NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|37577095|ref|NP_899204|]
View 

dystrobrevin beta isoform 4 [Homo sapiens]

Protein Classification

EFh_DTN and ZZ_dystrophin domain-containing protein( domain architecture ID 11610980)

EFh_DTN and ZZ_dystrophin domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
EFh_DTN cd16244
EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the ...
54-214 4.16e-112

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: 331.89  E-value: 4.16e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  54 DIWNMIEAFRDNGLNTLDHTTEISVSRLETVISSIYYQLNKRLPSTHQISVEQSISLLLNFMIAAYDSEGRGKLTVFSVK 133
Cdd:cd16244   1 DIWNVIEAFRENGLNTLDPTTELSVSRLETLLSSIYYQLNKRLPTTHQIDVDQSISLLLNWLLAAYDPEATGRLTVFSVK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095 134 AMLATMCGGKMLDKLRYVFSQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFGYTEHSVRTCFPQQRKIMLNMFLDTM 213
Cdd:cd16244  81 VALSTLCAGKLVDKLRYIFSQISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYNESAARSCFPGQSKVTVNDFLDVM 160

                .
gi 37577095 214 M 214
Cdd:cd16244 161 M 161
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
241-289 7.05e-25

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: 97.43  E-value: 7.05e-25
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 37577095 241 VECSYCRCESMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHSNQHQMKEH 289
Cdd:cd02334   1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
PRK12704 super family cl36166
phosphodiesterase; Provisional
431-525 4.65e-06

phosphodiesterase; Provisional


The actual alignment was detected with superfamily member PRK12704:

Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 49.39  E-value: 4.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  431 DANKQQRQLI----AELENKNREIL----QEIQRLRLEHEQasqptpEKAQQNPTLLAELRLLRQRKDELEQRMSALQES 502
Cdd:PRK12704  35 EAEEEAKRILeeakKEAEAIKKEALleakEEIHKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLELLEKR 108
                         90       100
                 ....*....|....*....|...
gi 37577095  503 RRELMVQLEELMKLLKEEEQKQA 525
Cdd:PRK12704 109 EEELEKKEKELEQKQQELEKKEE 131
 
Name Accession Description Interval E-value
EFh_DTN cd16244
EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the ...
54-214 4.16e-112

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: 331.89  E-value: 4.16e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  54 DIWNMIEAFRDNGLNTLDHTTEISVSRLETVISSIYYQLNKRLPSTHQISVEQSISLLLNFMIAAYDSEGRGKLTVFSVK 133
Cdd:cd16244   1 DIWNVIEAFRENGLNTLDPTTELSVSRLETLLSSIYYQLNKRLPTTHQIDVDQSISLLLNWLLAAYDPEATGRLTVFSVK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095 134 AMLATMCGGKMLDKLRYVFSQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFGYTEHSVRTCFPQQRKIMLNMFLDTM 213
Cdd:cd16244  81 VALSTLCAGKLVDKLRYIFSQISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYNESAARSCFPGQSKVTVNDFLDVM 160

                .
gi 37577095 214 M 214
Cdd:cd16244 161 M 161
EF-hand_2 pfam09068
EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
16-140 2.32e-62

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: stabilisation of the WW domain (pfam00397), enhancing dystroglycan binding.


Pssm-ID: 430392  Cd Length: 123  Bit Score: 201.60  E-value: 2.32e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095    16 RQLFIEMraQNFDVIRLSTYRTACKLRFVQKRCNLHLVDIWNMIEAFRDNGLNTLDHTTEISVSRLETVISSIYYQLNKR 95
Cdd:pfam09068   1 TELMQEL--QDFNNIRFSAYRTAMKLRALQKRLCLDLVDLWNLIEAFDEHGLNSLENDLLLDVSELETLLSSIYFALNKR 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 37577095    96 LPSTHQISVEQSISLLLNFMIAAYDSEGRGKLTVFSVKAMLATMC 140
Cdd:pfam09068  79 KPTTHQVNVPLSVDLLLNWLLNVYDPQRTGKIRVLSFKVALVLLC 123
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
241-289 7.05e-25

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: 97.43  E-value: 7.05e-25
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 37577095 241 VECSYCRCESMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHSNQHQMKEH 289
Cdd:cd02334   1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
237-281 7.94e-16

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: 71.32  E-value: 7.94e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 37577095    237 VFHPVECSYCRCEsMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHS 281
Cdd:smart00291   1 VHHSYSCDTCGKP-IVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
239-280 3.57e-07

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: 46.71  E-value: 3.57e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 37577095   239 HPVECSYCRCESMMGFRYRCQQCHNYQLCQNCFwRGHAGGPH 280
Cdd:pfam00569   3 KVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCF-QTHKGGNH 43
PRK12704 PRK12704
phosphodiesterase; Provisional
431-525 4.65e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 49.39  E-value: 4.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  431 DANKQQRQLI----AELENKNREIL----QEIQRLRLEHEQasqptpEKAQQNPTLLAELRLLRQRKDELEQRMSALQES 502
Cdd:PRK12704  35 EAEEEAKRILeeakKEAEAIKKEALleakEEIHKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLELLEKR 108
                         90       100
                 ....*....|....*....|...
gi 37577095  503 RRELMVQLEELMKLLKEEEQKQA 525
Cdd:PRK12704 109 EEELEKKEKELEQKQQELEKKEE 131
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
434-523 7.24e-06

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


Pssm-ID: 224259 [Multi-domain]  Cd Length: 294  Bit Score: 48.14  E-value: 7.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095 434 KQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEkaqqnptLLAELRLLRQRKDELEQRMSALQESRRELMVQLEEL 513
Cdd:COG1340  16 KQLKEEIEELKEKRDELRKEASELAEKRDELNAKVRE-------LREKAQELREERDEINEEVQELKEKRDEINAKLQEL 88
                        90
                ....*....|
gi 37577095 514 MKLLKEEEQK 523
Cdd:COG1340  89 RKEYRELKEK 98
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
441-523 1.45e-05

Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.


Pssm-ID: 428166 [Multi-domain]  Cd Length: 124  Bit Score: 44.71  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095   441 AELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKEE 520
Cdd:pfam04871  11 ASLKDENTELKAELQALSDQYQSLEQKKKAAESQAKELEAENKKLEEELKKLRAELSEEKQKEKEKQSELEDLLLLLGDL 90

                  ...
gi 37577095   521 EQK 523
Cdd:pfam04871  91 EEK 93
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
396-527 1.79e-05

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: 47.76  E-value: 1.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095    396 SRLDEEHRliaRYAARLAAEAGNVTRPPTDLSFNFDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN 475
Cdd:TIGR02169  801 SKLEEEVS---RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL 877
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 37577095    476 PTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKE-EEQKQAAQ 527
Cdd:TIGR02169  878 RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSElKAKLEALE 930
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
450-528 1.46e-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: 41.02  E-value: 1.46e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37577095 450 ILQEIQRLrLEHEQASQPTPEKAQQnptLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKEEEQKQAAQA 528
Cdd:cd16269 186 ILQADQAL-TEKEKEIEAERAKAEA---AEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERA 260
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
433-524 2.66e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 40.00  E-value: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095    433 NKQQRQLIAELEnKNREILQ-EIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSA-LQESRRELMVQL 510
Cdd:smart00787 139 MKLLEGLKEGLD-ENLEGLKeDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTeLDRAKEKLKKLL 217
                           90
                   ....*....|....
gi 37577095    511 EELMKLLKEEEQKQ 524
Cdd:smart00787 218 QEIMIKVKKLEELE 231
 
Name Accession Description Interval E-value
EFh_DTN cd16244
EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the ...
54-214 4.16e-112

