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Conserved domains on  [gi|1907085898|ref|XP_036013074|]
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dystrobrevin beta isoform X18 [Mus musculus]

Protein Classification

ZZ-type zinc finger protein( domain architecture ID 2041)

ZZ-type zinc finger protein may function as a molecular serve as scaffold in various cell signaling pathways

Gene Ontology:  GO:0008270
PubMed:  30691308|8848831

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZZ super family cl00295
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 1-39 4.76e-22

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.


The actual alignment was detected with superfamily member cd02334:

Pssm-ID: 412288  Cd Length: 49  Bit Score: 88.18  E-value: 4.76e-22
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907085898   1 MMGFRYRCQQCHNYQLCQNCFWRGHASGAHSNQHQMKEH 39
Cdd:cd02334    11 ITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
184-271 7.05e-06

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: 48.23  E-value: 7.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085898 184 KQQRQLIAELENKNREILQEIQRLRLEHEQA-SQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEG 262
Cdd:COG4717   152 EERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231


                  ....*....
gi 1907085898 263 LMKLLKAQA 271
Cdd:COG4717   232 LENELEAAA 240
 
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 4.76e-22

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: 88.18  E-value: 4.76e-22
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907085898   1 MMGFRYRCQQCHNYQLCQNCFWRGHASGAHSNQHQMKEH 39
Cdd:cd02334    11 ITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 1-31 6.85e-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: 59.76  E-value: 6.85e-12
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1907085898    1 MMGFRYRCQQCHNYQLCQNCFWRGHASGAHS 31
Cdd:smart00291  14 IVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
184-271 7.05e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 7.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085898 184 KQQRQLIAELENKNREILQEIQRLRLEHEQA-SQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEG 262
Cdd:COG4717   152 EERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231


                  ....*....
gi 1907085898 263 LMKLLKAQA 271
Cdd:COG4717   232 LENELEAAA 240
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 3-21 1.43e-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: 1.43e-05
                          10
                  ....*....|....*....
gi 1907085898   3 GFRYRCQQCHNYQLCQNCF 21
Cdd:pfam00569  17 GVRYHCLRCSDYDLCQSCF 35
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 190-260 6.85e-05

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 44.67  E-value: 6.85e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907085898 190 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN---PMLLAELRLLRQRKDELEQRMSALQESRRELMVQL 260
Cdd:PRK05431   30 LLELDEERRELQTELEELQAERNALSKEIGQAKRKGedaEALIAEVKELKEEIKALEAELDELEAELEELLLRI 103
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 146-271 7.57e-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: 41.59  E-value: 7.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085898  146 SRLDEEHRliaRYAARLAAEAGNMTRPPTDASFNFDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN 225
Cdd:TIGR02169  801 SKLEEEVS---RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL 877

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1907085898  226 PMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL---MKLLKAQA 271
Cdd:TIGR02169  878 RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKrkrLSELKAKL 926
Seryl_tRNA_N pfam02403
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ...
 190-264 2.54e-03

Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA synthetase class II domain (pfam00587) and represents the N-terminal domain of seryl-tRNA synthetase.


Pssm-ID: 426757 [Multi-domain]  Cd Length: 108  Bit Score: 37.18  E-value: 2.54e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907085898 190 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPmllaELRLLRQRKDELEQRMSALQESRRELMVQLEGLM 264
Cdd:pfam02403  31 LLELDEKRRELQVELEELQAERNELSKEIGQAKKKKE----DADALIAEVKELKDELKALEAELKELEAELDKLL 101
Prefoldin_alpha_GimC cd23160
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ...
 228-263 2.76e-03

Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


Pssm-ID: 467476 [Multi-domain]  Cd Length: 127  Bit Score: 37.47  E-value: 2.76e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1907085898 228 LLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 263
Cdd:cd23160     5 LLAELQQLEQQAEALQQQIELLQASINELNRAKETL 40
 
