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Conserved domains on  [gi|1034604399|ref|XP_016881364|]
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E3 ubiquitin-protein ligase MIB1 isoform X4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
 154-218 8.51e-30

Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect).


:

Pssm-ID: 461991  Cd Length: 66  Bit Score: 111.15  E-value: 8.51e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034604399 154 GARVVRGVDWQWEDQDGGNGRRGKVTEIQDWSASSPHSAAYVLWDNGAKNLYRVGFEGMSDLKCV 218
Cdd:pfam06701   1 GARVVRGPDWKWGDQDGGEGHVGTVVEIRDWDSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 83-127 9.96e-28

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: 104.85  E-value: 9.96e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1034604399  83 TMCDTCRQQPIIGIRWKCAECTNYDLCTVCYHGDKHHLRHRFYRI 127
Cdd:cd02339     1 IICDTCRKQGIIGIRWKCAECPNYDLCTTCYHGDKHDLEHRFYRY 45
SH3_15 pfam18346
Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate ...
 333-397 3.04e-26

Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate recognition domain for a second, membrane-distal epitope of the Notch ligand (C-box). Although the first Mib repeat of REP may play a dominant role in ligand binding, the two repeats appear to cooperate in the engagement of the Jag1 tail. Mind bomb (Mib) proteins are large, multi-domain E3 ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. The structure and functional analysis, show that Mib1 contains two independent substrate recognition domains that engage two distinct epitopes from the cytoplasmic tail of the ligand Jagged1, one in the intracellular membrane proximal region and the other near the C terminus. REP domains have a five-stranded anti-parallel twisted beta sheet topology similar to that of SH3 domains.


:

Pssm-ID: 465720  Cd Length: 67  Bit Score: 101.17  E-value: 3.04e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034604399 333 FQVGDLVQVCYDLERIKLLQRGHGEWAEAMLPTLGKVGRVQQIYSDSDLKVEV--CGTSWTYNPAAV 397
Cdd:pfam18346   1 FEVGDWVRVKDDLEKVKPLQEGHGGWNGGMAETLGSVGTVVKVDADGDLRVQFpgGGRRWTLNPAAL 67
SH3_15 pfam18346
Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate ...
 246-311 2.80e-25

Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate recognition domain for a second, membrane-distal epitope of the Notch ligand (C-box). Although the first Mib repeat of REP may play a dominant role in ligand binding, the two repeats appear to cooperate in the engagement of the Jag1 tail. Mind bomb (Mib) proteins are large, multi-domain E3 ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. The structure and functional analysis, show that Mib1 contains two independent substrate recognition domains that engage two distinct epitopes from the cytoplasmic tail of the ligand Jagged1, one in the intracellular membrane proximal region and the other near the C terminus. REP domains have a five-stranded anti-parallel twisted beta sheet topology similar to that of SH3 domains.


:

Pssm-ID: 465720  Cd Length: 67  Bit Score: 98.47  E-value: 2.80e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034604399 246 LQIGDLVNIDLDLEIVQSLQHGHGGWTDGMFETLTTTGTVCGIDEDHDIVVQYPS-GNRWTFNPAVL 311
Cdd:pfam18346   1 FEVGDWVRVKDDLEKVKPLQEGHGGWNGGMAETLGSVGTVVKVDADGDLRVQFPGgGRRWTLNPAAL 67
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
 15-72 3.45e-20

Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect).