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: 331.89  E-value: 4.16e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  54 DIWNMIEAFRDNGLNTLDHTTEISVSRLETVISSIYYQLNKRLPSTHQISVEQSISLLLNFMIAAYDSEGRGKLTVFSVK 133
Cdd:cd16244   1 DIWNVIEAFRENGLNTLDPTTELSVSRLETLLSSIYYQLNKRLPTTHQIDVDQSISLLLNWLLAAYDPEATGRLTVFSVK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095 134 AMLATMCGGKMLDKLRYVFSQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFGYTEHSVRTCFPQQRKIMLNMFLDTM 213
Cdd:cd16244  81 VALSTLCAGKLVDKLRYIFSQISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYNESAARSCFPGQSKVTVNDFLDVM 160

                .
gi 37577095 214 M 214
Cdd:cd16244 161 M 161
EFh_DTNB cd16250
EF-hand-like motif found in beta-dystrobrevin; Beta-dystrobrevin, also termed dystrobrevin ...
54-214 5.53e-111

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: 329.29  E-value: 5.53e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  54 DIWNMIEAFRDNGLNTLDHTTEISVSRLETVISSIYYQLNKRLPSTHQISVEQSISLLLNFMIAAYDSEGRGKLTVFSVK 133
Cdd:cd16250   1 DIWNMIEAFRDNGLNTLDHSTEISVSRLETIISSIYYQLNKRLPSTHQISVEQSISLLLNFMIAAYDSEGHGKLTVFSVK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095 134 AMLATMCGGKMLDKLRYVFSQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFGYTEHSVRTCFPQQRKIMLNMFLDTM 213
Cdd:cd16250  81 AMLATMCGGKILDKLRYTFSQMSDSNGLMIFLKFDQFLREVLKLPTAVFEGPSFGYTEHSVRTCFPQQKKIMLNMFLDTM 160

                .
gi 37577095 214 M 214
Cdd:cd16250 161 M 161
EFh_DTNA cd16249
EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin ...
54-214 2.26e-94

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: 286.41  E-value: 2.26e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  54 DIWNMIEAFRDNGLNTLDHTTEISVSRLETVISSIYYQLNKRLPSTHQISVEQSISLLLNFMIAAYDSEGRGKLTVFSVK 133
Cdd:cd16249   1 DIWNIIEALRENALNNLDPNTELNVARLEAVLSTIFYQLNKRMPTTHQINVEQSISLLLNFLLAAFDPEGHGKISVFAVK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095 134 AMLATMCGGKMLDKLRYVFSQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFGYTEHSVRTCFPQQRKIMLNMFLDTM 213
Cdd:cd16249  81 MALATLCGGKIMDKLRYIFSMISDSNGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSARSCFSQQKKVTLNGFLDTL 160

                .
gi 37577095 214 M 214
Cdd:cd16249 161 M 161
EF-hand_2 pfam09068
EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
16-140 2.32e-62

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: stabilisation of the WW domain (pfam00397), enhancing dystroglycan binding.


Pssm-ID: 430392  Cd Length: 123  Bit Score: 201.60  E-value: 2.32e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095    16 RQLFIEMraQNFDVIRLSTYRTACKLRFVQKRCNLHLVDIWNMIEAFRDNGLNTLDHTTEISVSRLETVISSIYYQLNKR 95
Cdd:pfam09068   1 TELMQEL--QDFNNIRFSAYRTAMKLRALQKRLCLDLVDLWNLIEAFDEHGLNSLENDLLLDVSELETLLSSIYFALNKR 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 37577095    96 LPSTHQISVEQSISLLLNFMIAAYDSEGRGKLTVFSVKAMLATMC 140
Cdd:pfam09068  79 KPTTHQVNVPLSVDLLLNWLLNVYDPQRTGKIRVLSFKVALVLLC 123
EFh_DMD_DYTN_DTN cd15901
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ...
54-214 1.25e-54

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: 182.86  E-value: 1.25e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  54 DIWNMIEAFRDNGLNTlDHTTEISVSRLETVISSIYYQLNKRLPstHQISVEQSISLLLNFMIAAYDSEGRGKLTVFSVK 133
Cdd:cd15901   1 DLSTVLSVFDRHGLSG-SQDSVLDCEELETILTELYIKLNKRRP--DLIDVPRASDLLLNWLLNLYDRNRTGCIRLLSVK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095 134 AMLATMCGGKMLDKLRYVFSQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFG--YTEHSVRTCFPQQRKIM---LNM 208
Cdd:cd15901  78 IALITLCAASLLDKYRYLFGQLADSSGFISRERLTQFLQDLLQIPDLIGESPAFGghNVEAAVESCFQLARSRVgvsEDT 157

                ....*.
gi 37577095 209 FLDTMM 214
Cdd:cd15901 158 FLSWLL 163
EF-hand_3 pfam09069
EF-hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
144-232 4.58e-43

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: stabilisation of the WW domain (pfam00397), enhancing dystroglycan binding.


Pssm-ID: 430393  Cd Length: 90  Bit Score: 148.98  E-value: 4.58e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095   144 MLDKLRYVFSQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFGYTEHSVRTCFPQQR---KIMLNMFLDTMMADppPQ 220
Cdd:pfam09069   1 LVDKYRYLFSQISDSNGLLDQRKLGLLLHELLQLPRQVGEVAAFGGIEPSVRSCFEQVGgkpKIELNHFLDWLMSE--PQ 78
                          90
                  ....*....|..
gi 37577095   221 CLVWLPLMHRLA 232
Cdd:pfam09069  79 SLVWLPVLHRLA 90
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
241-289 7.05e-25

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: 97.43  E-value: 7.05e-25
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 37577095 241 VECSYCRCESMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHSNQHQMKEH 289
Cdd:cd02334   1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
EFh_DMD_like cd16242
EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes ...
54-213 4.82e-21

EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes dystrophin and its two paralogs, utrophin and DRP-2. Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin also involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also termed dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homologue that increases dystrophic muscle function and reduces pathology. It is broadly expressed at both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with the dystroglycans (DGs) and the sarcoglycan-dystroglycans, sarcoglycans and sarcospan (SG-SSPN) subcomplex. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. DRP-2 is mainly expressed in the vertebrate central nervous system (CNS). It is associated with brain membrane fractions and highly enriched in the postsynaptic density. DRP-2 plays a role in the organization of central cholinergic synapses. It interacts with dystroglycan and L-Periaxin to form a transmembrane complex, which plays a role in Schwann cell-basal lamina interactions and in the regulation of the terminal stages of myelination. The dystrophins subfamily has been characterized by a compact cluster of domains comprising a WW domain, four EF-hand-like motifs and a ZZ-domain, followed by two syntrophin binding sites (SBSs) and a looser region with two coiled-coils.


Pssm-ID: 320000  Cd Length: 163  Bit Score: 90.37  E-value: 4.82e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  54 DIWNMIEAFRDNGLNTL-DHTteISVSRLETVISSIYYQLNKRLPstHQISVEQSISLLLNFMIAAYDSEGRGKLTVFSV 132
Cdd:cd16242   1 SLSTAIEAFDQHGLRAQnDKL--IDVPDMITCLTTIYEALEEEHP--TLVNVPLCVDLCLNWLLNVYDSGRSGKIRVLSF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095 133 KAMLATMCGGKMLDKLRYVFSQMSDSNGLMifskfDQ-----FLKEVLKLPTAVFEGPSFGYT--EHSVRTCFPQ---QR 202
Cdd:cd16242  77 KVGLVLLCNAHLEEKYRYLFSLIADPNGCV-----DQrrlglLLHDCIQIPRQLGEVAAFGGSniEPSVRSCFEKageKP 151
                       170
                ....*....|.
gi 37577095 203 KIMLNMFLDTM 213
Cdd:cd16242 152 EISAAHFLDWL 162
EFh_DAH cd16245
EF-hand-like motif found in Drosophila melanogaster discontinuous actin hexagon (DAH) and ...
67-198 2.98e-20

EF-hand-like motif found in Drosophila melanogaster discontinuous actin hexagon (DAH) and similar proteins; DAH, the product of the dah (discontinuous actin hexagon) gene, is a Drosophila homolog to vertebrate dystrotelin. It is tightly membrane-associated and highly phosphorylated in a time-dependent fashion. DAH plays an essential role in the process of cellularization, and is associated with vesicles that convene at the cleavage furrow. The absence of DAH leads the severe disruption of the cleavage furrows around the nuclei and development stalls. DAH contains a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils.


