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Conserved domains on  [gi|37577097|ref|NP_899205|]
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dystrobrevin beta isoform 5 [Homo sapiens]

Protein Classification

EFh_DTN and ZZ_dystrophin domain-containing protein( domain architecture ID 13006839)

EFh_DTN and ZZ_dystrophin domain-containing protein

Graphical summary

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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 7.57e-113

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: 332.28  E-value: 7.57e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097  54 DIWNMIEAFRDNGLNTLDHTTEISVSRLETVISSIYYQLNKRLPSTHQISVEQSISLLLNFMIAAYDSEGRGKLTVFSVK 133
Cdd:cd16244   1 DIWNVIEAFRENGLNTLDPTTELSVSRLETLLSSIYYQLNKRLPTTHQIDVDQSISLLLNWLLAAYDPEATGRLTVFSVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 134 AMLATMCGGKMLDKLRYVFSQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFGYTEHSVRTCFPQQRKIMLNMFLDTM 213
Cdd:cd16244  81 VALSTLCAGKLVDKLRYIFSQISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYNESAARSCFPGQSKVTVNDFLDVM 160


                .
gi 37577097 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 8.67e-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: 97.04  E-value: 8.67e-25
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 37577097 241 VECSYCRCESMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHSNQHQMKEH 289
Cdd:cd02334   1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 370-512 3.14e-08

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


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 55.93  E-value: 3.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 370 EEHRLIARYAARLAAEAGNVTRPPTDLSFNFD--------------ANKQQRQLIAELENKNREILQEIQRLRLEHEQAS 435
Cdd:COG4942  98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEdfldavrrlqylkyLAPARREQAEELRADLAELAALRAELEAERAELE 177

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 436 QPTPEKAQQNPTLLAE-------LRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKAQATGSPHTSPTHGGGRpMP 508
Cdd:COG4942 178 ALLAELEEERAALEALkaerqklLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK-LP 256


                ....
gi 37577097 509 MPVR 512
Cdd:COG4942 257 WPVS 260
 
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 7.57e-113

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: 332.28  E-value: 7.57e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097  54 DIWNMIEAFRDNGLNTLDHTTEISVSRLETVISSIYYQLNKRLPSTHQISVEQSISLLLNFMIAAYDSEGRGKLTVFSVK 133
Cdd:cd16244   1 DIWNVIEAFRENGLNTLDPTTELSVSRLETLLSSIYYQLNKRLPTTHQIDVDQSISLLLNWLLAAYDPEATGRLTVFSVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 134 AMLATMCGGKMLDKLRYVFSQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFGYTEHSVRTCFPQQRKIMLNMFLDTM 213
Cdd:cd16244  81 VALSTLCAGKLVDKLRYIFSQISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYNESAARSCFPGQSKVTVNDFLDVM 160


                .
gi 37577097 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 3.17e-63

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


Pssm-ID: 462668  Cd Length: 123  Bit Score: 203.15  E-value: 3.17e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097    16 RQLFIEMraQNFDVIRLSTYRTACKLRFVQKRCNLHLVDIWNMIEAFRDNGLNTLDHTTEISVSRLETVISSIYYQLNKR 95
Cdd:pfam09068   1 TELMQEL--QDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNSLENDLLLSVSELEALLSSIYFALNKR 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 37577097    96 LPSTHQISVEQSISLLLNFMIAAYDSEGRGKLTVFSVKAMLATMC 140
Cdd:pfam09068  79 KPTTHQINVPLSVDLLLNWLLNVYDPERTGKIRVLSFKVALATLC 123
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 241-289 8.67e-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: 97.04  E-value: 8.67e-25
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 37577097 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 8.56e-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: 8.56e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 37577097    237 VFHPVECSYCRCEsMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHS 281
Cdd:smart00291   1 VHHSYSCDTCGKP-IVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 370-512 3.14e-08

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 55.93  E-value: 3.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 370 EEHRLIARYAARLAAEAGNVTRPPTDLSFNFD--------------ANKQQRQLIAELENKNREILQEIQRLRLEHEQAS 435
Cdd:COG4942  98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEdfldavrrlqylkyLAPARREQAEELRADLAELAALRAELEAERAELE 177

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 436 QPTPEKAQQNPTLLAE-------LRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKAQATGSPHTSPTHGGGRpMP 508
Cdd:COG4942 178 ALLAELEEERAALEALkaerqklLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK-LP 256


                ....
gi 37577097 509 MPVR 512
Cdd:COG4942 257 WPVS 260
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 239-280 3.63e-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: 3.63e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 37577097   239 HPVECSYCRCESMMGFRYRCQQCHNYQLCQNCFwRGHAGGPH 280
Cdd:pfam00569   3 KVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCF-QTHKGGNH 43
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 366-491 5.42e-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: 46.21  E-value: 5.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097    366 SRLDEEHRliaRYAARLAAEAGNVTRPPTDLSFNFDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN 445
Cdd:TIGR02169  801 SKLEEEVS---RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL 877

