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Conserved domains on  [gi|1907085901|ref|XP_036013075|]
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dystrobrevin beta isoform X19 [Mus musculus]

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 1.98e-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: 88.95  E-value: 1.98e-22
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907085901   1 MMGFRYRCQQCHNYQLCQNCFWRGHASGAHSNQHQMKEH 39
Cdd:cd02334    11 ITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
154-248 1.02e-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: 50.54  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 154 KQQRQLIAELENKNREILQEIQRLRLEHEQA-SQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEG 232
Cdd:COG4717   152 EERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231

                          90
                  ....*....|....*..
gi 1907085901 233 L-MKLLKEEEQKQAAQA 248
Cdd:COG4717   232 LeNELEAAALEERLKEA 248
 
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 1.98e-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: 88.95  E-value: 1.98e-22
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907085901   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 6.33e-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: 6.33e-12
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1907085901    1 MMGFRYRCQQCHNYQLCQNCFWRGHASGAHS 31
Cdd:smart00291  14 IVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
154-248 1.02e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.54  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 154 KQQRQLIAELENKNREILQEIQRLRLEHEQA-SQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEG 232
Cdd:COG4717   152 EERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231

                          90
                  ....*....|....*..
gi 1907085901 233 L-MKLLKEEEQKQAAQA 248
Cdd:COG4717   232 LeNELEAAALEERLKEA 248
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 3-21 9.15e-06

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: 42.47  E-value: 9.15e-06
                          10
                  ....*....|....*....
gi 1907085901   3 GFRYRCQQCHNYQLCQNCF 21
Cdd:pfam00569  17 GVRYHCLRCSDYDLCQSCF 35
PRK12704 PRK12704
phosphodiesterase; Provisional
 151-245 1.46e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.69  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 151 DANKQQRQLI----AELENKNREIL----QEIQRLRLEHEQasqptpEKAQQNPMLLAELRLLRQRKDELEQRMSALQES 222
Cdd:PRK12704   35 EAEEEAKRILeeakKEAEAIKKEALleakEEIHKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLELLEKR 108

                          90       100
                  ....*....|....*....|...
gi 1907085901 223 RRELMVQLEGLMKLLKEEEQKQA 245
Cdd:PRK12704  109 EEELEKKEKELEQKQQELEKKEE 131
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 117-251 6.81e-05

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: 45.05  E-value: 6.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901  117 RLDEEHRLIARYAARLAAEAGNMTRPPTDASFNFDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNP 196
Cdd:TIGR02168  240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE 319

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907085901  197 MLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKEEEQKQAAQATGS 251
Cdd:TIGR02168  320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
Prefoldin_alpha_GimC cd23160
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ...
 198-241 1.10e-04

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: 41.32  E-value: 1.10e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1907085901 198 LLAELRLLRQRKDELEQRMSALQESRRELMV---QLEGLMKLLKEEE 241
Cdd:cd23160     5 LLAELQQLEQQAEALQQQIELLQASINELNRakeTLEELKKLKEGTE 51
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
 158-249 1.48e-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: 38.75  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 158 QLIAELEN------KNREILQEIQRLRLEHEQ-ASQPTPEKAQQnpmLLAELRLL------RQRKDELEQRMSALQESRR 224
Cdd:pfam09744  30 KVVNVLELleslasRNQEHNVELEELREDNEQlETQYEREKALR---KRAEEELEeiedqwEQETKDLLSQVESLEEENR 106

                          90       100
                  ....*....|....*....|....*
gi 1907085901 225 ELMVQLEGLMKLLKEEEQKQAAQAT 249
Cdd:pfam09744 107 RLEADHVSRLEEKEAELKKEYSKLH 131
 
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 1.98e-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: 88.95  E-value: 1.98e-22
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907085901   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 6.33e-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: 6.33e-12
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1907085901    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 3.21e-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: 46.27  E-value: 3.21e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1907085901   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 3.73e-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: 3.73e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1907085901   3 GFRYRCQQCHNYQLCQNCFWRGHASGAHSNQHQMK 37
Cdd:cd02338    13 GRRYKCLICYDYDLCADCYDSGVTTERHLFDHPMQ 47
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
154-248 1.02e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.54  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 154 KQQRQLIAELENKNREILQEIQRLRLEHEQA-SQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEG 232
Cdd:COG4717   152 EERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231