Pssm-ID: 320003 [Multi-domain]  Cd Length: 164  Bit Score: 88.12  E-value: 2.98e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  67 LNTLDHTTEISVSRLETVISSIYYQLNKRLPSThqISVEQSISLLLNFMIAAYDSEGRGKLTVFSVKAMLATMCGGKMLD 146
Cdd:cd16245  14 LSNSENNLCLPPDELEAVLHDIYFAAEKLGNFN--IDVDLATELLANLFLNVFDPERKKSISVLELKVFLTLLCGSSLQE 91
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 37577095 147 KLRYVFSQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFG--YTEHSVRTCF 198
Cdd:cd16245  92 KYLYLFQLLADHNNCVSRKRLEALLKSLAKLLSYLGEDVAFGshLIELAVEQCF 145
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
237-281 7.94e-16

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: 71.32  E-value: 7.94e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 37577095    237 VFHPVECSYCRCEsMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHS 281
Cdd:smart00291   1 VHHSYSCDTCGKP-IVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
EFh_DRP-2 cd16248
EF-hand-like motif found in dystrophin-related protein 2 (DRP-2); DRP-2 is a dystrophin ...
60-213 1.80e-12

EF-hand-like motif found in dystrophin-related protein 2 (DRP-2); DRP-2 is a dystrophin homologue mainly expressed in the vertebrate central nervous system (CNS). It is associated with brain membrane fractions and highly enriched in the postsynaptic density. DRP-2 plays a role in the organization of central cholinergic synapses. It interacts with dystroglycan and L-Periaxin to form a transmembrane complex, which plays a role in Schwann cell-basal lamina interactions and in the regulation of the terminal stages of myelination. Like dystrophin, DRP-2 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, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises only two spectrin repeats (SRs) and a WW domain.


Pssm-ID: 320006  Cd Length: 162  Bit Score: 65.59  E-value: 1.80e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  60 EAFRDNGLNTLDHTteISVSRLETVISSIYYQLNKRlpSTHQISVEQSISLLLNFMIAAYDSEGRGKLTVFSVKAMLATM 139
Cdd:cd16248   7 EIFTEHELQMSERV--MDVVEVIHCLTALYERLEEE--RGILVNVPLCVDMCLNWLLNVYDSGRNGKIRVLSFKTGIVCL 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37577095 140 CGGKMLDKLRYVFSQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFGYT--EHSVRTCF---PQQRKIMLNMFLDTM 213
Cdd:cd16248  83 CNADVKEKYQYLFSQVAGPGGQCDQRHLSLLLHEAIQIPRQLGEVAAFGGSnvEPSVRSCFrfaPGKPVIELSQFLEWM 161
EFh_DMD cd16246
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal ...
60-213 3.08e-12

EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). The dystrophin 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, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated abnormal cerebral diffusion and perfusion, acute Trypanosoma cruzi infection.


Pssm-ID: 320004  Cd Length: 162  Bit Score: 65.05  E-value: 3.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  60 EAFRDNGLNTLDHTTEISvsRLETVISSIYyqlnKRLPSTHQ--ISVEQSISLLLNFMIAAYDSEGRGKLTVFSVKAMLA 137
Cdd:cd16246   7 EALDQHNLKQNDQPMDIL--QIINCLTTIY----DRLEQEHNnlVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095 138 TMCGGKMLDKLRYVFSQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFGYT--EHSVRTCFP---QQRKIMLNMFLDT 212
Cdd:cd16246  81 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSniEPSVRSCFQfanNKPEIEAALFLDW 160

                .
gi 37577095 213 M 213
Cdd:cd16246 161 M 161
EFh_UTRO cd16247
EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 ...
60-213 9.56e-11

EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homologue that increases dystrophic muscle function and reduces pathology. It is broadly expressed at both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with the dystroglycans (DGs) and the sarcoglycan-dystroglycans, sarcoglycans and sarcospan (SG-SSPN) subcomplex. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, Utrophin 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, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs) and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs.


Pssm-ID: 320005  Cd Length: 162  Bit Score: 60.68  E-value: 9.56e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  60 EAFRDNGLNTLDHTteISVSRLETVISSIYYQLNKRlpstHQ--ISVEQSISLLLNFMIAAYDSEGRGKLTVFSVKAMLA 137
Cdd:cd16247   7 SVFKQHKLTQNDQL--LSVPDVINCLTTIYDGLEQK----HKdlVNVPLCVDMCLNWLLNVYDTGRTGKIRVLSLKIGLM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095 138 TMCGGKMLDKLRYVFSQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFGYT--EHSVRTCFPQQR---KIMLNMFLDT 212
Cdd:cd16247  81 SLSKGLLEEKYRYLFKEVAGPGDTCDQRQLGLLLHDAIQIPRQLGEVAAFGGSniEPSVRSCFQHANnkpEIDVKQFIDW 160

                .
gi 37577095 213 M 213
Cdd:cd16247 161 M 161
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
243-288 8.97e-09

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: 51.44  E-value: 8.97e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 37577095 243 CSYCRCESMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHSNQHQMKE 288
Cdd:cd02345   3 CSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLHIMYE 48
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
243-284 4.05e-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: 4.05e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 37577095 243 CSYCRCESMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHSNQH 284
Cdd:cd02335   3 CDYCSKDITGTIRIKCAECPDFDLCLECFSAGAEIGKHRNDH 44
EFh_DYTN cd16243
EF-hand-like motif found in dystrotelin and similar proteins; Dystrotelin is the vertebrate ...
65-198 1.54e-07

EF-hand-like motif found in dystrotelin and similar proteins; Dystrotelin is the vertebrate orthologue of Drosophila DAH, which is involved in the synchronised cellularization of thousands of nuclei in the syncytial early fly embryo (a specialised form of cytokinesis). Dystrotelin is mainly expressed in the developing central nervous system (CNS) and adult nervous and muscular tissues. Heterologously expressed dystrotelin protein localizes spontaneously to the cytoplasmic membrane, and possibly to the endoplasmic reticulum (ER). Dystrotelin is not critical for mammalian development. It may be involved in other forms of cytokinesis. Its N-terminal region contains 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. The C-terminal region is extremely divergent. Unlike other superfamily members, dystrophin or dystrobrevin, the residues directly involved in beta-dystroglycan binding are not conserved in dystrotelin, which makes it unlikely that dystrotelin interacts with this ligand. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize.


Pssm-ID: 320001  Cd Length: 163  Bit Score: 51.23  E-value: 1.54e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  65 NGLNT-LDHTTEISVSRLETVISSIYYQLNKRLP-STHQISVEQSISLLLnfmiAAYDSEGRGKLTVFSVKAMLATMCGG 142
Cdd:cd16243  10 NSLGGsIERTISLSVEEVSQALERLFQSASQEVPgQVSAEATEQTCRLLF----RLYDREQTGFVSLRSVEAALIALSGD 85
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095 143 KMLDKLRYVF----SQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFGYTEHSVRTCF 198
Cdd:cd16243  86 TLSAKYRALFqlyeSGQGGSSGSITRSGLRVLLQDLSQIPAVVQESHVFGNVETAVRSCF 145
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
241-289 2.73e-07

Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins.


