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Conserved domains on  [gi|1907085892|ref|XP_036013072|]
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dystrobrevin beta isoform X16 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EF-hand_3 pfam09069
EF-hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
 1-78 4.75e-36

EF-hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. However, since they do not contain the canonical pattern of calcium binding residues found in many EF hand domains, they do not bind calcium ions. The main function of this domain is the provision of specificity in beta-dystroglycan recognition, though in dystrophin it serves an additional role: stabilization of the WW domain (pfam00397), enhancing dystroglycan binding.


:

Pssm-ID: 462669  Cd Length: 90  Bit Score: 127.03  E-value: 4.75e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892   1 MSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFGYTEHAVRTCFPQ---QKKIMLNMFLDTMMADppPQCLVWLPLMHRL 77
Cdd:pfam09069  12 ISDSNGLLDQSKLGLLLHELLQLPRQVGEVPAFGGIEPSVRSCFEQvggKPKITLNHFLDWLMSE--PQSLVWLPVLHRL 89


                  .
gi 1907085892  78 A 78
Cdd:pfam09069  90 A 90
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 87-135 3.66e-26

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: 99.35  E-value: 3.66e-26
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1907085892  87 VECSYCHCESMMGFRYRCQQCHNYQLCQNCFWRGHASGAHSNQHQMKEH 135
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
250-344 3.21e-07

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: 52.46  E-value: 3.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 250 KQQRQLIAELENKNREILQEIQRLRLEHEQA-SQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEG 328
Cdd:COG4717   152 EERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231

                          90
                  ....*....|....*..
gi 1907085892 329 L-MKLLKEEEQKQAAQA 344
Cdd:COG4717   232 LeNELEAAALEERLKEA 248
 
Name Accession Description Interval E-value
EF-hand_3 pfam09069
EF-hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
 1-78 4.75e-36

EF-hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. However, since they do not contain the canonical pattern of calcium binding residues found in many EF hand domains, they do not bind calcium ions. The main function of this domain is the provision of specificity in beta-dystroglycan recognition, though in dystrophin it serves an additional role: stabilization of the WW domain (pfam00397), enhancing dystroglycan binding.


Pssm-ID: 462669  Cd Length: 90  Bit Score: 127.03  E-value: 4.75e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892   1 MSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFGYTEHAVRTCFPQ---QKKIMLNMFLDTMMADppPQCLVWLPLMHRL 77
Cdd:pfam09069  12 ISDSNGLLDQSKLGLLLHELLQLPRQVGEVPAFGGIEPSVRSCFEQvggKPKITLNHFLDWLMSE--PQSLVWLPVLHRL 89


                  .
gi 1907085892  78 A 78
Cdd:pfam09069  90 A 90
EFh_DTNB cd16250
EF-hand-like motif found in beta-dystrobrevin; Beta-dystrobrevin, also termed dystrobrevin ...
 1-60 1.34e-33

EF-hand-like motif found in beta-dystrobrevin; Beta-dystrobrevin, also termed dystrobrevin beta (DTN-B), is a dystrophin-related protein that is restricted to non-muscle tissues and is abundantly expressed in brain, lung, kidney, and liver. It may be involved in regulating chromatin dynamics, possibly playing a role in neuronal differentiation, through the interactions with the high mobility group HMG20 proteins iBRAF/HMG20a and BRAF35 /HMG20b. It also binds to and represses the promoter of synapsin I, a neuronal differentiation gene. Moreover, beta-dystrobrevin functions as a kinesin-binding receptor involved in brain development via the association with the extracellular matrix components pancortins. Furthermore, beta-dystrobrevin binds directly to dystrophin and is a cytoplasmic component of the dystrophin-associated glycoprotein complex, a multimeric protein complex that links the extracellular matrix to the cortical actin cytoskeleton and acts as a scaffold for signaling proteins such as protein kinase A. Absence of alpha- and beta-dystrobrevin causes cerebellar synaptic defects and abnormal motor behavior. Beta-dystrobrevin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, beta-dystrobrevin contain two syntrophin binding sites (SBSs).


Pssm-ID: 320008  Cd Length: 161  Bit Score: 123.21  E-value: 1.34e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892   1 MSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFGYTEHAVRTCFPQQKKIMLNMFLDTMM 60
Cdd:cd16250   102 MSDSNGLMIFLKFDQFLREVLKLPTAVFEGPSFGYTEHSVRTCFPQQKKIMLNMFLDTMM 161
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 87-135 3.66e-26

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: 99.35  E-value: 3.66e-26
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1907085892  87 VECSYCHCESMMGFRYRCQQCHNYQLCQNCFWRGHASGAHSNQHQMKEH 135
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 83-127 1.71e-15

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: 69.78  E-value: 1.71e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1907085892   83 VFHPVECSYCHCEsMMGFRYRCQQCHNYQLCQNCFWRGHASGAHS 127
Cdd:smart00291   1 VHHSYSCDTCGKP-IVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
250-344 3.21e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.46  E-value: 3.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 250 KQQRQLIAELENKNREILQEIQRLRLEHEQA-SQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEG 328
Cdd:COG4717   152 EERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231

                          90
                  ....*....|....*..
gi 1907085892 329 L-MKLLKEEEQKQAAQA 344
Cdd:COG4717   232 LeNELEAAALEERLKEA 248
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 85-117 1.10e-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: 45.17  E-value: 1.10e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1907085892  85 HPVECSYCHCESMMGFRYRCQQCHNYQLCQNCF 117
Cdd:pfam00569   3 KVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCF 35
PRK12704 PRK12704
phosphodiesterase; Provisional
 247-341 1.74e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.69  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 247 DANKQQRQLI----AELENKNREIL----QEIQRLRLEHEQasqptpEKAQQNPMLLAELRLLRQRKDELEQRMSALQES 318
Cdd:PRK12704   35 EAEEEAKRILeeakKEAEAIKKEALleakEEIHKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLELLEKR 108