                          90
                  ....*....|....*..
gi 1907085901 233 L-MKLLKEEEQKQAAQA 248
Cdd:COG4717   232 LeNELEAAALEERLKEA 248
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 3-38 2.52e-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: 44.12  E-value: 2.52e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1907085901   3 GFRYRCQQCHNYQLCQNCFWRGHASGAHSNQHQMKE 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 3.34e-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: 3.34e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1907085901   3 GFRYRCQQCHNYQLCQNCfwrgHASGAHSNqHQM 36
Cdd:cd02340    12 GVRYKCLVCPDYDLCESC----EAKGVHPE-HAM 40
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 154-249 5.46e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 5.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 154 KQQRQLIAELENKNREILQEIQRLRLEHEQASqptpEKAQQnpmLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 233
Cdd:COG1196   249 EELEAELEELEAELAELEAELEELRLELEELE----LELEE---AQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321

                          90
                  ....*....|....*.
gi 1907085901 234 MKLLKEEEQKQAAQAT 249
Cdd:COG1196   322 EEELAELEEELEELEE 337
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 3-21 9.15e-06

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: 42.47  E-value: 9.15e-06
                          10
                  ....*....|....*....
gi 1907085901   3 GFRYRCQQCHNYQLCQNCF 21
Cdd:pfam00569  17 GVRYHCLRCSDYDLCQSCF 35
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 5-34 1.16e-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: 1.16e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1907085901   5 RYRCQQCHNYQLCQNCFWRGHASGAHSNQH 34
Cdd:cd02335    15 RIKCAECPDFDLCLECFSAGAEIGKHRNDH 44
PRK12704 PRK12704
phosphodiesterase; Provisional
 151-245 1.46e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.69  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 151 DANKQQRQLI----AELENKNREIL----QEIQRLRLEHEQasqptpEKAQQNPMLLAELRLLRQRKDELEQRMSALQES 222
Cdd:PRK12704   35 EAEEEAKRILeeakKEAEAIKKEALleakEEIHKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLELLEKR 108

                          90       100
                  ....*....|....*....|...
gi 1907085901 223 RRELMVQLEGLMKLLKEEEQKQA 245
Cdd:PRK12704  109 EEELEKKEKELEQKQQELEKKEE 131
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
151-247 4.53e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.89  E-value: 4.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 151 DANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNpmllAELRLLRQRKDELEQRMSALQESRRELMVQL 230
Cdd:COG4372    56 QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ----EELESLQEEAEELQEELEELQKERQDLEQQR 131

                          90
                  ....*....|....*..
gi 1907085901 231 EGLMKLLKEEEQKQAAQ 247
Cdd:COG4372   132 KQLEAQIAELQSEIAER 148
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
130-248 4.66e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 4.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 130 ARLAAEAGNMTRP----PTDasfNFDANKQQRQLIAELENKNREILQEIQRL-RLEHEQAsqptpEKAQQNPMLLAELRL 204
Cdd:COG4717    49 ERLEKEADELFKPqgrkPEL---NLKELKELEEELKEAEEKEEEYAELQEELeELEEELE-----ELEAELEELREELEK 120

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907085901 205 LRQRKD--ELEQRMSALQESRRELMVQLEGLMKLLKEEEQKQAAQA 248
Cdd:COG4717   121 LEKLLQllPLYQELEALEAELAELPERLEELEERLEELRELEEELE 166
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 160-230 6.32e-05

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 44.67  E-value: 6.32e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907085901 160 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN---PMLLAELRLLRQRKDELEQRMSALQESRRELMVQL 230
Cdd:PRK05431   30 LLELDEERRELQTELEELQAERNALSKEIGQAKRKGedaEALIAEVKELKEEIKALEAELDELEAELEELLLRI 103
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 117-251 6.81e-05