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 37577097    446 PTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEEL---MKLLKAQA 491
Cdd:TIGR02169  878 RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKrkrLSELKAKL 926
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 410-480 8.18e-05

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 45.06  E-value: 8.18e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37577097  410 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN---PTLLAELRLLRQRKDELEQRMSALQESRRELMVQL 480
Cdd:PRK05431  30 LLELDEERRELQTELEELQAERNALSKEIGQAKRKGedaEALIAEVKELKEEIKALEAELDELEAELEELLLRI 103
Seryl_tRNA_N pfam02403
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ...
 410-484 1.52e-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: 38.34  E-value: 1.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37577097   410 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPtllaELRLLRQRKDELEQRMSALQESRRELMVQLEELM 484
Cdd:pfam02403  31 LLELDEKRRELQVELEELQAERNELSKEIGQAKKKKE----DADALIAEVKELKDELKALEAELKELEAELDKLL 101
Prefoldin_alpha_GimC cd23160
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ...
 448-486 3.67e-03

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


Pssm-ID: 467476 [Multi-domain]  Cd Length: 127  Bit Score: 37.85  E-value: 3.67e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 37577097 448 LLAELRLLRQRKDELEQRMSALQESRRELMV---QLEELMKL 486
Cdd:cd23160   5 LLAELQQLEQQAEALQQQIELLQASINELNRakeTLEELKKL 46
 
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 7.57e-113

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: 332.28  E-value: 7.57e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097  54 DIWNMIEAFRDNGLNTLDHTTEISVSRLETVISSIYYQLNKRLPSTHQISVEQSISLLLNFMIAAYDSEGRGKLTVFSVK 133
Cdd:cd16244   1 DIWNVIEAFRENGLNTLDPTTELSVSRLETLLSSIYYQLNKRLPTTHQIDVDQSISLLLNWLLAAYDPEATGRLTVFSVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 134 AMLATMCGGKMLDKLRYVFSQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFGYTEHSVRTCFPQQRKIMLNMFLDTM 213
Cdd:cd16244  81 VALSTLCAGKLVDKLRYIFSQISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYNESAARSCFPGQSKVTVNDFLDVM 160


                .
gi 37577097 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 1.56e-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: 1.56e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097  54 DIWNMIEAFRDNGLNTLDHTTEISVSRLETVISSIYYQLNKRLPSTHQISVEQSISLLLNFMIAAYDSEGRGKLTVFSVK 133
Cdd:cd16250   1 DIWNMIEAFRDNGLNTLDHSTEISVSRLETIISSIYYQLNKRLPSTHQISVEQSISLLLNFMIAAYDSEGHGKLTVFSVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 134 AMLATMCGGKMLDKLRYVFSQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFGYTEHSVRTCFPQQRKIMLNMFLDTM 213
Cdd:cd16250  81 AMLATMCGGKILDKLRYTFSQMSDSNGLMIFLKFDQFLREVLKLPTAVFEGPSFGYTEHSVRTCFPQQKKIMLNMFLDTM 160


                .
gi 37577097 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 4.36e-95

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: 286.79  E-value: 4.36e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097  54 DIWNMIEAFRDNGLNTLDHTTEISVSRLETVISSIYYQLNKRLPSTHQISVEQSISLLLNFMIAAYDSEGRGKLTVFSVK 133
Cdd:cd16249   1 DIWNIIEALRENALNNLDPNTELNVARLEAVLSTIFYQLNKRMPTTHQINVEQSISLLLNFLLAAFDPEGHGKISVFAVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 134 AMLATMCGGKMLDKLRYVFSQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFGYTEHSVRTCFPQQRKIMLNMFLDTM 213
Cdd:cd16249  81 MALATLCGGKIMDKLRYIFSMISDSNGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSARSCFSQQKKVTLNGFLDTL 160


                .
gi 37577097 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 3.17e-63

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


Pssm-ID: 462668  Cd Length: 123  Bit Score: 203.15  E-value: 3.17e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097    16 RQLFIEMraQNFDVIRLSTYRTACKLRFVQKRCNLHLVDIWNMIEAFRDNGLNTLDHTTEISVSRLETVISSIYYQLNKR 95
Cdd:pfam09068   1 TELMQEL--QDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNSLENDLLLSVSELEALLSSIYFALNKR 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 37577097    96 LPSTHQISVEQSISLLLNFMIAAYDSEGRGKLTVFSVKAMLATMC 140
Cdd:pfam09068  79 KPTTHQINVPLSVDLLLNWLLNVYDPERTGKIRVLSFKVALATLC 123
EFh_DMD_DYTN_DTN cd15901
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ...
 54-214 3.44e-55

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: 183.24  E-value: 3.44e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097  54 DIWNMIEAFRDNGLNTlDHTTEISVSRLETVISSIYYQLNKRLPstHQISVEQSISLLLNFMIAAYDSEGRGKLTVFSVK 133
Cdd:cd15901   1 DLSTVLSVFDRHGLSG-SQDSVLDCEELETILTELYIKLNKRRP--DLIDVPRASDLLLNWLLNLYDRNRTGCIRLLSVK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 134 AMLATMCGGKMLDKLRYVFSQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFG--YTEHSVRTCFPQQRKIM---LNM 208
Cdd:cd15901  78 IALITLCAASLLDKYRYLFGQLADSSGFISRERLTQFLQDLLQIPDLIGESPAFGghNVEAAVESCFQLARSRVgvsEDT 157


                ....*.
gi 37577097 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 1.75e-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: stabilization of the WW domain (pfam00397), enhancing dystroglycan binding.


