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Conserved domains on  [gi|2031263915|ref|NP_001381615|]
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dystrobrevin beta isoform 30 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EF-hand_3 pfam09069
EF-hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
 4-85 8.19e-39

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: 135.51  E-value: 8.19e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915   4 VFSQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFGYTEHSVRTCFPQQR---KIMLNMFLDTMMADppPQCLVWLPL 80
Cdd:pfam09069   8 LFSQISDSNGLLDQSKLGLLLHELLQLPRQVGEVPAFGGIEPSVRSCFEQVGgkpKITLNHFLDWLMSE--PQSLVWLPV 85


                  ....*
gi 2031263915  81 MHRLA 85
Cdd:pfam09069  86 LHRLA 90
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 94-142 6.61e-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: 96.66  E-value: 6.61e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2031263915  94 VECSYCRCESMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHSNQHQMKEH 142
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 253-395 2.24e-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: 2.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 253 EEHRLIARYAARLAAEAGNVTRPPTDLSFNFD--------------ANKQQRQLIAELENKNREILQEIQRLRLEHEQAS 318
Cdd:COG4942    98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEdfldavrrlqylkyLAPARREQAEELRADLAELAALRAELEAERAELE 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 319 QPTPEKAQQNPTLLAE-------LRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKAQATGSPHTSPTHGGGRpMP 391
Cdd:COG4942   178 ALLAELEEERAALEALkaerqklLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK-LP 256


                  ....
gi 2031263915 392 MPVR 395
Cdd:COG4942   257 WPVS 260
 
Name Accession Description Interval E-value
EF-hand_3 pfam09069
EF-hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
 4-85 8.19e-39

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: 135.51  E-value: 8.19e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915   4 VFSQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFGYTEHSVRTCFPQQR---KIMLNMFLDTMMADppPQCLVWLPL 80
Cdd:pfam09069   8 LFSQISDSNGLLDQSKLGLLLHELLQLPRQVGEVPAFGGIEPSVRSCFEQVGgkpKITLNHFLDWLMSE--PQSLVWLPV 85


                  ....*
gi 2031263915  81 MHRLA 85
Cdd:pfam09069  86 LHRLA 90
EFh_DTNB cd16250
EF-hand-like motif found in beta-dystrobrevin; Beta-dystrobrevin, also termed dystrobrevin ...
 4-67 2.30e-38

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: 136.69  E-value: 2.30e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2031263915   4 VFSQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFGYTEHSVRTCFPQQRKIMLNMFLDTMM 67
Cdd:cd16250    98 TFSQMSDSNGLMIFLKFDQFLREVLKLPTAVFEGPSFGYTEHSVRTCFPQQKKIMLNMFLDTMM 161
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 94-142 6.61e-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: 96.66  E-value: 6.61e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2031263915  94 VECSYCRCESMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHSNQHQMKEH 142
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 90-134 1.43e-15

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 70.16  E-value: 1.43e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2031263915   90 VFHPVECSYCRCEsMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHS 134
Cdd:smart00291   1 VHHSYSCDTCGKP-IVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 253-395 2.24e-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: 2.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 253 EEHRLIARYAARLAAEAGNVTRPPTDLSFNFD--------------ANKQQRQLIAELENKNREILQEIQRLRLEHEQAS 318
Cdd:COG4942    98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEdfldavrrlqylkyLAPARREQAEELRADLAELAALRAELEAERAELE 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 319 QPTPEKAQQNPTLLAE-------LRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKAQATGSPHTSPTHGGGRpMP 391
Cdd:COG4942   178 ALLAELEEERAALEALkaerqklLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK-LP 256


                  ....
gi 2031263915 392 MPVR 395
Cdd:COG4942   257 WPVS 260
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 92-133 4.96e-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: 46.32  E-value: 4.96e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2031263915  92 HPVECSYCRCESMMGFRYRCQQCHNYQLCQNCFwRGHAGGPH 133
Cdd:pfam00569   3 KVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCF-QTHKGGNH 43
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 249-374 3.48e-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: 46.60  E-value: 3.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915  249 SRLDEEHRliaRYAARLAAEAGNVTRPPTDLSFNFDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN 328
Cdd:TIGR02169  801 SKLEEEVS---RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL 877

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2031263915  329 PTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEEL---MKLLKAQA 374
Cdd:TIGR02169  878 RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKrkrLSELKAKL 926
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 293-363 6.01e-05

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 45.06  E-value: 6.01e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2031263915 293 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN---PTLLAELRLLRQRKDELEQRMSALQESRRELMVQL 363
Cdd:PRK05431   30 LLELDEERRELQTELEELQAERNALSKEIGQAKRKGedaEALIAEVKELKEEIKALEAELDELEAELEELLLRI 103
Seryl_tRNA_N pfam02403
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ...
 293-367 6.86e-04