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: 45.05  E-value: 6.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901  117 RLDEEHRLIARYAARLAAEAGNMTRPPTDASFNFDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNP 196
Cdd:TIGR02168  240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE 319

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907085901  197 MLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKEEEQKQAAQATGS 251
Cdd:TIGR02168  320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
ZZ_EF cd02343
Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif ...
 5-36 7.85e-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: 39.99  E-value: 7.85e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1907085901   5 RYRCQQCHNYQLCQNCFWRGHASGAHSNQHQM 36
Cdd:cd02343    14 RYRCLQCTDMDLCKTCFLGGVKPEGHEDDHEM 45
Prefoldin_alpha_GimC cd23160
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ...
 198-241 1.10e-04

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: 41.32  E-value: 1.10e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1907085901 198 LLAELRLLRQRKDELEQRMSALQESRRELMV---QLEGLMKLLKEEE 241
Cdd:cd23160     5 LLAELQQLEQQAEALQQQIELLQASINELNRakeTLEELKKLKEGTE 51
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 151-248 1.32e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 151 DANKQQRQLIAELEnknrEILQEIQRLRLEHEQASQptpEKAQqnpmLLAELRLLRQRKDELEQRMSALQESRRELMVQL 230
Cdd:COG1196   285 EAQAEEYELLAELA----RLEQDIARLEERRRELEE---RLEE----LEEELAELEEELEELEEELEELEEELEEAEEEL 353

                          90
                  ....*....|....*...
gi 1907085901 231 EGLMKLLKEEEQKQAAQA 248
Cdd:COG1196   354 EEAEAELAEAEEALLEAE 371
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 156-249 1.67e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 156 QRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMK 235
Cdd:COG1196   307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386

                          90
                  ....*....|....
gi 1907085901 236 LLKEEEQKQAAQAT 249
Cdd:COG1196   387 ELLEALRAAAELAA 400
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 1-39 1.81e-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: 1.81e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907085901   1 MMGFRYRCQQCHNYQLCQNCFwrghasgaHSNQHQMkEH 39
Cdd:cd02339    11 IIGIRWKCAECPNYDLCTTCY--------HGDKHDL-EH 40
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 116-247 2.18e-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: 43.52  E-value: 2.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901  116 SRLDEEHRliaRYAARLAAEAGNMTRPPTDASFNFDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN 195
Cdd:TIGR02169  801 SKLEEEVS---RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL 877

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907085901  196 PMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKE-EEQKQAAQ 247
Cdd:TIGR02169  878 RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSElKAKLEALE 930
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
157-254 2.18e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.59  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 157 RQLIAELENKNREILQEIQRLRLEHEQASQPTPEkaqqnpmLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKL 236
Cdd:COG1340    21 REEIEELKEKRDELNEELKELAEKRDELNAQVKE-------LREEAQELREKRDELNEKVKELKEERDELNEKLNELREE 93

                          90       100
                  ....*....|....*....|
gi 1907085901 237 LKE--EEQKQAAQATGSPHT 254
Cdd:COG1340    94 LDElrKELAELNKAGGSIDK 113
PRK12704 PRK12704
phosphodiesterase; Provisional
 150-240 3.72e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 3.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 150 FDANKQQRQLIAELENKNREILQEIQRL---------RLEHEQASQptpEKAQQNpmLLAELRLLRQRKDELEQRMSALQ 220
Cdd:PRK12704   60 LEAKEEIHKLRNEFEKELRERRNELQKLekrllqkeeNLDRKLELL---EKREEE--LEKKEKELEQKQQELEKKEEELE 134

                          90       100
                  ....*....|....*....|
gi 1907085901 221 ESRRELMVQLEGLMKLLKEE 240
Cdd:PRK12704  135 ELIEEQLQELERISGLTAEE 154
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 156-247 6.25e-04

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: 41.29  E-value: 6.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 156 QRQLIAELENKNREILQEIQRLRLEHEQASQptpEKAQqnpmLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMK 235
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELEKELAALKK---EEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90

