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Conserved domains on  [gi|151175482|emb|CAJ35021|]
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Ref(2)P protein, partial [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 121-165 3.50e-20

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: 83.30  E-value: 3.50e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 151175482  121 IHDAVECDGCGLAPLIGFRYKCVQCSNYDLCQKCELAHKHPEHLM 165
Cdd:pfam00569   1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQTHKGGNHQM 45
PB1 super family cl02720
The PB1 domain is a modular domain mediating specific protein-protein interactions which play ...
 6-88 4.25e-05

The PB1 domain is a modular domain mediating specific protein-protein interactions which play a role in many critical cell processes, such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domain, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as a noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.


The actual alignment was detected with superfamily member pfam00564:

Pssm-ID: 413452  Cd Length: 84  Bit Score: 41.89  E-value: 4.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151175482    6 LKITYQGAgpqKKINAYLRMPSqNYTALRREIELYLflerQLPKCDVRTFWIDAYKDEIEIVNQNDYEIFLAKCES---- 81
Cdd:pfam00564   4 LKLRYGGG---IRRFLSVSRGI-SFEELRALVEQRF----GLDDVDFKLKYPDEDGDLVSLTSDEDLEEALEEARSlgsk 75


                  ....*....
gi 151175482   82 --NMHVQVA 88
Cdd:pfam00564  76 slRLHVFPT 84
PRK13335 super family cl31400
superantigen-like protein SSL3; Reviewed;
243-315 2.93e-03

superantigen-like protein SSL3; Reviewed;


The actual alignment was detected with superfamily member PRK13335:

Pssm-ID: 139494 [Multi-domain]  Cd Length: 356  Bit Score: 39.72  E-value: 2.93e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 151175482 243 NTTTATAPAEPQkpkaaEQTESPPQAEPTVTAEKAAESEAKPTEPKKVNTDQ------SVPRTEDPVTTPRSTQPTTPV 315
Cdd:PRK13335  59 NSATTQAANTRQ-----ERTPKLEKAPNTNEEKTSASKIEKISQPKQEEQKSlnisatPAPKQEQSQTTTESTTPKTKV 132
 
Name Accession Description Interval E-value
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 121-165 3.50e-20

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: 83.30  E-value: 3.50e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 151175482  121 IHDAVECDGCGLAPLIGFRYKCVQCSNYDLCQKCELAHKHPEHLM 165
Cdd:pfam00569   1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQTHKGGNHQM 45
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 125-168 5.18e-20

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: 82.69  E-value: 5.18e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 151175482 125 VECDGCGlAPLIGFRYKCVQCSNYDLCQKCELAHKHPEHLMLRM 168
Cdd:cd02340    1 VICDGCQ-GPIVGVRYKCLVCPDYDLCESCEAKGVHPEHAMLKI 43
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 121-163 1.92e-13

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: 64.38  E-value: 1.92e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 151175482   121 IHDAVECDGCGlAPLIGFRYKCVQCSNYDLCQKCELA-HKHPEH 163
Cdd:smart00291   1 VHHSYSCDTCG-KPIVGVRYHCLVCPDYDLCQSCFAKgSAGGEH 43
PB1 pfam00564
PB1 domain;
6-88 4.25e-05

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 41.89  E-value: 4.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151175482    6 LKITYQGAgpqKKINAYLRMPSqNYTALRREIELYLflerQLPKCDVRTFWIDAYKDEIEIVNQNDYEIFLAKCES---- 81
Cdd:pfam00564   4 LKLRYGGG---IRRFLSVSRGI-SFEELRALVEQRF----GLDDVDFKLKYPDEDGDLVSLTSDEDLEEALEEARSlgsk 75


                  ....*....
gi 151175482   82 --NMHVQVA 88
Cdd:pfam00564  76 slRLHVFPT 84
PRK13335 PRK13335
superantigen-like protein SSL3; Reviewed;
243-315 2.93e-03

superantigen-like protein SSL3; Reviewed;


Pssm-ID: 139494 [Multi-domain]  Cd Length: 356  Bit Score: 39.72  E-value: 2.93e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 151175482 243 NTTTATAPAEPQkpkaaEQTESPPQAEPTVTAEKAAESEAKPTEPKKVNTDQ------SVPRTEDPVTTPRSTQPTTPV 315
Cdd:PRK13335  59 NSATTQAANTRQ-----ERTPKLEKAPNTNEEKTSASKIEKISQPKQEEQKSlnisatPAPKQEQSQTTTESTTPKTKV 132
 
Name Accession Description Interval E-value
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 121-165 3.50e-20

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: 83.30  E-value: 3.50e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 151175482  121 IHDAVECDGCGLAPLIGFRYKCVQCSNYDLCQKCELAHKHPEHLM 165
Cdd:pfam00569   1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQTHKGGNHQM 45
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 125-168 5.18e-20

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: 82.69  E-value: 5.18e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 151175482 125 VECDGCGlAPLIGFRYKCVQCSNYDLCQKCELAHKHPEHLMLRM 168
Cdd:cd02340    1 VICDGCQ-GPIVGVRYKCLVCPDYDLCESCEAKGVHPEHAMLKI 43
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 121-163 1.92e-13

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: 64.38  E-value: 1.92e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 151175482   121 IHDAVECDGCGlAPLIGFRYKCVQCSNYDLCQKCELA-HKHPEH 163
Cdd:smart00291   1 VHHSYSCDTCG-KPIVGVRYHCLVCPDYDLCQSCFAKgSAGGEH 43
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 125-165 1.81e-12

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: 61.59  E-value: 1.81e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 151175482 125 VECDGCGLAPLIGFRYKCVQCSNYDLCQKC-ELAHKHPEHLM 165
Cdd:cd02338    1 VSCDGCGKSNFTGRRYKCLICYDYDLCADCyDSGVTTERHLF 42
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 125-168 2.75e-12

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


Pssm-ID: 239069 [Multi-domain]  Cd Length: 46  Bit Score: 60.91  E-value: 2.75e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 151175482 125 VECDGCGlAPLIGFRYKCVQCSNYDLCQKC--ELAHKH-PEHLMLRM 168
Cdd:cd02249    1 YSCDGCL-KPIVGVRYHCLVCEDFDLCSSCyaKGKKGHpPDHSFTEI 46
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 127-167 2.97e-12

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: 60.94  E-value: 2.97e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 151175482 127 CDGCGLAPLIGFRYKCVQCSNYDLCQKCELAHKH-PEHLMLR 167
Cdd:cd02339    3 CDTCRKQGIIGIRWKCAECPNYDLCTTCYHGDKHdLEHRFYR 44
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 125-160 2.56e-10

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: 55.44  E-value: 2.56e-10
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 151175482 125 VECDGCGLAPLIGFRYKCVQCSNYDLCQKCELAHKH 160
Cdd:cd02334    1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRT 36
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 125-163 2.66e-08

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: 49.89  E-value: 2.66e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 151175482 125 VECDGCGLAPLIGFRYKCVQCSNYDLCQKCELAHKH-PEH 163
Cdd:cd02344    1 VTCDGCQMFPINGPRFKCRNCDDFDFCENCFKTRKHnTRH 40
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
 125-154 1.01e-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: 45.50  E-value: 1.01e-06
                         10        20        30
                 ....*....|....*....|....*....|..
gi 151175482 125 VECDGCGLAPLIGFRYKCVQCSN--YDLCQKC 154
Cdd:cd02341    1 FKCDSCGIEPIPGTRYHCSECDDgdFDLCQDC 32
ZZ_EF cd02343
Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif ...
 125-168 2.86e-06

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: 44.23  E-value: 2.86e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 151175482 125 VECDGCG-LAPLigFRYKCVQCSNYDLCQKCELAHKHPE-----HLMLRM 168
Cdd:cd02343    1 ISCDGCDeIAPW--HRYRCLQCTDMDLCKTCFLGGVKPEgheddHEMVNM 48
ZZ_UBA_plant cd02342
Zinc finger, ZZ type. Zinc finger present in plant ubiquitin-associated (UBA) proteins. The ZZ ...
 125-154 9.74e-06

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: 42.57  E-value: 9.74e-06
                         10        20        30
                 ....*....|....*....|....*....|
gi 151175482 125 VECDGCGLAPLIGFRYKCVQCSNYDLCQKC 154
Cdd:cd02342    1 IQCDGCGVLPITGPRYKSKVKEDYDLCTIC 30
PB1 pfam00564
PB1 domain;
6-88 4.25e-05

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 41.89  E-value: 4.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151175482    6 LKITYQGAgpqKKINAYLRMPSqNYTALRREIELYLflerQLPKCDVRTFWIDAYKDEIEIVNQNDYEIFLAKCES---- 81
Cdd:pfam00564   4 LKLRYGGG---IRRFLSVSRGI-SFEELRALVEQRF----GLDDVDFKLKYPDEDGDLVSLTSDEDLEEALEEARSlgsk 75


                  ....*....
gi 151175482   82 --NMHVQVA 88
Cdd:pfam00564  76 slRLHVFPT 84
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 127-163 2.16e-04

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: 38.81  E-value: 2.16e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 151175482 127 CDGCGLAPLIGFRYKCVQCSNYDLCQKC-----ELAHKHPEH 163
Cdd:cd02335    3 CDYCSKDITGTIRIKCAECPDFDLCLECfsagaEIGKHRNDH 44
PRK13335 PRK13335
superantigen-like protein SSL3; Reviewed;
243-315 2.93e-03

superantigen-like protein SSL3; Reviewed;


Pssm-ID: 139494 [Multi-domain]  Cd Length: 356  Bit Score: 39.72  E-value: 2.93e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 151175482 243 NTTTATAPAEPQkpkaaEQTESPPQAEPTVTAEKAAESEAKPTEPKKVNTDQ------SVPRTEDPVTTPRSTQPTTPV 315
Cdd:PRK13335  59 NSATTQAANTRQ-----ERTPKLEKAPNTNEEKTSASKIEKISQPKQEEQKSlnisatPAPKQEQSQTTTESTTPKTKV 132
 
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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