                          90       100
                  ....*....|....*....|...
gi 1907085892 319 RRELMVQLEGLMKLLKEEEQKQA 341
Cdd:PRK12704  109 EEELEKKEKELEQKQQELEKKEE 131
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 213-347 3.63e-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: 46.20  E-value: 3.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892  213 RLDEEHRLIARYAARLAAEAGNMTRPPTDASFNFDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNP 292
Cdd:TIGR02168  240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE 319

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907085892  293 MLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKEEEQKQAAQATGS 347
Cdd:TIGR02168  320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
Prefoldin_alpha_GimC cd23160
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ...
 294-337 1.00e-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: 41.70  E-value: 1.00e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1907085892 294 LLAELRLLRQRKDELEQRMSALQESRRELMV---QLEGLMKLLKEEE 337
Cdd:cd23160     5 LLAELQQLEQQAEALQQQIELLQASINELNRakeTLEELKKLKEGTE 51
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 221-351 1.03e-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: 40.90  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 221 IARYAARLAAEAGNMTRPPTDASFNFDANKQQRQliaELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPMLLAELRL 300
Cdd:pfam09787  77 LQELEAQQQEEAESSREQLQELEEQLATERSARR---EAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRN 153

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907085892 301 LRQRK-------DELEQRMSALQESRRELMVQLEGL--------MKLLKEEEQKQAAQATGSPHTS 351
Cdd:pfam09787 154 QLTSKsqssssqSELENRLHQLTETLIQKQTMLEALsteknslvLQLERMEQQIKELQGEGSNGTS 219
 
Name Accession Description Interval E-value
EF-hand_3 pfam09069
EF-hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
 1-78 4.75e-36

EF-hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. However, since they do not contain the canonical pattern of calcium binding residues found in many EF hand domains, they do not bind calcium ions. The main function of this domain is the provision of specificity in beta-dystroglycan recognition, though in dystrophin it serves an additional role: stabilization of the WW domain (pfam00397), enhancing dystroglycan binding.


Pssm-ID: 462669  Cd Length: 90  Bit Score: 127.03  E-value: 4.75e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892   1 MSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFGYTEHAVRTCFPQ---QKKIMLNMFLDTMMADppPQCLVWLPLMHRL 77
Cdd:pfam09069  12 ISDSNGLLDQSKLGLLLHELLQLPRQVGEVPAFGGIEPSVRSCFEQvggKPKITLNHFLDWLMSE--PQSLVWLPVLHRL 89


                  .
gi 1907085892  78 A 78
Cdd:pfam09069  90 A 90
EFh_DTNB cd16250
EF-hand-like motif found in beta-dystrobrevin; Beta-dystrobrevin, also termed dystrobrevin ...
 1-60 1.34e-33

EF-hand-like motif found in beta-dystrobrevin; Beta-dystrobrevin, also termed dystrobrevin beta (DTN-B), is a dystrophin-related protein that is restricted to non-muscle tissues and is abundantly expressed in brain, lung, kidney, and liver. It may be involved in regulating chromatin dynamics, possibly playing a role in neuronal differentiation, through the interactions with the high mobility group HMG20 proteins iBRAF/HMG20a and BRAF35 /HMG20b. It also binds to and represses the promoter of synapsin I, a neuronal differentiation gene. Moreover, beta-dystrobrevin functions as a kinesin-binding receptor involved in brain development via the association with the extracellular matrix components pancortins. Furthermore, beta-dystrobrevin binds directly to dystrophin and is a cytoplasmic component of the dystrophin-associated glycoprotein complex, a multimeric protein complex that links the extracellular matrix to the cortical actin cytoskeleton and acts as a scaffold for signaling proteins such as protein kinase A. Absence of alpha- and beta-dystrobrevin causes cerebellar synaptic defects and abnormal motor behavior. Beta-dystrobrevin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, beta-dystrobrevin contain two syntrophin binding sites (SBSs).


Pssm-ID: 320008  Cd Length: 161  Bit Score: 123.21  E-value: 1.34e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892   1 MSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFGYTEHAVRTCFPQQKKIMLNMFLDTMM 60
Cdd:cd16250   102 MSDSNGLMIFLKFDQFLREVLKLPTAVFEGPSFGYTEHSVRTCFPQQKKIMLNMFLDTMM 161
EFh_DTN cd16244
EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the ...
 1-60 6.06e-33

EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the dystrophin-glycoprotein complex (DGC). They physically associate with members of the dystrophin family and with the syntrophins through their homologous C-terminal coiled coil motifs. The family includes two paralogs dystrobrevins, alpha- and beta-dystrobrevin, both of which are cytoplasmic components of the dystrophin-associated protein complex that function as scaffold proteins in signal transduction and intracellular transport. Absence of alpha- and beta-dystrobrevin causes cerebellar synaptic defects and abnormal motor behavior. The dystrobrevins subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrobrevins contain one or two syntrophin binding sites (SBSs).


