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Conserved domains on  [gi|815890985|ref|NP_001295166|]
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ZZ-type zinc finger-containing protein 3 isoform 2 [Homo sapiens]

Protein Classification

SANT/Myb-like DNA-binding domain-containing protein( domain architecture ID 10073776)

SANT (SWI3, ADA2, N-CoR and TFIIIB)/Myb-like DNA-binding domain-containing protein binds DNA and may function as a transcription factor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
 327-378 4.40e-21

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: 85.56  E-value: 4.40e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 815890985 327 FKCDNCGIEPIQGVRWHCQDCPPemslDFCDSCSDCLHETDIHKEDHQLEPI 378
Cdd:cd02341    1 FKCDSCGIEPIPGTRYHCSECDD----GDFDLCQDCVVKGESHQEDHWLVKI 48
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 161-209 2.05e-09

'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.


:

Pssm-ID: 238096 [Multi-domain]  Cd Length: 45  Bit Score: 52.58  E-value: 2.05e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 815890985 161 WTVEEQKKLEQLLIKYPPeevesRRWQKIADELGNRTAKQVASRVQKYF 209
Cdd:cd00167    2 WTEEEDELLLEAVKKYGK-----NNWEKIAKELPGRTPKQCRERWRNLL 45
 
Name Accession Description Interval E-value
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
 327-378 4.40e-21

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: 85.56  E-value: 4.40e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 815890985 327 FKCDNCGIEPIQGVRWHCQDCPPemslDFCDSCSDCLHETDIHKEDHQLEPI 378
Cdd:cd02341    1 FKCDSCGIEPIPGTRYHCSECDD----GDFDLCQDCVVKGESHQEDHWLVKI 48
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 161-209 2.05e-09

'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.


Pssm-ID: 238096 [Multi-domain]  Cd Length: 45  Bit Score: 52.58  E-value: 2.05e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 815890985 161 WTVEEQKKLEQLLIKYPPeevesRRWQKIADELGNRTAKQVASRVQKYF 209
Cdd:cd00167    2 WTEEEDELLLEAVKKYGK-----NNWEKIAKELPGRTPKQCRERWRNLL 45
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 161-209 2.41e-09

Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family.


Pssm-ID: 459731 [Multi-domain]  Cd Length: 46  Bit Score: 52.51  E-value: 2.41e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 815890985  161 WTVEEQKKLEQLLIKYPpeevesRRWQKIADELGNRTAKQVASRVQKYF 209
Cdd:pfam00249   4 WTPEEDELLLEAVEKLG------NRWKKIAKLLPGRTDNQCKNRWQNYL 46
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
161-211 9.62e-09

SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 51.07  E-value: 9.62e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 815890985   161 WTVEEQKKLEQLLIKYPPeevesRRWQKIADELGNRTAKQVASRVQKYFIK 211
Cdd:smart00717   4 WTEEEDELLIELVKKYGK-----NNWEKIAKELPGRTAEQCRERWRNLLKP 49
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 324-359 7.59e-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: 42.86  E-value: 7.59e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 815890985  324 HVGFKCDNCGIEPIQGVRWHCQDCPpemSLDFCDSC 359
Cdd:pfam00569   2 HKVYTCNGCSNDPSIGVRYHCLRCS---DYDLCQSC 34
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 324-359 1.46e-05

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: 42.04  E-value: 1.46e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 815890985   324 HVGFKCDNCGiEPIQGVRWHCQDCPpemSLDFCDSC 359
Cdd:smart00291   2 HHSYSCDTCG-KPIVGVRYHCLVCP---DYDLCQSC 33
 
Name Accession Description Interval E-value
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
 327-378 4.40e-21

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: 85.56  E-value: 4.40e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 815890985 327 FKCDNCGIEPIQGVRWHCQDCPPemslDFCDSCSDCLHETDIHKEDHQLEPI 378
Cdd:cd02341    1 FKCDSCGIEPIPGTRYHCSECDD----GDFDLCQDCVVKGESHQEDHWLVKI 48
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 327-378 3.93e-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: 57.83  E-value: 3.93e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 815890985 327 FKCDNCGIePIQGVRWHCQDCPpemsldFCDSCSDCLHE-TDIHKEDHQLEPI 378
Cdd:cd02249    1 YSCDGCLK-PIVGVRYHCLVCE------DFDLCSSCYAKgKKGHPPDHSFTEI 46
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 161-209 2.05e-09

'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.


