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Conserved domains on  [gi|966658712|gb|KTF93566|]
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hypothetical protein cypCar_00034773 [Cyprinus carpio]

Protein Classification

ZZ domain-containing protein( domain architecture ID 10218796)

ZZ domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZZ super family cl00295
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 444-491 1.61e-29

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.


The actual alignment was detected with superfamily member cd02343:

Pssm-ID: 412288  Cd Length: 48  Bit Score: 111.25  E-value: 1.61e-29
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 966658712  444 ISCDGCERIAPWHRYRCLQCTDMDLCKTCFLSGAKPEGHEDDHEMVNM 491
Cdd:cd02343     1 ISCDGCDEIAPWHRYRCLQCTDMDLCKTCFLGGVKPEGHEDDHEMVNM 48
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 493-540 2.89e-15

Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins.


:

Pssm-ID: 239069 [Multi-domain]  Cd Length: 46  Bit Score: 70.54  E-value: 2.89e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 966658712  493 YACDHCQGLIVGSRINCNVCEDFDLCFGCYNAKKypDSHLPTHRITVY 540
Cdd:cd02249     1 YSCDGCLKPIVGVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46
 
Name Accession Description Interval E-value
ZZ_EF cd02343
Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif ...
 444-491 1.61e-29

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: 111.25  E-value: 1.61e-29
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 966658712  444 ISCDGCERIAPWHRYRCLQCTDMDLCKTCFLSGAKPEGHEDDHEMVNM 491
Cdd:cd02343     1 ISCDGCDEIAPWHRYRCLQCTDMDLCKTCFLGGVKPEGHEDDHEMVNM 48
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 493-540 2.89e-15

Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins.


Pssm-ID: 239069 [Multi-domain]  Cd Length: 46  Bit Score: 70.54  E-value: 2.89e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 966658712  493 YACDHCQGLIVGSRINCNVCEDFDLCFGCYNAKKypDSHLPTHRITVY 540
Cdd:cd02249     1 YSCDGCLKPIVGVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 491-531 3.24e-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: 58.99  E-value: 3.24e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 966658712    491 MEYACDHCQGLIVGSRINCNVCEDFDLCFGCYNAKKYPDSH 531
Cdd:smart00291    3 HSYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEH 43
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 443-483 3.48e-07

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: 47.82  E-value: 3.48e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 966658712    443 EISCDGCERIAPWHRYRCLQCTDMDLCKTCFLSGAKPEGHE 483
Cdd:smart00291    4 SYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 491-529 3.71e-06

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: 44.78  E-value: 3.71e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 966658712   491 MEYACDHCQ-GLIVGSRINCNVCEDFDLCFGCYNAKKYPD 529
Cdd:pfam00569    3 KVYTCNGCSnDPSIGVRYHCLRCSDYDLCQSCFQTHKGGN 42
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
488-535 1.85e-04

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


Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 45.45  E-value: 1.85e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 966658712  488 MVNMEYACDHCQGLIVGS-RINCNVCEDFDLCFGCYNAKKYPDSHLPTH 535
Cdd:COG5114     1 MGGVKIHCDVCFLDMTDLtFIKCNECPAVDLCLPCFVNGIETGVHSPYH 49
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 443-488 2.89e-03

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: 36.69  E-value: 2.89e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 966658712   443 EISCDGCERIAPWH-RYRCLQCTDMDLCKTCFLSGAKPeghedDHEM 488
Cdd:pfam00569    4 VYTCNGCSNDPSIGvRYHCLRCSDYDLCQSCFQTHKGG-----NHQM 45
 
Name Accession Description Interval E-value
ZZ_EF cd02343
Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif ...
 444-491 1.61e-29

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: 111.25  E-value: 1.61e-29
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 966658712  444 ISCDGCERIAPWHRYRCLQCTDMDLCKTCFLSGAKPEGHEDDHEMVNM 491
Cdd:cd02343     1 ISCDGCDEIAPWHRYRCLQCTDMDLCKTCFLGGVKPEGHEDDHEMVNM 48
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 493-540 2.89e-15

Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins.


Pssm-ID: 239069 [Multi-domain]  Cd Length: 46  Bit Score: 70.54  E-value: 2.89e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 966658712  493 YACDHCQGLIVGSRINCNVCEDFDLCFGCYNAKKypDSHLPTHRITVY 540
Cdd:cd02249     1 YSCDGCLKPIVGVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 444-491 2.80e-11

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: 59.37  E-value: 2.80e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 966658712  444 ISCDGCERIAPWHRYRCLQCTDMDLCKTCFLSGAKpeGHEDDHEMVNM 491
Cdd:cd02249     1 YSCDGCLKPIVGVRYHCLVCEDFDLCSSCYAKGKK--GHPPDHSFTEI 46
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 491-531 3.24e-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: 58.99  E-value: 3.24e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 966658712    491 MEYACDHCQGLIVGSRINCNVCEDFDLCFGCYNAKKYPDSH 531
Cdd:smart00291    3 HSYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEH 43
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 444-488 2.13e-09

