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Conserved domains on  [gi|189491869|ref|NP_001121664|]
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E3 ubiquitin-protein ligase KCMF1 [Rattus norvegicus]

Protein Classification

ZZ-type zinc finger protein( domain architecture ID 10115790)

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
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 7-55 8.49e-24

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: 92.80  E-value: 8.49e-24
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 189491869   7 VSCDACLKGNFRGRRYKCLICYDYDLCASCYESGATTTRHTTDHPMQCI 55
Cdd:cd02338    1 VSCDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFDHPMQCI 49
zf-Di19 pfam05605
Drought induced 19 protein (Di19), zinc-binding; This family consists of several drought ...
 76-137 2.62e-21

Drought induced 19 protein (Di19), zinc-binding; This family consists of several drought induced 19 (Di19) like proteins. Di19 has been found to be strongly expressed in both the roots and leaves of Arabidopsis thaliana during progressive drought. This domain is a zinc-binding domain.


:

Pssm-ID: 428539  Cd Length: 54  Bit Score: 86.20  E-value: 2.62e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189491869   76 QSFTCPYCGKmGYTETSLQEHVTSEHAETSTEVICPICAalpggdpNHVTDDFAAHLTLEHR 137
Cdd:pfam05605   1 DEFTCPFCGE-DFDVVSLCEHVEDEHPVESKNVVCPVCA-------AKVGKDMIGHLTLQHG 54
 
Name Accession Description Interval E-value
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 7-55 8.49e-24

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: 92.80  E-value: 8.49e-24
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 189491869   7 VSCDACLKGNFRGRRYKCLICYDYDLCASCYESGATTTRHTTDHPMQCI 55
Cdd:cd02338    1 VSCDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFDHPMQCI 49
zf-Di19 pfam05605
Drought induced 19 protein (Di19), zinc-binding; This family consists of several drought ...
 76-137 2.62e-21

Drought induced 19 protein (Di19), zinc-binding; This family consists of several drought induced 19 (Di19) like proteins. Di19 has been found to be strongly expressed in both the roots and leaves of Arabidopsis thaliana during progressive drought. This domain is a zinc-binding domain.


Pssm-ID: 428539  Cd Length: 54  Bit Score: 86.20  E-value: 2.62e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189491869   76 QSFTCPYCGKmGYTETSLQEHVTSEHAETSTEVICPICAalpggdpNHVTDDFAAHLTLEHR 137
Cdd:pfam05605   1 DEFTCPFCGE-DFDVVSLCEHVEDEHPVESKNVVCPVCA-------AKVGKDMIGHLTLQHG 54
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 3-46 5.42e-12

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: 60.15  E-value: 5.42e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 189491869     3 RHEGVSCDACLKgNFRGRRYKCLICYDYDLCASCYESGATTTRH 46
Cdd:smart00291   1 VHHSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEH 43
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 4-52 4.06e-08

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: 49.02  E-value: 4.06e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 189491869    4 HEGVSCDACLKGNFRGRRYKCLICYDYDLCASCYesgatTTRHTTDHPM 52
Cdd:pfam00569   2 HKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCF-----QTHKGGNHQM 45
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
9-57 7.26e-06

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


Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 47.76  E-value: 7.26e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 189491869   9 CDACLKGNFRGRRYKCLICYDYDLCASCYESGATTTRHTTDHPMQCILT 57
Cdd:COG5114    8 CDVCFLDMTDLTFIKCNECPAVDLCLPCFVNGIETGVHSPYHGYRIIET 56
 
Name Accession Description Interval E-value
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 7-55 8.49e-24

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: 92.80  E-value: 8.49e-24
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 189491869   7 VSCDACLKGNFRGRRYKCLICYDYDLCASCYESGATTTRHTTDHPMQCI 55
Cdd:cd02338    1 VSCDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFDHPMQCI 49
zf-Di19 pfam05605
Drought induced 19 protein (Di19), zinc-binding; This family consists of several drought ...
 76-137 2.62e-21

Drought induced 19 protein (Di19), zinc-binding; This family consists of several drought induced 19 (Di19) like proteins. Di19 has been found to be strongly expressed in both the roots and leaves of Arabidopsis thaliana during progressive drought. This domain is a zinc-binding domain.


