485  Cd Length: 189  Bit Score: 51.90  E-value: 8.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410150  265 IDKMTNGETSSYWQSDGSAcSHWIRLKMKPDVVLRHLSIAVAAT-DQSYMPQQVTVAVGRNASDLQEVRDVHIpSNVTGY 343
Cdd:COG5156    43 LRELLDDNMDTYWQSDGVQ-PHSIQISFDKRRYIQSVQLFLSFTqDESYTPSKIGVRAGLTREDVREISSVEV-VEPEGW 120

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 530410150  344 VTL-----LENANVSQLYVQINIKRCLSDGCDTRIHGLR 377
Cdd:COG5156   121 VTLsvadkREDDLLKCIYILVVINSNHQEGKDSHVRHIK 159
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 1783-1826 4.36e-05

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: 42.86  E-value: 4.36e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 530410150  1783 SCDGC--DEIAPWhRYRCLQCSDMDLCKTCFlggvkPEGHGDDHEM 1826
Cdd:pfam00569    6 TCNGCsnDPSIGV-RYHCLRCSDYDLCQSCF-----QTHKGGNHQM 45
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 1829-1865 4.72e-05

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: 42.86  E-value: 4.72e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 530410150  1829 MEFTCDHCQ-GLIIGRRMNCNVCDDFDLCYGCYAAKKY 1865
Cdd:pfam00569    3 KVYTCNGCSnDPSIGVRYHCLRCSDYDLCQSCFQTHKG 40
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
95-141 3.50e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 43.24  E-value: 3.50e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 530410150   95 VTLEQFRELLEARGAgcSSEQFEEAFAQFDAEGDGTVDAENMLEALK 141
Cdd:COG5126    86 ISADEFRRLLTALGV--SEEEADELFARLDTDGDGKISFEEFVAAVR 130
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 1120-1190 4.18e-04

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 41.99  E-value: 4.18e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530410150   1120 TYFEVEFDDRCetekRYDYLEFTDARGRKTRYDTKVGTDKWPKKVTFKAGPRLQFLFHSDSSHNEWGYKFT 1190
Cdd:smart00042   35 TDFDLESSDNC----EYDYVEIYDGPSASSPLLGRFCGSEAPPPVISSSSNSLTLTFVSDSSVQKRGFSAR 101
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 1120-1193 1.32e-03

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 40.86  E-value: 1.32e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530410150 1120 TYFEVEFDDRCetekRYDYLEFTDARGRKTRYDTKVGTDKWPKKVTFkAGPRLQFLFHSDSSHNEWGYKFTVTA 1193
Cdd:cd00041    45 EDFDLESSPNC----SYDYLEIYDGPSTSSPLLGRFCGSTLPPPIIS-SGNSLTVRFRSDSSVTGRGFKATYSA 113
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
1826-1873 3.14e-03

Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];


Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 42.75  E-value: 3.14e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 530410150 1826 MVNMEFTCDHCQGLIIGR-RMNCNVCDDFDLCYGCYAAKKYSYGHLPTH 1873
Cdd:COG5114     1 MGGVKIHCDVCFLDMTDLtFIKCNECPAVDLCLPCFVNGIETGVHSPYH 49
 
Name Accession Description Interval E-value
APC10-ZZEF1 cd08667
APC10/DOC1-like domain of uncharacterized Zinc finger ZZ-type and EF-hand domain-containing ...
 251-380 6.05e-83

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: 268.31  E-value: 6.05e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410150  251 KCYAYIETSSNSADIDKMTNGETSSYWQSDGSACSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVAVGRNASDLQE 330
Cdd:cd08667     2 KCYAYIEVSSNSADIDRMTDGETSTYWQSDGSARSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVSVGRSASSLQE 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 530410150  331 VRDVHIPSNVTGYVTLLENANVSQLYVQINIKRCLSDGCDTRIHGLRAVG 380
Cdd:cd08667    82 VRDVHIPSNVTGYVTLLENANISYLVVQINIKRCHSDGCDTRIHGLKTIG 131
APC10-like1 cd08365
APC10-like DOC1 domains of E3 ubiquitin ligases that mediate substrate ubiquitination; This ...
 251-379 1.02e-68