Pssm-ID: 462669  Cd Length: 90  Bit Score: 149.76  E-value: 1.75e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097   144 MLDKLRYVFSQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFGYTEHSVRTCFPQQR---KIMLNMFLDTMMADppPQ 220
Cdd:pfam09069   1 LVDKYRYLFSQISDSNGLLDQSKLGLLLHELLQLPRQVGEVPAFGGIEPSVRSCFEQVGgkpKITLNHFLDWLMSE--PQ 78

                          90
                  ....*....|..
gi 37577097   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 8.67e-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: 97.04  E-value: 8.67e-25
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 37577097 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 3.82e-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: 3.82e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097  54 DIWNMIEAFRDNGLNTL-DHTteISVSRLETVISSIYYQLNKRLPstHQISVEQSISLLLNFMIAAYDSEGRGKLTVFSV 132
Cdd:cd16242   1 SLSTAIEAFDQHGLRAQnDKL--IDVPDMITCLTTIYEALEEEHP--TLVNVPLCVDLCLNWLLNVYDSGRSGKIRVLSF 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 133 KAMLATMCGGKMLDKLRYVFSQMSDSNGLMifskfDQ-----FLKEVLKLPTAVFEGPSFGYT--EHSVRTCFPQ---QR 202
Cdd:cd16242  77 KVGLVLLCNAHLEEKYRYLFSLIADPNGCV-----DQrrlglLLHDCIQIPRQLGEVAAFGGSniEPSVRSCFEKageKP 151

                       170
                ....*....|.
gi 37577097 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 1.77e-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: 88.51  E-value: 1.77e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097  67 LNTLDHTTEISVSRLETVISSIYYQLNKRLPSThqISVEQSISLLLNFMIAAYDSEGRGKLTVFSVKAMLATMCGGKMLD 146
Cdd:cd16245  14 LSNSENNLCLPPDELEAVLHDIYFAAEKLGNFN--IDVDLATELLANLFLNVFDPERKKSISVLELKVFLTLLCGSSLQE 91

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 37577097 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 8.56e-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: 8.56e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 37577097    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 1.47e-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: 1.47e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097  60 EAFRDNGLNTLDHTteISVSRLETVISSIYYQLNKRlpSTHQISVEQSISLLLNFMIAAYDSEGRGKLTVFSVKAMLATM 139
Cdd:cd16248   7 EIFTEHELQMSERV--MDVVEVIHCLTALYERLEEE--RGILVNVPLCVDMCLNWLLNVYDSGRNGKIRVLSFKTGIVCL 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37577097 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 2.69e-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: 2.69e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097  60 EAFRDNGLNTLDHTTEISvsRLETVISSIYyqlnKRLPSTHQ--ISVEQSISLLLNFMIAAYDSEGRGKLTVFSVKAMLA 137
Cdd:cd16246   7 EALDQHNLKQNDQPMDIL--QIINCLTTIY----DRLEQEHNnlVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 138 TMCGGKMLDKLRYVFSQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFGYT--EHSVRTCFP---QQRKIMLNMFLDT 212
Cdd:cd16246  81 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSniEPSVRSCFQfanNKPEIEAALFLDW 160


                .
gi 37577097 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 8.68e-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: 8.68e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097  60 EAFRDNGLNTLDHTteISVSRLETVISSIYYQLNKRlpstHQ--ISVEQSISLLLNFMIAAYDSEGRGKLTVFSVKAMLA 137
Cdd:cd16247   7 SVFKQHKLTQNDQL--LSVPDVINCLTTIYDGLEQK----HKdlVNVPLCVDMCLNWLLNVYDTGRTGKIRVLSLKIGLM 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 138 TMCGGKMLDKLRYVFSQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFGYT--EHSVRTCFPQQR---KIMLNMFLDT 212
Cdd:cd16247  81 SLSKGLLEEKYRYLFKEVAGPGDTCDQRQLGLLLHDAIQIPRQLGEVAAFGGSniEPSVRSCFQHANnkpEIDVKQFIDW 160


                .
gi 37577097 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 9.67e-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: 9.67e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 37577097 243 CSYCRCESMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHSNQHQMKE 288
Cdd:cd02345   3 CSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLHIMYE 48
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 370-512 3.14e-08