                          90
                  ....*....|..
gi 1907085901 236 LLKEEEQKQAAQ 247
Cdd:COG4942    91 EIAELRAELEAQ 102
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 153-243 9.11e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.16  E-value: 9.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 153 NKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEG 232
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQ 486

                          90
                  ....*....|.
gi 1907085901 233 LMKLLKEEEQK 243
Cdd:TIGR04523 487 KQKELKSKEKE 497
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 151-248 9.68e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 9.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 151 DANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQqnpmLLAELRLLRQRKDELEQRMSALQESRRELMVQL 230
Cdd:COG1196   278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE----LEEELAELEEELEELEEELEELEEELEEAEEEL 353

                          90
                  ....*....|....*...
gi 1907085901 231 EglmkLLKEEEQKQAAQA 248
Cdd:COG1196   354 E----EAEAELAEAEEAL 367
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
154-248 1.07e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 154 KQQRQLIAELENKNREILQEIQRLrlEHEQASQPTPEKAQQNPMLLAEL-----RLLRQRKD--ELEQRMSALQESRREL 226
Cdd:COG4717    98 EELEEELEELEAELEELREELEKL--EKLLQLLPLYQELEALEAELAELperleELEERLEElrELEEELEELEAELAEL 175

                          90       100
                  ....*....|....*....|..
gi 1907085901 227 MVQLEGLMKLLKEEEQKQAAQA 248
Cdd:COG4717   176 QEELEELLEQLSLATEEELQDL 197
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
 153-224 1.38e-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: 1.38e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907085901 153 NKQQRQLIAELENKNREILQEIQRLRLEHE---QASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRR 224
Cdd:TIGR04211  89 LAELRQENQELKQQLSTLEAELEELQKELErikQISANAIELDEENRELREELAELKQENEALEAENERLQENEQ 163
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
 158-249 1.48e-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: 38.75  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 158 QLIAELEN------KNREILQEIQRLRLEHEQ-ASQPTPEKAQQnpmLLAELRLL------RQRKDELEQRMSALQESRR 224
Cdd:pfam09744  30 KVVNVLELleslasRNQEHNVELEELREDNEQlETQYEREKALR---KRAEEELEeiedqwEQETKDLLSQVESLEEENR 106

                          90       100
                  ....*....|....*....|....*
gi 1907085901 225 ELMVQLEGLMKLLKEEEQKQAAQAT 249
Cdd:pfam09744 107 RLEADHVSRLEEKEAELKKEYSKLH 131
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
159-243 1.61e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 159 LIAELENKNREILQEIQRLRLEHEQASQPTpEKAQQNPMLLAELRL----LRQRKDELEQRMSALQESRRELMVQLEGLM 234
Cdd:PRK03918  194 LIKEKEKELEEVLREINEISSELPELREEL-EKLEKEVKELEELKEeieeLEKELESLEGSKRKLEEKIRELEERIEELK 272


                  ....*....
gi 1907085901 235 KLLKEEEQK 243
Cdd:PRK03918  273 KEIEELEEK 281
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
154-248 1.74e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 154 KQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 233
Cdd:COG4372    97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176

                          90
                  ....*....|....*
gi 1907085901 234 MKLLKEEEQKQAAQA 248
Cdd:COG4372   177 SEAEAEQALDELLKE 191
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 150-243 1.75e-03

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: 40.44  E-value: 1.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901  150 FDANKQQ--------RQLIAELENKNREILQEIQRLRLEHEQAS-----QPTPEKAQQNpMLLAELRLLRQRKDELEQRM 216
Cdd:TIGR02169  168 FDRKKEKaleeleevEENIERLDLIIDEKRQQLERLRREREKAEryqalLKEKREYEGY-ELLKEKEALERQKEAIERQL 246

