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Conserved domains on  [gi|312147278|ref|NP_001185872|]
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dystrobrevin alpha isoform 15 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 1-39 6.60e-23

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: 90.88  E-value: 6.60e-23
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 312147278   1 MMGFRYRCQQCHNYQLCQDCFWRGHAGGSHSNQHQMKEY 39
Cdd:cd02334   11 ITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
118-239 2.79e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


The actual alignment was detected with superfamily member COG4717:

Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 2.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147278 118 NRLDEEHRLIARYAARLAAESSSSQPPQQrsapdisftIDANKQQRQLIAELENKNREILQEIQRLRLEHEQA-SQPTPE 196
Cdd:COG4717  119 EKLEKLLQLLPLYQELEALEAELAELPER---------LEELEERLEELRELEEELEELEAELAELQEELEELlEQLSLA 189

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 312147278 197 KAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 239
Cdd:COG4717  190 TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
 
Name Accession Description Interval E-value
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 1-39 6.60e-23

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: 90.88  E-value: 6.60e-23
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 312147278   1 MMGFRYRCQQCHNYQLCQDCFWRGHAGGSHSNQHQMKEY 39
Cdd:cd02334   11 ITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 1-31 1.39e-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: 61.69  E-value: 1.39e-12
                           10        20        30
                   ....*....|....*....|....*....|.
gi 312147278     1 MMGFRYRCQQCHNYQLCQDCFWRGHAGGSHS 31
Cdd:smart00291  14 IVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 3-36 1.70e-05

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: 41.70  E-value: 1.70e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 312147278    3 GFRYRCQQCHNYQLCQDCFWRGHAGGshsnqHQM 36
Cdd:pfam00569  17 GVRYHCLRCSDYDLCQSCFQTHKGGN-----HQM 45
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
118-239 2.79e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 2.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147278 118 NRLDEEHRLIARYAARLAAESSSSQPPQQrsapdisftIDANKQQRQLIAELENKNREILQEIQRLRLEHEQA-SQPTPE 196
Cdd:COG4717  119 EKLEKLLQLLPLYQELEALEAELAELPER---------LEELEERLEELRELEEELEELEAELAELQEELEELlEQLSLA 189

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 312147278 197 KAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 239
Cdd:COG4717  190 TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 166-236 6.68e-05

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 45.06  E-value: 6.68e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312147278 166 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN---PTLLAELRLLRQRKDELEQRMSALQESRRELMVQL 236
Cdd:PRK05431  30 LLELDEERRELQTELEELQAERNALSKEIGQAKRKGedaEALIAEVKELKEEIKALEAELDELEAELEELLLRI 103
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 115-248 4.97e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 4.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147278   115 ESSNRLDEEHRLIARYAARLAAESSSSQPPQQRSAPDIsftidANKQQRqlIAELENKNREILQEIQRLRLEHEQASQPT 194
Cdd:TIGR02169  798 AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI-----QELQEQ--RIDLKEQIKSIEKEIENLNGKKEELEEEL 870

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 312147278   195 PEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKTQGA 248
Cdd:TIGR02169  871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA 924
 
Name Accession Description Interval E-value
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 1-39 6.60e-23

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: 90.88  E-value: 6.60e-23
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 312147278   1 MMGFRYRCQQCHNYQLCQDCFWRGHAGGSHSNQHQMKEY 39
Cdd:cd02334   11 ITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 1-31 1.39e-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: 61.69  E-value: 1.39e-12
                           10        20        30
                   ....*....|....*....|....*....|.
gi 312147278     1 MMGFRYRCQQCHNYQLCQDCFWRGHAGGSHS 31
Cdd:smart00291  14 IVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 3-37 9.64e-08

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: 48.11  E-value: 9.64e-08
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 312147278   3 GFRYRCQQCHNYQLCQDCFWRGHAGGSHSNQHQMK 37
Cdd:cd02338   13 GRRYKCLICYDYDLCADCYDSGVTTERHLFDHPMQ 47
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 2-39 2.37e-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: 47.04  E-value: 2.37e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 312147278   2 MGFRYRCQQCHNYQLCQDCFWRGHagGSHSNQHQMKEY 39
Cdd:cd02249   11 VGVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 3-38 1.40e-06

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: 44.89  E-value: 1.40e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 312147278   3 GFRYRCQQCHNYQLCQDCFWRGHAGGSHSNQHQMKE 38
Cdd:cd02345   13 GIRFPCQVCRDYSLCLGCYTKGRETKRHNSLHIMYE 48
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 3-36 2.87e-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: 43.79  E-value: 2.87e-06
                         10        20        30
                 ....*....|....*....|....*....|....
gi 312147278   3 GFRYRCQQCHNYQLCQDCfwrgHAGGSHSNqHQM 36
Cdd:cd02340   12 GVRYKCLVCPDYDLCESC----EAKGVHPE-HAM 40
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 3-36 1.70e-05

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: 41.70  E-value: 1.70e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 312147278    3 GFRYRCQQCHNYQLCQDCFWRGHAGGshsnqHQM 36
Cdd:pfam00569  17 GVRYHCLRCSDYDLCQSCFQTHKGGN-----HQM 45
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
118-239 2.79e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 2.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147278 118 NRLDEEHRLIARYAARLAAESSSSQPPQQrsapdisftIDANKQQRQLIAELENKNREILQEIQRLRLEHEQA-SQPTPE 196
Cdd:COG4717  119 EKLEKLLQLLPLYQELEALEAELAELPER---------LEELEERLEELRELEEELEELEAELAELQEELEELlEQLSLA 189