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 4.76e-22

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: 88.18  E-value: 4.76e-22
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907085898   1 MMGFRYRCQQCHNYQLCQNCFWRGHASGAHSNQHQMKEH 39
Cdd:cd02334    11 ITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 1-31 6.85e-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: 59.76  E-value: 6.85e-12
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1907085898    1 MMGFRYRCQQCHNYQLCQNCFWRGHASGAHS 31
Cdd:smart00291  14 IVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 2-39 3.42e-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: 46.27  E-value: 3.42e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1907085898   2 MGFRYRCQQCHNYQLCQNCFWRGHasGAHSNQHQMKEH 39
Cdd:cd02249    11 VGVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 3-37 5.22e-07

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: 46.19  E-value: 5.22e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1907085898   3 GFRYRCQQCHNYQLCQNCFWRGHASGAHSNQHQMK 37
Cdd:cd02338    13 GRRYKCLICYDYDLCADCYDSGVTTERHLFDHPMQ 47
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 3-36 3.55e-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: 43.40  E-value: 3.55e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1907085898   3 GFRYRCQQCHNYQLCQNCfwrgHASGAHSNqHQM 36
Cdd:cd02340    12 GVRYKCLVCPDYDLCESC----EAKGVHPE-HAM 40
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 3-38 4.94e-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: 43.35  E-value: 4.94e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1907085898   3 GFRYRCQQCHNYQLCQNCFWRGHASGAHSNQHQMKE 38
Cdd:cd02345    13 GIRFPCQVCRDYSLCLGCYTKGRETKRHNSLHIMYE 48
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
184-271 7.05e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 7.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085898 184 KQQRQLIAELENKNREILQEIQRLRLEHEQA-SQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEG 262
Cdd:COG4717   152 EERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231


                  ....*....
gi 1907085898 263 LMKLLKAQA 271
Cdd:COG4717   232 LENELEAAA 240
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 5-34 1.23e-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: 42.28  E-value: 1.23e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1907085898   5 RYRCQQCHNYQLCQNCFWRGHASGAHSNQH 34
Cdd:cd02335    15 RIKCAECPDFDLCLECFSAGAEIGKHRNDH 44
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 3-21 1.43e-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: 1.43e-05
                          10
                  ....*....|....*....
gi 1907085898   3 GFRYRCQQCHNYQLCQNCF 21
Cdd:pfam00569  17 GVRYHCLRCSDYDLCQSCF 35
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 190-260 6.85e-05

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 44.67  E-value: 6.85e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907085898 190 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN---PMLLAELRLLRQRKDELEQRMSALQESRRELMVQL 260
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 9.97e-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: 39.61  E-value: 9.97e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1907085898   5 RYRCQQCHNYQLCQNCFWRGHASGAHSNQHQM 36
Cdd:cd02343    14 RYRCLQCTDMDLCKTCFLGGVKPEGHEDDHEM 45
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 1-39 1.93e-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: 38.59  E-value: 1.93e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907085898   1 MMGFRYRCQQCHNYQLCQNCFwrghasgaHSNQHQMkEH 39
Cdd:cd02339    11 IIGIRWKCAECPNYDLCTTCY--------HGDKHDL-EH 40
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
181-268 3.10e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 3.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085898 181 DANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNpmllAELRLLRQRKDELEQRMSALQESRRELMVQL 260
Cdd:COG4372    56 QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ----EELESLQEEAEELQEELEELQKERQDLEQQR 131


                  ....*...
gi 1907085898 261 EGLMKLLK 268
Cdd:COG4372   132 KQLEAQIA 139
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 184-263 3.45e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 3.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085898 184 KQQRQLIAELENKNREILQEIQRLRLEHEQASqptpEKAQQnpmLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 263
Cdd:COG1196   249 EELEAELEELEAELAELEAELEELRLELEELE----LELEE---AQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 146-271 7.57e-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: 41.59  E-value: 7.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085898  146 SRLDEEHRliaRYAARLAAEAGNMTRPPTDASFNFDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN 225
Cdd:TIGR02169  801 SKLEEEVS---RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL 877

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1907085898  226 PMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL---MKLLKAQA 271
Cdd:TIGR02169  878 RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKrkrLSELKAKL 926
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
160-265 9.91e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 9.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085898 160 ARLAAEAGNMTRP----PTDasfNFDANKQQRQLIAELENKNREILQEIQRL-RLEHEQAsqptpEKAQQNPMLLAELRL 234
Cdd:COG4717    49 ERLEKEADELFKPqgrkPEL---NLKELKELEEELKEAEEKEEEYAELQEELeELEEELE-----ELEAELEELREELEK 120