Pssm-ID: 239069 [Multi-domain]  Cd Length: 46  Bit Score: 47.43  E-value: 2.73e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 37577095 241 VECSYCRCESMmGFRYRCQQCHNYQLCQNCFWRGHagGPHSNQHQMKEH 289
Cdd:cd02249   1 YSCDGCLKPIV-GVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
241-287 3.37e-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: 46.96  E-value: 3.37e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 37577095 241 VECSYCRCESMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHSNQHQMK 287
Cdd:cd02338   1 VSCDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFDHPMQ 47
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
239-280 3.57e-07

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: 46.71  E-value: 3.57e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 37577095   239 HPVECSYCRCESMMGFRYRCQQCHNYQLCQNCFwRGHAGGPH 280
Cdd:pfam00569   3 KVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCF-QTHKGGNH 43
PRK12704 PRK12704
phosphodiesterase; Provisional
431-525 4.65e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 49.39  E-value: 4.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  431 DANKQQRQLI----AELENKNREIL----QEIQRLRLEHEQasqptpEKAQQNPTLLAELRLLRQRKDELEQRMSALQES 502
Cdd:PRK12704  35 EAEEEAKRILeeakKEAEAIKKEALleakEEIHKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLELLEKR 108
                         90       100
                 ....*....|....*....|...
gi 37577095  503 RRELMVQLEELMKLLKEEEQKQA 525
Cdd:PRK12704 109 EEELEKKEKELEQKQQELEKKEE 131
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
243-289 5.24e-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: 43.60  E-value: 5.24e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 37577095 243 CSYCRCESMMGFRYRCQQCHNYQLCQNCFwrghaggpHSNQHQMkEH 289
Cdd:cd02339   3 CDTCRKQGIIGIRWKCAECPNYDLCTTCY--------HGDKHDL-EH 40
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
434-523 7.24e-06

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


Pssm-ID: 224259 [Multi-domain]  Cd Length: 294  Bit Score: 48.14  E-value: 7.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095 434 KQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEkaqqnptLLAELRLLRQRKDELEQRMSALQESRRELMVQLEEL 513
Cdd:COG1340  16 KQLKEEIEELKEKRDELRKEASELAEKRDELNAKVRE-------LREKAQELREERDEINEEVQELKEKRDEINAKLQEL 88
                        90
                ....*....|
gi 37577095 514 MKLLKEEEQK 523
Cdd:COG1340  89 RKEYRELKEK 98
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
437-527 7.51e-06

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 49.33  E-value: 7.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  437 RQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMKL 516
Cdd:COG1196  280 REELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEA 359
                         90
                 ....*....|.
gi 37577095  517 LKEEEQKQAAQ 527
Cdd:COG1196  360 KEELEEKLSAL 370
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
253-286 1.25e-05

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: 42.63  E-value: 1.25e-05
                        10        20        30
                ....*....|....*....|....*....|....
gi 37577095 253 GFRYRCQQCHNYQLCQNCfwrgHAGGPHSNqHQM 286
Cdd:cd02340  12 GVRYKCLVCPDYDLCESC----EAKGVHPE-HAM 40
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
441-523 1.45e-05

Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.


Pssm-ID: 428166 [Multi-domain]  Cd Length: 124  Bit Score: 44.71  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095   441 AELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKEE 520
Cdd:pfam04871  11 ASLKDENTELKAELQALSDQYQSLEQKKKAAESQAKELEAENKKLEEELKKLRAELSEEKQKEKEKQSELEDLLLLLGDL 90

                  ...
gi 37577095   521 EQK 523
Cdd:pfam04871  91 EEK 93
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
396-527 1.79e-05

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: 47.76  E-value: 1.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095    396 SRLDEEHRliaRYAARLAAEAGNVTRPPTDLSFNFDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN 475
Cdd:TIGR02169  801 SKLEEEVS---RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL 877
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 37577095    476 PTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKE-EEQKQAAQ 527
Cdd:TIGR02169  878 RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSElKAKLEALE 930
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
369-523 4.85e-05

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 46.29  E-value: 4.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095 369 SHLADEHALIASYVARLQHCARVLDSPSR-LDEEHRLIARYAARLAAEAGNVTRPPTDLSFNFDANKQQRQLIAELENKn 447
Cdd:COG0419 249 ERLEELKARLLEIESLELEALKIREEELReLERLLEELEEKIERLEELEREIEELEEELEGLRALLEELEELLEKLKSL- 327
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37577095 448 REILQEIQRLR--LEHEQASQpTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKEEEQK 523
Cdd:COG0419 328 EERLEKLEEKLekLESELEEL-AEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQELKEELAELSAA 404
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
396-529 6.52e-05

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 46.25  E-value: 6.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  396 SRLDEEHRLIARYAARLAAEAGNVTRPPTDLSFNFDA----NKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEK 471
Cdd:COG1196  337 EELEERETLLEELEQLLAELEEAKEELEEKLSALLEEleelFEALREELAELEAELAEIRNELEELKREIESLEERLERL 416
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 37577095  472 AQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKEEEQKQAAQAT 529
Cdd:COG1196  417 SERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQE 474
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
431-527 7.98e-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: 45.82  E-value: 7.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095    431 DANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQL 510
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
                           90
                   ....*....|....*..
gi 37577095    511 EELMKLLKEEEQKQAAQ 527
Cdd:TIGR02168  771 EEAEEELAEAEAEIEEL 787
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
440-510 9.37e-05

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 45.06  E-value: 9.37e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37577095  440 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN---PTLLAELRLLRQRKDELEQRMSALQESRRELMVQL 510
Cdd:PRK05431  30 LLELDEERRELQTELEELQAERNALSKEIGQAKRKGedaEALIAEVKELKEEIKALEAELDELEAELEELLLRI 103
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
397-523 1.01e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 45.48  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  397 RLDEEHRLIARYAARLAAEAGNVTrppTDLSFNFDANKQQRQLIAELENKNREILQEIQRL---RLEHEQASQptpEKAQ 473
Cdd:COG1196  734 QLQSRLEELEEELEELEEELEELQ---ERLEELEEELESLEEALAKLKEEIEELEEKRQALqeeLEELEEELE---EAER 807
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 37577095  474 QNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKEEEQK 523
Cdd:COG1196  808 RLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKE 857
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
396-529 1.11e-04

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 45.14  E-value: 1.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095 396 SRLDEEHRLIARYAARLAAEAGNVTRPPTDL----SFNFDANKQQRQLIAELENKNREILQEIQRLrleHEQASqptpEK 471
Cdd:COG0419 228 EELEQEIEALEERLAELEEEKERLEELKARLleieSLELEALKIREEELRELERLLEELEEKIERL---EELER----EI 300
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 37577095 472 AQQNpTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKEEEQKQAAQAT 529
Cdd:COG0419 301 EELE-EELEGLRALLEELEELLEKLKSLEERLEKLEEKLEKLESELEELAEEKNELAK 357
PRK12704 PRK12704
phosphodiesterase; Provisional
430-520 1.26e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.77  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  430 FDANKQQRQLIAELENKNREILQEIQRL---------RLEHEQASQptpEKAQQNptLLAELRLLRQRKDELEQRMSALQ 500
Cdd:PRK12704  60 LEAKEEIHKLRNEFEKELRERRNELQKLekrllqkeeNLDRKLELL---EKREEE--LEKKEKELEQKQQELEKKEEELE 134
                         90       100
                 ....*....|....*....|
gi 37577095  501 ESRRELMVQLEELMKLLKEE 520
Cdd:PRK12704 135 ELIEEQLQELERISGLTAEE 154
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
431-529 1.39e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 45.09  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  431 DANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQL 510
Cdd:COG1196  695 NELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEAL 774
                         90       100
                 ....*....|....*....|
gi 37577095  511 EELMKLLKE-EEQKQAAQAT 529
Cdd:COG1196  775 AKLKEEIEElEEKRQALQEE 794
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
440-529 1.64e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 44.71  E-value: 1.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  440 IAELENKNREILQEIQRLRLEHEQASQPTPEkaqqnptLLAELRLLRQRKDELEQRMSALQESRRELMVQLEEL---MKL 516
Cdd:COG1196  830 IEELEEEIEELEEKLDELEEELEELEKELEE-------LKEELEELEAEKEELEDELKELEEEKEELEEELRELeseLAE 902
                         90
                 ....*....|...
gi 37577095  517 LKEEEQKQAAQAT 529
Cdd:COG1196  903 LKEEIEKLRERLE 915
YkyA pfam10368
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ...
433-528 2.13e-04

Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defense system. It is thus likely to belong to pathways important for pathogenicity.