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: 39.11  E-value: 6.86e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2031263915 293 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPtllaELRLLRQRKDELEQRMSALQESRRELMVQLEELM 367
Cdd:pfam02403  31 LLELDEKRRELQVELEELQAERNELSKEIGQAKKKKE----DADALIAEVKELKDELKALEAELKELEAELDKLL 101
Prefoldin_alpha_GimC cd23160
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ...
 331-369 2.23e-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: 2.23e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2031263915 331 LLAELRLLRQRKDELEQRMSALQESRRELMV---QLEELMKL 369
Cdd:cd23160     5 LLAELQQLEQQAEALQQQIELLQASINELNRakeTLEELKKL 46
growth_prot_Scy NF041483
polarized growth protein Scy;
218-374 3.00e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 40.19  E-value: 3.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915  218 QDIPSHLADEHALIASYVARLQHCARVLDSPSRLDEEHRLIARY--AARLAAEAgnvtrpptdlsfnfdankqQRQLIAE 295
Cdd:NF041483   141 QTVESHVNENVAWAEQLRARTESQARRLLDESRAEAEQALAAARaeAERLAEEA-------------------RQRLGSE 201

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915  296 LENKNREILQEIQRLRLEHE--------QASQPTPEKAQQNPTLLAELRLLRQRKDEL----EQRMSALQESRRELMVQL 363
Cdd:NF041483   202 AESARAEAEAILRRARKDAErllnaastQAQEATDHAEQLRSSTAAESDQARRQAAELsraaEQRMQEAEEALREARAEA 281

                          170
                   ....*....|.
gi 2031263915  364 EELMKLLKAQA 374
Cdd:NF041483   282 EKVVAEAKEAA 292
 
Name Accession Description Interval E-value
EF-hand_3 pfam09069
EF-hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
 4-85 8.19e-39

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: 135.51  E-value: 8.19e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915   4 VFSQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFGYTEHSVRTCFPQQR---KIMLNMFLDTMMADppPQCLVWLPL 80
Cdd:pfam09069   8 LFSQISDSNGLLDQSKLGLLLHELLQLPRQVGEVPAFGGIEPSVRSCFEQVGgkpKITLNHFLDWLMSE--PQSLVWLPV 85


                  ....*
gi 2031263915  81 MHRLA 85
Cdd:pfam09069  86 LHRLA 90
EFh_DTNB cd16250
EF-hand-like motif found in beta-dystrobrevin; Beta-dystrobrevin, also termed dystrobrevin ...
 4-67 2.30e-38

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: 136.69  E-value: 2.30e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2031263915   4 VFSQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFGYTEHSVRTCFPQQRKIMLNMFLDTMM 67
Cdd:cd16250    98 TFSQMSDSNGLMIFLKFDQFLREVLKLPTAVFEGPSFGYTEHSVRTCFPQQKKIMLNMFLDTMM 161
EFh_DTN cd16244
EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the ...
 2-67 1.47e-37

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: 134.67  E-value: 1.47e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2031263915   2 TDVFSQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFGYTEHSVRTCFPQQRKIMLNMFLDTMM 67
Cdd:cd16244    96 RYIFSQISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYNESAARSCFPGQSKVTVNDFLDVMM 161
EFh_DTNA cd16249
EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin ...
 3-67 1.15e-34

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: 126.94  E-value: 1.15e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2031263915   3 DVFSQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFGYTEHSVRTCFPQQRKIMLNMFLDTMM 67
Cdd:cd16249    97 YIFSMISDSNGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSARSCFSQQKKVTLNGFLDTLM 161
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 94-142 6.61e-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: 96.66  E-value: 6.61e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2031263915  94 VECSYCRCESMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHSNQHQMKEH 142
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
EFh_DMD_DYTN_DTN cd15901
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ...
 3-67 6.08e-16

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: 75.00  E-value: 6.08e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915   3 DVFSQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFG--YTEHSVRTCFPQQRKIM---LNMFLDTMM 67
Cdd:cd15901    94 YLFGQLADSSGFISRERLTQFLQDLLQIPDLIGESPAFGghNVEAAVESCFQLARSRVgvsEDTFLSWLL 163
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 90-134 1.43e-15

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 70.16  E-value: 1.43e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2031263915   90 VFHPVECSYCRCEsMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHS 134
Cdd:smart00291   1 VHHSYSCDTCGKP-IVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 96-141 1.15e-08

Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dah (discontinuous actin hexagon) is a membrane associated protein essential for cortical furrow formation in Drosophila.