                           90       100
                   ....*....|....*....|....*..
gi 1907085901  217 SALQESRRELMVQLEGLMKLLKEEEQK 243
Cdd:TIGR02169  247 ASLEEELEKLTEEISELEKRLEEIEQL 273
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 154-251 2.33e-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: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 154 KQQRQLIAELENKNREILQEIQRLRLEHEQASQptpekaqqnpmllaELRLLRQRKDELEQRMSALQESRRELMVQLEGL 233
Cdd:COG4942    37 AELEKELAALKKEEKALLKQLAALERRIAALAR--------------RIRALEQELAALEAELAELEKEIAELRAELEAQ 102

                          90
                  ....*....|....*...
gi 1907085901 234 MKLLKeeEQKQAAQATGS 251
Cdd:COG4942   103 KEELA--ELLRALYRLGR 118
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
154-249 2.59e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 2.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901  154 KQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPMLL--------AELRLLRQRKDELEQRMSALQESRRE 225
Cdd:COG4913    248 REQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLeaeleelrAELARLEAELERLEARLDALREELDE 327

                           90       100
                   ....*....|....*....|....*....
gi 1907085901  226 LMVQLEG-----LMKLLKEEEQKQAAQAT 249
Cdd:COG4913    328 LEAQIRGnggdrLEQLEREIERLERELEE 356
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 125-255 2.92e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 38.97  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 125 IARYAARLAAEAGNMTRPPTDASFNFDANKQQRQliaELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPMLLAELRL 204
Cdd:pfam09787  77 LQELEAQQQEEAESSREQLQELEEQLATERSARR---EAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRN 153

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907085901 205 LRQRK-------DELEQRMSALQESRRELMVQLEGL--------MKLLKEEEQKQAAQATGSPHTS 255
Cdd:pfam09787 154 QLTSKsqssssqSELENRLHQLTETLIQKQTMLEALsteknslvLQLERMEQQIKELQGEGSNGTS 219
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
117-253 3.03e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 3.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901  117 RLDEEHRLIARYAARLAAEAgnmtrpptdasfnfDANKQQRQLIAELENKNREIL------QEIQRLRLEHEQASQPTPE 190
Cdd:COG4913    621 ELEEELAEAEERLEALEAEL--------------DALQERREALQRLAEYSWDEIdvasaeREIAELEAELERLDASSDD 686

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907085901  191 KAQqnpmLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKE-EEQKQAAQATGSPH 253
Cdd:COG4913    687 LAA----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDElQDRLEAAEDLARLE 746
Seryl_tRNA_N pfam02403
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ...
 160-234 3.23e-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: 36.80  E-value: 3.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907085901 160 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPmllaELRLLRQRKDELEQRMSALQESRRELMVQLEGLM 234
Cdd:pfam02403  31 LLELDEKRRELQVELEELQAERNELSKEIGQAKKKKE----DADALIAEVKELKDELKALEAELKELEAELDKLL 101
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
 128-222 3.37e-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: 3.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 128 YAARLAAEAGNMTRppTDASFNFDANKQQRQLIAELENKNREILQEIQRL--RLEHEQASQPTPEKAQQNPMLLAELRLL 205
Cdd:pfam03961 131 KAKELGSPAGTKTE--IEVGVDFPELKEKLEELEKELEELEEELEKLKKRlkKLPKKARGQLPPEKREQLEKLLETKNKL 208

                          90
                  ....*....|....*..
gi 1907085901 206 RQRKDELEQRMSALQES 222
Cdd:pfam03961 209 SEELEELEEELKELKEE 225
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 151-303 3.55e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 3.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 151 DANKQQRQLIAELENKNREILQEIQRLRLEHEQAsqptpEKAQQNpmllaelrlLRQRKDELEQRMSALQESRRELMVQL 230
Cdd:COG3883   133 DLLEELKADKAELEAKKAELEAKLAELEALKAEL-----EAAKAE---------LEAQQAEQEALLAQLSAEEAAAEAQL 198