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 55.93  E-value: 3.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 370 EEHRLIARYAARLAAEAGNVTRPPTDLSFNFD--------------ANKQQRQLIAELENKNREILQEIQRLRLEHEQAS 435
Cdd:COG4942  98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEdfldavrrlqylkyLAPARREQAEELRADLAELAALRAELEAERAELE 177

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 436 QPTPEKAQQNPTLLAE-------LRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKAQATGSPHTSPTHGGGRpMP 508
Cdd:COG4942 178 ALLAELEEERAALEALkaerqklLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK-LP 256


                ....
gi 37577097 509 MPVR 512
Cdd:COG4942 257 WPVS 260
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 243-284 4.12e-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: 4.12e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 37577097 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 8.34e-08

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: 52.00  E-value: 8.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097  65 NGLNT-LDHTTEISVSRLETVISSIYYQLNKRLP-STHQISVEQSISLLLnfmiAAYDSEGRGKLTVFSVKAMLATMCGG 142
Cdd:cd16243  10 NSLGGsIERTISLSVEEVSQALERLFQSASQEVPgQVSAEATEQTCRLLF----RLYDREQTGFVSLRSVEAALIALSGD 85

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 143 KMLDKLRYVF----SQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFGYTEHSVRTCF 198
Cdd:cd16243  86 TLSAKYRALFqlyeSGQGGSSGSITRSGLRVLLQDLSQIPAVVQESHVFGNVETAVRSCF 145
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 241-287 3.30e-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: 3.30e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 37577097 241 VECSYCRCESMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHSNQHQMK 287
Cdd:cd02338   1 VSCDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFDHPMQ 47
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 241-289 3.38e-07

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


Pssm-ID: 239069 [Multi-domain]  Cd Length: 46  Bit Score: 47.04  E-value: 3.38e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 37577097 241 VECSYCRCESMmGFRYRCQQCHNYQLCQNCFWRGHagGPHSNQHQMKEH 289
Cdd:cd02249   1 YSCDGCLKPIV-GVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 239-280 3.63e-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: 3.63e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 37577097   239 HPVECSYCRCESMMGFRYRCQQCHNYQLCQNCFwRGHAGGPH 280
Cdd:pfam00569   3 KVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCF-QTHKGGNH 43
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
404-491 1.09e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 51.31  E-value: 1.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 404 KQQRQLIAELENKNREILQEIQRLRLEHEQA-SQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEE 482
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231


                ....*....
gi 37577097 483 LMKLLKAQA 491
Cdd:COG4717 232 LENELEAAA 240
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 243-289 5.02e-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: 5.02e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 37577097 243 CSYCRCESMMGFRYRCQQCHNYQLCQNCFwrghaggpHSNQHQMkEH 289
Cdd:cd02339   3 CDTCRKQGIIGIRWKCAECPNYDLCTTCY--------HGDKHDL-EH 40
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 253-286 1.20e-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: 1.20e-05
                        10        20        30
                ....*....|....*....|....*....|....
gi 37577097 253 GFRYRCQQCHNYQLCQNCfwrgHAGGPHSNqHQM 286
Cdd:cd02340  12 GVRYKCLVCPDYDLCESC----EAKGVHPE-HAM 40
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
401-489 2.55e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.82  E-value: 2.55e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 401 DANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNptllAELRLLRQRKDELEQRMSALQESRRELMVQL 480
Cdd:COG4372  56 QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ----EELESLQEEAEELQEELEELQKERQDLEQQR 131


                ....*....
gi 37577097 481 EELMKLLKA 489
Cdd:COG4372 132 KQLEAQIAE 140
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 366-491 5.42e-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: 46.21  E-value: 5.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097    366 SRLDEEHRliaRYAARLAAEAGNVTRPPTDLSFNFDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN 445
Cdd:TIGR02169  801 SKLEEEVS---RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL 877

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 37577097    446 PTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEEL---MKLLKAQA 491
Cdd:TIGR02169  878 RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKrkrLSELKAKL 926
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
399-485 7.54e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 7.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 399 NFDANKQQRQLIAELENKNREILQEIQRL-RLEHEQAsqptpEKAQQNPTLLAELRLLRQRKD--ELEQRMSALQESRRE 475
Cdd:COG4717  69 NLKELKELEEELKEAEEKEEEYAELQEELeELEEELE-----ELEAELEELREELEKLEKLLQllPLYQELEALEAELAE 143

                        90
                ....*....|
gi 37577097 476 LMVQLEELMK 485
Cdd:COG4717 144 LPERLEELEE 153
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 410-480 8.18e-05

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 45.06  E-value: 8.18e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37577097  410 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN---PTLLAELRLLRQRKDELEQRMSALQESRRELMVQL 480
Cdd:PRK05431  30 LLELDEERRELQTELEELQAERNALSKEIGQAKRKGedaEALIAEVKELKEEIKALEAELDELEAELEELLLRI 103
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 406-490 2.18e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.60  E-value: 2.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 406 QRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMK 485
Cdd:COG4942  18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97