Pssm-ID: 239085  Cd Length: 49  Bit Score: 51.05  E-value: 1.15e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2031263915  96 CSYCRCESMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHSNQHQMKE 141
Cdd:cd02345     3 CSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLHIMYE 48
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 253-395 2.24e-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: 2.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 253 EEHRLIARYAARLAAEAGNVTRPPTDLSFNFD--------------ANKQQRQLIAELENKNREILQEIQRLRLEHEQAS 318
Cdd:COG4942    98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEdfldavrrlqylkyLAPARREQAEELRADLAELAALRAELEAERAELE 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 319 QPTPEKAQQNPTLLAE-------LRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKAQATGSPHTSPTHGGGRpMP 391
Cdd:COG4942   178 ALLAELEEERAALEALkaerqklLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK-LP 256


                  ....
gi 2031263915 392 MPVR 395
Cdd:COG4942   257 WPVS 260
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 96-137 4.48e-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: 49.21  E-value: 4.48e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2031263915  96 CSYCRCESMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHSNQH 137
Cdd:cd02335     3 CDYCSKDITGTIRIKCAECPDFDLCLECFSAGAEIGKHRNDH 44
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 94-140 3.48e-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: 46.57  E-value: 3.48e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2031263915  94 VECSYCRCESMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHSNQHQMK 140
Cdd:cd02338     1 VSCDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFDHPMQ 47
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 94-142 3.76e-07

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


Pssm-ID: 239069 [Multi-domain]  Cd Length: 46  Bit Score: 46.66  E-value: 3.76e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2031263915  94 VECSYCRCESMmGFRYRCQQCHNYQLCQNCFWRGHagGPHSNQHQMKEH 142
Cdd:cd02249     1 YSCDGCLKPIV-GVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 92-133 4.96e-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: 46.32  E-value: 4.96e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2031263915  92 HPVECSYCRCESMMGFRYRCQQCHNYQLCQNCFwRGHAGGPH 133
Cdd:pfam00569   3 KVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCF-QTHKGGNH 43
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
212-374 5.73e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.08  E-value: 5.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 212 KRLQYSQDIPSHLADEHALIASYVARLQHCARVLdspSRLDEEHRLIARY--AARLAAEAGNVTRPPTDLSFNFDANKQQ 289
Cdd:COG4717    78 EELKEAEEKEEEYAELQEELEELEEELEELEAEL---EELREELEKLEKLlqLLPLYQELEALEAELAELPERLEELEER 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 290 RQLIAELENKNREILQEIQRLRLEHEQA-SQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMK 368
Cdd:COG4717   155 LEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234


                  ....*.
gi 2031263915 369 LLKAQA 374
Cdd:COG4717   235 ELEAAA 240
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 96-142 4.91e-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: 43.22  E-value: 4.91e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2031263915  96 CSYCRCESMMGFRYRCQQCHNYQLCQNCFwrghaggpHSNQHQMkEH 142
Cdd:cd02339     3 CDTCRKQGIIGIRWKCAECPNYDLCTTCY--------HGDKHDL-EH 40
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
284-372 1.09e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 284 DANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNptllAELRLLRQRKDELEQRMSALQESRRELMVQL 363
Cdd:COG4372    56 QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ----EELESLQEEAEELQEELEELQKERQDLEQQR 131


                  ....*....
gi 2031263915 364 EELMKLLKA 372
Cdd:COG4372   132 KQLEAQIAE 140
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 106-139 1.54e-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: 41.86  E-value: 1.54e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2031263915 106 GFRYRCQQCHNYQLCQNCfwrgHAGGPHSNqHQM 139
Cdd:cd02340    12 GVRYKCLVCPDYDLCESC----EAKGVHPE-HAM 40
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 249-374 3.48e-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: 46.60  E-value: 3.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915  249 SRLDEEHRliaRYAARLAAEAGNVTRPPTDLSFNFDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN 328
Cdd:TIGR02169  801 SKLEEEVS---RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL 877

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2031263915  329 PTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEEL---MKLLKAQA 374
Cdd:TIGR02169  878 RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKrkrLSELKAKL 926
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
220-368 3.83e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 3.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 220 IPSHLADEHALiaSYVARLQHCARVLDSPSRLDEEHRLIARYAAR--LAAEAGNVTRppTDLSFNFDANKQQRQLIAELE 297
Cdd:COG4717   330 LPPDLSPEELL--ELLDRIEELQELLREAEELEEELQLEELEQEIaaLLAEAGVEDE--EELRAALEQAEEYQELKEELE 405

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2031263915 298 NKNREILQEiqrLRLEHEQASQPTPEkaqqnpTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMK 368
Cdd:COG4717   406 ELEEQLEEL---LGELEELLEALDEE------ELEEELEELEEELEELEEELEELREELAELEAELEQLEE 467
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
282-368 5.65e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 5.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 282 NFDANKQQRQLIAELENKNREILQEIQRL-RLEHEQAsqptpEKAQQNPTLLAELRLLRQRKD--ELEQRMSALQESRRE 358
Cdd:COG4717    69 NLKELKELEEELKEAEEKEEEYAELQEELeELEEELE-----ELEAELEELREELEKLEKLLQllPLYQELEALEAELAE 143

                          90
                  ....*....|
gi 2031263915 359 LMVQLEELMK 368
Cdd:COG4717   144 LPERLEELEE 153
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 293-363 6.01e-05