Pssm-ID: 320002 [Multi-domain]  Cd Length: 161  Bit Score: 121.19  E-value: 6.06e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892   1 MSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFGYTEHAVRTCFPQQKKIMLNMFLDTMM 60
Cdd:cd16244   102 ISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYNESAARSCFPGQSKVTVNDFLDVMM 161
EFh_DTNA cd16249
EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin ...
 1-60 1.17e-30

EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin alpha (DTN-A), or dystrophin-related protein 3 (DRP-3), is the mammalian ortholog of the Torpedo 87 kDa postsynaptic protein that tightly associates with dystrophin. It is a cytoplasmic protein expressed predominantly in skeletal muscle, heart, lung, and brain. Alpha-dystrobrevin has been implicated in the regulation of acetylcholine receptor (AChR) aggregate density and patterning. It is also essential in the pathogenesis of dystrophin-dependent muscular dystrophies. It plays a critical role in the full functionality of dystrophin through increasing dystrophin's binding to the dystrophin-glycoprotein complex (DGC), and provides protection during cardiac stress. Alpha-dystrobrevin binds to the intermediate filament proteins syncoilin and beta-synemin, thereby linking the dystrophin-associated protein complex (DAPC) to the intermediate filament network. Moreover, alpha-dystrobrevin involves in cell signaling via interaction with other proteins such as syntrophin, a modular adaptor protein that coordinates the assembly of the signaling proteins nitric oxide synthase, stress-activated protein kinase-3, and Grb2 to the DAPC. Furthermore, alpha-dystrobrevin plays an important role in muscle function, as well as in nuclear morphology maintenance through specific interaction with the nuclear lamina component lamin B1. In addition, alpha-dystrobrevin is required in dystrophin-associated protein scaffolding in brain. Absence of glial alpha-dystrobrevin causes abnormalities of the blood-brain barrier and progressive brain edema. Alpha-dystrobrevin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, alpha-dystrobrevin contain two syntrophin binding sites (SBSs).


Pssm-ID: 320007  Cd Length: 161  Bit Score: 114.99  E-value: 1.17e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892   1 MSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFGYTEHAVRTCFPQQKKIMLNMFLDTMM 60
Cdd:cd16249   102 ISDSNGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSARSCFSQQKKVTLNGFLDTLM 161
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 87-135 3.66e-26

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: 99.35  E-value: 3.66e-26
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1907085892  87 VECSYCHCESMMGFRYRCQQCHNYQLCQNCFWRGHASGAHSNQHQMKEH 135
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 83-127 1.71e-15

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: 69.78  E-value: 1.71e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1907085892   83 VFHPVECSYCHCEsMMGFRYRCQQCHNYQLCQNCFWRGHASGAHS 127
Cdd:smart00291   1 VHHSYSCDTCGKP-IVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
EFh_DMD_DYTN_DTN cd15901
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ...
 1-60 7.39e-12

EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin/dystrobrevin/dystrotelin family has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. Dystrophin is the founder member of this family. It is a sub-membrane cytoskeletal protein associated with the inner surface membrane. Dystrophin and its close paralog utrophin have a large N-terminal extension of actin-binding CH domains, up to 24 spectrin repeats, and a WW domain. Its further paralog, dystrophin-related protein 2 (DRP-2), retains only two of the spectrin repeats. Dystrophin, utrophin or DRP2 can form the core of a membrane-bound complex consisting of dystroglycan, sarcoglycans and syntrophins, known as the dystrophin-glycoprotein complex (DGC) that plays an important role in brain development and disease, as well as in the prevention of muscle damage. Dystrobrevins, including alpha- and beta-dystrobrevin, lack the large N-terminal extension found in dystrophin, but alpha-dystrobrevin has a characteristic C-terminal extension. Dystrobrevins are part of the DGC. They physically associate with members of the dystrophin family and with the syntrophins through their homologous C-terminal coiled coil motifs. In contrast, dystrotelins lack both the large N-terminal extension found in dystrophin and the obvious syntrophin-binding sites (SBSs). Dystrotelins are not critical for mammalian development. They may be involved in other forms of cytokinesis. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize.


Pssm-ID: 319999  Cd Length: 163  Bit Score: 63.06  E-value: 7.39e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907085892   1 MSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFG--YTEHAVRTCFPQQKKIM---LNMFLDTMM 60
Cdd:cd15901    99 LADSSGFISRERLTQFLQDLLQIPDLIGESPAFGghNVEAAVESCFQLARSRVgvsEDTFLSWLL 163
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 89-134 2.28e-08

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: 49.90  E-value: 2.28e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1907085892  89 CSYCHCESMMGFRYRCQQCHNYQLCQNCFWRGHASGAHSNQHQMKE 134
Cdd:cd02345     3 CSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLHIMYE 48
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 89-130 2.64e-08

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: 49.60  E-value: 2.64e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1907085892  89 CSYCHCESMMGFRYRCQQCHNYQLCQNCFWRGHASGAHSNQH 130
Cdd:cd02335     3 CDYCSKDITGTIRIKCAECPDFDLCLECFSAGAEIGKHRNDH 44
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 87-133 3.69e-08

Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Human potassium channel modulatory factor 1 or FIGC has been shown to possess intrinsic E3 ubiquitin ligase activity and to promote ubiquitination.


Pssm-ID: 239078  Cd Length: 49  Bit Score: 49.27  E-value: 3.69e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1907085892  87 VECSYCHCESMMGFRYRCQQCHNYQLCQNCFWRGHASGAHSNQHQMK 133
Cdd:cd02338     1 VSCDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFDHPMQ 47
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
250-344 3.21e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.46  E-value: 3.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 250 KQQRQLIAELENKNREILQEIQRLRLEHEQA-SQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEG 328
Cdd:COG4717   152 EERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231