                ....*
gi 37577097 486 LLKAQ 490
Cdd:COG4942  98 ELEAQ 102
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
404-485 2.26e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 2.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 404 KQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEEL 483
Cdd:COG4372  97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176


                ..
gi 37577097 484 MK 485
Cdd:COG4372 177 SE 178
mukB PRK04863
chromosome partition protein MukB;
404-487 2.68e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 44.18  E-value: 2.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097   404 KQQRQLIAELENKNREILQEIQRLrleHEQASQ-----------PTPEkaqqnptllAELRLLRQRKDELEQRMSALQE- 471
Cdd:PRK04863  792 RAEREELAERYATLSFDVQKLQRL---HQAFSRfigshlavafeADPE---------AELRQLNRRRVELERALADHESq 859

                          90
                  ....*....|....*...
gi 37577097   472 --SRRELMVQLEELMKLL 487
Cdd:PRK04863  860 eqQQRSQLEQAKEGLSAL 877
PRK12704 PRK12704
phosphodiesterase; Provisional
 401-488 2.76e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.61  E-value: 2.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097  401 DANKQQRQLI----AELENKNREIL----QEIQRLRLEHEQasqptpEKAQQNPTLLAELRLLRQRKDELEQRMSALQES 472
Cdd:PRK12704  35 EAEEEAKRILeeakKEAEAIKKEALleakEEIHKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLELLEKR 108

                         90
                 ....*....|....*.
gi 37577097  473 RRELMVQLEELMKLLK 488
Cdd:PRK12704 109 EEELEKKEKELEQKQQ 124
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
 403-474 2.92e-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: 42.30  E-value: 2.92e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37577097   403 NKQQRQLIAELENKNREILQEIQRLRLEHE---QASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRR 474
Cdd:TIGR04211  89 LAELRQENQELKQQLSTLEAELEELQKELErikQISANAIELDEENRELREELAELKQENEALEAENERLQENEQ 163
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 241-271 3.69e-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: 38.33  E-value: 3.69e-04
                        10        20        30
                ....*....|....*....|....*....|.
gi 37577097 241 VECSYCRCESMMGFRYRCQQCHNYQLCQNCF 271
Cdd:cd02344   1 VTCDGCQMFPINGPRFKCRNCDDFDFCENCF 31
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
410-490 3.91e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.59  E-value: 3.91e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 410 IAELENKNREILQEIQRLRLE----HEQASQPTPEKAQQN---PTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEE 482
Cdd:COG1340  10 LEELEEKIEELREEIEELKEKrdelNEELKELAEKRDELNaqvKELREEAQELREKRDELNEKVKELKEERDELNEKLNE 89


                ....*...
gi 37577097 483 LMKLLKAQ 490
Cdd:COG1340  90 LREELDEL 97
ZZ_EF cd02343
Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif ...
 248-286 4.19e-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: 4.19e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 37577097 248 CESMMGF-RYRCQQCHNYQLCQNCFWRGHAGGPHSNQHQM 286
Cdd:cd02343   6 CDEIAPWhRYRCLQCTDMDLCKTCFLGGVKPEGHEDDHEM 45
PRK12704 PRK12704
phosphodiesterase; Provisional
 400-491 4.88e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 4.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097  400 FDANKQQRQLIAELENKNREILQEIQRL---------RLEHEQASQptpEKAQQNptLLAELRLLRQRKDELEQRMSALQ 470
Cdd:PRK12704  60 LEAKEEIHKLRNEFEKELRERRNELQKLekrllqkeeNLDRKLELL---EKREEE--LEKKEKELEQKQQELEKKEEELE 134

                         90       100
                 ....*....|....*....|.
gi 37577097  471 ESRRELMVQLEELMKLLKAQA 491
Cdd:PRK12704 135 ELIEEQLQELERISGLTAEEA 155
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 404-490 6.02e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.44  E-value: 6.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 404 KQQRQLIAELENKNREILQEIQRLRLEHEQASQptpekaqqnptllaELRLLRQRKDELEQRMSALQESRRELMVQLEEL 483
Cdd:COG4942  37 AELEKELAALKKEEKALLKQLAALERRIAALAR--------------RIRALEQELAALEAELAELEKEIAELRAELEAQ 102


                ....*..
gi 37577097 484 MKLLKAQ 490
Cdd:COG4942 103 KEELAEL 109
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
366-485 1.07e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 1.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 366 SRLDEEHRLIARYAAR--LAAEAGNVTRppTDLSFNFDANKQQRQLIAELENKNREILQEiqrLRLEHEQASQPTPEkaq 443
Cdd:COG4717 357 EELEEELQLEELEQEIaaLLAEAGVEDE--EELRAALEQAEEYQELKEELEELEEQLEEL---LGELEELLEALDEE--- 428