:

Pssm-ID: 461991  Cd Length: 66  Bit Score: 84.19  E-value: 3.45e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034604399  15 GARVVRGPDWKWGKQDGGEGHVGTVR-----SFESPEEVVVV-WDNGTAANYR--CSGAYDLRILD 72
Cdd:pfam06701   1 GARVVRGPDWKWGDQDGGEGHVGTVVeirdwDSESPRSTVRVqWDNGSTNVYRvgYEGKYDLKVVD 66
ANKYR super family cl34000
Ankyrin repeat [Signal transduction mechanisms];
406-492 3.32e-09

Ankyrin repeat [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG0666:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.04  E-value: 3.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604399 406 AISNASGERLSQLLKKLFETQESGDLNEELVKAAANGDVAKVEDLLKRpDVDVNGQCA-GHTAMQAASQNGHVDILKLLL 484
Cdd:COG0666    62 ALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKdGETPLHLAAYNGNLEIVKLLL 140


                  ....*...
gi 1034604399 485 KQNVDVEA 492
Cdd:COG0666   141 EAGADVNA 148
 
Name Accession Description Interval E-value
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
 154-218 8.51e-30

Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect).


Pssm-ID: 461991  Cd Length: 66  Bit Score: 111.15  E-value: 8.51e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034604399 154 GARVVRGVDWQWEDQDGGNGRRGKVTEIQDWSASSPHSAAYVLWDNGAKNLYRVGFEGMSDLKCV 218
Cdd:pfam06701   1 GARVVRGPDWKWGDQDGGEGHVGTVVEIRDWDSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 83-127 9.96e-28

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: 104.85  E-value: 9.96e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1034604399  83 TMCDTCRQQPIIGIRWKCAECTNYDLCTVCYHGDKHHLRHRFYRI 127
Cdd:cd02339     1 IICDTCRKQGIIGIRWKCAECPNYDLCTTCYHGDKHDLEHRFYRY 45
SH3_15 pfam18346
Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate ...
 333-397 3.04e-26

Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate recognition domain for a second, membrane-distal epitope of the Notch ligand (C-box). Although the first Mib repeat of REP may play a dominant role in ligand binding, the two repeats appear to cooperate in the engagement of the Jag1 tail. Mind bomb (Mib) proteins are large, multi-domain E3 ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. The structure and functional analysis, show that Mib1 contains two independent substrate recognition domains that engage two distinct epitopes from the cytoplasmic tail of the ligand Jagged1, one in the intracellular membrane proximal region and the other near the C terminus. REP domains have a five-stranded anti-parallel twisted beta sheet topology similar to that of SH3 domains.


Pssm-ID: 465720  Cd Length: 67  Bit Score: 101.17  E-value: 3.04e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034604399 333 FQVGDLVQVCYDLERIKLLQRGHGEWAEAMLPTLGKVGRVQQIYSDSDLKVEV--CGTSWTYNPAAV 397
Cdd:pfam18346   1 FEVGDWVRVKDDLEKVKPLQEGHGGWNGGMAETLGSVGTVVKVDADGDLRVQFpgGGRRWTLNPAAL 67
SH3_15 pfam18346
Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate ...
 246-311 2.80e-25

Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate recognition domain for a second, membrane-distal epitope of the Notch ligand (C-box). Although the first Mib repeat of REP may play a dominant role in ligand binding, the two repeats appear to cooperate in the engagement of the Jag1 tail. Mind bomb (Mib) proteins are large, multi-domain E3 ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. The structure and functional analysis, show that Mib1 contains two independent substrate recognition domains that engage two distinct epitopes from the cytoplasmic tail of the ligand Jagged1, one in the intracellular membrane proximal region and the other near the C terminus. REP domains have a five-stranded anti-parallel twisted beta sheet topology similar to that of SH3 domains.


Pssm-ID: 465720  Cd Length: 67  Bit Score: 98.47  E-value: 2.80e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034604399 246 LQIGDLVNIDLDLEIVQSLQHGHGGWTDGMFETLTTTGTVCGIDEDHDIVVQYPS-GNRWTFNPAVL 311
Cdd:pfam18346   1 FEVGDWVRVKDDLEKVKPLQEGHGGWNGGMAETLGSVGTVVKVDADGDLRVQFPGgGRRWTLNPAAL 67
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
 15-72 3.45e-20

Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect).