                          90
                  ....*....|....*..
gi 1907085892 329 L-MKLLKEEEQKQAAQA 344
Cdd:COG4717   232 LeNELEAAALEERLKEA 248
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 92-135 7.77e-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: 45.50  E-value: 7.77e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1907085892  92 CHCESM--MGFRYRCQQCHNYQLCQNCFWRGHasGAHSNQHQMKEH 135
Cdd:cd02249     3 CDGCLKpiVGVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 85-117 1.10e-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: 45.17  E-value: 1.10e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1907085892  85 HPVECSYCHCESMMGFRYRCQQCHNYQLCQNCF 117
Cdd:pfam00569   3 KVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCF 35
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 250-345 2.01e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 2.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 250 KQQRQLIAELENKNREILQEIQRLRLEHEQASqptpEKAQQnpmLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 329
Cdd:COG1196   249 EELEAELEELEAELAELEAELEELRLELEELE----LELEE---AQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321

                          90
                  ....*....|....*.
gi 1907085892 330 MKLLKEEEQKQAAQAT 345
Cdd:COG1196   322 EEELAELEEELEELEE 337
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
247-343 4.09e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.36  E-value: 4.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 247 DANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNpmllAELRLLRQRKDELEQRMSALQESRRELMVQL 326
Cdd:COG4372    56 QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ----EELESLQEEAEELQEELEELQKERQDLEQQR 131

                          90
                  ....*....|....*..
gi 1907085892 327 EGLMKLLKEEEQKQAAQ 343
Cdd:COG4372   132 KQLEAQIAELQSEIAER 148
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 87-132 4.84e-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: 43.02  E-value: 4.84e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1907085892  87 VECsyCHCES-MMGFRYRCQQCHNYQLCQNCfwrgHASGAHSNqHQM 132
Cdd:cd02340     1 VIC--DGCQGpIVGVRYKCLVCPDYDLCESC----EAKGVHPE-HAM 40
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 89-135 9.77e-06

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: 42.45  E-value: 9.77e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1907085892  89 CSYCHCESMMGFRYRCQQCHNYQLCQNCFwrghasgaHSNQHQMkEH 135
Cdd:cd02339     3 CDTCRKQGIIGIRWKCAECPNYDLCTTCY--------HGDKHDL-EH 40
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
226-344 1.13e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 226 ARLAAEAGNMTRP----PTDasfNFDANKQQRQLIAELENKNREILQEIQRL-RLEHEQAsqptpEKAQQNPMLLAELRL 300
Cdd:COG4717    49 ERLEKEADELFKPqgrkPEL---NLKELKELEEELKEAEEKEEEYAELQEELeELEEELE-----ELEAELEELREELEK 120

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907085892 301 LRQRKD--ELEQRMSALQESRRELMVQLEGLMKLLKEEEQKQAAQA 344
Cdd:COG4717   121 LEKLLQllPLYQELEALEAELAELPERLEELEERLEELRELEEELE 166
PRK12704 PRK12704
phosphodiesterase; Provisional
 247-341 1.74e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.69  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 247 DANKQQRQLI----AELENKNREIL----QEIQRLRLEHEQasqptpEKAQQNPMLLAELRLLRQRKDELEQRMSALQES 318
Cdd:PRK12704   35 EAEEEAKRILeeakKEAEAIKKEALleakEEIHKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLELLEKR 108

                          90       100
                  ....*....|....*....|...
gi 1907085892 319 RRELMVQLEGLMKLLKEEEQKQA 341
Cdd:PRK12704  109 EEELEKKEKELEQKQQELEKKEE 131
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 87-127 2.32e-05

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: 41.42  E-value: 2.32e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1907085892  87 VECSYCHCESMMGFRYRCQQCHNYQLCQNCFWRGHASGAHS 127
Cdd:cd02344     1 VTCDGCQMFPINGPRFKCRNCDDFDFCENCFKTRKHNTRHT 41
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 213-347 3.63e-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: 46.20  E-value: 3.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892  213 RLDEEHRLIARYAARLAAEAGNMTRPPTDASFNFDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNP 292
Cdd:TIGR02168  240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE 319

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907085892  293 MLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKEEEQKQAAQATGS 347
Cdd:TIGR02168  320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 247-344 4.70e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 4.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 247 DANKQQRQLIAELEnknrEILQEIQRLRLEHEQASQptpEKAQqnpmLLAELRLLRQRKDELEQRMSALQESRRELMVQL 326
Cdd:COG1196   285 EAQAEEYELLAELA----RLEQDIARLEERRRELEE---RLEE----LEEELAELEEELEELEEELEELEEELEEAEEEL 353

                          90
                  ....*....|....*...
gi 1907085892 327 EGLMKLLKEEEQKQAAQA 344
Cdd:COG1196   354 EEAEAELAEAEEALLEAE 371
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 256-326 7.28e-05

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 44.67  E-value: 7.28e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907085892 256 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN---PMLLAELRLLRQRKDELEQRMSALQESRRELMVQL 326
Cdd:PRK05431   30 LLELDEERRELQTELEELQAERNALSKEIGQAKRKGedaEALIAEVKELKEEIKALEAELDELEAELEELLLRI 103
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 252-345 8.63e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 8.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 252 QRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMK 331
Cdd:COG1196   307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386

                          90
                  ....*....|....
gi 1907085892 332 LLKEEEQKQAAQAT 345
Cdd:COG1196   387 ELLEALRAAAELAA 400
Prefoldin_alpha_GimC cd23160
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ...
 294-337 1.00e-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: 41.70  E-value: 1.00e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1907085892 294 LLAELRLLRQRKDELEQRMSALQESRRELMV---QLEGLMKLLKEEE 337
Cdd:cd23160     5 LLAELQQLEQQAEALQQQIELLQASINELNRakeTLEELKKLKEGTE 51
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
253-350 1.20e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 43.75  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 253 RQLIAELENKNREILQEIQRLRLEHEQASQPTPEkaqqnpmLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKL 332
Cdd:COG1340    21 REEIEELKEKRDELNEELKELAEKRDELNAQVKE-------LREEAQELREKRDELNEKVKELKEERDELNEKLNELREE 93