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907085901 231 EGLMKLLKEEEQKQAAQATGSPHTSPTHGGGRPMPMPVRSTSAGSTPTHGPQDSLSGVGGDVQEAFAQGTRRN 303
Cdd:COG3883   199 AELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGA 271
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 151-249 3.87e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.37  E-value: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 151 DANKQQRQLIAELENKNREILQ---EIQRLRLEHEQASQPTpEKAQQNPMLLA---ELRLLRQRKDELEQRMSALQESRR 224
Cdd:COG1579    35 ELEDELAALEARLEAAKTELEDlekEIKRLELEIEEVEARI-KKYEEQLGNVRnnkEYEALQKEIESLKRRISDLEDEIL 113

                          90       100
                  ....*....|....*....|....*
gi 1907085901 225 ELMVQLEGLMKLLKEEEQKQAAQAT 249
Cdd:COG1579   114 ELMERIEELEEELAELEAELAELEA 138
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 3-34 3.88e-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: 3.88e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1907085901   3 GFRYRCQQCHNYQLCQNCFWrghaSGAHSNQH 34
Cdd:cd02344    13 GPRFKCRNCDDFDFCENCFK----TRKHNTRH 40
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 160-248 4.02e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 39.05  E-value: 4.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 160 IAELENKNREILQEIQRL--RLEHEQASQPTPEKAQ------------QNPMLLAELRLLRQR----KDELEqrmsalqe 221
Cdd:PRK04778  277 LDEAEEKNEEIQERIDQLydILEREVKARKYVEKNSdtlpdflehakeQNKELKEEIDRVKQSytlnESELE-------- 348

                          90       100
                  ....*....|....*....|....*..
gi 1907085901 222 SRRELMVQLEGLMKLLKEEEQKQAAQA 248
Cdd:PRK04778  349 SVRQLEKQLESLEKQYDEITERIAEQE 375
Bbox1 cd19757
B-box-type 1 zinc finger (Bbox1); The B-box-type zinc finger is a short zinc binding domain of ...
 6-38 4.20e-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: 34.78  E-value: 4.20e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1907085901   6 YRCQQCHNYqLCQNCFWRGHASGAHSNQHQMKE 38
Cdd:cd19757    12 VYCLECEEF-LCDDCSDAIHRRGKLTRSHKLVP 43
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 170-248 4.40e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 38.33  E-value: 4.40e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907085901 170 ILQEIQRLrLEHEQASQPTPEKAQQnpmLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKEEEQKQAAQA 248
Cdd:cd16269   186 ILQADQAL-TEKEKEIEAERAKAEA---AEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERA 260
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 154-247 4.74e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 38.36  E-value: 4.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 154 KQQRQLIAELENKNREIL----QEIQRLRLEHEQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQ 229
Cdd:pfam13868 123 EKQRQLREEIDEFNEEQAewkeLEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAE 202

                          90
                  ....*....|....*....
gi 1907085901 230 LEGL-MKLLKEEEQKQAAQ 247
Cdd:pfam13868 203 RDELrAKLYQEEQERKERQ 221
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 155-243 4.84e-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: 38.88  E-value: 4.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901  155 QQRQLIAELENKNREILQEIQRL-----RLEHEQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQ 229
Cdd:TIGR02168  383 TLRSKVAQLELQIASLNNEIERLearleRLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEA 462

                           90
                   ....*....|....
gi 1907085901  230 LEGLMKLLKEEEQK 243
Cdd:TIGR02168  463 LEELREELEEAEQA 476
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 154-247 5.13e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 37.98  E-value: 5.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 154 KQQRQLIAELENK------NRE---ILQEIQRLRLEHEQAsqptpEKAQQNpmLLAELRLLRQRKDELEQRMSALQESRR 224
Cdd:COG1579    69 EEVEARIKKYEEQlgnvrnNKEyeaLQKEIESLKRRISDL-----EDEILE--LMERIEELEEELAELEAELAELEAELE 141

                          90       100
                  ....*....|....*....|...
gi 1907085901 225 ELMVQLEGLMKLLKEEEQKQAAQ 247
Cdd:COG1579   142 EKKAELDEELAELEAELEELEAE 164
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 198-249 5.37e-03