Pssm-ID: 461991  Cd Length: 66  Bit Score: 84.19  E-value: 3.45e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034604399  15 GARVVRGPDWKWGKQDGGEGHVGTVR-----SFESPEEVVVV-WDNGTAANYR--CSGAYDLRILD 72
Cdd:pfam06701   1 GARVVRGPDWKWGDQDGGEGHVGTVVeirdwDSESPRSTVRVqWDNGSTNVYRvgYEGKYDLKVVD 66
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 85-123 3.96e-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: 57.83  E-value: 3.96e-11
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1034604399   85 CDTCrQQPIIGIRWKCAECTNYDLCTVCYHGDKHHLRHR 123
Cdd:smart00291   7 CDTC-GKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 79-119 3.57e-10

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 55.18  E-value: 3.57e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1034604399  79 KHDGTMCDTCRQQPIIGIRWKCAECTNYDLCTVCYHGDKHH 119
Cdd:pfam00569   1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQTHKGG 41
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
406-492 3.32e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.04  E-value: 3.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604399 406 AISNASGERLSQLLKKLFETQESGDLNEELVKAAANGDVAKVEDLLKRpDVDVNGQCA-GHTAMQAASQNGHVDILKLLL 484
Cdd:COG0666    62 ALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKdGETPLHLAAYNGNLEIVKLLL 140


                  ....*...
gi 1034604399 485 KQNVDVEA 492
Cdd:COG0666   141 EAGADVNA 148
Ank_2 pfam12796
Ankyrin repeats (3 copies);
406-492 2.62e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.27  E-value: 2.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604399 406 AISNASGERLSQLLKKLFETQESGDLNEE-LVKAAANGDVAKVEDLLKRpdVDVNGQCAGHTAMQAASQNGHVDILKLLL 484
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTaLHLAAKNGHLEIVKLLLEH--ADVNLKDNGRTALHYAARSGHLEIVKLLL 81


                  ....*...
gi 1034604399 485 KQNVDVEA 492
Cdd:pfam12796  82 EKGADINV 89
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
85-138 1.04e-03

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


Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 41.59  E-value: 1.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034604399  85 CDTCRQQPIIGIRWKCAECTNYDLCTVCY----HGDKHHLRHRfYRITTPGSERVLLE 138
Cdd:COG5114     8 CDVCFLDMTDLTFIKCNECPAVDLCLPCFvngiETGVHSPYHG-YRIIETNSYPIGEE 64
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 464-492 2.45e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 2.45e-03
                           10        20
                   ....*....|....*....|....*....
gi 1034604399  464 GHTAMQAASQNGHVDILKLLLKQNVDVEA 492
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 425-491 4.53e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.85  E-value: 4.53e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034604399 425 TQESGDLNEE--LVKAAANGDVAKVEDLLK-RPDVDVnGQCAGHTAMQAASQNGHVDILKLLLKQ--NVDVE 491
Cdd:PLN03192  517 GGEHDDPNMAsnLLTVASTGNAALLEELLKaKLDPDI-GDSKGRTPLHIAASKGYEDCVLVLLKHacNVHIR 587
 
Name Accession Description Interval E-value
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
 154-218 8.51e-30

Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect).


Pssm-ID: 461991  Cd Length: 66  Bit Score: 111.15  E-value: 8.51e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034604399 154 GARVVRGVDWQWEDQDGGNGRRGKVTEIQDWSASSPHSAAYVLWDNGAKNLYRVGFEGMSDLKCV 218
Cdd:pfam06701   1 GARVVRGPDWKWGDQDGGEGHVGTVVEIRDWDSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 83-127 9.96e-28

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: 104.85  E-value: 9.96e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1034604399  83 TMCDTCRQQPIIGIRWKCAECTNYDLCTVCYHGDKHHLRHRFYRI 127
Cdd:cd02339     1 IICDTCRKQGIIGIRWKCAECPNYDLCTTCYHGDKHDLEHRFYRY 45
SH3_15 pfam18346
Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate ...
 333-397 3.04e-26

Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate recognition domain for a second, membrane-distal epitope of the Notch ligand (C-box). Although the first Mib repeat of REP may play a dominant role in ligand binding, the two repeats appear to cooperate in the engagement of the Jag1 tail. Mind bomb (Mib) proteins are large, multi-domain E3 ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. The structure and functional analysis, show that Mib1 contains two independent substrate recognition domains that engage two distinct epitopes from the cytoplasmic tail of the ligand Jagged1, one in the intracellular membrane proximal region and the other near the C terminus. REP domains have a five-stranded anti-parallel twisted beta sheet topology similar to that of SH3 domains.


Pssm-ID: 465720  Cd Length: 67  Bit Score: 101.17  E-value: 3.04e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034604399 333 FQVGDLVQVCYDLERIKLLQRGHGEWAEAMLPTLGKVGRVQQIYSDSDLKVEV--CGTSWTYNPAAV 397
Cdd:pfam18346   1 FEVGDWVRVKDDLEKVKPLQEGHGGWNGGMAETLGSVGTVVKVDADGDLRVQFpgGGRRWTLNPAAL 67
SH3_15 pfam18346
Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate ...
 246-311 2.80e-25

Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate recognition domain for a second, membrane-distal epitope of the Notch ligand (C-box). Although the first Mib repeat of REP may play a dominant role in ligand binding, the two repeats appear to cooperate in the engagement of the Jag1 tail. Mind bomb (Mib) proteins are large, multi-domain E3 ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. The structure and functional analysis, show that Mib1 contains two independent substrate recognition domains that engage two distinct epitopes from the cytoplasmic tail of the ligand Jagged1, one in the intracellular membrane proximal region and the other near the C terminus. REP domains have a five-stranded anti-parallel twisted beta sheet topology similar to that of SH3 domains.


Pssm-ID: 465720  Cd Length: 67  Bit Score: 98.47  E-value: 2.80e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034604399 246 LQIGDLVNIDLDLEIVQSLQHGHGGWTDGMFETLTTTGTVCGIDEDHDIVVQYPS-GNRWTFNPAVL 311
Cdd:pfam18346   1 FEVGDWVRVKDDLEKVKPLQEGHGGWNGGMAETLGSVGTVVKVDADGDLRVQFPGgGRRWTLNPAAL 67
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
 15-72 3.45e-20

Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect).


Pssm-ID: 461991  Cd Length: 66  Bit Score: 84.19  E-value: 3.45e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034604399  15 GARVVRGPDWKWGKQDGGEGHVGTVR-----SFESPEEVVVV-WDNGTAANYR--CSGAYDLRILD 72
Cdd:pfam06701   1 GARVVRGPDWKWGDQDGGEGHVGTVVeirdwDSESPRSTVRVqWDNGSTNVYRvgYEGKYDLKVVD 66
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 85-127 1.46e-13

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: 1.46e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1034604399  85 CDTCrQQPIIGIRWKCAECTNYDLCTVCYHG--DKHHLRHRFYRI 127
Cdd:cd02249     3 CDGC-LKPIVGVRYHCLVCEDFDLCSSCYAKgkKGHPPDHSFTEI 46
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 85-127 3.82e-11

Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain.