                          90       100
                  ....*....|....*....|
gi 1907085892 333 LKE--EEQKQAAQATGSPHT 350
Cdd:COG1340    94 LDElrKELAELNKAGGSIDK 113
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 212-343 1.34e-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: 44.29  E-value: 1.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892  212 SRLDEEHRliaRYAARLAAEAGNMTRPPTDASFNFDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN 291
Cdd:TIGR02169  801 SKLEEEVS---RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL 877

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907085892  292 PMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKE-EEQKQAAQ 343
Cdd:TIGR02169  878 RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSElKAKLEALE 930
ZZ_EF cd02343
Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif ...
 94-132 1.50e-04

Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239083  Cd Length: 48  Bit Score: 39.22  E-value: 1.50e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1907085892  94 CESMMGF-RYRCQQCHNYQLCQNCFWRGHASGAHSNQHQM 132
Cdd:cd02343     6 CDEIAPWhRYRCLQCTDMDLCKTCFLGGVKPEGHEDDHEM 45
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 252-343 1.81e-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: 43.21  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 252 QRQLIAELENKNREILQEIQRLRLEHEQASQptpEKAQqnpmLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMK 331
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELEKELAALKK---EEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90

                          90
                  ....*....|..
gi 1907085892 332 LLKEEEQKQAAQ 343
Cdd:COG4942    91 EIAELRAELEAQ 102
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
250-344 2.63e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 2.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 250 KQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 329
Cdd:COG4372    97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176

                          90
                  ....*....|....*
gi 1907085892 330 MKLLKEEEQKQAAQA 344
Cdd:COG4372   177 SEAEAEQALDELLKE 191
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
250-344 3.64e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 3.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 250 KQQRQLIAELENKNREILQEIQRLrlEHEQASQPTPEKAQQNPMLLAEL-----RLLRQRKD--ELEQRMSALQESRREL 322
Cdd:COG4717    98 EELEEELEELEAELEELREELEKL--EKLLQLLPLYQELEALEAELAELperleELEERLEElrELEEELEELEAELAEL 175

                          90       100
                  ....*....|....*....|..
gi 1907085892 323 MVQLEGLMKLLKEEEQKQAAQA 344
Cdd:COG4717   176 QEELEELLEQLSLATEEELQDL 197
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 247-344 4.28e-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: 4.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 247 DANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQqnpmLLAELRLLRQRKDELEQRMSALQESRRELMVQL 326
Cdd:COG1196   278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE----LEEELAELEEELEELEEELEELEEELEEAEEEL 353

                          90
                  ....*....|....*...
gi 1907085892 327 EglmkLLKEEEQKQAAQA 344
Cdd:COG1196   354 E----EAEAELAEAEEAL 367
PRK12704 PRK12704
phosphodiesterase; Provisional
 246-336 4.38e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 4.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 246 FDANKQQRQLIAELENKNREILQEIQRL---------RLEHEQASQptpEKAQQNpmLLAELRLLRQRKDELEQRMSALQ 316
Cdd:PRK12704   60 LEAKEEIHKLRNEFEKELRERRNELQKLekrllqkeeNLDRKLELL---EKREEE--LEKKEKELEQKQQELEKKEEELE 134

                          90       100
                  ....*....|....*....|
gi 1907085892 317 ESRRELMVQLEGLMKLLKEE 336
Cdd:PRK12704  135 ELIEEQLQELERISGLTAEE 154
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
 249-320 6.04e-04

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: 40.76  E-value: 6.04e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907085892 249 NKQQRQLIAELENKNREILQEIQRLRLEHE---QASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRR 320
Cdd:TIGR04211  89 LAELRQENQELKQQLSTLEAELEELQKELErikQISANAIELDEENRELREELAELKQENEALEAENERLQENEQ 163
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 250-347 6.80e-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: 41.67  E-value: 6.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 250 KQQRQLIAELENKNREILQEIQRLRLEHEQASQptpekaqqnpmllaELRLLRQRKDELEQRMSALQESRRELMVQLEGL 329
Cdd:COG4942    37 AELEKELAALKKEEKALLKQLAALERRIAALAR--------------RIRALEQELAALEAELAELEKEIAELRAELEAQ 102

                          90
                  ....*....|....*...
gi 1907085892 330 MKLLKeeEQKQAAQATGS 347
Cdd:COG4942   103 KEELA--ELLRALYRLGR 118
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 247-401 7.03e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 7.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 247 DANKQQRQLIAELENKNREILQEIQRLRLEHEQAsqptpEKAQQNpmllaelrlLRQRKDELEQRMSALQESRRELMVQL 326
Cdd:COG3883   133 DLLEELKADKAELEAKKAELEAKLAELEALKAEL-----EAAKAE---------LEAQQAEQEALLAQLSAEEAAAEAQL 198

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907085892 327 EGLMKLLKEEEQKQAAQATGSPHTSPTHGGGRPMPMPVRSTSAGSTPTHGPQDSLSGVGGDVQEAFAQGEVTPVS 401
Cdd:COG3883   199 AELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAG 273
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
247-342 8.14e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 8.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 247 DANKQQRQLIAELENKNREILQ---EIQRLRLEHEQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELM 323
Cdd:COG4372    42 KLQEELEQLREELEQAREELEQleeELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121