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: 53.89  E-value: 2.13e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 966658712  444 ISCDGCERIAPW-HRYRCLQCTDMDLCKTCFLSGAKPEGHEDDHEM 488
Cdd:cd02338     1 VSCDGCGKSNFTgRRYKCLICYDYDLCADCYDSGVTTERHLFDHPM 46
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 444-493 5.91e-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: 5.91e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 966658712  444 ISCDGCERIaPWH--RYRCLQCTDMDLCKTCFLSGAKPEGHEDDHEMvnMEY 493
Cdd:cd02334     1 AKCNICKEF-PITgfRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPM--KEY 49
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
 493-528 9.37e-08

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: 49.10  E-value: 9.37e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 966658712  493 YACDHCQgLIVGSRINCNVCEDFDLCFGCYNAKKYP 528
Cdd:cd02337     1 YTCNECK-HHVETRWHCTVCEDYDLCITCYNTKNHP 35
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 443-483 3.48e-07

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: 47.82  E-value: 3.48e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 966658712    443 EISCDGCERIAPWHRYRCLQCTDMDLCKTCFLSGAKPEGHE 483
Cdd:smart00291    4 SYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 495-521 4.08e-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: 47.25  E-value: 4.08e-07
                          10        20
                  ....*....|....*....|....*..
gi 966658712  495 CDHCQGLIVGSRINCNVCEDFDLCFGC 521
Cdd:cd02340     3 CDGCQGPIVGVRYKCLVCPDYDLCESC 29
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 444-491 1.66e-06

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: 45.71  E-value: 1.66e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 966658712  444 ISCDGCERIAPWHRYRCLQCTDMDLCKTCFLSGAKPEgheddHEMVNM 491
Cdd:cd02340     1 VICDGCQGPIVGVRYKCLVCPDYDLCESCEAKGVHPE-----HAMLKI 43
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 493-535 3.03e-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: 44.98  E-value: 3.03e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 966658712  493 YACDHCQGLIVGS-RINCNVCEDFDLCFGCYNAKKYPDSHLPTH 535
Cdd:cd02335     1 YHCDYCSKDITGTiRIKCAECPDFDLCLECFSAGAEIGKHRNDH 44
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 444-486 3.12e-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: 44.98  E-value: 3.12e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 966658712  444 ISCDGC-ERIAPWHRYRCLQCTDMDLCKTCFLSGAKPEGHEDDH 486
Cdd:cd02335     1 YHCDYCsKDITGTIRIKCAECPDFDLCLECFSAGAEIGKHRNDH 44
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 491-529 3.71e-06

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: 44.78  E-value: 3.71e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 966658712   491 MEYACDHCQ-GLIVGSRINCNVCEDFDLCFGCYNAKKYPD 529
Cdd:pfam00569    3 KVYTCNGCSnDPSIGVRYHCLRCSDYDLCQSCFQTHKGGN 42
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 495-540 1.39e-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: 1.39e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 966658712  495 CDHCQ-GLIVGSRINCNVCEDFDLCFGCYNAKKYPDSHLPTHRITVY 540
Cdd:cd02338     3 CDGCGkSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFDHPMQCI 49
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 495-531 3.18e-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: 42.19  E-value: 3.18e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 966658712  495 CDHCQGL-IVGSRINCNVCEDFDLCFGCYNAKKYPDSH 531
Cdd:cd02344     3 CDGCQMFpINGPRFKCRNCDDFDFCENCFKTRKHNTRH 40
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
488-535 1.85e-04

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


Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 45.45  E-value: 1.85e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 966658712  488 MVNMEYACDHCQGLIVGS-RINCNVCEDFDLCFGCYNAKKYPDSHLPTH 535
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. ...
 495-531 1.34e-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: 37.44  E-value: 1.34e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 966658712  495 CDHCQGL-IVGSRINCNVCEDFDLCFGCYNAKKYPDSH 531
Cdd:cd02339     3 CDTCRKQgIIGIRWKCAECPNYDLCTTCYHGDKHDLEH 40
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 444-488 1.92e-03

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: 37.18  E-value: 1.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 966658712  444 ISCDGCERI-APWHRYRCLQCTDMDLCKTCFLSGAKPEGHEDDHEM 488
Cdd:cd02345     1 LSCSACRKQdISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLHIM 46
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 444-488 2.48e-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: 36.67  E-value: 2.48e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 966658712  444 ISCDGCER--IAPWhRYRCLQCTDMDLCKTCFlsgakpegHEDDHEM 488
Cdd:cd02339     1 IICDTCRKqgIIGI-RWKCAECPNYDLCTTCY--------HGDKHDL 38
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 443-488 2.89e-03

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: 36.69  E-value: 2.89e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 966658712   443 EISCDGCERIAPWH-RYRCLQCTDMDLCKTCFLSGAKPeghedDHEM 488
Cdd:pfam00569    4 VYTCNGCSNDPSIGvRYHCLRCSDYDLCQSCFQTHKGG-----NHQM 45
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 502-536 4.66e-03

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: 36.03  E-value: 4.66e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 966658712  502 IVGSRINCNVCEDFDLCFGCYNAKKYPDSHLPTHR 536
Cdd:cd02345    11 ISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLHI 45
 
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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