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 312147278 197 KAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 239
Cdd:COG4717  190 TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 5-34 3.05e-05

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: 41.12  E-value: 3.05e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 312147278   5 RYRCQQCHNYQLCQDCFWRGHAGGSHSNQH 34
Cdd:cd02335   15 RIKCAECPDFDLCLECFSAGAEIGKHRNDH 44
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 166-236 6.68e-05

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 45.06  E-value: 6.68e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312147278 166 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN---PTLLAELRLLRQRKDELEQRMSALQESRRELMVQL 236
Cdd:PRK05431  30 LLELDEERRELQTELEELQAERNALSKEIGQAKRKGedaEALIAEVKELKEEIKALEAELDELEAELEELLLRI 103
ZZ_EF cd02343
Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif ...
 5-36 2.00e-04

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: 38.84  E-value: 2.00e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 312147278   5 RYRCQQCHNYQLCQDCFWRGHAGGSHSNQHQM 36
Cdd:cd02343   14 RYRCLQCTDMDLCKTCFLGGVKPEGHEDDHEM 45
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 115-248 4.97e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 4.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147278   115 ESSNRLDEEHRLIARYAARLAAESSSSQPPQQRSAPDIsftidANKQQRqlIAELENKNREILQEIQRLRLEHEQASQPT 194
Cdd:TIGR02169  798 AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI-----QELQEQ--RIDLKEQIKSIEKEIENLNGKKEELEEEL 870

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 312147278   195 PEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKTQGA 248
Cdd:TIGR02169  871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA 924
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 1-34 5.39e-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: 5.39e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 312147278   1 MMGFRYRCQQCHNYQLCQDCFwrghaggsHSNQH 34
Cdd:cd02339   11 IIGIRWKCAECPNYDLCTTCY--------HGDKH 36
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
 3-36 1.07e-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: 36.64  E-value: 1.07e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 312147278   3 GFRYRCQQCHN--YQLCQDCFwrgHAGGSHSNQHQM 36
Cdd:cd02341   13 GTRYHCSECDDgdFDLCQDCV---VKGESHQEDHWL 45
PRK12704 PRK12704
phosphodiesterase; Provisional
 157-245 1.44e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147278 157 DANKQQRQLI----AELENKNREIL----QEIQRLRLEHEQasqptpEKAQQNPTLLAELRLLRQRKDELEQRMSALQES 228
Cdd:PRK12704  35 EAEEEAKRILeeakKEAEAIKKEALleakEEIHKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLELLEKR 108

                         90
                 ....*....|....*..
gi 312147278 229 RRELMVQLEGLMKLLKT 245
Cdd:PRK12704 109 EEELEKKEKELEQKQQE 125
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
 159-230 1.61e-03

SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.


Pssm-ID: 275056 [Multi-domain]  Cd Length: 198  Bit Score: 39.61  E-value: 1.61e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312147278  159 NKQQRQLIAELENKNREILQEIQRLRLEHE---QASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRR 230
Cdd:TIGR04211  89 LAELRQENQELKQQLSTLEAELEELQKELErikQISANAIELDEENRELREELAELKQENEALEAENERLQENEQ 163
Bbox1 cd19757
B-box-type 1 zinc finger (Bbox1); The B-box-type zinc finger is a short zinc binding domain of ...
 6-38 1.88e-03

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: 35.93  E-value: 1.88e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 312147278   6 YRCQQCHNYqLCQDCFWRGHAGGSHSNQHQMKE 38
Cdd:cd19757   12 VYCLECEEF-LCDDCSDAIHRRGKLTRSHKLVP 43
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 160-239 1.95e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147278 160 KQQRQLIAELENKNREILQEIQRLRLEHEQASqptpEKAQQnptLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 239
Cdd:COG1196  249 EELEAELEELEAELAELEAELEELRLELEELE----LELEE---AQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 160-239 5.11e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 5.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147278 160 KQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 239
Cdd:COG1196  256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 162-246 5.31e-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: 38.98  E-value: 5.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147278 162 QRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMK 241
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97


                 ....*
gi 312147278 242 LLKTQ 246
Cdd:COG4942   98 ELEAQ 102
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
156-241 8.98e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.21  E-value: 8.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147278 156 IDANKQQRQLIAELENKNREILQEIQRL-RLEHEQAsqptpEKAQQNPTLLAELRLLRQRKD--ELEQRMSALQESRREL 232
Cdd:COG4717   70 LKELKELEEELKEAEEKEEEYAELQEELeELEEELE-----ELEAELEELREELEKLEKLLQllPLYQELEALEAELAEL 144


                 ....*....
gi 312147278 233 MVQLEGLMK 241
Cdd:COG4717  145 PERLEELEE 153
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
160-247 8.98e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.36  E-value: 8.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147278  160 KQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLL-AELRLLRQRKDELEQRMSALQESRRELMVQLEG 238
Cdd:COG4913   248 REQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLeAELEELRAELARLEAELERLEARLDALREELDE 327


                  ....*....
gi 312147278  239 LMKLLKTQG 247
Cdd:COG4913   328 LEAQIRGNG 336
 
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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