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: 227.77  E-value: 1.02e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410150  251 KCY-AYIETSSNSADIDKMTNGETSSYWQSDGSACSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVAVGRNASDLQ 329
Cdd:cd08365     2 KCYvESIEVSSNPADASRLTDGNTSTYWQSDGSQGSHWIRLKMKPDVLVRHLSLAVDATDSSYMPQRVVVAGGRSASNLQ 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 530410150  330 EVRDVHIPSNVTGYVTLLENANVSQLYVQINIKRCLSDGCDTRIHGLRAV 379
Cdd:cd08365    82 ELRDVNIPPSVTGYVTLLEDATISQPYIEIRIKRCRSDGIDTRIHGLRIL 131
APC10-like cd08159
APC10-like DOC1 domains in E3 ubiquitin ligases that mediate substrate ubiquitination; This ...
 251-379 1.01e-62

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: 210.41  E-value: 1.01e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410150  251 KCY-AYIETSSNSADIDKMTNGETSSYWQSDGSACSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVAVGRNASDLQ 329
Cdd:cd08159     1 KCYtASIEVSSNPLPVSRLTDGNYDTYWQSDGSQGSHWIRLFMKKDVLIRVLAIFVDMADSSYMPSLVVVYGGHSPSDLR 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 530410150  330 EVRDVHIPsNVTGYVTLLENANVSQLYVQINIKRCLSDGCDTRIHGLRAV 379
Cdd:cd08159    81 ELKDVNIR-PSNGWVALLEDDTLKCPYIEIRIKRCRSDGIDTRIRGLRLL 129
APC10-HECTD3 cd08666
APC10-like DOC1 domain of HECTD3, a HECT E3 ubiquitin ligase protein that mediates substrate ...
 248-377 5.32e-33

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: 125.60  E-value: 5.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410150  248 SVAKCYAYIETSSNSADIDK--MTNGETSSYWQSDGSACSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVAvGRNA 325
Cdd:cd08666     2 SVKQYVESIEVSSYTDDFNVscLTDGDPDTYWESDGSQGQHWIRLHMKKGTIIKKLLLTVDATDDNYMPKRVAVY-GGEG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530410150  326 SDLQEVRDVHIPSNVTGYVTLLENANVSQLYVQINIKRCLSDGCDTRIHGLR 377
Cdd:cd08666    81 DNLKKLNDVSIDETLIGDVCILEDMTTHLPVIEIRIKECKDEGIDVRIRGIK 132
ZZ_EF cd02343
Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif ...
 1782-1829 1.13e-30

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: 115.88  E-value: 1.13e-30
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 530410150 1782 ISCDGCDEIAPWHRYRCLQCSDMDLCKTCFLGGVKPEGHGDDHEMVNM 1829
Cdd:cd02343     1 ISCDGCDEIAPWHRYRCLQCTDMDLCKTCFLGGVKPEGHEDDHEMVNM 48
APC10-CUL7 cd08665
APC10-like DOC1 domain of CUL7, subunit of the SCF-ROC1-like E3 ubiquitin ligase complex that ...
 251-380 2.77e-29

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: 115.02  E-value: 2.77e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410150  251 KCYAYIETSSNSADIDKMTNGETSSYWQSDGSACSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVAVGRNASDLQ- 329
Cdd:cd08665     2 KCWEKVEVSSNPHRANKLTDGNPKTYWESNGSTGSHYINIHMHRGVVIRQLYMLVASEDSSYMPARVVVLGGDSPSCITt 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 530410150  330 EVRDVHIpSNVTGYVTLLENANVSQLYVQINIKRCLSDGCDTRIHGLRAVG 380
Cdd:cd08665    82 ELNAVNV-SPTASRVVLLENMTRFWPIIQIRIKRCQQGGIDTRVRGLEILG 131
APC10-HERC2 cd08664
APC10-like DOC1 domain present in HERC2 (HECT domain and RLD2); This model represents the ...
 241-376 1.20e-28