                          90
                  ....*....|....*....
gi 1907085892 324 VQLEGLMKLLKEEEQKQAA 342
Cdd:COG4372   122 KERQDLEQQRKQLEAQIAE 140
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
213-349 9.15e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 9.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892  213 RLDEEHRLIARYAARLAAEAgnmtrpptdasfnfDANKQQRQLIAELENKNREIL------QEIQRLRLEHEQASQPTPE 286
Cdd:COG4913    621 ELEEELAEAEERLEALEAEL--------------DALQERREALQRLAEYSWDEIdvasaeREIAELEAELERLDASSDD 686

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907085892  287 KAQqnpmLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKE-EEQKQAAQATGSPH 349
Cdd:COG4913    687 LAA----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDElQDRLEAAEDLARLE 746
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 246-339 9.80e-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: 9.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892  246 FDANKQQ--------RQLIAELENKNREILQEIQRLRLEHEQAS-----QPTPEKAQQNpMLLAELRLLRQRKDELEQRM 312
Cdd:TIGR02169  168 FDRKKEKaleeleevEENIERLDLIIDEKRQQLERLRREREKAEryqalLKEKREYEGY-ELLKEKEALERQKEAIERQL 246

                           90       100
                   ....*....|....*....|....*..
gi 1907085892  313 SALQESRRELMVQLEGLMKLLKEEEQK 339
Cdd:TIGR02169  247 ASLEEELEKLTEEISELEKRLEEIEQL 273
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
250-345 1.01e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892  250 KQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPMLL--------AELRLLRQRKDELEQRMSALQESRRE 321
Cdd:COG4913    248 REQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLeaeleelrAELARLEAELERLEARLDALREELDE 327

                           90       100
                   ....*....|....*....|....*....
gi 1907085892  322 LMVQLEG-----LMKLLKEEEQKQAAQAT 345
Cdd:COG4913    328 LEAQIRGnggdrLEQLEREIERLERELEE 356
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 221-351 1.03e-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: 40.90  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 221 IARYAARLAAEAGNMTRPPTDASFNFDANKQQRQliaELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPMLLAELRL 300
Cdd:pfam09787  77 LQELEAQQQEEAESSREQLQELEEQLATERSARR---EAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRN 153

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907085892 301 LRQRK-------DELEQRMSALQESRRELMVQLEGL--------MKLLKEEEQKQAAQATGSPHTS 351
Cdd:pfam09787 154 QLTSKsqssssqSELENRLHQLTETLIQKQTMLEALsteknslvLQLERMEQQIKELQGEGSNGTS 219
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 249-339 1.07e-03

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: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 249 NKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEG 328
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQ 486

                          90
                  ....*....|.
gi 1907085892 329 LMKLLKEEEQK 339
Cdd:TIGR04523 487 KQKELKSKEKE 497
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
 254-345 1.18e-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: 39.14  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 254 QLIAELEN------KNREILQEIQRLRLEHEQ-ASQPTPEKAQQnpmLLAELRLL------RQRKDELEQRMSALQESRR 320
Cdd:pfam09744  30 KVVNVLELleslasRNQEHNVELEELREDNEQlETQYEREKALR---KRAEEELEeiedqwEQETKDLLSQVESLEEENR 106

                          90       100
                  ....*....|....*....|....*
gi 1907085892 321 ELMVQLEGLMKLLKEEEQKQAAQAT 345
Cdd:pfam09744 107 RLEADHVSRLEEKEAELKKEYSKLH 131
DASH_Spc19 pfam08287
Spc19; Spc19 is a component of the DASH complex. The DASH complex associates with the spindle ...
 249-315 1.50e-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: 38.77  E-value: 1.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907085892 249 NKQQRQLiAELENKNreilqEIQRLRLEH------------EQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSAL 315
Cdd:pfam08287  76 EKLERRE-ETLKAKL-----ELNEGRLSNaessardeegsqESDEEVNSSEGDATNEELERLRALRQKKERLKYSLERL 148
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
214-344 1.79e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.39  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 214 LDEEhrlIARYAARLAA---------EAGNMTRPPTDASFNFDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPT 284
Cdd:COG3206   180 LEEQ---LPELRKELEEaeaaleefrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDAL 256

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907085892 285 PEkAQQNPM---LLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKEEEQKQAAQA 344
Cdd:COG3206   257 PE-LLQSPViqqLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASL 318
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
255-339 1.89e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 255 LIAELENKNREILQEIQRLRLEHEQASQPTpEKAQQNPMLLAELRL----LRQRKDELEQRMSALQESRRELMVQLEGLM 330
Cdd:PRK03918  194 LIKEKEKELEEVLREINEISSELPELREEL-EKLEKEVKELEELKEeieeLEKELESLEGSKRKLEEKIRELEERIEELK 272


                  ....*....
gi 1907085892 331 KLLKEEEQK 339
Cdd:PRK03918  273 KEIEELEEK 281
Caldesmon pfam02029
Caldesmon;
281-343 2.22e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 40.24  E-value: 2.22e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907085892 281 SQPTPEKAQQNPMLLAELRL--LRQRKDELE-QRMSALQESRRELMVQLEGLM-------KLLKEEEQKQAAQ 343
Cdd:pfam02029 231 SQSQEREEEAEVFLEAEQKLeeLRRRRQEKEsEEFEKLRQKQQEAELELEELKkkreerrKLLEEEEQRRKQE 303
mukB PRK04863
chromosome partition protein MukB;
250-329 2.31e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.33  E-value: 2.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892  250 KQQRQLIAELENKNREILQEIQRLrleHEQASQ-----------PTPEkaqqnpmllAELRLLRQRKDELEQRMSALQES 318
Cdd:PRK04863   792 RAEREELAERYATLSFDVQKLQRL---HQAFSRfigshlavafeADPE---------AELRQLNRRRVELERALADHESQ 859