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 45.06  E-value: 6.01e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2031263915 293 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN---PTLLAELRLLRQRKDELEQRMSALQESRRELMVQL 363
Cdd:PRK05431   30 LLELDEERRELQTELEELQAERNALSKEIGQAKRKGedaEALIAEVKELKEEIKALEAELDELEAELEELLLRI 103
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
293-373 8.42e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 44.13  E-value: 8.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 293 IAELENKNREILQEIQRLRLE----HEQASQPTPEKAQQN---PTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEE 365
Cdd:COG1340    10 LEELEEKIEELREEIEELKEKrdelNEELKELAEKRDELNaqvKELREEAQELREKRDELNEKVKELKEERDELNEKLNE 89


                  ....*...
gi 2031263915 366 LMKLLKAQ 373
Cdd:COG1340    90 LREELDEL 97
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
287-368 1.11e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 287 KQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEEL 366
Cdd:COG4372    97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176


                  ..
gi 2031263915 367 MK 368
Cdd:COG4372   177 SE 178
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 289-373 1.62e-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: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 289 QRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMK 368
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97


                  ....*
gi 2031263915 369 LLKAQ 373
Cdd:COG4942    98 ELEAQ 102
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
 286-357 1.73e-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: 42.69  E-value: 1.73e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2031263915 286 NKQQRQLIAELENKNREILQEIQRLRLEHE---QASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRR 357
Cdd:TIGR04211  89 LAELRQENQELKQQLSTLEAELEELQKELErikQISANAIELDEENRELREELAELKQENEALEAENERLQENEQ 163
PRK12704 PRK12704
phosphodiesterase; Provisional
 284-371 2.03e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.61  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 284 DANKQQRQLI----AELENKNREIL----QEIQRLRLEHEQasqptpEKAQQNPTLLAELRLLRQRKDELEQRMSALQES 355
Cdd:PRK12704   35 EAEEEAKRILeeakKEAEAIKKEALleakEEIHKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLELLEKR 108

                          90
                  ....*....|....*.
gi 2031263915 356 RRELMVQLEELMKLLK 371
Cdd:PRK12704  109 EEELEKKEKELEQKQQ 124
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 94-124 2.91e-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: 2.91e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2031263915  94 VECSYCRCESMMGFRYRCQQCHNYQLCQNCF 124
Cdd:cd02344     1 VTCDGCQMFPINGPRFKCRNCDDFDFCENCF 31
mukB PRK04863
chromosome partition protein MukB;
287-370 3.52e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.41  E-value: 3.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915  287 KQQRQLIAELENKNREILQEIQRLrleHEQASQ-----------PTPEkaqqnptllAELRLLRQRKDELEQRMSALQE- 354
Cdd:PRK04863   792 RAEREELAERYATLSFDVQKLQRL---HQAFSRfigshlavafeADPE---------AELRQLNRRRVELERALADHESq 859

                           90
                   ....*....|....*...
gi 2031263915  355 --SRRELMVQLEELMKLL 370
Cdd:PRK04863   860 eqQQRSQLEQAKEGLSAL 877
PRK12704 PRK12704
phosphodiesterase; Provisional
 283-374 3.61e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 3.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 283 FDANKQQRQLIAELENKNREILQEIQRL---------RLEHEQASQptpEKAQQNptLLAELRLLRQRKDELEQRMSALQ 353
Cdd:PRK12704   60 LEAKEEIHKLRNEFEKELRERRNELQKLekrllqkeeNLDRKLELL---EKREEE--LEKKEKELEQKQQELEKKEEELE 134

                          90       100
                  ....*....|....*....|.
gi 2031263915 354 ESRRELMVQLEELMKLLKAQA 374
Cdd:PRK12704  135 ELIEEQLQELERISGLTAEEA 155
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 287-373 4.49e-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: 4.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 287 KQQRQLIAELENKNREILQEIQRLRLEHEQASQptpekaqqnptllaELRLLRQRKDELEQRMSALQESRRELMVQLEEL 366
Cdd:COG4942    37 AELEKELAALKKEEKALLKQLAALERRIAALAR--------------RIRALEQELAALEAELAELEKEIAELRAELEAQ 102


                  ....*..
gi 2031263915 367 MKLLKAQ 373
Cdd:COG4942   103 KEELAEL 109
ZZ_EF cd02343
Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif ...
 101-139 5.19e-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: 37.68  E-value: 5.19e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2031263915 101 CESMMGF-RYRCQQCHNYQLCQNCFWRGHAGGPHSNQHQM 139
Cdd:cd02343     6 CDEIAPWhRYRCLQCTDMDLCKTCFLGGVKPEGHEDDHEM 45
Seryl_tRNA_N pfam02403
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ...
 293-367 6.86e-04

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: 39.11  E-value: 6.86e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2031263915 293 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPtllaELRLLRQRKDELEQRMSALQESRRELMVQLEELM 367
Cdd:pfam02403  31 LLELDEKRRELQVELEELQAERNELSKEIGQAKKKKE----DADALIAEVKELKDELKALEAELKELEAELDKLL 101
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
285-366 1.23e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 285 ANKQQRQLIAELENKNREI---LQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMV 361
Cdd:COG4372    71 ARSELEQLEEELEELNEQLqaaQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREE 150


                  ....*
gi 2031263915 362 QLEEL 366
Cdd:COG4372   151 ELKEL 155
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 258-381 1.26e-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: 40.51  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 258 IARYAARLAAEAGNVTRPPTDLSFNFDANKQQRQliaELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRL 337
Cdd:pfam09787  77 LQELEAQQQEEAESSREQLQELEEQLATERSARR---EAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRN 153

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2031263915 338 LRQRK-------DELEQRMSALQES--------------RRELMVQLEELMKLLK-AQATGSPHTS 381
Cdd:pfam09787 154 QLTSKsqssssqSELENRLHQLTETliqkqtmlealsteKNSLVLQLERMEQQIKeLQGEGSNGTS 219
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 218-369 1.37e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 1.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915  218 QDIPSHLADEHALIASYVARLQHCARVLDSPSR-----LDEEHRLIARYAARLAAEAGNVTRpptdlsfNFDANKQQRQl 292
Cdd:TIGR02169  247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdlGEEEQLRVKEKIGELEAEIASLER-------SIAEKERELE- 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915  293 iaELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSAL----QESRRELMVQLEELMK 368
Cdd:TIGR02169  319 --DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVdkefAETRDELKDYREKLEK 396


                   .
gi 2031263915  369 L 369
Cdd:TIGR02169  397 L 397
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 283-368 1.44e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915  283 FDANKQQ--------RQLIAELENKNREILQEIQRLRLEHEQAS-----QPTPEKAQQNpTLLAELRLLRQRKDELEQRM 349
Cdd:TIGR02169  168 FDRKKEKaleeleevEENIERLDLIIDEKRQQLERLRREREKAEryqalLKEKREYEGY-ELLKEKEALERQKEAIERQL 246

                           90
                   ....*....|....*....
gi 2031263915  350 SALQESRRELMVQLEELMK 368
Cdd:TIGR02169  247 ASLEEELEKLTEEISELEK 265
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 289-375 1.49e-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: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 289 QRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRElmvQLEELMK 368
Cdd:COG1196   307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE---AEEELEE 383


                  ....*..
gi 2031263915 369 LLKAQAT 375
Cdd:COG1196   384 LAEELLE 390
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 287-374 1.50e-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: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 287 KQQRQLIAELENKNREILQEIQRLRLEHEQASqptpEKAQQnptLLAELRLLRQRKDELEQRMSALQEsrrelmvQLEEL 366
Cdd:COG3883    19 QAKQKELSELQAELEAAQAELDALQAELEELN----EEYNE---LQAELEALQAEIDKLQAEIAEAEA-------EIEER 84


                  ....*...
gi 2031263915 367 MKLLKAQA 374
Cdd:COG3883    85 REELGERA 92
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 250-372 1.57e-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: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 250 RLDEEHRLIARYAARLAAEAgnvtrpptdlsfnfdANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNP 329
Cdd:COG1196   692 ELELEEALLAEEEEERELAE---------------AEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEEL 756

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2031263915 330 TLLAELRLLRQRKDELEQRMSAL--------------QESRRELMVQLEELMK----LLKA 372
Cdd:COG1196   757 PEPPDLEELERELERLEREIEALgpvnllaieeyeelEERYDFLSEQREDLEEaretLEEA 817
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 237-375 1.74e-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: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 237 RLQHCARVLdspsRLDEEHRLIARYAARLAAEAGNVTRpptdlsfnfdANKQQRQLIAELEnknrEILQEIQRLRLEHEQ 316
Cdd:COG1196   224 ELEAELLLL----KLRELEAELEELEAELEELEAELEE----------LEAELAELEAELE----ELRLELEELELELEE 285

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 317 ASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQL-----------EELMKLLKAQAT 375
Cdd:COG1196   286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELeeleeeleeleEELEEAEEELEE 355
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
226-372 2.04e-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: 2.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915  226 DEHALIASYV------ARLQHCARVLDspsRLDEEHRLIARYAARLAAEAgnvtrpptdlsfnfDANKQQRQLIAELENK 299
Cdd:COG4913    594 DRRRIRSRYVlgfdnrAKLAALEAELA---ELEEELAEAEERLEALEAEL--------------DALQERREALQRLAEY 656

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915  300 NREIL------QEIQRLRLEHEQASQPTPE----KAQQNpTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMKL 369
Cdd:COG4913    657 SWDEIdvasaeREIAELEAELERLDASSDDlaalEEQLE-ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735