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: 114.01  E-value: 1.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410150  241 PEMDKLKSVAKCYAYIETSSNSADIDKMTNGeTSSYWQSDGSACSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVA 320
Cdd:cd08664    16 GEGDLIDDWSRCVRSLTVSSNENQAKRLIDG-SGSYWQSSGSQGKHWIRLELHPDVLIHSLKIIVDPADSSYMPSLVVVS 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530410150  321 VGRNASDLQEVRDVHIPSNVTgYVTLLENANVSQLYVQINIKRCLSDGCDTRIHGL 376
Cdd:cd08664    95 GGDSLNSLKELKTINVNATDT-LVTLLQDVKEYYRYIEIAIKQCRNNGIDCKIHGL 149
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 1831-1878 5.77e-17

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: 76.70  E-value: 5.77e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 530410150 1831 FTCDHCQGLIIGRRMNCNVCDDFDLCYGCYAAKKysYGHLPTHSITAH 1878
Cdd:cd02249     1 YSCDGCLKPIVGVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 1782-1829 1.03e-12

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: 64.76  E-value: 1.03e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 530410150 1782 ISCDGCDEIAPWHRYRCLQCSDMDLCKTCFLGGVKpeGHGDDHEMVNM 1829
Cdd:cd02249     1 YSCDGCLKPIVGVRYHCLVCEDFDLCSSCYAKGKK--GHPPDHSFTEI 46
APC10 cd08366
APC10 subunit of the anaphase-promoting complex (APC) that mediates substrate ubiquitination; ...
 265-377 8.75e-12

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: 64.89  E-value: 8.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410150  265 IDKMTNGETSSYWQSDGSAcSHWIRLKMKPDVVLRHLSIAVA-ATDQSYMPQQVTVAVGRNASDLQEVRDVHIpSNVTGY 343
Cdd:cd08366    20 VDQLRDDSLDTYWQSDGPQ-PHLINIQFSKKTDISAVALYLDyKLDESYTPSKISIRAGTSPHDLQEVRTVEL-EEPNGW 97

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 530410150  344 VTL-LENANVSQL----YVQINIKRCLSDGCDTRIHGLR 377
Cdd:cd08366    98 VHIpLEDNRDGKPlrtfFLQIAILSNHQNGRDTHIRQIK 136
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 1829-1869 2.38e-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: 60.53  E-value: 2.38e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 530410150   1829 MEFTCDHCQGLIIGRRMNCNVCDDFDLCYGCYAAKKYSYGH 1869
Cdd:smart00291    3 HSYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEH 43
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 1782-1826 9.78e-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: 56.20  E-value: 9.78e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 530410150 1782 ISCDGCDEIAPW-HRYRCLQCSDMDLCKTCFLGGVKPEGHGDDHEM 1826
Cdd:cd02338     1 VSCDGCGKSNFTgRRYKCLICYDYDLCADCYDSGVTTERHLFDHPM 46
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 1831-1883 3.57e-09

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: 54.57  E-value: 3.57e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530410150 1831 FTCDHCQGLIIGRRMNCNVCDDFDLCYGCYAAkkysyghlPTHsiTAHPMVTI 1883
Cdd:cd02340     1 VICDGCQGPIVGVRYKCLVCPDYDLCESCEAK--------GVH--PEHAMLKI 43
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 1782-1827 5.07e-08

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: 51.20  E-value: 5.07e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 530410150 1782 ISCDGCDEIaPWH--RYRCLQCSDMDLCKTCFLGGVKPEGHGDDHEMV 1827
Cdd:cd02334     1 AKCNICKEF-PITgfRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMK 47
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 1781-1820 7.62e-08

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: 50.90  E-value: 7.62e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 530410150   1781 DISCDGCDEIAPWHRYRCLQCSDMDLCKTCFLGGVKPEGH 1820
Cdd:smart00291    4 SYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEH 43
ANAPC10 pfam03256
Anaphase-promoting complex, subunit 10 (APC10);
265-375 1.67e-07

Anaphase-promoting complex, subunit 10 (APC10);


Pssm-ID: 367420  Cd Length: 185  Bit Score: 53.99  E-value: 1.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410150   265 IDKMTNGETSSYWQSDGSAcSHWIRLKMKPDVVLRHLSIAV-AATDQSYMPQQVTVAVGRNASDLQEVRDVHIpSNVTGY 343
Cdd:pfam03256   42 VDLLRDDNLDTYWQSDGSQ-PHLVNIQFRKKTPVKYVAIYLdYKLDESYTPSKISVRAGTGFNDLQEVRVVDL-EEPTGW 119