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 37577097 444 qnpTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMK 485
Cdd:COG4717 429 ---ELEEELEELEEELEELEEELEELREELAELEAELEQLEE 467
Seryl_tRNA_N pfam02403
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ...
 410-484 1.52e-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: 38.34  E-value: 1.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37577097   410 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPtllaELRLLRQRKDELEQRMSALQESRRELMVQLEELM 484
Cdd:pfam02403  31 LLELDEKRRELQVELEELQAERNELSKEIGQAKKKKE----DADALIAEVKELKDELKALEAELKELEAELDKLL 101
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 375-498 1.57e-03

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


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 40.90  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097   375 IARYAARLAAEAGNVTRPPTDLSFNFDANKQQRQliaELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRL 454
Cdd:pfam09787  77 LQELEAQQQEEAESSREQLQELEEQLATERSARR---EAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRN 153

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37577097   455 LRQRK-------DELEQRMSALQES--------------RRELMVQLEELMKLLK-AQATGSPHTS 498
Cdd:pfam09787 154 QLTSKsqssssqSELENRLHQLTETliqkqtmlealsteKNSLVLQLERMEQQIKeLQGEGSNGTS 219
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 367-492 1.69e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 1.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 367 RLDEEHRLIARYAARLAAEAGNVTRpptdlsfnfdANKQQRQLIAELEnknrEILQEIQRLRLEHEQASqptpEKAQQnp 446
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEE----------LEAELAELEAELE----ELRLELEELELELEEAQ----AEEYE-- 292

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 37577097 447 tLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKAQAT 492
Cdd:COG1196 293 -LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 366-493 1.97e-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 characteriztic 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: 40.82  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097   366 SRLDEEHRLIARYAARLAAEAGNVTRPPTDLSFNFDANKQQRQLIAELE---NKNREIL----QEIQRLRLEHEQASQPT 438
Cdd:pfam19220 111 IELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEgelATARERLalleQENRRLQALSEEQAAEL 190

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 37577097   439 PEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKAQATG 493
Cdd:pfam19220 191 AELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERAS 245
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 404-491 2.00e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 2.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 404 KQQRQLIAELENKNREILQEIQRLRLEHEQASqptpEKAQQnptLLAELRLLRQRKDELEQRMSALQEsrrelmvQLEEL 483
Cdd:COG3883  19 QAKQKELSELQAELEAAQAELDALQAELEELN----EEYNE---LQAELEALQAEIDKLQAEIAEAEA-------EIEER 84


                ....*...
gi 37577097 484 MKLLKAQA 491
Cdd:COG3883  85 REELGERA 92
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 406-492 2.01e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 2.01e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 406 QRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRElmvQLEELMK 485
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE---AEEELEE 383


                ....*..
gi 37577097 486 LLKAQAT 492
Cdd:COG1196 384 LAEELLE 390
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 367-489 2.09e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 2.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 367 RLDEEHRLIARYAARLAAEAgnvtrpptdlsfnfdANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNP 446
Cdd:COG1196 692 ELELEEALLAEEEEERELAE---------------AEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEEL 756

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37577097 447 TLLAELRLLRQRKDELEQRMSAL--------------QESRRELMVQLEELMK----LLKA 489
Cdd:COG1196 757 PEPPDLEELERELERLEREIEALgpvnllaieeyeelEERYDFLSEQREDLEEaretLEEA 817
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 400-485 2.16e-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: 2.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097    400 FDANKQQ--------RQLIAELENKNREILQEIQRLRLEHEQAS-----QPTPEKAQQNpTLLAELRLLRQRKDELEQRM 466
Cdd:TIGR02169  168 FDRKKEKaleeleevEENIERLDLIIDEKRQQLERLRREREKAEryqalLKEKREYEGY-ELLKEKEALERQKEAIERQL 246

                           90
                   ....*....|....*....
gi 37577097    467 SALQESRRELMVQLEELMK 485
Cdd:TIGR02169  247 ASLEEELEKLTEEISELEK 265
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
404-483 2.57e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 2.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097  404 KQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLL-AELRLLRQRKDELEQRMSALQESRRELMVQLEE 482
Cdd:COG4913  248 REQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLeAELEELRAELARLEAELERLEARLDALREELDE 327


                 .
gi 37577097  483 L 483
Cdd:COG4913  328 L 328
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
402-483 2.73e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 2.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 402 ANKQQRQLIAELENKNREI---LQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMV 478
Cdd:COG4372  71 ARSELEQLEEELEELNEQLqaaQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREE 150


                ....*
gi 37577097 479 QLEEL 483
Cdd:COG4372 151 ELKEL 155
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
401-482 2.89e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 2.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097  401 DANKQQRQL--IAELENKNREILQEIQRLR-----LEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESR 473
Cdd:COG4913  246 DAREQIELLepIRELAERYAAARERLAELEylraaLRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREEL 325