Pssm-ID: 431235 [Multi-domain]  Cd Length: 185  Bit Score: 42.58  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095   433 NKQQRQLIaELENKNREILQEIQRLRLEHEQASQPTPEKAQQNptllaelrlLRQRKDELEQRMSALQESRRElMVQLEE 512
Cdd:pfam10368  21 EEQQEPLV-ELEKKEQELYEEIIELGMDEFDEIKKLSDEALEN---------VEEREELLEKEKESIEEAKEE-FKKIKE 89
                          90
                  ....*....|....*.
gi 37577095   513 LMKLLKEEEQKQAAQA 528
Cdd:pfam10368  90 IIEEIEDEELKKEAEE 105
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
241-271 2.95e-04

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: 38.72  E-value: 2.95e-04
                        10        20        30
                ....*....|....*....|....*....|.
gi 37577095 241 VECSYCRCESMMGFRYRCQQCHNYQLCQNCF 271
Cdd:cd02344   1 VTCDGCQMFPINGPRFKCRNCDDFDFCENCF 31
ZZ_EF cd02343
Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif ...
248-286 3.74e-04

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


Pssm-ID: 239083  Cd Length: 48  Bit Score: 38.45  E-value: 3.74e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 37577095 248 CESMMGF-RYRCQQCHNYQLCQNCFWRGHAGGPHSNQHQM 286
Cdd:cd02343   6 CDEIAPWhRYRCLQCTDMDLCKTCFLGGVKPEGHEDDHEM 45
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
437-528 3.75e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 43.55  E-value: 3.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  437 RQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMKL 516
Cdd:COG1196  778 KEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKE 857
                         90
                 ....*....|...
gi 37577095  517 LKE-EEQKQAAQA 528
Cdd:COG1196  858 LEElKEELEELEA 870
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
433-504 4.14e-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: 41.92  E-value: 4.14e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37577095   433 NKQQRQLIAELENKNREILQEIQRLRLEHE---QASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRR 504
Cdd:TIGR04211  89 LAELRQENQELKQQLSTLEAELEELQKELErikQISANAIELDEENRELREELAELKQENEALEAENERLQENEQ 163
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
432-531 4.44e-04

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: 43.51  E-value: 4.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095    432 ANKQQRQLIAELENKNREILQEIQRLRLEHEQASqptpekaqqnptllAELRLLRQRKDELEQRMSALQESRRELMVQLE 511
Cdd:TIGR02168  289 ELYALANEISRLEQQKQILRERLANLERQLEELE--------------AQLEELESKLDELAEELAELEEKLEELKEELE 354
                           90       100
                   ....*....|....*....|
gi 37577095    512 ELMKLLKEEEQKQAAQATGS 531
Cdd:TIGR02168  355 SLEAELEELEAELEELESRL 374
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
405-535 4.59e-04

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: 430825 [Multi-domain]  Cd Length: 305  Bit Score: 42.42  E-value: 4.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095   405 IARYAARLAAEAGNVTRPPTDLSFNFDANKQQRQliaELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRL 484
Cdd:pfam09787  77 LQELEAQQQEEAESSREQLQDLEEQLATERQARR---EAEAELERLQEELRYLEEELRRTKATLQSRIKDREAEIEKLRN 153
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37577095   485 LRQRK-------DELEQRMSALQESRRELMVQLEEL--------MKLLKEEEQKQAAQATGSPHTS 535
Cdd:pfam09787 154 QLTNKsqssssqSELENRLHQLTESLIQKQTMLEALsteknslvLQLERLEQQIKELQGEASNGTS 219
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
433-523 5.53e-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: 43.09  E-value: 5.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095   433 NKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEE 512
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQ 486
                          90
                  ....*....|.
gi 37577095   513 LMKLLKEEEQK 523
Cdd:TIGR04523 487 KQKELKSKEKE 497
mukB PRK04863
chromosome partition protein MukB;
434-519 5.77e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.02  E-value: 5.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095   434 KQQRQLIAELENKNREILQEIQRLrleHEQASQ-----------PTPEkaqqnptllAELRLLRQRKDELEQRMSALQE- 501
Cdd:PRK04863  792 RAEREELAERYATLSFDVQKLQRL---HQAFSRfigshlavafeADPE---------AELRQLNRRRVELERALADHESq 859
                          90       100
                  ....*....|....*....|
gi 37577095   502 --SRRELMVQLEELMKLLKE 519
Cdd:PRK04863  860 eqQQRSQLEQAKEGLSALNR 879
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
434-523 6.00e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 43.16  E-value: 6.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  434 KQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEEL 513
Cdd:COG1196  789 QALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEEL 868
                         90
                 ....*....|
gi 37577095  514 MKLLKEEEQK 523
Cdd:COG1196  869 EAEKEELEDE 878
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
432-527 6.76e-04

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 42.83  E-value: 6.76e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095 432 ANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLE 511
Cdd:COG0419 637 SELEKLNLQAELEELLQAALEELEEKVEELEAEIRRELQRIENEEQLEEKLEELEQLEEELEQLREELEELLKKLGEIEQ 716
                        90
                ....*....|....*.
gi 37577095 512 ELMKLLKEEEQKQAAQ 527
Cdd:COG0419 717 LIEELESRKAELEELK 732
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
364-530 7.30e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 42.78  E-value: 7.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  364 SQDIPSHLADEHALIASYVARLQHCARVLDSpsRLDEEHRLIARYAARLAAEAGNVTRpptDLSFNFDANKQQRQLIAEL 443
Cdd:COG1196  342 RETLLEELEQLLAELEEAKEELEEKLSALLE--ELEELFEALREELAELEAELAEIRN---ELEELKREIESLEERLERL 416
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  444 ENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKE-EEQ 522
Cdd:COG1196  417 SERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRlEAE 496

                 ....*...
gi 37577095  523 KQAAQATG 530
Cdd:COG1196  497 QRASQGVR 504
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
440-526 7.61e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 42.78  E-value: 7.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  440 IAELENKNREILQEIQRLRLEHEQAS--------QPTPEKAQQN-------------PTLLAELRLLRQRKDELEQRMSA 498
Cdd:COG1196  690 LKSLKNELRSLEDLLEELRRQLEELErqleelkrELAALEEELEqlqsrleeleeelEELEEELEELQERLEELEEELES 769
                         90       100
                 ....*....|....*....|....*...
gi 37577095  499 LQESRRELMVQLEELMKLLKEEEQKQAA 526
Cdd:COG1196  770 LEEALAKLKEEIEELEEKRQALQEELEE 797
COG1579 COG1579
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ...
432-527 7.75e-04

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


Pssm-ID: 224495 [Multi-domain]  Cd Length: 239  Bit Score: 41.58  E-value: 7.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095 432 ANKQQRqlIAELENKNREILQEIQRLRLEHEQAsqptpEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLE 511
Cdd:COG1579  48 EALEIE--LEDLENQVSQLESEIQEIRERIKRA-----EEKLSAVKDERELRALNIEIQIAKERINSLEDELAELMEEIE 120
                        90
                ....*....|....*.
gi 37577095 512 ELMKLLKEEEQKQAAQ 527
Cdd:COG1579 121 KLEKEIEDLKERLERL 136
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
428-524 8.27e-04