                   ...
gi 2031263915  370 LKA 372
Cdd:COG4913    736 LEA 738
Prefoldin_alpha_GimC cd23160
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ...
 331-369 2.23e-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: 2.23e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2031263915 331 LLAELRLLRQRKDELEQRMSALQESRRELMV---QLEELMKL 369
Cdd:cd23160     5 LLAELQQLEQQAEALQQQIELLQASINELNRakeTLEELKKL 46
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 231-376 2.26e-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: 40.05  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 231 IASYVARLQHCARVLDSPSRLDEEHRL--------IARYAARLAAEAGNVTRPPTDLSFNFDANKQQRQLIAELE---NK 299
Cdd:pfam19220  85 LEELVARLAKLEAALREAEAAKEELRIelrdktaqAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEgelAT 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 300 NREIL----QEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKAQAT 375
Cdd:pfam19220 165 ARERLalleQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERA 244


                  .
gi 2031263915 376 G 376
Cdd:pfam19220 245 S 245
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
287-366 2.28e-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: 2.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915  287 KQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLL-AELRLLRQRKDELEQRMSALQESRRELMVQLEE 365
Cdd:COG4913    248 REQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLeAELEELRAELARLEAELERLEARLDALREELDE 327


                   .
gi 2031263915  366 L 366
Cdd:COG4913    328 L 328
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
 291-365 2.52e-03

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


Pssm-ID: 462875 [Multi-domain]  Cd Length: 150  Bit Score: 38.37  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 291 QLIAELEN------KNREILQEIQRLRLEHEQ-ASQPTPEKAQQnptLLAELRLL------RQRKDELEQRMSALQESRR 357
Cdd:pfam09744  30 KVVNVLELleslasRNQEHNVELEELREDNEQlETQYEREKALR---KRAEEELEeiedqwEQETKDLLSQVESLEEENR 106

                          90
                  ....*....|..
gi 2031263915 358 ELM----VQLEE 365
Cdd:pfam09744 107 RLEadhvSRLEE 118
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 288-372 2.64e-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: 40.43  E-value: 2.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915  288 QQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELM 367
Cdd:TIGR02168  723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802


                   ....*
gi 2031263915  368 KLLKA 372
Cdd:TIGR02168  803 EALDE 807
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
284-365 2.66e-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: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915  284 DANKQQRQL--IAELENKNREILQEIQRLR-----LEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESR 356
Cdd:COG4913    246 DAREQIELLepIRELAERYAAARERLAELEylraaLRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREEL 325


                   ....*....
gi 2031263915  357 RELMVQLEE 365
Cdd:COG4913    326 DELEAQIRG 334
growth_prot_Scy NF041483
polarized growth protein Scy;
218-374 3.00e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 40.19  E-value: 3.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915  218 QDIPSHLADEHALIASYVARLQHCARVLDSPSRLDEEHRLIARY--AARLAAEAgnvtrpptdlsfnfdankqQRQLIAE 295
Cdd:NF041483   141 QTVESHVNENVAWAEQLRARTESQARRLLDESRAEAEQALAAARaeAERLAEEA-------------------RQRLGSE 201

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915  296 LENKNREILQEIQRLRLEHE--------QASQPTPEKAQQNPTLLAELRLLRQRKDEL----EQRMSALQESRRELMVQL 363
Cdd:NF041483   202 AESARAEAEAILRRARKDAErllnaastQAQEATDHAEQLRSSTAAESDQARRQAAELsraaEQRMQEAEEALREARAEA 281

                          170
                   ....*....|.
gi 2031263915  364 EELMKLLKAQA 374
Cdd:NF041483   282 EKVVAEAKEAA 292
DASH_Spc19 pfam08287
Spc19; Spc19 is a component of the DASH complex. The DASH complex associates with the spindle ...
 286-352 3.05e-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: 3.05e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2031263915 286 NKQQRQLiAELENKNreilqEIQRLRLEH------------EQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSAL 352
Cdd:pfam08287  76 EKLERRE-ETLKAKL-----ELNEGRLSNaessardeegsqESDEEVNSSEGDATNEELERLRALRQKKERLKYSLERL 148
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
284-367 3.24e-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: 3.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915  284 DANKQQRQL---IAELENKNREILQEIQRLRLEHEQAsqptPEKAQQNPTLLAELRLLRQRKDELEQRMS--------AL 352
Cdd:COG4913    703 ELEEELDELkgeIGRLEKELEQAEEELDELQDRLEAA----EDLARLELRALLEERFAAALGDAVERELRenleeridAL 778

                           90
                   ....*....|....*
gi 2031263915  353 QESRRELMVQLEELM 367
Cdd:COG4913    779 RARLNRAEEELERAM 793
STAT5_CCD cd16855
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ...
 288-373 3.31e-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: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 288 QQRQLIAELENKNREI----------LQEIQRLRLEHEQASQptpekaQQNPTLLAELRLLRQRKDELEQRMSA----LQ 353
Cdd:cd16855    12 ELRQRTQETENDLRNLqqkqesfviqYQESQKIQAQLQQLQQ------QPQNERIELEQQLQQQKEQLEQLLNAkaqeLL 85