                 ....*....
gi 37577097  474 RELMVQLEE 482
Cdd:COG4913  326 DELEAQIRG 334
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 401-486 2.94e-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: 40.82  E-value: 2.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097    401 DANKQQRQLIAELENKNREILQ---EIQRLRLEHEQASQPTPEKAQqnptllaELRLLRQRKDELEQRmsaLQESRRELM 477
Cdd:TIGR02169  319 DAEERLAKLEAEIDKLLAEIEElerEIEEERKRRDKLTEEYAELKE-------ELEDLRAELEEVDKE---FAETRDELK 388


                   ....*....
gi 37577097    478 VQLEELMKL 486
Cdd:TIGR02169  389 DYREKLEKL 397
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
401-484 3.23e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 3.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097  401 DANKQQRQL---IAELENKNREILQEIQRLRLEHEQAsqptPEKAQQNPTLLAELRLLRQRKDELEQRMS--------AL 469
Cdd:COG4913  703 ELEEELDELkgeIGRLEKELEQAEEELDELQDRLEAA----EDLARLELRALLEERFAAALGDAVERELRenleeridAL 778

                         90
                 ....*....|....*
gi 37577097  470 QESRRELMVQLEELM 484
Cdd:COG4913  779 RARLNRAEEELERAM 793
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
367-489 3.49e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 3.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097  367 RLDEEHRLIARYAARLAAEAgnvtrpptdlsfnfDANKQQRQLIAELENKNREIL------QEIQRLRLEHEQASQPTPE 440
Cdd:COG4913  621 ELEEELAEAEERLEALEAEL--------------DALQERREALQRLAEYSWDEIdvasaeREIAELEAELERLDASSDD 686

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 37577097  441 ----KAQQNpTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKA 489
Cdd:COG4913  687 laalEEQLE-ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
Prefoldin_alpha_GimC cd23160
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ...
 448-486 3.67e-03

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


Pssm-ID: 467476 [Multi-domain]  Cd Length: 127  Bit Score: 37.85  E-value: 3.67e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 37577097 448 LLAELRLLRQRKDELEQRMSALQESRRELMV---QLEELMKL 486
Cdd:cd23160   5 LLAELQQLEQQAEALQQQIELLQASINELNRakeTLEELKKL 46
STAT5_CCD cd16855
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ...
 405-490 3.70e-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: 3.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 405 QQRQLIAELENKNREI----------LQEIQRLRLEHEQASQptpekaQQNPTLLAELRLLRQRKDELEQRMSA----LQ 470
Cdd:cd16855  12 ELRQRTQETENDLRNLqqkqesfviqYQESQKIQAQLQQLQQ------QPQNERIELEQQLQQQKEQLEQLLNAkaqeLL 85

                        90       100
                ....*....|....*....|
gi 37577097 471 ESRRELMVQLEELMKLLKAQ 490
Cdd:cd16855  86 QLRMELADKFKKTIQLLSKL 105
DASH_Spc19 pfam08287
Spc19; Spc19 is a component of the DASH complex. The DASH complex associates with the spindle ...
 403-469 3.75e-03

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


Pssm-ID: 429900 [Multi-domain]  Cd Length: 148  Bit Score: 38.00  E-value: 3.75e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37577097   403 NKQQRQLiAELENKNreilqEIQRLRLEH------------EQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSAL 469
Cdd:pfam08287  76 EKLERRE-ETLKAKL-----ELNEGRLSNaessardeegsqESDEEVNSSEGDATNEELERLRALRQKKERLKYSLERL 148
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
403-489 4.05e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 4.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097  403 NKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTllAELRLLRQRKDELEQRMSALQESRRElmvqLEE 482
Cdd:PRK02224 622 NDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVE--EKLDELREERDDLQAEIGAVENELEE----LEE 695


                 ....*..
gi 37577097  483 LMKLLKA 489
Cdd:PRK02224 696 LRERREA 702
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
 408-482 4.13e-03

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


Pssm-ID: 462875 [Multi-domain]  Cd Length: 150  Bit Score: 37.98  E-value: 4.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097   408 QLIAELEN------KNREILQEIQRLRLEHEQ-ASQPTPEKAQQnptLLAELRLL------RQRKDELEQRMSALQESRR 474
Cdd:pfam09744  30 KVVNVLELleslasRNQEHNVELEELREDNEQlETQYEREKALR---KRAEEELEeiedqwEQETKDLLSQVESLEEENR 106

                          90
                  ....*....|..
gi 37577097   475 ELM----VQLEE 482
Cdd:pfam09744 107 RLEadhvSRLEE 118
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 405-489 4.28e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 4.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097    405 QQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELM 484
Cdd:TIGR02168  723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802