Pssm-ID: 238096 [Multi-domain]  Cd Length: 45  Bit Score: 52.58  E-value: 2.05e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 815890985 161 WTVEEQKKLEQLLIKYPPeevesRRWQKIADELGNRTAKQVASRVQKYF 209
Cdd:cd00167    2 WTEEEDELLLEAVKKYGK-----NNWEKIAKELPGRTPKQCRERWRNLL 45
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 161-209 2.41e-09

Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family.


Pssm-ID: 459731 [Multi-domain]  Cd Length: 46  Bit Score: 52.51  E-value: 2.41e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 815890985  161 WTVEEQKKLEQLLIKYPpeevesRRWQKIADELGNRTAKQVASRVQKYF 209
Cdd:pfam00249   4 WTPEEDELLLEAVEKLG------NRWKKIAKLLPGRTDNQCKNRWQNYL 46
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
161-211 9.62e-09

SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 51.07  E-value: 9.62e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 815890985   161 WTVEEQKKLEQLLIKYPPeevesRRWQKIADELGNRTAKQVASRVQKYFIK 211
Cdd:smart00717   4 WTEEEDELLIELVKKYGK-----NNWEKIAKELPGRTAEQCRERWRNLLKP 49
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 324-359 7.59e-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: 42.86  E-value: 7.59e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 815890985  324 HVGFKCDNCGIEPIQGVRWHCQDCPpemSLDFCDSC 359
Cdd:pfam00569   2 HKVYTCNGCSNDPSIGVRYHCLRCS---DYDLCQSC 34
Bbox1 cd19757
B-box-type 1 zinc finger (Bbox1); The B-box-type zinc finger is a short zinc binding domain of ...
 328-378 1.39e-05

B-box-type 1 zinc finger (Bbox1); The B-box-type zinc finger is a short zinc binding domain of around 40 amino acid residues in length. It has been found in transcription factors, ribonucleoproteins and proto-oncoproteins, such as in TRIM (tripartite motif) proteins that consist of an N-terminal RING finger (originally called an A-box), followed by 1-2 B-box domains and a coiled-coil domain (also called RBCC for Ring, B-box, Coiled-Coil). The B-box-type zinc finger often presents in combination with other motifs, like RING zinc finger, NHL motif, coiled-coil or RFP domain, in functionally unrelated proteins, most likely mediating protein-protein interactions. Based on different consensus sequences and the spacing of the 7-8 zinc-binding residues, the B-box-type zinc fingers can be divided into two groups, type 1 (Bbox1: C6H2) and type 2 (Bbox2: CHC3H2). This family corresponds to the type 1 B-box (Bbox1).


Pssm-ID: 380815 [Multi-domain]  Cd Length: 44  Bit Score: 42.10  E-value: 1.39e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 815890985 328 KCDNCGIEPiqgVRWHCQDCppemSLDFCDSCSDCLHETDIHKEDHQLEPI 378
Cdd:cd19757    1 LCDECEERE---ATVYCLEC----EEFLCDDCSDAIHRRGKLTRSHKLVPL 44
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 324-359 1.46e-05

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: 42.04  E-value: 1.46e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 815890985   324 HVGFKCDNCGiEPIQGVRWHCQDCPpemSLDFCDSC 359
Cdd:smart00291   2 HHSYSCDTCG-KPIVGVRYHCLVCP---DYDLCQSC 33
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 329-371 5.43e-05