                           90
                   ....*....|.
gi 1907085892  319 RRELMVQLEGL 329
Cdd:PRK04863   860 EQQQRSQLEQA 870
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
253-348 2.57e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 253 RQLIAELENKNREILQEIQRLRLEHEQASQptpekaqqnpMLLAELRLLRQRKDELEQRMSALQESRRELM-------VQ 325
Cdd:COG3206   294 IALRAQIAALRAQLQQEAQRILASLEAELE----------ALQAREASLQAQLAQLEARLAELPELEAELRrlereveVA 363

                          90       100
                  ....*....|....*....|...
gi 1907085892 326 LEGLMKLLKEEEQKQAAQATGSP 348
Cdd:COG3206   364 RELYESLLQRLEEARLAEALTVG 386
Seryl_tRNA_N pfam02403
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ...
 256-330 2.57e-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: 2.57e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907085892 256 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPmllaELRLLRQRKDELEQRMSALQESRRELMVQLEGLM 330
Cdd:pfam02403  31 LLELDEKRRELQVELEELQAERNELSKEIGQAKKKKE----DADALIAEVKELKDELKALEAELKELEAELDKLL 101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 251-339 2.65e-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: 40.04  E-value: 2.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892  251 QQRQLIAELENKNREILQEIQRL-----RLEHEQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQ 325
Cdd:TIGR02168  383 TLRSKVAQLELQIASLNNEIERLearleRLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEA 462

                           90
                   ....*....|....
gi 1907085892  326 LEGLMKLLKEEEQK 339
Cdd:TIGR02168  463 LEELREELEEAEQA 476
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 247-345 2.65e-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: 39.14  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 247 DANKQQRQLIAELENKNREILQ---EIQRLRLEHEQASQPTpEKAQQNPMLLA---ELRLLRQRKDELEQRMSALQESRR 320
Cdd:COG1579    35 ELEDELAALEARLEAAKTELEDlekEIKRLELEIEEVEARI-KKYEEQLGNVRnnkEYEALQKEIESLKRRISDLEDEIL 113

                          90       100
                  ....*....|....*....|....*
gi 1907085892 321 ELMVQLEGLMKLLKEEEQKQAAQAT 345
Cdd:COG1579   114 ELMERIEELEEELAELEAELAELEA 138
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 256-344 3.09e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 39.82  E-value: 3.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 256 IAELENKNREILQEIQRL--RLEHEQASQPTPEKAQ------------QNPMLLAELRLLRQR----KDELEqrmsalqe 317
Cdd:PRK04778  277 LDEAEEKNEEIQERIDQLydILEREVKARKYVEKNSdtlpdflehakeQNKELKEEIDRVKQSytlnESELE-------- 348

                          90       100
                  ....*....|....*....|....*..
gi 1907085892 318 SRRELMVQLEGLMKLLKEEEQKQAAQA 344
Cdd:PRK04778  349 SVRQLEKQLESLEKQYDEITERIAEQE 375
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 250-343 3.42e-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: 38.75  E-value: 3.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 250 KQQRQLIAELENK------NRE---ILQEIQRLRLEHEQAsqptpEKAQQNpmLLAELRLLRQRKDELEQRMSALQESRR 320
Cdd:COG1579    69 EEVEARIKKYEEQlgnvrnNKEyeaLQKEIESLKRRISDL-----EDEILE--LMERIEELEEELAELEAELAELEAELE 141

                          90       100
                  ....*....|....*....|...
gi 1907085892 321 ELMVQLEGLMKLLKEEEQKQAAQ 343
Cdd:COG1579   142 EKKAELDEELAELEAELEELEAE 164
STAT5_CCD cd16855
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ...
 251-335 3.64e-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: 38.40  E-value: 3.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 251 QQRQLIAELENKNREI----------LQEIQRLRLEHEQASQptpekaQQNPMLLAELRLLRQRKDELEQRMSA----LQ 316
Cdd:cd16855    12 ELRQRTQETENDLRNLqqkqesfviqYQESQKIQAQLQQLQQ------QPQNERIELEQQLQQQKEQLEQLLNAkaqeLL 85

                          90
                  ....*....|....*....
gi 1907085892 317 ESRRELMVQLEGLMKLLKE 335
Cdd:cd16855    86 QLRMELADKFKKTIQLLSK 104
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 294-345 3.67e-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: 39.67  E-value: 3.67e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907085892  294 LLAELRLLRQRKDELEQRMSALQESRRELMVQLEglmkLLKEEEQKQAAQAT 345
Cdd:TIGR02169  693 LQSELRRIENRLDELSQELSDASRKIGEIEKEIE----QLEQEEEKLKERLE 740
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 250-343 3.79e-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: 39.13  E-value: 3.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 250 KQQRQLIAELENKNREIL----QEIQRLRLEHEQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQ 325
Cdd:pfam13868 123 EKQRQLREEIDEFNEEQAewkeLEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAE 202

                          90
                  ....*....|....*....
gi 1907085892 326 LEGL-MKLLKEEEQKQAAQ 343
Cdd:pfam13868 203 RDELrAKLYQEEQERKERQ 221
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
 224-318 3.88e-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: 3.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 224 YAARLAAEAGNMTRppTDASFNFDANKQQRQLIAELENKNREILQEIQRL--RLEHEQASQPTPEKAQQNPMLLAELRLL 301
Cdd:pfam03961 131 KAKELGSPAGTKTE--IEVGVDFPELKEKLEELEKELEELEEELEKLKKRlkKLPKKARGQLPPEKREQLEKLLETKNKL 208

                          90
                  ....*....|....*..
gi 1907085892 302 RQRKDELEQRMSALQES 318
Cdd:pfam03961 209 SEELEELEEELKELKEE 225
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
250-341 4.00e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 4.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 250 KQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 329
Cdd:COG4372    69 EQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER 148

