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Conserved domains on  [gi|119581356|gb|EAW60952|]
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neighbor of BRCA1 gene 1, isoform CRA_d, partial [Homo sapiens]

Protein Classification

next to BRCA1 gene 1 protein( domain architecture ID 10157311)

next to BRCA1 gene 1 protein (NBR1) acts probably as a receptor for selective autophagosomal degradation of ubiquitinated targets

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NBR1_like cd14947
Functionally uncharacterized domain in neighbor of Brca1 Gene 1 and related proteins; NBR1 has ...
 369-479 7.27e-45

Functionally uncharacterized domain in neighbor of Brca1 Gene 1 and related proteins; NBR1 has been characterized as a specific late endosomal protein, which might play a role in receptor (RTK) trafficking. Specifically, NBR1 was shown to inhibit ligand-mediated receptor internalization from the cell surface. The region covered by this domain model may be involved in that function, as the C-terminus (which contains a UBA domain) was shown to be essential but not sufficient by itself. In an earlier yeast two-hybrid study, the region in mouse NBR1 covered by this domain has been shown to interact with CIB (calcium and integrin-binding protein) and FEZ1 (fasciculation and elongation protein zeta-1). Thus, NBR1 may play a role in cellular signalling pathways and possibly in neural development.


:

Pssm-ID: 271343 [Multi-domain]  Cd Length: 112  Bit Score: 157.07  E-value: 7.27e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581356 369 PMLSAAFV-DENLPDGTHLQPGTKFIKHWRMKNTGNVKWSADTKLKFMWGNLTLASTeKKDVLVPCLKAGHVGVVSVEFI 447
Cdd:cd14947    1 PGLSAAFVeDVTIPDGTVVPPGTEFTKTWRLRNTGTVPWPAGTLLRFVGGDPGLLSA-PERVPVPSTVPGEEVDVSVELR 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 119581356 448 APALEGTYTSHWRLSHK-GQQFGPRVWCSIIVD 479
Cdd:cd14947   80 APSEPGRYISYWRLVTPdGLPFGDRLWVDITVE 112
PB1_NBR1 cd06396
The PB1 domain is an essential part of NBR1 protein, next to BRCA1, a scaffold protein ...
 5-85 8.02e-44

The PB1 domain is an essential part of NBR1 protein, next to BRCA1, a scaffold protein mediating specific protein-protein interaction with both titin protein kinase and with another scaffold protein p62. 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. The NBR1 protein contains a type I PB1 domain.


:

Pssm-ID: 99718  Cd Length: 81  Bit Score: 153.08  E-value: 8.02e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581356   5 VTLNVTFKNEIQSFLVSDPENTTWADIEAMVKVSFDLNTIQIKYLDEENEEVSINSQGEYEEALKMAVKQGNQLQMQVHE 84
Cdd:cd06396    1 VNLKVTYNGESQSFLVSDSENTTWASVEAMVKVSFGLNDIQIKYVDEENEEVSVNSQGEYEEALKSAVRQGNLLQMNVYE 80


                 .
gi 119581356  85 G 85
Cdd:cd06396   81 H 81
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 215-259 3.85e-17

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: 75.76  E-value: 3.85e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 119581356 215 IACNNCQRRIVGVRYQCSLCPSYNICEDCEAGPyGHdTNHVLLKL 259
Cdd:cd02340    1 VICDGCQGPIVGVRYKCLVCPDYDLCESCEAKG-VH-PEHAMLKI 43
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 279-328 5.21e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 5.21e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 119581356 279 RLPAALEQVRLQKQVDKNFLKAEKQRLRAEKKQRKAEVKELKKQLKLHRK 328
Cdd:COG4942  164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA 213
 
Name Accession Description Interval E-value
NBR1_like cd14947
Functionally uncharacterized domain in neighbor of Brca1 Gene 1 and related proteins; NBR1 has ...
 369-479 7.27e-45

Functionally uncharacterized domain in neighbor of Brca1 Gene 1 and related proteins; NBR1 has been characterized as a specific late endosomal protein, which might play a role in receptor (RTK) trafficking. Specifically, NBR1 was shown to inhibit ligand-mediated receptor internalization from the cell surface. The region covered by this domain model may be involved in that function, as the C-terminus (which contains a UBA domain) was shown to be essential but not sufficient by itself. In an earlier yeast two-hybrid study, the region in mouse NBR1 covered by this domain has been shown to interact with CIB (calcium and integrin-binding protein) and FEZ1 (fasciculation and elongation protein zeta-1). Thus, NBR1 may play a role in cellular signalling pathways and possibly in neural development.