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: 40.32  E-value: 5.43e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 815890985 329 CDNCGIePIQGVRWHCQDCPpemslDFcDSCSDClHETDIHKE 371
Cdd:cd02340    3 CDGCQG-PIVGVRYKCLVCP-----DY-DLCESC-EAKGVHPE 37
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 329-376 6.40e-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: 40.02  E-value: 6.40e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 815890985 329 CDNCGIEPIQGVRWHCQDCPpemSLDFCDSCSDCLHETDIHKEDHQLE 376
Cdd:cd02338    3 CDGCGKSNFTGRRYKCLICY---DYDLCADCYDSGVTTERHLFDHPMQ 47
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 329-376 5.67e-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: 37.44  E-value: 5.67e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 815890985 329 CDNCGIEPIQGVRWHCQDCPpemSLDFCDSCSDclheTDIHKEDHQLE 376
Cdd:cd02339    3 CDTCRKQGIIGIRWKCAECP---NYDLCTTCYH----GDKHDLEHRFY 43
Myb_DNA-bind_6 pfam13921
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 161-204 6.62e-04

Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family.


Pssm-ID: 372817 [Multi-domain]  Cd Length: 60  Bit Score: 37.67  E-value: 6.62e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 815890985  161 WTVEEQKKLEQLLIKYppeeveSRRWQKIADELGNRTAKQVASR 204
Cdd:pfam13921   1 WTEEEDEKLLKLVEKY------GNDWKQIAKELGRRTPKQCFDR 38
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 327-378 1.83e-03

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: 36.12  E-value: 1.83e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 815890985 327 FKCDNCGIEPIQGVRWHCQDCPPemsLDFCDSCSDCLHETDIHKEDHQLEPI 378
Cdd:cd02335    1 YHCDYCSKDITGTIRIKCAECPD---FDLCLECFSAGAEIGKHRNDHNYRVV 49
UBR-box_UBR4_5_6_7 cd19671
UBR-box found in UBR4, UBR5, UBR6/FBOX11, UBR7 and similar proteins; This family includes UBR4 ...
 333-394 4.58e-03

UBR-box found in UBR4, UBR5, UBR6/FBOX11, UBR7 and similar proteins; This family includes UBR4 (EC 2.3.2.27), UBR5 (EC 2.3.2.26), UBR6/FBOX11 and UBR7 (EC 2.3.2.27). Both UBR4 (also called 600 kDa retinoblastoma protein-associated factor, or N-recognin-4, or retinoblastoma-associated factor of 600 kDa, or RBAF600, or p600, or zinc finger UBR1-type protein 1) and UBR7 (also called N-recognin-7) are RING-type E3 ubiquitin ligases of the Arg/N-end rule degradation pathway. They recognize and bind to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. UBR5 (also called E3 ubiquitin-protein ligase, HECT domain-containing 1, E3 ligase identified by differential display (EDD), hyperplastic discs protein homolog (HYD), progestin-induced protein, or N-recognin-5) is a HECT (homologous to E6-AP C-terminus)-type E3 ubiquitin-protein ligase that acts as a key regulator of the ubiquitin proteasome system in both cancer and developmental biology. It is required for Wnt signal responses in Drosophila and human cell lines downstream of activated Armadillo/beta-catenin. It also plays a key role in ciliogenesis by regulating centriolar satellite stability and primary cilia. UBR6 (also called FBOX11, protein arginine N-methyltransferase 9 (PRMT9), or vitiligo-associated protein 1 (VIT-1)), is an E3 ubiquitin ligase and a type II methyltransferase, which functions as a key regulator of tumor initiation and progression. UBR6 is a substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as DTL/CDT2, BCL6 and PRDM1/BLIMP1. UBR6 does not bind N-terminal signals.


Pssm-ID: 439069  Cd Length: 67  Bit Score: 35.51  E-value: 4.58e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 815890985 333 GIEPIQGVRWHCQDCPPEMSLDFCDSCSD-ClhetdiHKeDHQLEPIYRSETFLDrdyCVSQG 394
Cdd:cd19671    7 GRKYIKQPWYHCYTCGLIDGLGVCEACARkC------HK-GHDLVYIGYSNFYCD---CGSSG 59
 
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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