Pssm-ID: 239080  Cd Length: 43  Bit Score: 58.04  E-value: 3.82e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1034604399  85 CDTCrQQPIIGIRWKCAECTNYDLCTVCyHGDKHHLRHRFYRI 127
Cdd:cd02340     3 CDGC-QGPIVGVRYKCLVCPDYDLCESC-EAKGVHPEHAMLKI 43
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 85-123 3.96e-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: 57.83  E-value: 3.96e-11
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1034604399   85 CDTCrQQPIIGIRWKCAECTNYDLCTVCYHGDKHHLRHR 123
Cdd:smart00291   7 CDTC-GKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 85-127 7.54e-11

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: 57.21  E-value: 7.54e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1034604399  85 CDTCRQQPIIGIRWKCAECTNYDLCTVCYHGDKHHLRHRFYRI 127
Cdd:cd02344     3 CDGCQMFPINGPRFKCRNCDDFDFCENCFKTRKHNTRHTFGRI 45
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 79-119 3.57e-10

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 55.18  E-value: 3.57e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1034604399  79 KHDGTMCDTCRQQPIIGIRWKCAECTNYDLCTVCYHGDKHH 119
Cdd:pfam00569   1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQTHKGG 41
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 83-122 2.62e-09

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: 52.74  E-value: 2.62e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1034604399  83 TMCDTCRQQPIIGIRWKCAECTNYDLCTVCY----HGDKHHLRH 122
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFfsgrTSKSHKNSH 44
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
406-492 3.32e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.04  E-value: 3.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604399 406 AISNASGERLSQLLKKLFETQESGDLNEELVKAAANGDVAKVEDLLKRpDVDVNGQCA-GHTAMQAASQNGHVDILKLLL 484
Cdd:COG0666    62 ALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKdGETPLHLAAYNGNLEIVKLLL 140


                  ....*...
gi 1034604399 485 KQNVDVEA 492
Cdd:COG0666   141 EAGADVNA 148
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
435-492 7.59e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 56.89  E-value: 7.59e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034604399 435 LVKAAANGDVAKVEDLLKRpDVDVNGQCA-GHTAMQAASQNGHVDILKLLLKQNVDVEA 492
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEA-GADVNAQDNdGNTPLHLAAANGNLEIVKLLLEAGADVNA 181
Ank_2 pfam12796
Ankyrin repeats (3 copies);
406-492 2.62e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.27  E-value: 2.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604399 406 AISNASGERLSQLLKKLFETQESGDLNEE-LVKAAANGDVAKVEDLLKRpdVDVNGQCAGHTAMQAASQNGHVDILKLLL 484
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTaLHLAAKNGHLEIVKLLLEH--ADVNLKDNGRTALHYAARSGHLEIVKLLL 81


                  ....*...
gi 1034604399 485 KQNVDVEA 492
Cdd:pfam12796  82 EKGADINV 89
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 85-125 8.69e-08

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: 48.50  E-value: 8.69e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1034604399  85 CDTCRQQPIIGIRWKCAECTNYDLCTVCYHGDKHHLRHRFY 125
Cdd:cd02338     3 CDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFD 43
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
435-492 1.76e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 52.65  E-value: 1.76e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034604399 435 LVKAAANGDVAKVEDLLKRpDVDVNGQCA-GHTAMQAASQNGHVDILKLLLKQNVDVEA 492
Cdd:COG0666   157 LHLAAANGNLEIVKLLLEA-GADVNARDNdGETPLHLAAENGHLEIVKLLLEAGADVNA 214
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 85-127 6.23e-07

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: 46.04  E-value: 6.23e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1034604399  85 CDTCRQQPIIGIRWKCAECTNYDLCTVCY----HGDKHHLRHRFYRI 127
Cdd:cd02345     3 CSACRKQDISGIRFPCQVCRDYSLCLGCYtkgrETKRHNSLHIMYEL 49
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
 85-127 1.31e-06

Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239081  Cd Length: 48  Bit Score: 45.12  E-value: 1.31e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1034604399  85 CDTCRQQPIIGIRWKCAECTN--YDLCTVCYH-GDKHHLRHRFYRI 127
Cdd:cd02341     3 CDSCGIEPIPGTRYHCSECDDgdFDLCQDCVVkGESHQEDHWLVKI 48
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 85-123 5.66e-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: 43.44  E-value: 5.66e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1034604399  85 CDTCRQQPIIGIRWKCAECTNYDLCTVCYHGDKHHLRHR 123
Cdd:cd02335     3 CDYCSKDITGTIRIKCAECPDFDLCLECFSAGAEIGKHR 41
ZZ_UBA_plant cd02342
Zinc finger, ZZ type. Zinc finger present in plant ubiquitin-associated (UBA) proteins. The ZZ ...
 85-114 6.98e-05