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907085898 235 LRQRKD--ELEQRMSALQESRRELMVQLEGLMK 265
Cdd:COG4717   121 LEKLLQllPLYQELEALEAELAELPERLEELEE 153
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
 183-254 1.17e-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: 1.17e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907085898 183 NKQQRQLIAELENKNREILQEIQRLRLEHE---QASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRR 254
Cdd:TIGR04211  89 LAELRQENQELKQQLSTLEAELEELQKELErikQISANAIELDEENRELREELAELKQENEALEAENERLQENEQ 163
PRK12704 PRK12704
phosphodiesterase; Provisional
 181-268 1.22e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085898 181 DANKQQRQLI----AELENKNREIL----QEIQRLRLEHEQasqptpEKAQQNPMLLAELRLLRQRKDELEQRMSALQES 252
Cdd:PRK12704   35 EAEEEAKRILeeakKEAEAIKKEALleakEEIHKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLELLEKR 108

                          90
                  ....*....|....*.
gi 1907085898 253 RRELMVQLEGLMKLLK 268
Cdd:PRK12704  109 EEELEKKEKELEQKQQ 124
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
187-270 1.51e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.89  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085898 187 RQLIAELENKNREILQEIQRLRLEHEQASQPTPEkaqqnpmLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKL 266
Cdd:COG1340    21 REEIEELKEKRDELNEELKELAEKRDELNAQVKE-------LREEAQELREKRDELNEKVKELKEERDELNEKLNELREE 93


                  ....
gi 1907085898 267 LKAQ 270
Cdd:COG1340    94 LDEL 97
PRK12704 PRK12704
phosphodiesterase; Provisional
 180-271 2.06e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085898 180 FDANKQQRQLIAELENKNREILQEIQRL---------RLEHEQASQptpEKAQQNpmLLAELRLLRQRKDELEQRMSALQ 250
Cdd:PRK12704   60 LEAKEEIHKLRNEFEKELRERRNELQKLekrllqkeeNLDRKLELL---EKREEE--LEKKEKELEQKQQELEKKEEELE 134

                          90       100
                  ....*....|....*....|.
gi 1907085898 251 ESRRELMVQLEGLMKLLKAQA 271
Cdd:PRK12704  135 ELIEEQLQELERISGLTAEEA 155
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
184-265 2.14e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085898 184 KQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 263
Cdd:COG4372    97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176


                  ..
gi 1907085898 264 MK 265
Cdd:COG4372   177 SE 178
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 186-270 2.41e-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: 39.75  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085898 186 QRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMK 265
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97


                  ....*
gi 1907085898 266 LLKAQ 270
Cdd:COG4942    98 ELEAQ 102
Seryl_tRNA_N pfam02403
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ...
 190-264 2.54e-03

Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA synthetase class II domain (pfam00587) and represents the N-terminal domain of seryl-tRNA synthetase.


Pssm-ID: 426757 [Multi-domain]  Cd Length: 108  Bit Score: 37.18  E-value: 2.54e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907085898 190 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPmllaELRLLRQRKDELEQRMSALQESRRELMVQLEGLM 264
Cdd:pfam02403  31 LLELDEKRRELQVELEELQAERNELSKEIGQAKKKKE----DADALIAEVKELKDELKALEAELKELEAELDKLL 101
Prefoldin_alpha_GimC cd23160
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ...
 228-263 2.76e-03

Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


Pssm-ID: 467476 [Multi-domain]  Cd Length: 127  Bit Score: 37.47  E-value: 2.76e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1907085898 228 LLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 263
Cdd:cd23160     5 LLAELQQLEQQAEALQQQIELLQASINELNRAKETL 40
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 184-270 3.34e-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: 39.36  E-value: 3.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085898 184 KQQRQLIAELENKNREILQEIQRLRLEHEQASQptpekaqqnpmllaELRLLRQRKDELEQRMSALQESRRELMVQLEGL 263
Cdd:COG4942    37 AELEKELAALKKEEKALLKQLAALERRIAALAR--------------RIRALEQELAALEAELAELEKEIAELRAELEAQ 102


                  ....*..
gi 1907085898 264 MKLLKAQ 270
Cdd:COG4942   103 KEELAEL 109
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
 158-252 3.69e-03

Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.