                   ....*
gi 37577097    485 KLLKA 489
Cdd:TIGR02168  803 EALDE 807
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
 241-286 4.37e-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: 4.37e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 37577097 241 VECSYCRCESMMGFRYRCQQCHN--YQLCQNCFwrgHAGGPHSNQHQM 286
Cdd:cd02341   1 FKCDSCGIEPIPGTRYHCSECDDgdFDLCQDCV---VKGESHQEDHWL 45
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
399-490 5.00e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 5.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097  399 NFDANKQQRQLIAELENKnREILQEIQRLRLEHEQASqptpEKAQQNPTLLAELRL--LRQRKDELEQRMSALQESRREL 476
Cdd:COG4913  233 HFDDLERAHEALEDAREQ-IELLEPIRELAERYAAAR----ERLAELEYLRAALRLwfAQRRLELLEAELEELRAELARL 307

                         90
                 ....*....|....
gi 37577097  477 MVQLEELMKLLKAQ 490
Cdd:COG4913  308 EAELERLEARLDAL 321
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
 378-472 5.43e-03

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


Pssm-ID: 461111 [Multi-domain]  Cd Length: 272  Bit Score: 38.82  E-value: 5.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097   378 YAARLAAEAGNVTRppTDLSFNFDANKQQRQLIAELENKNREILQEIQRL--RLEHEQASQPTPEKAQQNPTLLAELRLL 455
Cdd:pfam03961 131 KAKELGSPAGTKTE--IEVGVDFPELKEKLEELEKELEELEEELEKLKKRlkKLPKKARGQLPPEKREQLEKLLETKNKL 208

                          90
                  ....*....|....*..
gi 37577097   456 RQRKDELEQRMSALQES 472
Cdd:pfam03961 209 SEELEELEEELKELKEE 225
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 402-492 5.67e-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: 5.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097    402 ANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELE---QRMSALQESRRELMV 478
Cdd:TIGR02168  289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKeelESLEAELEELEAELE 368

                           90
                   ....*....|....
gi 37577097    479 QLEELMKLLKAQAT 492
Cdd:TIGR02168  369 ELESRLEELEEQLE 382
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
407-481 5.77e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.61  E-value: 5.77e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37577097 407 RQLIAELENKNREILQEIQRLRLEHEQASQptpekaqqnpTLLAELRLLRQRKDELEQRMSALQESRRELMvQLE 481
Cdd:COG3206 294 IALRAQIAALRAQLQQEAQRILASLEAELE----------ALQAREASLQAQLAQLEARLAELPELEAELR-RLE 357
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 381-489 5.82e-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: 5.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097    381 RLAAEAGNVTRPPTDLSFNFDANKQQrqlIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAE-------LR 453
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERR---LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNErasleeaLA 890

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 37577097    454 LLRQRKDELEQRMSALQESRRELMVQLEELMKLLKA 489
Cdd:TIGR02168  891 LLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
360-489 6.67e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 6.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097  360 SVLDSPSRLDEEHRLIARYAARLaaeagnvtrpptdlsfnfdanKQQRQLIAELENKNREILQEIQRLRL-----EHEQA 434
Cdd:PRK03918 606 ELKDAEKELEREEKELKKLEEEL---------------------DKAFEELAETEKRLEELRKELEELEKkyseeEYEEL 664

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 37577097  435 SQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKA 489
Cdd:PRK03918 665 REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKA 719
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 367-491 7.75e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 7.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 367 RLDEEHRLIARYAARLAAEAGNVTRppTDLSFNfDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQqnp 446
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEE--LRLELE-ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE--- 320

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 37577097 447 tLLAELRLLRQRKDELEQRMSALQESRRELmvqlEELMKLLKAQA 491
Cdd:COG1196 321 -LEEELAELEEELEELEEELEELEEELEEA----EEELEEAEAEL 360
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
405-489 8.13e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 8.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097  405 QQRQLIAELENKNREILQEIQRLRLEHEQASQptpEKAQQNptllAELRLLR--------QRKDELEQRMSALQESRREL 476
Cdd:COG4913  285 FAQRRLELLEAELEELRAELARLEAELERLEA---RLDALR----EELDELEaqirgnggDRLEQLEREIERLERELEER 357

                         90
                 ....*....|...
gi 37577097  477 MVQLEELMKLLKA 489
Cdd:COG4913  358 ERRRARLEALLAA 370
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
409-490 9.02e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 9.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 409 LIAELENKNREI-----------LQEIQRLRLEHEQASQptpekaqqnptLLAELRLLRQRKDELEQRMSALQESRRELM 477
Cdd:COG4717  47 LLERLEKEADELfkpqgrkpelnLKELKELEEELKEAEE-----------KEEEYAELQEELEELEEELEELEAELEELR 115

                        90
                ....*....|...
gi 37577097 478 VQLEELMKLLKAQ 490
Cdd:COG4717 116 EELEKLEKLLQLL 128
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 405-489 9.73e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 37.98  E-value: 9.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577097 405 QQRQLIAELENKNREILQEIQRLRLEHEQASQptpEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEElm 484
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEA---ELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP-- 174


                ....*
gi 37577097 485 KLLKA 489
Cdd:COG1579 175 ELLAL 179
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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