                          90       100
                  ....*....|....*....|
gi 2031263915 354 ESRRELMVQLEELMKLLKAQ 373
Cdd:cd16855    86 QLRMELADKFKKTIQLLSKL 105
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 285-375 3.33e-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: 3.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915  285 ANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELE---QRMSALQESRRELMV 361
Cdd:TIGR02168  289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKeelESLEAELEELEAELE 368

                           90
                   ....*....|....
gi 2031263915  362 QLEELMKLLKAQAT 375
Cdd:TIGR02168  369 ELESRLEELEEQLE 382
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 264-372 3.62e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 3.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915  264 RLAAEAGNVTRPPTDLSFNFDANKQQrqlIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAE-------LR 336
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERR---LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNErasleeaLA 890

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2031263915  337 LLRQRKDELEQRMSALQESRRELMVQLEELMKLLKA 372
Cdd:TIGR02168  891 LLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 231-374 4.00e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.94  E-value: 4.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915  231 IASYVARLQHCARVLDSpSRLDEEHRL-IARYAAR--------LAAEAGNVTRPptdlsfnfDANKQQRQLI-------- 293
Cdd:COG3096    439 AEDYLAAFRAKEQQATE-EVLELEQKLsVADAARRqfekayelVCKIAGEVERS--------QAWQTARELLrryrsqqa 509

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915  294 ------------AELENKNREiLQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRllrQRKDELEQRMSALQESRRELMV 361
Cdd:COG3096    510 laqrlqqlraqlAELEQRLRQ-QQNAERLLEEFCQRIGQQLDAAEELEELLAELE---AQLEELEEQAAEAVEQRSELRQ 585

                          170
                   ....*....|....*.
gi 2031263915  362 QLEEL---MKLLKAQA 374
Cdd:COG3096    586 QLEQLrarIKELAARA 601
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
 261-355 4.13e-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: 4.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 261 YAARLAAEAGNVTRppTDLSFNFDANKQQRQLIAELENKNREILQEIQRL--RLEHEQASQPTPEKAQQNPTLLAELRLL 338
Cdd:pfam03961 131 KAKELGSPAGTKTE--IEVGVDFPELKEKLEELEKELEELEEELEKLKKRlkKLPKKARGQLPPEKREQLEKLLETKNKL 208

                          90
                  ....*....|....*..
gi 2031263915 339 RQRKDELEQRMSALQES 355
Cdd:pfam03961 209 SEELEELEEELKELKEE 225
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
243-372 4.34e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 4.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 243 RVLDSPSRLDEEHRLIARYAARLaaeagnvtrpptdlsfnfdanKQQRQLIAELENKNREILQEIQRLRL-----EHEQA 317
Cdd:PRK03918  606 ELKDAEKELEREEKELKKLEEEL---------------------DKAFEELAETEKRLEELRKELEELEKkyseeEYEEL 664

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2031263915 318 SQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKA 372
Cdd:PRK03918  665 REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKA 719
EFh_DMD_like cd16242
EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes ...
 4-66 4.38e-03

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: 37.99  E-value: 4.38e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2031263915   4 VFSQMSDSNGLMifskfDQ-----FLKEVLKLPTAVFEGPSFGYT--EHSVRTCFPQ---QRKIMLNMFLDTM 66
Cdd:cd16242    95 LFSLIADPNGCV-----DQrrlglLLHDCIQIPRQLGEVAAFGGSniEPSVRSCFEKageKPEISAAHFLDWL 162
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
282-373 4.78e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 4.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915  282 NFDANKQQRQLIAELENKnREILQEIQRLRLEHEQASqptpEKAQQNPTLLAELRL--LRQRKDELEQRMSALQESRREL 359
Cdd:COG4913    233 HFDDLERAHEALEDAREQ-IELLEPIRELAERYAAAR----ERLAELEYLRAALRLwfAQRRLELLEAELEELRAELARL 307

                           90
                   ....*....|....
gi 2031263915  360 MVQLEELMKLLKAQ 373
Cdd:COG4913    308 EAELERLEARLDAL 321
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 286-371 5.31e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.23  E-value: 5.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 286 NKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEE 365
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQ 486


                  ....*.
gi 2031263915 366 LMKLLK 371
Cdd:TIGR04523 487 KQKELK 492
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
290-364 5.37e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.23  E-value: 5.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2031263915 290 RQLIAELENKNREILQEIQRLRLEHEQASQptpekaqqnpTLLAELRLLRQRKDELEQRMSALQESRRELMvQLE 364
Cdd:COG3206   294 IALRAQIAALRAQLQQEAQRILASLEAELE----------ALQAREASLQAQLAQLEARLAELPELEAELR-RLE 357
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 251-372 5.58e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.37  E-value: 5.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 251 LDEEHRLIARYAARLaaeaGNVtRPPTDLSfnfDANKQ---QRQLIAELENKNREILQEIQRLRLEHEQASQptpEKAQQ 327
Cdd:COG1579    68 IEEVEARIKKYEEQL----GNV-RNNKEYE---ALQKEiesLKRRISDLEDEILELMERIEELEEELAELEA---ELAEL 136