Pssm-ID: 461111 [Multi-domain]  Cd Length: 272  Bit Score: 38.82  E-value: 3.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085898 158 YAARLAAEAGNMTRppTDASFNFDANKQQRQLIAELENKNREILQEIQRL--RLEHEQASQPTPEKAQQNPMLLAELRLL 235
Cdd:pfam03961 131 KAKELGSPAGTKTE--IEVGVDFPELKEKLEELEKELEELEEELEKLKKRlkKLPKKARGQLPPEKREQLEKLLETKNKL 208

                          90
                  ....*....|....*..
gi 1907085898 236 RQRKDELEQRMSALQES 252
Cdd:pfam03961 209 SEELEELEEELKELKEE 225
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 3-34 4.13e-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: 34.87  E-value: 4.13e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1907085898   3 GFRYRCQQCHNYQLCQNCFWrghaSGAHSNQH 34
Cdd:cd02344    13 GPRFKCRNCDDFDFCENCFK----TRKHNTRH 40
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
 188-256 4.46e-03

JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.


Pssm-ID: 462875 [Multi-domain]  Cd Length: 150  Bit Score: 37.21  E-value: 4.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085898 188 QLIAELEN------KNREILQEIQRLRLEHEQ-ASQPTPEKAQQnpmLLAELRLL------RQRKDELEQRMSALQESRR 254
Cdd:pfam09744  30 KVVNVLELleslasRNQEHNVELEELREDNEQlETQYEREKALR---KRAEEELEeiedqwEQETKDLLSQVESLEEENR 106


                  ..
gi 1907085898 255 EL 256
Cdd:pfam09744 107 RL 108
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 124-269 4.62e-03

chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.27  E-value: 4.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085898  124 EHALIASYVARLQhctrvlDSPSRLDEEHRLIARYAARLAAEAGNMTRPPTDASFNFDANKQQRQLIAELENKNREILQE 203
Cdd:TIGR02168  223 RELELALLVLRLE------ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907085898  204 IQRLRLEHEQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKA 269
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE 362
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 121-263 5.12e-03

chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.27  E-value: 5.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085898  121 LADEHALIASYVARLQHCTRVLDSPSR-LDEEHRLIARYAARLAAEAGNMtrpptdASFNFDANKQQRQLiAELENKNRE 199
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERrLEDLEEQIEELSEDIESLAAEI------EELEELIEELESEL-EALLNERAS 884

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907085898  200 ILQEIQRLRLEHEQASqptpekaqqnpmllAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 263
Cdd:TIGR02168  885 LEEALALLRSELEELS--------------EELRELESKRSELRRELEELREKLAQLELRLEGL 934
DASH_Spc19 pfam08287
Spc19; Spc19 is a component of the DASH complex. The DASH complex associates with the spindle ...
 183-249 5.76e-03

Spc19; Spc19 is a component of the DASH complex. The DASH complex associates with the spindle pole body and is important for spindle and kinetochore integrity during cell division.


Pssm-ID: 429900 [Multi-domain]  Cd Length: 148  Bit Score: 36.84  E-value: 5.76e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907085898 183 NKQQRQLiAELENKNreilqEIQRLRLEH------------EQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSAL 249
Cdd:pfam08287  76 EKLERRE-ETLKAKL-----ELNEGRLSNaessardeegsqESDEEVNSSEGDATNEELERLRALRQKKERLKYSLERL 148
mukB PRK04863
chromosome partition protein MukB;
184-261 6.09e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 38.78  E-value: 6.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085898  184 KQQRQLIAELENKNREILQEIQRLrleHEQASQ-----------PTPEkaqqnpmllAELRLLRQRKDELEQRMSALQES 252
Cdd:PRK04863   792 RAEREELAERYATLSFDVQKLQRL---HQAFSRfigshlavafeADPE---------AELRQLNRRRVELERALADHESQ 859