Pssm-ID: 428539  Cd Length: 54  Bit Score: 86.20  E-value: 2.62e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189491869   76 QSFTCPYCGKmGYTETSLQEHVTSEHAETSTEVICPICAalpggdpNHVTDDFAAHLTLEHR 137
Cdd:pfam05605   1 DEFTCPFCGE-DFDVVSLCEHVEDEHPVESKNVVCPVCA-------AKVGKDMIGHLTLQHG 54
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 7-55 9.65e-14

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: 9.65e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 189491869   7 VSCDACLKgNFRGRRYKCLICYDYDLCASCYESGAttTRHTTDHPMQCI 55
Cdd:cd02249    1 YSCDGCLK-PIVGVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 3-46 5.42e-12

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: 60.15  E-value: 5.42e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 189491869     3 RHEGVSCDACLKgNFRGRRYKCLICYDYDLCASCYESGATTTRH 46
Cdd:smart00291   1 VHHSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEH 43
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 7-53 3.05e-11

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: 58.14  E-value: 3.05e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 189491869   7 VSCDACLKGNFRGRRYKCLICYDYDLCASCYESGATTTRHTTDHPMQ 53
Cdd:cd02334    1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMK 47
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 7-52 5.69e-10

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: 54.19  E-value: 5.69e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 189491869   7 VSCDACLKGNfRGRRYKCLICYDYDLCASCYESGAtttrHTTdHPM 52
Cdd:cd02340    1 VICDGCQGPI-VGVRYKCLVCPDYDLCESCEAKGV----HPE-HAM 40
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 9-51 2.99e-08

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: 49.38  E-value: 2.99e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 189491869   9 CDACLKGNFRGRRYKCLICYDYDLCASCYEsgatTTRHTTDHP 51
Cdd:cd02339    3 CDTCRKQGIIGIRWKCAECPNYDLCTTCYH----GDKHDLEHR 41
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 4-52 4.06e-08

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: 49.02  E-value: 4.06e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 189491869    4 HEGVSCDACLKGNFRGRRYKCLICYDYDLCASCYesgatTTRHTTDHPM 52
Cdd:pfam00569   2 HKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCF-----QTHKGGNHQM 45
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 8-52 9.88e-08

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: 47.97  E-value: 9.88e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 189491869   8 SCDACLKGNFRGRRYKCLICYDYDLCASCYESGATTTRHTTDHPM 52
Cdd:cd02345    2 SCSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLHIM 46
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 9-53 1.78e-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: 44.59  E-value: 1.78e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 189491869   9 CDACLKGNFRGRRYKCLICYDYDLCASCYESGATTTRHTTDHPMQ 53
Cdd:cd02335    3 CDYCSKDITGTIRIKCAECPDFDLCLECFSAGAEIGKHRNDHNYR 47
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
9-57 7.26e-06

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


Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 47.76  E-value: 7.26e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 189491869   9 CDACLKGNFRGRRYKCLICYDYDLCASCYESGATTTRHTTDHPMQCILT 57
Cdd:COG5114    8 CDVCFLDMTDLTFIKCNECPAVDLCLPCFVNGIETGVHSPYHGYRIIET 56
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 7-47 1.18e-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: 1.18e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 189491869   7 VSCDACLKGNFRGRRYKCLICYDYDLCASCYESGATTTRHT 47
Cdd:cd02344    1 VTCDGCQMFPINGPRFKCRNCDDFDFCENCFKTRKHNTRHT 41
ZZ_EF cd02343
Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif ...
 7-52 2.48e-05

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: 41.15  E-value: 2.48e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 189491869   7 VSCDACLKGNfRGRRYKCLICYDYDLCASCYESGATTTRHTTDHPM 52
Cdd:cd02343    1 ISCDGCDEIA-PWHRYRCLQCTDMDLCKTCFLGGVKPEGHEDDHEM 45
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
 7-52 3.97e-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: 35.10  E-value: 3.97e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 189491869   7 VSCDACLKGNFRGRRYKCLIC--YDYDLCASCYESGATttrHTTDHPM 52
Cdd:cd02341    1 FKCDSCGIEPIPGTRYHCSECddGDFDLCQDCVVKGES---HQEDHWL 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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