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 530410150   344 VTL-LENANVSQLYV---QINIKRCLSDGCDT-----RIHG 375
Cdd:pfam03256  120 VHIpLRDANGKPLRTfmlQIAVLSNHQNGRDThvrqiKIYG 160
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 1782-1829 2.08e-07

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: 49.57  E-value: 2.08e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 530410150 1782 ISCDGCDEIAPWHRYRCLQCSDMDLCKTCFLGGVKPEghgddHEMVNM 1829
Cdd:cd02340     1 VICDGCQGPIVGVRYKCLVCPDYDLCESCEAKGVHPE-----HAMLKI 43
DOC1 COG5156
Anaphase-promoting complex (APC), subunit 10 [Cell division and chromosome partitioning / ...
 265-377 8.67e-07

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


Pssm-ID: 227485  Cd Length: 189  Bit Score: 51.90  E-value: 8.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410150  265 IDKMTNGETSSYWQSDGSAcSHWIRLKMKPDVVLRHLSIAVAAT-DQSYMPQQVTVAVGRNASDLQEVRDVHIpSNVTGY 343
Cdd:COG5156    43 LRELLDDNMDTYWQSDGVQ-PHSIQISFDKRRYIQSVQLFLSFTqDESYTPSKIGVRAGLTREDVREISSVEV-VEPEGW 120

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 530410150  344 VTL-----LENANVSQLYVQINIKRCLSDGCDTRIHGLR 377
Cdd:COG5156   121 VTLsvadkREDDLLKCIYILVVINSNHQEGKDSHVRHIK 159
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
 1831-1878 4.87e-06

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: 45.63  E-value: 4.87e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 530410150 1831 FTCDHCQgLIIGRRMNCNVCDDFDLCYGCYAAKkysyGHlpTHSITAH 1878
Cdd:cd02337     1 YTCNECK-HHVETRWHCTVCEDYDLCITCYNTK----NH--PHKMEKL 41
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 1831-1874 7.95e-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: 45.36  E-value: 7.95e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 530410150 1831 FTCDHCQGLIIGR-RMNCNVCDDFDLCYGCYAAKKYSYGHLPTHS 1874
Cdd:cd02335     1 YHCDYCSKDITGTiRIKCAECPDFDLCLECFSAGAEIGKHRNDHN 45
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 1832-1874 2.77e-05

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: 43.73  E-value: 2.77e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 530410150 1832 TCDHCQGLII-GRRMNCNVCDDFDLCYGCYAAKKysygHLPTHS 1874
Cdd:cd02344     2 TCDGCQMFPInGPRFKCRNCDDFDFCENCFKTRK----HNTRHT 41
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 1782-1824 3.98e-05

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: 43.05  E-value: 3.98e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 530410150 1782 ISCDGCD-EIAPWHRYRCLQCSDMDLCKTCFLGGVKPEGHGDDH 1824
Cdd:cd02335     1 YHCDYCSkDITGTIRIKCAECPDFDLCLECFSAGAEIGKHRNDH 44
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 1783-1826 4.36e-05

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: 42.86  E-value: 4.36e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 530410150  1783 SCDGC--DEIAPWhRYRCLQCSDMDLCKTCFlggvkPEGHGDDHEM 1826
Cdd:pfam00569    6 TCNGCsnDPSIGV-RYHCLRCSDYDLCQSCF-----QTHKGGNHQM 45
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 1832-1876 4.53e-05

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: 43.10  E-value: 4.53e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 530410150 1832 TCDHCQ-GLIIGRRMNCNVCDDFDLCYGCYAAKKYSYGHLPTHSIT 1876
Cdd:cd02338     2 SCDGCGkSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFDHPMQ 47
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 1829-1865 4.72e-05

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: 42.86  E-value: 4.72e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 530410150  1829 MEFTCDHCQ-GLIIGRRMNCNVCDDFDLCYGCYAAKKY 1865
Cdd:pfam00569    3 KVYTCNGCSnDPSIGVRYHCLRCSDYDLCQSCFQTHKG 40
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 1833-1869 2.58e-04