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: 38.90  E-value: 5.37e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907085901  198 LLAELRLLRQRKDELEQRMSALQESRRELMVQLEglmkLLKEEEQKQAAQAT 249
Cdd:TIGR02169  693 LQSELRRIENRLDELSQELSDASRKIGEIEKEIE----QLEQEEEKLKERLE 740
Caldesmon pfam02029
Caldesmon;
185-247 5.49e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 38.70  E-value: 5.49e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907085901 185 SQPTPEKAQQNPMLLAELRL--LRQRKDELE-QRMSALQESRRELMVQLEGLM-------KLLKEEEQKQAAQ 247
Cdd:pfam02029 231 SQSQEREEEAEVFLEAEQKLeeLRRRRQEKEsEEFEKLRQKQQEAELELEELKkkreerrKLLEEEEQRRKQE 303
mukB PRK04863
chromosome partition protein MukB;
154-233 5.80e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 38.78  E-value: 5.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901  154 KQQRQLIAELENKNREILQEIQRLrleHEQASQ-----------PTPEkaqqnpmllAELRLLRQRKDELEQRMSALQES 222
Cdd:PRK04863   792 RAEREELAERYATLSFDVQKLQRL---HQAFSRfigshlavafeADPE---------AELRQLNRRRVELERALADHESQ 859

                           90
                   ....*....|.
gi 1907085901  223 RRELMVQLEGL 233
Cdd:PRK04863   860 EQQQRSQLEQA 870
STAT5_CCD cd16855
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ...
 155-239 6.27e-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: 37.24  E-value: 6.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 155 QQRQLIAELENKNREI----------LQEIQRLRLEHEQASQptpekaQQNPMLLAELRLLRQRKDELEQRMSA----LQ 220
Cdd:cd16855    12 ELRQRTQETENDLRNLqqkqesfviqYQESQKIQAQLQQLQQ------QPQNERIELEQQLQQQKEQLEQLLNAkaqeLL 85

                          90
                  ....*....|....*....
gi 1907085901 221 ESRRELMVQLEGLMKLLKE 239
Cdd:cd16855    86 QLRMELADKFKKTIQLLSK 104
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
151-245 6.29e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.34  E-value: 6.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 151 DANKQQRQLIAELENKNREILQ---EIQRLRLEHEQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELM 227
Cdd:COG4372    42 KLQEELEQLREELEQAREELEQleeELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121

                          90
                  ....*....|....*...
gi 1907085901 228 VQLEGLMKLLKEEEQKQA 245
Cdd:COG4372   122 KERQDLEQQRKQLEAQIA 139
DASH_Spc19 pfam08287
Spc19; Spc19 is a component of the DASH complex. The DASH complex associates with the spindle ...
 153-219 6.63e-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: 6.63e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907085901 153 NKQQRQLiAELENKNreilqEIQRLRLEH------------EQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSAL 219
Cdd:pfam08287  76 EKLERRE-ETLKAKL-----ELNEGRLSNaessardeegsqESDEEVNSSEGDATNEELERLRALRQKKERLKYSLERL 148
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
117-248 7.71e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.46  E-value: 7.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901 117 RLDEEHRLIARYAARLAA--EAGNMTRPPTDASFNFDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEkAQQ 194
Cdd:COG3206   183 QLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE-LLQ 261

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907085901 195 NPM---LLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKEEEQKQAAQA 248
Cdd:COG3206   262 SPViqqLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASL 318
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
 5-39 8.50e-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: 8.50e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1907085901   5 RYRCQQCHNYQLCQNCFWR-GHasgahsnQHQMKEH 39
Cdd:cd02337    13 RWHCTVCEDYDLCITCYNTkNH-------PHKMEKL 41
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 155-248 9.19e-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: 38.11  E-value: 9.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085901  155 QQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEglm 234
Cdd:TIGR02168  723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK--- 799

                           90
                   ....*....|....
gi 1907085901  235 kllKEEEQKQAAQA 248
Cdd:TIGR02168  800 ---ALREALDELRA 810
 
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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