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2031263915 328 NPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEElmKLLKA 372
Cdd:COG1579   137 EAELEEKKAELDEELAELEAELEELEAEREELAAKIPP--ELLAL 179
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 227-374 5.59e-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: 5.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 227 EHALIASYVARLQHCARVLDSpsRLDEEHRLIARYAARLAAEAGNVTRppTDLSFNfDANKQQRQLIAELENKNREILQE 306
Cdd:COG1196   226 EAELLLLKLRELEAELEELEA--ELEELEAELEELEAELAELEAELEE--LRLELE-ELELELEEAQAEEYELLAELARL 300

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2031263915 307 IQRLRLEHEQASQPTPEKAQqnptLLAELRLLRQRKDELEQRMSALQESRRELmvqlEELMKLLKAQA 374
Cdd:COG1196   301 EQDIARLEERRRELEERLEE----LEEELAELEEELEELEEELEELEEELEEA----EEELEEAEAEL 360
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 249-374 6.23e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.27  E-value: 6.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915  249 SRLDEEHRLIARY---AARLAAEAGNVTRPPTDLSFNFDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKA 325
Cdd:TIGR02168  719 KELEELSRQISALrkdLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2031263915  326 QQNPTLL----AELRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKAQA 374
Cdd:TIGR02168  799 KALREALdelrAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS 851
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
247-372 6.52e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 38.35  E-value: 6.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 247 SPSRLDEEHRLIARyAARLAAEAgnvtrpptdlsfnfdaNKQQRQLiaELENKNREILQEIQRLRLE----HEQASQpTP 322
Cdd:COG1340   128 EVLSPEEEKELVEK-IKELEKEL----------------EKAKKAL--EKNEKLKELRAELKELRKEaeeiHKKIKE-LA 187

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2031263915 323 EKAQQNPTLLAELR----LLRQRKDEL-------EQRMSALQESRRELMVQLEELMKLLKA 372
Cdd:COG1340   188 EEAQELHEEMIELYkeadELRKEADELhkeiveaQEKADELHEEIIELQKELRELRKELKK 248
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
 94-139 6.72e-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: 34.72  E-value: 6.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2031263915  94 VECSYCRCESMMGFRYRCQQCHN--YQLCQNCFwrgHAGGPHSNQHQM 139
Cdd:cd02341     1 FKCDSCGIEPIPGTRYHCSECDDgdFDLCQDCV---VKGESHQEDHWL 45
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
286-373 6.94e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 38.35  E-value: 6.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 286 NKQQRQL---IAELENKNREILQEIQRL---RLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSAL---QESR 356
Cdd:COG1340    49 NAQVKELreeAQELREKRDELNEKVKELkeeRDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLewrQQTE 128

                          90       100
                  ....*....|....*....|....
gi 2031263915 357 -------RELMVQLEELMKLLKAQ 373
Cdd:COG1340   129 vlspeeeKELVEKIKELEKELEKA 152
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
288-372 7.86e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 7.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915  288 QQRQLIAELENKNREILQEIQRLRLEHEQASQptpEKAQQNptllAELRLLR--------QRKDELEQRMSALQESRREL 359
Cdd:COG4913    285 FAQRRLELLEAELEELRAELARLEAELERLEA---RLDALR----EELDELEaqirgnggDRLEQLEREIERLERELEER 357

                           90
                   ....*....|...
gi 2031263915  360 MVQLEELMKLLKA 372
Cdd:COG4913    358 ERRRARLEALLAA 370
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 236-375 8.22e-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: 8.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263915 236 ARLQHCARVLDS-PSRLDEEHRLIARYAARLAAEAGNVTrpptdlsfnfDANKQQRQLIAELEnknrEILQEIQRLRleh 314
Cdd:COG1579    17 SELDRLEHRLKElPAELAELEDELAALEARLEAAKTELE----------DLEKEIKRLELEIE----EVEARIKKYE--- 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2031263915 315 EQASQPTPEKAQQNptLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKAQAT 375
Cdd:COG1579    80 EQLGNVRNNKEYEA--LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA 138
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 296-368 9.30e-03

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 37.94  E-value: 9.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2031263915 296 LENKN---REILQEIQRLrLEHEQASQPTPEKAQQnptLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMK 368
Cdd:cd16269   176 LQSKEaeaEAILQADQAL-TEKEKEIEAERAKAEA---AEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKME 247
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
 291-365 9.37e-03

Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.


Pssm-ID: 428718 [Multi-domain]  Cd Length: 71  Bit Score: 34.93  E-value: 9.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2031263915 291 QLIAELENKNREILQEIQRLRLEHEQASQptpekaqQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEE 365
Cdd:pfam06005   4 ELLEQLETKIQAAVDTIALLQMENEELKE-------ENEELKEEANELEEENQQLKQERNQWQERIRGLLGKLDE 71
 
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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