                          90
                  ....*....|..
gi 1907085892 330 MKLLKEEEQKQA 341
Cdd:COG4372   149 EEELKELEEQLE 160
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
201-341 4.29e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 4.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 201 PTPTKSVLDSPSRLDEEHRLIARYAARLAAEAGNMTRPPTDASFNFDANKQQRQLIAELEnKNREILQEIQRLRLEHEQA 280
Cdd:COG4717   336 PEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAE-EYQELKEELEELEEQLEEL 414

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907085892 281 SQPTPEKAQQN--PMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL------MKLLKEEEQKQA 341
Cdd:COG4717   415 LGELEELLEALdeEELEEELEELEEELEELEEELEELREELAELEAELEQLeedgelAELLQELEELKA 483
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 251-344 4.72e-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: 4.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892  251 QQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEglm 330
Cdd:TIGR02168  723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK--- 799

                           90
                   ....*....|....
gi 1907085892  331 kllKEEEQKQAAQA 344
Cdd:TIGR02168  800 ---ALREALDELRA 810
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 251-344 5.81e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 38.80  E-value: 5.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892  251 QQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQqnpMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLM 330
Cdd:TIGR00618  779 ELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDED---ILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYE 855

                           90
                   ....*....|....
gi 1907085892  331 KLLKEEEQKQAAQA 344
Cdd:TIGR00618  856 ECSKQLAQLTQEQA 869
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 266-344 6.13e-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: 6.13e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907085892 266 ILQEIQRLrLEHEQASQPTPEKAQQnpmLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKEEEQKQAAQA 344
Cdd:cd16269   186 ILQADQAL-TEKEKEIEAERAKAEA---AEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERA 260
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
255-341 6.56e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 6.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 255 LIAELENKNREI-----------LQEIQRLRLEHEQASQPTPEKAQqnpmLLAELRLLRQRKDELEQRMSALQESRRELM 323
Cdd:COG4717    47 LLERLEKEADELfkpqgrkpelnLKELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKLE 122

                          90
                  ....*....|....*...
gi 1907085892 324 VQLEgLMKLLKEEEQKQA 341
Cdd:COG4717   123 KLLQ-LLPLYQELEALEA 139
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
248-344 7.21e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.34  E-value: 7.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 248 ANKQQRQLIAELENKNREI----------LQEIQRLRLEHEQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQE 317
Cdd:COG4372    71 ARSELEQLEEELEELNEQLqaaqaelaqaQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREE 150

                          90       100
                  ....*....|....*....|....*..
gi 1907085892 318 SRRELMVQLEGLMKLLKEEEQKQAAQA 344
Cdd:COG4372   151 ELKELEEQLESLQEELAALEQELQALS 177
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 213-315 7.30e-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: 7.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 213 RLDEEHRLIARYAARLAAEAgnmtrpptdasfnfdANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNP 292
Cdd:COG1196   692 ELELEEALLAEEEEERELAE---------------AEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEEL 756

                          90       100
                  ....*....|....*....|...
gi 1907085892 293 MLLAELRLLRQRKDELEQRMSAL 315
Cdd:COG1196   757 PEPPDLEELERELERLEREIEAL 779
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 255-344 7.34e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 38.50  E-value: 7.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892  255 LIAELENKNREILQEIQRlRLEhEQASQPTPEKAQQNPMLLAELRLLRQRKDELE------------QRMSA--LQESRR 320
Cdd:PRK10929   141 QLPQQQTEARRQLNEIER-RLQ-TLGTPNTPLAQAQLTALQAESAALKALVDELElaqlsannrqelARLRSelAKKRSQ 218

                           90       100
                   ....*....|....*....|....
gi 1907085892  321 ELMVQLEGLMKLLKEEEQKQAAQA 344
Cdd:PRK10929   219 QLDAYLQALRNQLNSQRQREAERA 242
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
246-344 7.94e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 37.96  E-value: 7.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 246 FDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQptpekaqqnpmllaelrLLRQRKDELEQRMSALQESRRELMVQ 325
Cdd:COG4372    16 FGLRPKTGILIAALSEQLRKALFELDKLQEELEQLRE-----------------ELEQAREELEQLEEELEQARSELEQL 78

                          90
                  ....*....|....*....
gi 1907085892 326 LEGLMKLLKEEEQKQAAQA 344
Cdd:COG4372    79 EEELEELNEQLQAAQAELA 97
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
 87-132 8.95e-03

Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239081  Cd Length: 48  Bit Score: 33.95  E-value: 8.95e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1907085892  87 VECSYCHCESMMGFRYRCQQCHN--YQLCQNCFwrgHASGAHSNQHQM 132
Cdd:cd02341     1 FKCDSCGIEPIPGTRYHCSECDDgdFDLCQDCV---VKGESHQEDHWL 45
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
210-344 9.71e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 37.58  E-value: 9.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085892 210 SPSRLDEEHRLIARyAARLAAEAgnmtrpptdasfnfdaNKQQRQLiaELENKNREILQEIQRLRLE----HEQASQpTP 285
Cdd:COG1340   128 EVLSPEEEKELVEK-IKELEKEL----------------EKAKKAL--EKNEKLKELRAELKELRKEaeeiHKKIKE-LA 187

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907085892 286 EKAQQnpmLLAELRLLRQRKDEL--------------EQRMSALQESRRELMVQLEGLMKLLKEEEQKQAAQA 344
Cdd:COG1340   188 EEAQE---LHEEMIELYKEADELrkeadelhkeiveaQEKADELHEEIIELQKELRELRKELKKLRKKQRALK 257
 
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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