Zinc finger, ZZ type. Zinc finger present in plant ubiquitin-associated (UBA) proteins. The ZZ motif coordinates a zinc ion and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239082  Cd Length: 43  Bit Score: 40.26  E-value: 6.98e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1034604399  85 CDTCRQQPIIGIRWKCAECTNYDLCTVCYH 114
Cdd:cd02342     3 CDGCGVLPITGPRYKSKVKEDYDLCTICFS 32
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
401-492 7.38e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 44.56  E-value: 7.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604399 401 ASAGSAISNASGERLSQLLKKLFETQESGDLNEELVKAAANGDVAKVEDLLKRPDVDVNGQCAGHTAMQAASQNGHVDIL 480
Cdd:COG0666    24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                          90
                  ....*....|..
gi 1034604399 481 KLLLKQNVDVEA 492
Cdd:COG0666   104 KLLLEAGADVNA 115
Ank_4 pfam13637
Ankyrin repeats (many copies);
435-484 2.68e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 2.68e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034604399 435 LVKAAANGDVAKVEDLLKRPdVDVNGQCA-GHTAMQAASQNGHVDILKLLL 484
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKG-ADINAVDGnGETALHFAASNGNVEVLKLLL 54
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
 83-119 6.74e-04

Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. CREB-binding protein (CBP) is a large multidomain protein that provides binding sites for transcriptional coactivators, the role of the ZZ domain in CBP/p300 is unclear.


Pssm-ID: 239077  Cd Length: 41  Bit Score: 37.54  E-value: 6.74e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1034604399  83 TMCDTCRQqpIIGIRWKCAECTNYDLCTVCYHGDKHH 119
Cdd:cd02337     1 YTCNECKH--HVETRWHCTVCEDYDLCITCYNTKNHP 35
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
85-138 1.04e-03

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


Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 41.59  E-value: 1.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034604399  85 CDTCRQQPIIGIRWKCAECTNYDLCTVCY----HGDKHHLRHRfYRITTPGSERVLLE 138
Cdd:COG5114     8 CDVCFLDMTDLTFIKCNECPAVDLCLPCFvngiETGVHSPYHG-YRIIETNSYPIGEE 64
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 464-492 2.16e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 2.16e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1034604399 464 GHTA-MQAASQNGHVDILKLLLKQNVDVEA 492
Cdd:pfam00023   2 GNTPlHLAAGRRGNLEIVKLLLSKGADVNA 31
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 464-492 2.45e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 2.45e-03
                           10        20
                   ....*....|....*....|....*....
gi 1034604399  464 GHTAMQAASQNGHVDILKLLLKQNVDVEA 492
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 425-491 4.53e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.85  E-value: 4.53e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034604399 425 TQESGDLNEE--LVKAAANGDVAKVEDLLK-RPDVDVnGQCAGHTAMQAASQNGHVDILKLLLKQ--NVDVE 491
Cdd:PLN03192  517 GGEHDDPNMAsnLLTVASTGNAALLEELLKaKLDPDI-GDSKGRTPLHIAASKGYEDCVLVLLKHacNVHIR 587
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 426-492 5.06e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.47  E-value: 5.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034604399 426 QESGDLneeLVKAAANGDVAKVEDLLKRP-DVDVNGQcAGHTAMQAASQNGHVDILKLLLKQNVDVEA 492
Cdd:PLN03192  620 HAAGDL---LCTAAKRNDLTAMKELLKQGlNVDSEDH-QGATALQVAMAEDHVDMVRLLIMNGADVDK 683
 
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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