                   ....*....
gi 1907085898  253 RRELMVQLE 261
Cdd:PRK04863   860 EQQQRSQLE 868
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 181-271 6.12e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 6.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085898 181 DANKQQRQLIAELEnknrEILQEIQRLRLEHEQASQptpEKAQqnpmLLAELRLLRQRKDELEQRMSALQESRRELMVQL 260
Cdd:COG1196   285 EAQAEEYELLAELA----RLEQDIARLEERRRELEE---RLEE----LEEELAELEEELEELEEELEELEEELEEAEEEL 353

                          90
                  ....*....|.
gi 1907085898 261 EGLMKLLKAQA 271
Cdd:COG1196   354 EEAEAELAEAE 364
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 108-271 6.59e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 38.78  E-value: 6.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085898  108 TKRLQYSQ------------DMPNLLADEHA-LIASYVARLQHCTRvldspSRLDEEHRL-IARYAARLAAEAGNMTR-- 171
Cdd:COG3096    410 TRAIQYQQavqalekaralcGLPDLTPENAEdYLAAFRAKEQQATE-----EVLELEQKLsVADAARRQFEKAYELVCki 484

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085898  172 -PPTDASFNFDANKQQ-----------------RQLIAELENKNREiLQEIQRLRLEHEQASQPTPEKAQQNPMLLAELR 233
Cdd:COG3096    485 aGEVERSQAWQTARELlrryrsqqalaqrlqqlRAQLAELEQRLRQ-QQNAERLLEEFCQRIGQQLDAAEELEELLAELE 563

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1907085898  234 llrQRKDELEQRMSALQESRREL---MVQLEGLMKLLKAQA 271
Cdd:COG3096    564 ---AQLEELEEQAAEAVEQRSELrqqLEQLRARIKELAARA 601
Bbox1 cd19757
B-box-type 1 zinc finger (Bbox1); The B-box-type zinc finger is a short zinc binding domain of ...
 6-38 7.17e-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: 34.39  E-value: 7.17e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1907085898   6 YRCQQCHNYqLCQNCFWRGHASGAHSNQHQMKE 38
Cdd:cd19757    12 VYCLECEEF-LCDDCSDAIHRRGKLTRSHKLVP 43
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
126-265 7.85e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.21  E-value: 7.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085898 126 ALIASYVARLQHCTRVLDSPSRLDEEHRLIARYAAR--LAAEAGnmTRPPTDASFNFDANKQQRQLIAELENKNREILQE 203
Cdd:COG4717   337 EELLELLDRIEELQELLREAEELEEELQLEELEQEIaaLLAEAG--VEDEEELRAALEQAEEYQELKEELEELEEQLEEL 414

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907085898 204 iqrLRLEHEQASQPTPEKaqqnpmLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMK 265
Cdd:COG4717   415 ---LGELEELLEALDEEE------LEEELEELEEELEELEEELEELREELAELEAELEQLEE 467
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 186-256 8.43e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.38  E-value: 8.43e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907085898 186 QRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRREL 256
Cdd:COG1196   307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
STAT5_CCD cd16855
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ...
 185-270 8.98e-03

Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the coiled-coil (alpha) domain of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 5) which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The coiled-coil domain (CCD) of STAT5A and STAT5B appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency.


Pssm-ID: 341080 [Multi-domain]  Cd Length: 194  Bit Score: 36.86  E-value: 8.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085898 185 QQRQLIAELENKNREI----------LQEIQRLRLEHEQASQptpekaQQNPMLLAELRLLRQRKDELEQRMSA----LQ 250
Cdd:cd16855    12 ELRQRTQETENDLRNLqqkqesfviqYQESQKIQAQLQQLQQ------QPQNERIELEQQLQQQKEQLEQLLNAkaqeLL 85

                          90       100
                  ....*....|....*....|
gi 1907085898 251 ESRRELMVQLEGLMKLLKAQ 270
Cdd:cd16855    86 QLRMELADKFKKTIQLLSKL 105
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
 5-39 9.04e-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: 33.69  E-value: 9.04e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1907085898   5 RYRCQQCHNYQLCQNCFWR-GHasgahsnQHQMKEH 39
Cdd:cd02337    13 RWHCTVCEDYDLCITCYNTkNH-------PHKMEKL 41
 
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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