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: 42.35  E-value: 8.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095    428 FNFDANKQQRQLiAELENKNREILQEIQRLRLEHEQASQptpEKAQQNPTLLAelrlLRQRKDELEQRMSALQESRRELM 507
Cdd:TIGR02168  244 LQEELKEAEEEL-EELTAELQELEEKLEELRLEVSELEE---EIEELQKELYA----LANEISRLEQQKQILRERLANLE 315
                           90
                   ....*....|....*..
gi 37577095    508 VQLEELMKLLKEEEQKQ 524
Cdd:TIGR02168  316 RQLEELEAQLEELESKL 332
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
359-528 8.47e-04

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


Pssm-ID: 227278 [Multi-domain]  Cd Length: 420  Bit Score: 42.02  E-value: 8.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095 359 KRLQYSQDIPSHLADEHALIASYVARLQHcaRVLDSPSRLDEEHRLIARYAARLAAEAgnvtrpptdlsfnfDANKQQRQ 438
Cdd:COG4942  52 KKIREQQDQRAKLEKQLKSLETEIASLEA--QLIETADDLKKLRKQIADLNARLNALE--------------VQEREQRR 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095 439 LIAELenknreiLQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLL----RQRKDELEQRMSALQESRRELMVQLEELM 514
Cdd:COG4942 116 RLAEQ-------LAALQRSGRNPPPALLVSPEDAQRSVRLAIYYGALnparAERIDALKATLKQLAAVRAEIAAEQAELT 188
                       170
                ....*....|....
gi 37577095 515 KLLKEEEQKQAAQA 528
Cdd:COG4942 189 TLLSEQRAQQAKLA 202
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
409-526 9.24e-04

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: 42.35  E-value: 9.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095    409 AARLAAEAGNVTRPPTDLSFNFDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLL----AELRL 484
Cdd:TIGR02168  735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdelrAELTL 814
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 37577095    485 LRQRKDELEQRMSALQESRRELMVQLEELMKLLKEEEQKQAA 526
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
439-523 1.17e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  439 LIAELENKNREILQEIQRLRLEHEQASQPTpEKAQQNPTLLAELRL----LRQRKDELEQRMSALQESRRELMVQLEELM 514
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELREEL-EKLEKEVKELEELKEeieeLEKELESLEGSKRKLEEKIRELEERIEELK 272

                 ....*....
gi 37577095  515 KLLKEEEQK 523
Cdd:PRK03918 273 KEIEELEEK 281
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
437-523 1.31e-03

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 41.67  E-value: 1.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095 437 RQLIAELENKNREILQEIQRL------RLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRElmvqL 510
Cdd:COG0419 653 QAALEELEEKVEELEAEIRRElqrienEEQLEEKLEELEQLEEELEQLREELEELLKKLGEIEQLIEELESRKAE----L 728
                        90
                ....*....|...
gi 37577095 511 EELMKLLKEEEQK 523
Cdd:COG0419 729 EELKKELEKLEKA 741
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
434-527 1.38e-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: 433539 [Multi-domain]  Cd Length: 341  Bit Score: 41.05  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095   434 KQQRQLIAELENKNREIL----QEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQ 509
Cdd:pfam13868 123 EKQRQLREEIDEFNEEQAkwkeLEKEEEKEEDLRILEYLKEKAEREEEREAERREIKEEKEREIARLRAQQEKAQDEKAE 202
                          90
                  ....*....|....*....
gi 37577095   510 LEEL-MKLLKEEEQKQAAQ 527
Cdd:pfam13868 203 RDELrAKLYQEEQERKWRQ 221
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
450-528 1.46e-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: 41.02  E-value: 1.46e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37577095 450 ILQEIQRLrLEHEQASQPTPEKAQQnptLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKEEEQKQAAQA 528
Cdd:cd16269 186 ILQADQAL-TEKEKEIEAERAKAEA---AEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERA 260
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
449-528 1.61e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 40.98  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095   449 EILQEIQRLRLEHEQASQPTPE--------KAQQNPTLLAElrllRQRKDELEQRMSALQESRRElmvqleELMKLLKEE 520
Cdd:TIGR02794  47 AVAQQANRIQQQKKPAAKKEQErqkkleqqAEEAEKQRAAE----QARQKELEQRAAAEKAAKQA------EQAAKQAEE 116

                  ....*...
gi 37577095   521 EQKQAAQA 528
Cdd:TIGR02794 117 KQKQAEEA 124
MscK COG3264
Small-conductance mechanosensitive channel [Cell wall/membrane/envelope biogenesis];
432-529 1.64e-03

Small-conductance mechanosensitive channel [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 225803 [Multi-domain]  Cd Length: 835  Bit Score: 41.60  E-value: 1.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095 432 ANKQQRQLIAELENKNREILQ---EIQRLRLEHEQASQPTPEKAQQNPTLLAEL--------RLLRQRKDELEQRMSALQ 500
Cdd:COG3264   6 NNVLQELLQSRRELLTAESAQleaALQLLQEAVNSKRQEEAEPAAEEAELQAELiqqelainDQLSQALNQQTERLNALA 85
                        90       100       110
                ....*....|....*....|....*....|
gi 37577095 501 ESRRELMVQLEELMKLLKE-EEQKQAAQAT 529
Cdd:COG3264  86 SDDRQLANLLLQLLQSSRTiREQIAVLRGS 115
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
411-525 1.72e-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: 41.58  E-value: 1.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095    411 RLAAEAGNVTRPPTDLSFNFDANKQQrqlIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAE-------LR 483
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERR---LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNErasleeaLA 890
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 37577095    484 LLRQRKDELEQRMSALQESRRELMVQLEELMKLLKEEEQKQA 525
Cdd:TIGR02168  891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
371-523 1.73e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 41.62  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  371 LADEHALIASYVARLQHCARVLdspSRLDEEhrlIARYAARLAAEAGNVTRPPTDLSFNFDANKQQRQLIAELENKNREI 450
Cdd:COG1196  725 LAALEEELEQLQSRLEELEEEL---EELEEE---LEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEEL 798
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37577095  451 LQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKEEEQK 523
Cdd:COG1196  799 EEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAE 871
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
400-528 1.73e-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: 41.49  E-value: 1.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095    400 EEHRLIARYAARLAAEAGNVTRpptdlsfnfdANKQQRQLIAELENKNREILQEIQRlRLEHEQASQPTPEKAQQNPTLL 479
Cdd:TIGR00618  283 QERINRARKAAPLAAHIKAVTQ----------IEQQAQRIHTELQSKMRSRAKLLMK-RAAHVKQQSSIEEQRRLLQTLH 351
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37577095    480 AELRLLRQ-------------RKDELEQRMSALQEsRRELMVQLEELMKLLKEEEQKQAAQA 528
Cdd:TIGR00618  352 SQEIHIRDahevatsireiscQQHTLTQHIHTLQQ-QKTTLTQKLQSLCKELDILQREQATI 412
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
365-528 1.84e-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: 41.21  E-value: 1.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095    365 QDIPSHLADEHALIASYVARLQHCARVLDSPSR-----LDEEHRLIARYAARLAAEAGNVTRpptdlsfNFDANKQQRQl 439
Cdd:TIGR02169  247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdlGEEEQLRVKEKIGELEAEIASLER-------SIAEKERELE- 318
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095    440 iaELENKNREILQEIQRLRLEHEQasqptpekaqqnptLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKE 519
Cdd:TIGR02169  319 --DAEERLAKLEAEIDKLLAEIEE--------------LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE 382
                          170
                   ....*....|.
gi 37577095    520 --EEQKQAAQA 528
Cdd:TIGR02169  383 trDELKDYREK 393
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
434-529 1.86e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 41.24  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  434 KQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRREL---MVQL 510
Cdd:COG1196  796 EELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELeaeKEEL 875
                         90
                 ....*....|....*....
gi 37577095  511 EELMKLLKEEEQKQAAQAT 529
Cdd:COG1196  876 EDELKELEEEKEELEEELR 894
Seryl_tRNA_N pfam02403
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ...
440-514 2.00e-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: 37.95  E-value: 2.00e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37577095   440 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPtllaELRLLRQRKDELEQRMSALQESRRELMVQLEELM 514
Cdd:pfam02403  31 LLELDEKRRELQVELEELQAERNELSKEIGQAKKKKE----DADALIAEVKELKDELKALEAELKELEAELDKLL 101
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
396-526 2.05e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 41.24  E-value: 2.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  396 SRLDEEHRLIARYAARLAAEAGNVTRPPTDLSFNFDANKQQrqlIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN 475
Cdd:COG1196  719 EELKRELAALEEELEQLQSRLEELEEELEELEEELEELQER---LEELEEELESLEEALAKLKEEIEELEEKRQALQEEL 795
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 37577095  476 PTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKEEEQKQAA 526
Cdd:COG1196  796 EELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDE 846
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
435-528 2.33e-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: 41.11  E-value: 2.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095    435 QQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQnptLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELM 514
Cdd:TIGR00618  779 ELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDI---LNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYE 855
                           90
                   ....*....|....
gi 37577095    515 KLLKEEEQKQAAQA 528
Cdd:TIGR00618  856 ECSKQLAQLTQEQA 869
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
430-523 2.38e-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: 41.21  E-value: 2.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095    430 FDANKQQ--------RQLIAELENKNREILQEIQRLRLEHEQAS-----QPTPEKAQQNpTLLAELRLLRQRKDELEQRM 496
Cdd:TIGR02169  168 FDRKKEKaleeleevEENIERLDLIIDEKRQQLERLRREREKAEryqalLKEKREYEGY-ELLKEKEALERQKEAIERQL 246
                           90       100       110
                   ....*....|....*....|....*....|....
gi 37577095    497 SALQESRRELMVQLEELMK-------LLKEEEQK 523
Cdd:TIGR02169  247 ASLEEELEKLTEEISELEKrleeieqLLEELNKK 280
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
434-523 2.63e-03