Pssm-ID: 271343 [Multi-domain]  Cd Length: 112  Bit Score: 157.07  E-value: 7.27e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581356 369 PMLSAAFV-DENLPDGTHLQPGTKFIKHWRMKNTGNVKWSADTKLKFMWGNLTLASTeKKDVLVPCLKAGHVGVVSVEFI 447
Cdd:cd14947    1 PGLSAAFVeDVTIPDGTVVPPGTEFTKTWRLRNTGTVPWPAGTLLRFVGGDPGLLSA-PERVPVPSTVPGEEVDVSVELR 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 119581356 448 APALEGTYTSHWRLSHK-GQQFGPRVWCSIIVD 479
Cdd:cd14947   80 APSEPGRYISYWRLVTPdGLPFGDRLWVDITVE 112
PB1_NBR1 cd06396
The PB1 domain is an essential part of NBR1 protein, next to BRCA1, a scaffold protein ...
 5-85 8.02e-44

The PB1 domain is an essential part of NBR1 protein, next to BRCA1, a scaffold protein mediating specific protein-protein interaction with both titin protein kinase and with another scaffold protein p62. 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. The NBR1 protein contains a type I PB1 domain.


Pssm-ID: 99718  Cd Length: 81  Bit Score: 153.08  E-value: 8.02e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581356   5 VTLNVTFKNEIQSFLVSDPENTTWADIEAMVKVSFDLNTIQIKYLDEENEEVSINSQGEYEEALKMAVKQGNQLQMQVHE 84
Cdd:cd06396    1 VNLKVTYNGESQSFLVSDSENTTWASVEAMVKVSFGLNDIQIKYVDEENEEVSVNSQGEYEEALKSAVRQGNLLQMNVYE 80


                 .
gi 119581356  85 G 85
Cdd:cd06396   81 H 81
N_BRCA1_IG pfam16158
Ig-like domain from next to BRCA1 gene; Domain present between positions 365-485 in the human ...
 379-478 1.20e-41

Ig-like domain from next to BRCA1 gene; Domain present between positions 365-485 in the human next to BRCA1 gene 1 protein Q14596 (NBR1_HUMAN) Distant homology and fold prediction analysis suggests this domain has an immunoglobulin like fold and is distantly homologous to domains involved in cell adhesion such as CARDB (PF07705). JCSG construct was crystalized confirming the domain boundaries


Pssm-ID: 465035  Cd Length: 98  Bit Score: 147.34  E-value: 1.20e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581356  379 NLPDGTHLQPGTKFIKHWRMKNTGNVKWSADTKLKFMWGNLTLASTekkDVLVPCLKAGHVGVVSVEFIAPALEGTYTSH 458
Cdd:pfam16158   1 TIPDGTVVPPGTEFTKTWRLRNSGNVAWPAGTSLRFVGGDNMGNVS---TVLVPPVAPGEEVDVSVELKAPSRPGRYISY 77

                          90       100
                  ....*....|....*....|.
gi 119581356  459 WRLSHK-GQQFGPRVWCSIIV 478
Cdd:pfam16158  78 WRLKTPdGTPFGDRLWVDITV 98
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 215-259 3.85e-17

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: 75.76  E-value: 3.85e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 119581356 215 IACNNCQRRIVGVRYQCSLCPSYNICEDCEAGPyGHdTNHVLLKL 259
Cdd:cd02340    1 VICDGCQGPIVGVRYKCLVCPDYDLCESCEAKG-VH-PEHAMLKI 43
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
 4-83 1.21e-15

PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. The domain adopts a beta-grasp fold, similar to that found in ubiquitin and Ras-binding domains. A motif, variously termed OPR, PC and AID, represents the most conserved region of the majority of PB1 domains, and is necessary for PB1 domain function. This function is the formation of PB1 domain heterodimers, although not all PB1 domain pairs associate.


Pssm-ID: 214770  Cd Length: 81  Bit Score: 72.62  E-value: 1.21e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581356     4 QVTLNVTFKNEIQSFLVsdPENTTWADIEAMVKVSFDL--NTIQIKYLDEENEEVSINSQGEYEEALKMAVKQGNQ-LQM 80
Cdd:smart00666   1 TVDVKLRYGGETRRLSV--PRDISFEDLRSKVAKRFGLdnQSFTLKYQDEDGDLVSLTSDEDLEEAIEEYDSLGSKkLRL 78


                   ...
gi 119581356    81 QVH 83
Cdd:smart00666  79 HVF 81
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 211-255 2.37e-14

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: 67.85  E-value: 2.37e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 119581356   211 FSWHIACNNCQRRIVGVRYQCSLCPSYNICEDCEAGPyGHDTNHV 255
Cdd:smart00291   1 VHHSYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKG-SAGGEHS 44
PB1 pfam00564
PB1 domain;
4-85 2.45e-13

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 66.16  E-value: 2.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581356    4 QVTLNVTFKNEIQSFLVSDPeNTTWADIEAMVKVSF--DLNTIQIKYLDEENEEVSINSQGEYEEALKMAVKQG-NQLQM 80
Cdd:pfam00564   1 TVRLKLRYGGGIRRFLSVSR-GISFEELRALVEQRFglDDVDFKLKYPDEDGDLVSLTSDEDLEEALEEARSLGsKSLRL 79


                  ....*
gi 119581356   81 QVHEG 85
Cdd:pfam00564  80 HVFPT 84
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 217-251 3.27e-04

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: 39.00  E-value: 3.27e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 119581356  217 CNNCQ-RRIVGVRYQCSLCPSYNICEDCEAGPYGHD 251
Cdd:pfam00569   7 CNGCSnDPSIGVRYHCLRCSDYDLCQSCFQTHKGGN 42
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 279-328 5.21e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 5.21e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 119581356 279 RLPAALEQVRLQKQVDKNFLKAEKQRLRAEKKQRKAEVKELKKQLKLHRK 328
Cdd:COG4942  164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA 213
 
Name Accession Description Interval E-value
NBR1_like cd14947
Functionally uncharacterized domain in neighbor of Brca1 Gene 1 and related proteins; NBR1 has ...
 369-479 7.27e-45

Functionally uncharacterized domain in neighbor of Brca1 Gene 1 and related proteins; NBR1 has been characterized as a specific late endosomal protein, which might play a role in receptor (RTK) trafficking. Specifically, NBR1 was shown to inhibit ligand-mediated receptor internalization from the cell surface. The region covered by this domain model may be involved in that function, as the C-terminus (which contains a UBA domain) was shown to be essential but not sufficient by itself. In an earlier yeast two-hybrid study, the region in mouse NBR1 covered by this domain has been shown to interact with CIB (calcium and integrin-binding protein) and FEZ1 (fasciculation and elongation protein zeta-1). Thus, NBR1 may play a role in cellular signalling pathways and possibly in neural development.


Pssm-ID: 271343 [Multi-domain]  Cd Length: 112  Bit Score: 157.07  E-value: 7.27e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581356 369 PMLSAAFV-DENLPDGTHLQPGTKFIKHWRMKNTGNVKWSADTKLKFMWGNLTLASTeKKDVLVPCLKAGHVGVVSVEFI 447
Cdd:cd14947    1 PGLSAAFVeDVTIPDGTVVPPGTEFTKTWRLRNTGTVPWPAGTLLRFVGGDPGLLSA-PERVPVPSTVPGEEVDVSVELR 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 119581356 448 APALEGTYTSHWRLSHK-GQQFGPRVWCSIIVD 479
Cdd:cd14947   80 APSEPGRYISYWRLVTPdGLPFGDRLWVDITVE 112
PB1_NBR1 cd06396
The PB1 domain is an essential part of NBR1 protein, next to BRCA1, a scaffold protein ...
 5-85 8.02e-44

The PB1 domain is an essential part of NBR1 protein, next to BRCA1, a scaffold protein mediating specific protein-protein interaction with both titin protein kinase and with another scaffold protein p62. 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. The NBR1 protein contains a type I PB1 domain.


Pssm-ID: 99718  Cd Length: 81  Bit Score: 153.08  E-value: 8.02e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581356   5 VTLNVTFKNEIQSFLVSDPENTTWADIEAMVKVSFDLNTIQIKYLDEENEEVSINSQGEYEEALKMAVKQGNQLQMQVHE 84
Cdd:cd06396    1 VNLKVTYNGESQSFLVSDSENTTWASVEAMVKVSFGLNDIQIKYVDEENEEVSVNSQGEYEEALKSAVRQGNLLQMNVYE 80


                 .
gi 119581356  85 G 85
Cdd:cd06396   81 H 81
N_BRCA1_IG pfam16158
Ig-like domain from next to BRCA1 gene; Domain present between positions 365-485 in the human ...
 379-478 1.20e-41

Ig-like domain from next to BRCA1 gene; Domain present between positions 365-485 in the human next to BRCA1 gene 1 protein Q14596 (NBR1_HUMAN) Distant homology and fold prediction analysis suggests this domain has an immunoglobulin like fold and is distantly homologous to domains involved in cell adhesion such as CARDB (PF07705). JCSG construct was crystalized confirming the domain boundaries


Pssm-ID: 465035  Cd Length: 98  Bit Score: 147.34  E-value: 1.20e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581356  379 NLPDGTHLQPGTKFIKHWRMKNTGNVKWSADTKLKFMWGNLTLASTekkDVLVPCLKAGHVGVVSVEFIAPALEGTYTSH 458
Cdd:pfam16158   1 TIPDGTVVPPGTEFTKTWRLRNSGNVAWPAGTSLRFVGGDNMGNVS---TVLVPPVAPGEEVDVSVELKAPSRPGRYISY 77

                          90       100
                  ....*....|....*....|.
gi 119581356  459 WRLSHK-GQQFGPRVWCSIIV 478
Cdd:pfam16158  78 WRLKTPdGTPFGDRLWVDITV 98
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 215-259 3.85e-17

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: 75.76  E-value: 3.85e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 119581356 215 IACNNCQRRIVGVRYQCSLCPSYNICEDCEAGPyGHdTNHVLLKL 259
Cdd:cd02340    1 VICDGCQGPIVGVRYKCLVCPDYDLCESCEAKG-VH-PEHAMLKI 43
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
 4-83 1.21e-15

PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. The domain adopts a beta-grasp fold, similar to that found in ubiquitin and Ras-binding domains. A motif, variously termed OPR, PC and AID, represents the most conserved region of the majority of PB1 domains, and is necessary for PB1 domain function. This function is the formation of PB1 domain heterodimers, although not all PB1 domain pairs associate.


Pssm-ID: 214770  Cd Length: 81  Bit Score: 72.62  E-value: 1.21e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581356     4 QVTLNVTFKNEIQSFLVsdPENTTWADIEAMVKVSFDL--NTIQIKYLDEENEEVSINSQGEYEEALKMAVKQGNQ-LQM 80
Cdd:smart00666   1 TVDVKLRYGGETRRLSV--PRDISFEDLRSKVAKRFGLdnQSFTLKYQDEDGDLVSLTSDEDLEEAIEEYDSLGSKkLRL 78


                   ...
gi 119581356    81 QVH 83
Cdd:smart00666  79 HVF 81
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 211-255 2.37e-14

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: 67.85  E-value: 2.37e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 119581356   211 FSWHIACNNCQRRIVGVRYQCSLCPSYNICEDCEAGPyGHDTNHV 255
Cdd:smart00291   1 VHHSYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKG-SAGGEHS 44
PB1 pfam00564
PB1 domain;
4-85 2.45e-13

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 66.16  E-value: 2.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581356    4 QVTLNVTFKNEIQSFLVSDPeNTTWADIEAMVKVSF--DLNTIQIKYLDEENEEVSINSQGEYEEALKMAVKQG-NQLQM 80
Cdd:pfam00564   1 TVRLKLRYGGGIRRFLSVSR-GISFEELRALVEQRFglDDVDFKLKYPDEDGDLVSLTSDEDLEEALEEARSLGsKSLRL 79


                  ....*
gi 119581356   81 QVHEG 85
Cdd:pfam00564  80 HVFPT 84
PB1 cd05992
The PB1 domain is a modular domain mediating specific protein-protein interactions which play ...
 5-83 5.37e-12

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.


Pssm-ID: 99716 [Multi-domain]  Cd Length: 81  Bit Score: 62.30  E-value: 5.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581356   5 VTLNVTFKNEIQSFLVSDPeNTTWADIEAMVKVSFDLN--TIQIKYLDEENEEVSINSQGEYEEALKMAVKQGN-QLQMQ 81
Cdd:cd05992    1 VRVKVKYGGEIRRFVVVSR-SISFEDLRSKIAEKFGLDavSFKLKYPDEDGDLVTISSDEDLEEAIEEARRSGSkKLRLF 79


                 ..
gi 119581356  82 VH 83
Cdd:cd05992   80 VF 81
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 215-254 3.21e-07

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: 47.81  E-value: 3.21e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 119581356 215 IACNNCQRRIVGVRYQCSLCPSYNICEDC-EAGPYGHDTNH 254
Cdd:cd02249    1 YSCDGCLKPIVGVRYHCLVCEDFDLCSSCyAKGKKGHPPDH 41
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
 215-258 1.28e-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: 45.89  E-value: 1.28e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 119581356 215 IACNNCQRR-IVGVRYQCSLCPS--YNICEDCEAGPYGHDTNHVLLK 258
Cdd:cd02341    1 FKCDSCGIEpIPGTRYHCSECDDgdFDLCQDCVVKGESHQEDHWLVK 47
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 215-254 3.64e-05

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: 41.68  E-value: 3.64e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 119581356 215 IACNNCQRR-IVGVRYQCSLCPSYNICEDCeagpYGHDTNH 254
Cdd:cd02339    1 IICDTCRKQgIIGIRWKCAECPNYDLCTTC----YHGDKHD 37
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 215-254 1.28e-04

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: 40.41  E-value: 1.28e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 119581356 215 IACNNCQRR-IVGVRYQCSLCPSYNICEDC-EAGPYG--HDTNH 254
Cdd:cd02338    1 VSCDGCGKSnFTGRRYKCLICYDYDLCADCyDSGVTTerHLFDH 44
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 217-251 3.27e-04

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: 39.00  E-value: 3.27e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 119581356  217 CNNCQ-RRIVGVRYQCSLCPSYNICEDCEAGPYGHD 251
Cdd:pfam00569   7 CNGCSnDPSIGVRYHCLRCSDYDLCQSCFQTHKGGN 42
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 217-254 1.11e-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: 37.66  E-value: 1.11e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 119581356 217 CNNCQRRIVG-VRYQCSLCPSYNICEDC-----EAGPygHDTNH 254
Cdd:cd02335    3 CDYCSKDITGtIRIKCAECPDFDLCLECfsagaEIGK--HRNDH 44
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 217-243 2.41e-03

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: 36.95  E-value: 2.41e-03
                         10        20
                 ....*....|....*....|....*...
gi 119581356 217 CNNCQRR-IVGVRYQCSLCPSYNICEDC 243
Cdd:cd02334    3 CNICKEFpITGFRYRCLKCFNYDLCQSC 30
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 215-243 4.57e-03

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: 36.02  E-value: 4.57e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 119581356 215 IACNNCQR-RIVGVRYQCSLCPSYNICEDC 243
Cdd:cd02344    1 VTCDGCQMfPINGPRFKCRNCDDFDFCENC 30
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 279-328 5.21e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 5.21e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 119581356 279 RLPAALEQVRLQKQVDKNFLKAEKQRLRAEKKQRKAEVKELKKQLKLHRK 328
Cdd:COG4942  164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA 213
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
 217-243 5.35e-03

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: 35.62  E-value: 5.35e-03
                         10        20
                 ....*....|....*....|....*..
gi 119581356 217 CNNCqRRIVGVRYQCSLCPSYNICEDC 243
Cdd:cd02337    3 CNEC-KHHVETRWHCTVCEDYDLCITC 28
 
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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