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: 40.90  E-value: 2.58e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 530410150 1833 CDHCQGL-IIGRRMNCNVCDDFDLCYGCYAAKKYSYGH 1869
Cdd:cd02339     3 CDTCRKQgIIGIRWKCAECPNYDLCTTCYHGDKHDLEH 40
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 1832-1873 3.49e-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: 3.49e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 530410150 1832 TCDHCQGL-IIGRRMNCNVCDDFDLCYGCYAAKKYSYGHLPTH 1873
Cdd:cd02345     2 SCSACRKQdISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLH 44
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
95-141 3.50e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 43.24  E-value: 3.50e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 530410150   95 VTLEQFRELLEARGAgcSSEQFEEAFAQFDAEGDGTVDAENMLEALK 141
Cdd:COG5126    86 ISADEFRRLLTALGV--SEEEADELFARLDTDGDGKISFEEFVAAVR 130
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 1120-1190 4.18e-04

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 41.99  E-value: 4.18e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530410150   1120 TYFEVEFDDRCetekRYDYLEFTDARGRKTRYDTKVGTDKWPKKVTFKAGPRLQFLFHSDSSHNEWGYKFT 1190
Cdd:smart00042   35 TDFDLESSDNC----EYDYVEIYDGPSASSPLLGRFCGSEAPPPVISSSSNSLTLTFVSDSSVQKRGFSAR 101
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 256-362 7.71e-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: 42.05  E-value: 7.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410150   256 IETSSNSAD---IDKMTNGETSSYWQSDGSACSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVAVGRNASDLQEVR 332
Cdd:pfam00754    2 ITASSSYSGegpAAAALDGDPNTAWSAWSGDDPQWIQVDLGKPKKITGVVTQGRQDGSNGYVTSYKIEYSLDGENWTTVK 81

                           90       100       110
                   ....*....|....*....|....*....|..
gi 530410150   333 DVHIPSNVTGY--VTLLENANVSQLYVQINIK 362
Cdd:pfam00754   82 DEKIPGNNDNNtpVTNTFDPPIKARYVRIVPT 113
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 1120-1193 1.32e-03

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 40.86  E-value: 1.32e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530410150 1120 TYFEVEFDDRCetekRYDYLEFTDARGRKTRYDTKVGTDKWPKKVTFkAGPRLQFLFHSDSSHNEWGYKFTVTA 1193
Cdd:cd00041    45 EDFDLESSPNC----SYDYLEIYDGPSTSSPLLGRFCGSTLPPPIIS-SGNSLTVRFRSDSSVTGRGFKATYSA 113
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
 1782-1827 1.63e-03

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: 38.57  E-value: 1.63e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 530410150 1782 ISCDGCD-EIAPWHRYRCLQCS--DMDLCKTCFlggVKPEGHGDDHEMV 1827
Cdd:cd02341     1 FKCDSCGiEPIPGTRYHCSECDdgDFDLCQDCV---VKGESHQEDHWLV 46
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
1826-1873 3.14e-03

Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];


Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 42.75  E-value: 3.14e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 530410150 1826 MVNMEFTCDHCQGLIIGR-RMNCNVCDDFDLCYGCYAAKKYSYGHLPTH 1873
Cdd:COG5114     1 MGGVKIHCDVCFLDMTDLtFIKCNECPAVDLCLPCFVNGIETGVHSPYH 49
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 1782-1826 5.56e-03

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: 37.05  E-value: 5.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 530410150 1782 ISCDGCDE--IAPWhRYRCLQCSDMDLCKTCFlggvkpegHGDDHEM 1826
Cdd:cd02339     1 IICDTCRKqgIIGI-RWKCAECPNYDLCTTCY--------HGDKHDL 38
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 1782-1811 9.49e-03

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: 36.41  E-value: 9.49e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 530410150 1782 ISCDGCdEIAPWH--RYRCLQCSDMDLCKTCF 1811
Cdd:cd02344     1 VTCDGC-QMFPINgpRFKCRNCDDFDFCENCF 31
 
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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