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 40.90  E-value: 2.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095 434 KQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAE-LRLLRQRKDELEQRMSALQESRRELMVQLEE 512
Cdd:COG0419 342 ESELEELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEaIQELKEELAELSAALEEIQEELEELEKELEE 421
                        90
                ....*....|.
gi 37577095 513 LMKLLKEEEQK 523
Cdd:COG0419 422 LERELEELEEE 432
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
433-524 2.66e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 40.00  E-value: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095    433 NKQQRQLIAELEnKNREILQ-EIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSA-LQESRRELMVQL 510
Cdd:smart00787 139 MKLLEGLKEGLD-ENLEGLKeDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTeLDRAKEKLKKLL 217
                           90
                   ....*....|....
gi 37577095    511 EELMKLLKEEEQKQ 524
Cdd:smart00787 218 QEIMIKVKKLEELE 231
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
440-528 2.74e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 40.59  E-value: 2.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  440 IAELENKNREILQEIQRL--RLEHEQASQPTPEKAQ------------QNPTLLAELRLLRQR----KDELEqrmsalqe 501
Cdd:PRK04778 277 LDEAEEKNEEIQERIDQLydILEREVKARKYVEKNSdtlpdflehakeQNKELKEEIDRVKQSytlnESELE-------- 348
                         90       100
                 ....*....|....*....|....*..
gi 37577095  502 SRRELMVQLEELMKLLKEEEQKQAAQA 528
Cdd:PRK04778 349 SVRQLEKQLESLEKQYDEITERIAEQE 375
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
425-523 2.74e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 40.85  E-value: 2.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  425 DLSFNFDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRR 504
Cdd:COG1196  717 QLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELE 796
                         90
                 ....*....|....*....
gi 37577095  505 ELMVQLEELMKLLKEEEQK 523
Cdd:COG1196  797 ELEEELEEAERRLDALERE 815
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
435-523 3.18e-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: 40.81  E-value: 3.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095    435 QQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELM 514
Cdd:TIGR02168  723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802

                   ....*....
gi 37577095    515 KLLKEEEQK 523
Cdd:TIGR02168  803 EALDELRAE 811
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
434-525 3.30e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 40.47  E-value: 3.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  434 KQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQL-EE 512
Cdd:COG1196  305 SLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALrEE 384
                         90
                 ....*....|...
gi 37577095  513 LMKLLKEEEQKQA 525
Cdd:COG1196  385 LAELEAELAEIRN 397
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
437-523 3.36e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 40.47  E-value: 3.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  437 RQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMKL 516
Cdd:COG1196  848 EEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVE 927

                 ....*..
gi 37577095  517 LKEEEQK 523
Cdd:COG1196  928 LPELEEE 934
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
431-525 3.55e-03

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 40.51  E-value: 3.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095 431 DANKQQRQLIAELENKNREIL---QEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELM 507
Cdd:COG0419 222 QEEQEEEELEQEIEALEERLAeleEEKERLEELKARLLEIESLELEALKIREEELRELERLLEELEEKIERLEELEREIE 301
                        90
                ....*....|....*...
gi 37577095 508 VQLEELMKLLKEEEQKQA 525
Cdd:COG0419 302 ELEEELEGLRALLEELEE 319
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
450-527 3.85e-03

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 397124 [Multi-domain]  Cd Length: 297  Bit Score: 39.58  E-value: 3.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37577095   450 ILQEIQRLrLEHEQASQPTPEKAQqnpTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMKllKEEEQKQAAQ 527
Cdd:pfam02841 192 ILQTDQAL-TAKEKAIEAERAKAE---AAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIEKME--AEREQLLAEQ 263
STAT5_CCD cd16855
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ...
435-519 3.97e-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: 38.78  E-value: 3.97e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095 435 QQRQLIAELENKNREI----------LQEIQRLRLEHEQASQptpekaQQNPTLLAELRLLRQRKDELEQRMSA----LQ 500
Cdd:cd16855  12 ELRQRTQETENDLRNLqqkqesfviqYQESQKIQAQLQQLQQ------QPQNERIELEQQLQQQKEQLEQLLNAkaqeLL 85
                        90
                ....*....|....*....
gi 37577095 501 ESRRELMVQLEELMKLLKE 519
Cdd:cd16855  86 QLRMELADKFKKTIQLLSK 104
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
440-528 4.19e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 40.14  E-value: 4.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095    440 IAELENKNREILQEIQRlRLEHEQASQPTPEKAQQ-----NPTLLAELRLLRQRKDELEQRmsalqesRRELMVQLEELM 514
Cdd:pfam01576  347 LQEMRQKHTQALEELTE-QLEQAKRNKASLEKAKQaleseNAELQAELRSLQQAKQDSEHK-------RKKLEGQLQELQ 418
                           90
                   ....*....|....
gi 37577095    515 KLLKEEEQKQAAQA 528
Cdd:pfam01576  419 SRLSESERQRAELA 432
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
241-286 4.21e-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: 35.49  E-value: 4.21e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 37577095 241 VECSYCRCESMMGFRYRCQQCHN--YQLCQNCFwrgHAGGPHSNQHQM 286
Cdd:cd02341   1 FKCDSCGIEPIPGTRYHCSECDDgdFDLCQDCV---VKGESHQEDHWL 45
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
431-528 4.47e-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: 40.05  E-value: 4.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095    431 DANKQQRQLIAELENKNREILQ---EIQRLRLEHEQASQPTPEKAQQNPTLLAELRLL----RQRKDELEQRMSALQESR 503
Cdd:TIGR02169  319 DAEERLAKLEAEIDKLLAEIEElerEIEEERKRRDKLTEEYAELKEELEDLRAELEEVdkefAETRDELKDYREKLEKLK 398
                           90       100
                   ....*....|....*....|....*
gi 37577095    504 RELMVQLEELMKLLKEEEQKQAAQA 528
Cdd:TIGR02169  399 REINELKRELDRLQEELQRLSEELA 423
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
436-529 4.55e-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: 40.05  E-value: 4.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095    436 QRQLIAELENKNREIlQEIQRLRleheqasqptpekaqqnPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEElmk 515
Cdd:TIGR02169  669 SRSEPAELQRLRERL-EGLKREL-----------------SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ--- 727
                           90
                   ....*....|....
gi 37577095    516 lLKEEEQKQAAQAT 529
Cdd:TIGR02169  728 -LEQEEEKLKERLE 740
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
434-526 5.23e-03

Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 39.62  E-value: 5.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095 434 KQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEel 513
Cdd:COG4372  91 GTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAQQELARLTKQAQDLQTRLKTLAEQRRQLEAQAQ-- 168
                        90
                ....*....|...
gi 37577095 514 mKLLKEEEQKQAA 526
Cdd:COG4372 169 -SLQASQKQLQAS 180
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
431-520 5.42e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 39.70  E-value: 5.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  431 DANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEK-------AQQNPTLLAELRLLRQRKDELEQRMSALQESR 503
Cdd:COG1196  288 EELLELKEEIEELEGEISLLRERLEELENELEELEERLEELkekiealKEELEERETLLEELEQLLAELEEAKEELEEKL 367
                         90
                 ....*....|....*..
gi 37577095  504 RELMVQLEELMKLLKEE 520
Cdd:COG1196  368 SALLEELEELFEALREE 384
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
435-523 5.83e-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: 39.65  E-value: 5.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095    435 QQRQLIAELENKNREILQEIQRL-----RLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQ 509
Cdd:TIGR02168  383 TLRSKVAQLELQIASLNNEIERLearleRLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEA 462
                           90
                   ....*....|....
gi 37577095    510 LEELMKLLKEEEQK 523
Cdd:TIGR02168  463 LEELREELEEAEQA 476
V_HD-PTP_like cd09234
Protein-interacting V-domain of mammalian His-Domain type N23 protein tyrosine phosphatase and ...
437-538 6.84e-03

Protein-interacting V-domain of mammalian His-Domain type N23 protein tyrosine phosphatase and related domains; This family contains the V-shaped (V) domain of mammalian His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23) and related domains. It belongs to the V_Alix_like superfamily which includes the V domains of Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, mammalian Alix (apoptosis-linked gene-2 interacting protein X/ also known as apoptosis-linked gene-2 interacting protein 1, AIP1), and related domains. HD_PTP interacts with the ESCRT (Endosomal Sorting Complexes Required for Transport) system, and participates in cell migration and endosomal trafficking. The related Alix V-domain (belonging to a different family in this superfamily) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. In addition to the V-domain, HD_PTP also has an N-terminal Bro1-like domain, a proline-rich region (PRR), a catalytically inactive tyrosine phosphatase domain, and a region containing a PEST motif. Bro1-like domains bind components of the ESCRT-III complex, specifically to CHMP4 in the case of HD-PTP. The Bro1-like domain of HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate frequently absent in human kidney, breast, lung, and cervical tumors. This family also contains Drosophila Myopic, which promotes epidermal growth factor receptor (EGFR) signaling, and Caenorhabditis elegans (enhancer of glp-1) EGO-2 which promotes Notch signaling.


Pssm-ID: 185747 [Multi-domain]  Cd Length: 337  Bit Score: 38.81  E-value: 6.84e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095 437 RQLIAELENKNREILQEIQRLRLEHEQasQPTPEKAQQNPTLLAELRL-LRQRKD---ELEQRMSALQESRRELMVQLEE 512
Cdd:cd09234  20 REVVSEIEDKDEELDQFLSSLQLDPLN--VMDMDGQFELPQDLVERCAaLSVRPDtikNLVEAMGELSDVYQDVEAMLNE 97
                        90       100
                ....*....|....*....|....*...
gi 37577095 513 LMKLLKEEEQ--KQAAQATGSPHTSPTH 538
Cdd:cd09234  98 IESLLEEEELqeKEFQEAVGKRGSSIAH 125
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
432-525 7.10e-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: 39.65  E-value: 7.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095    432 ANKQQRQLIAELE--NKNREILQEIQRLrLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELmvq 509
Cdd:TIGR02168  398 LNNEIERLEARLErlEDRRERLQQEIEE-LLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEA--- 473
                           90
                   ....*....|....*.
gi 37577095    510 LEELMKLLKEEEQKQA 525
Cdd:TIGR02168  474 EQALDAAERELAQLQA 489
DASH_Spc19 pfam08287
Spc19; Spc19 is a component of the DASH complex. The DASH complex associates with the spindle ...
433-499 7.47e-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: 37.23  E-value: 7.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37577095   433 NKQQRQLiAELENKNreilqEIQRLRLEH------------EQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSAL 499
Cdd:pfam08287  76 EKLERRE-ETLKAKL-----ELNEGRLSNaessardeegsqESDEEVNSSEGDATNEELERLRALRQKKERLKYSLERL 148
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
378-520 7.70e-03

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteristic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 38.90  E-value: 7.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095   378 IASYVARLQHCARVLDSPSRLDEEHRL--------IARYAARLAAEAGNVTRPPTDLSFNFDANKQQRQLIAELE---NK 446
Cdd:pfam19220  85 LEELVARLAKLEAALREAEAAKEELRIelrdktaqAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEgelAT 164
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37577095   447 NREIL----QEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKEE 520
Cdd:pfam19220 165 ARERLalleQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAE 242
PRK08476 PRK08476
F0F1 ATP synthase subunit B'; Validated
441-527 7.94e-03

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 181442 [Multi-domain]  Cd Length: 141  Bit Score: 36.98  E-value: 7.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  441 AELENKNREILQEIQRLRLEHEQASQptpeKAQQNPTLLAElRLLRQRKDELEQRMSA----LQESRRELMVQLEELMKL 516
Cdd:PRK08476  55 SDVSEIEHEIETILKNAREEANKIRQ----KAIAKAKEEAE-KKIEAKKAELESKYEAfakqLANQKQELKEQLLSQMPE 129
                         90
                 ....*....|.
gi 37577095  517 LKEEEQKQAAQ 527
Cdd:PRK08476 130 FKEALNAKLSK 140
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
442-527 9.59e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 38.93  E-value: 9.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095  442 ELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRREL---MVQLEELMKLLK 518
Cdd:COG1196  236 ELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELegeISLLRERLEELE 315

                 ....*....
gi 37577095  519 EEEQKQAAQ 527
Cdd:COG1196  316 NELEELEER 324
mukB PRK04863
chromosome partition protein MukB;
435-529 9.67e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.17  E-value: 9.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095   435 QQRQLIAELENKNREiLQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRllrQRKDELEQRMSALQESRRELMVQLEElm 514
Cdd:PRK04863  517 QLRMRLSELEQRLRQ-QQRAERLLAEFCKRLGKNLDDEDELEQLQEELE---ARLESLSESVSEARERRMALRQQLEQ-- 590
                          90
                  ....*....|....*
gi 37577095   515 klLKEEEQKQAAQAT 529
Cdd:PRK04863  591 --LQARIQRLAARAP 603
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
433-526 9.73e-03

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


Pssm-ID: 224259 [Multi-domain]  Cd Length: 294  Bit Score: 38.51  E-value: 9.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577095 433 NKQQRQLIAE---LENKNREILQEIQRLRlehEQASqptpEKAQQNPTLLAELRLLRQRKDELEQ-------RMSALQES 502
Cdd:COG1340 157 NEKLKELKAEideLKKKAREIHEKIQELA---NEAQ----EYHEEMIKLFEEADELRKEADELHEefvelskKIDELHEE 229
                        90       100
                ....*....|....*....|....
gi 37577095 503 RRELMVQLEELMKLLKEEEQKQAA 526
Cdd:COG1340 230 FRNLQNELRELEKKIKALRAKEKA 253
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH