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Conserved domains on  [gi|386765584|ref|NP_001247050|]
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sarcomere length short, isoform E [Drosophila melanogaster]

Protein Classification

WH2 domain-containing protein( domain architecture ID 1750155)

WH2 (WASP-Homology 2, or Wiskott-Aldrich homology 2) domain-containing protein similar to Homo sapiens actin-binding protein WASF2, which is a downstream effector molecule involved in the transmission of signals from tyrosine kinase receptors and small GTPases to the actin cytoskeleton

Gene Ontology:  GO:0003779
PubMed:  16275905|11911886|17468236
SCOP:  4006720

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 202-434 5.76e-05

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 5.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765584   202 DELDDIDKIRDDLQSTKQMLALELRNREAQ------------------DRENKKLLAKIRTLETELEREKSREKNLEYGS 263
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQELEEKleelrlevseleeeieelQKELYALANEISRLEQQKQILRERLANLERQL 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765584   264 NVIVATMDPTPTAEQTY---VNSLKREVEDARKVSKEVEQNYQSTAEQLVEAKTEIEEQRRQIQLLERKLAAALQGGGSL 340
Cdd:TIGR02168  319 EELEAQLEELESKLDELaeeLAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765584   341 DGSRRPSDANFGR--DSSPELEPEVSE--SDPDEPEEKKVERRERRSGKELKILRSKLTKLKVKEEAAKKEKDALKQAMK 416
Cdd:TIGR02168  399 NNEIERLEARLERleDRRERLQQEIEEllKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478

                          250
                   ....*....|....*...
gi 386765584   417 KNQSILKEENKKFKKLEK 434
Cdd:TIGR02168  479 AAERELAQLQARLDSLER 496
WH2 super family cl41728
Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif), and similar proteins; This ...
 113-139 6.33e-03

Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif), and similar proteins; This family contains the Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) as well as thymosin-beta (Tbeta; also called beta-thymosin or betaT) domains that are small, widespread intrinsically disordered actin-binding peptides displaying significant sequence variability and different regulations of actin self-assembly in motile and morphogenetic processes. These WH2/betaT peptides are identified by a central consensus actin-binding motif LKKT/V flanked by variable N-terminal and C-terminal extensions; the betaT shares a more extended and conserved C-terminal half than WH2. These single or repeated domains are found in actin-binding proteins (ABPs) such as the hematopoietic-specific protein WASP, its ubiquitously expressed ortholog neural-WASP (N-WASP), WASP-interacting protein (WAS/WASL-interacting protein family members 1 and 2), and WASP-family verprolin homologous protein (WAVE/SCAR) isoforms: WAVE1, WAVE2, and WAVE3. Also included are the WH2 domains found in inverted formin FH2 domain-containing protein (INF2), Cordon bleu (Cobl) protein, vasodilator-stimulated phosphoprotein (VASP) homology protein and actobindin (found in amoebae). These ABPs are commonly multidomain proteins that contain signaling domains and structurally conserved actin-binding motifs, the most important being the WH2 domain motif through which they bind actin in order to direct the location, rate, and timing for actin assembly in the cell into different structures, such as filopodia, lamellipodia, stress fibers, and focal adhesions. The WH2 domain motif is one of the most abundant actin-binding motifs in Wiskott-Aldrich syndrome proteins (WASPs) where they activate Arp2/3-dependent actin nucleation and branching in response to signals mediated by Rho-family GTPases. The thymosin beta (Tbeta) domains in metazoans act in cells as major actin-sequestering peptides; their complex with monomeric ATP-actin (G-ATP-actin) cannot polymerize at either filament (F-actin) end.


The actual alignment was detected with superfamily member cd22076:

Pssm-ID: 425359 [Multi-domain]  Cd Length: 32  Bit Score: 34.56  E-value: 6.33e-03
                         10        20
                 ....*....|....*....|....*..
gi 386765584 113 NKLLKQIQGGIKLKPTKTNDRSKPVLD 139
Cdd:cd22076    6 NALLSDINKGKKLKKTVTNDRSAPILD 32
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 202-434 5.76e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 5.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765584   202 DELDDIDKIRDDLQSTKQMLALELRNREAQ------------------DRENKKLLAKIRTLETELEREKSREKNLEYGS 263
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQELEEKleelrlevseleeeieelQKELYALANEISRLEQQKQILRERLANLERQL 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765584   264 NVIVATMDPTPTAEQTY---VNSLKREVEDARKVSKEVEQNYQSTAEQLVEAKTEIEEQRRQIQLLERKLAAALQGGGSL 340
Cdd:TIGR02168  319 EELEAQLEELESKLDELaeeLAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765584   341 DGSRRPSDANFGR--DSSPELEPEVSE--SDPDEPEEKKVERRERRSGKELKILRSKLTKLKVKEEAAKKEKDALKQAMK 416
Cdd:TIGR02168  399 NNEIERLEARLERleDRRERLQQEIEEllKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478

                          250
                   ....*....|....*...
gi 386765584   417 KNQSILKEENKKFKKLEK 434
Cdd:TIGR02168  479 AAERELAQLQARLDSLER 496
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 276-442 5.13e-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: 5.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765584 276 AEQTYVNSLKREVEDARKVSKEVEQNYQSTAEQLVEAKTEIEEQRRQIQLLERKLAAALQgggSLDGSRRP----SDANF 351
Cdd:COG4942   38 ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA---ELEAQKEElaelLRALY 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765584 352 GRDSSPELEPEVSESDPDE------------PEEKKVERRERRSGKELKILRSKLT----KLKVKEEAAKKEKDALKQAM 415
Cdd:COG4942  115 RLGRQPPLALLLSPEDFLDavrrlqylkylaPARREQAEELRADLAELAALRAELEaeraELEALLAELEEERAALEALK 194

                        170       180
                 ....*....|....*....|....*..
gi 386765584 416 KKNQSILKEENKKFKKLEKEVQKMAAS 442
Cdd:COG4942  195 AERQKLLARLEKELAELAAELAELQQE 221
WH2_WAS_WASL-1 cd22076
Wiskott Aldrich syndrome homology region 2 (WH2 motif) in WAS/WASL-interacting protein family ...
 113-139 6.33e-03

Wiskott Aldrich syndrome homology region 2 (WH2 motif) in WAS/WASL-interacting protein family member 1; This family contains the Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) in WAS/WASL-interacting protein family (WIPF, also known as WASP-interacting protein or WIP) member 1 (WIPF1). WIPF1 is a ubiquitously expressed proline-rich multidomain protein and is a binding partner and chaperone of WASP. It stabilizes actin filaments and regulates actin organization and polymerization which are associated with cell migration and invasion. Mutations in the WIPF1 binding site of WASP or in WIPF1 itself cause Wiskott-Aldrich syndrome (WAS), a rare X-linked recessive disease characterized by eczema, thrombocytopenia, immune deficiency, and bloody diarrhea. Aberrant expression of WIPF1 contributes to the invasion and metastasis of several malignancies such breast cancer, glioma and colorectal cancer; it has been identified as an oncoprotein in human pancreatic ductal adenocarcinoma (PDAC) and is associated with poor survival.


Pssm-ID: 409219 [Multi-domain]  Cd Length: 32  Bit Score: 34.56  E-value: 6.33e-03
                         10        20
                 ....*....|....*....|....*..
gi 386765584 113 NKLLKQIQGGIKLKPTKTNDRSKPVLD 139
Cdd:cd22076    6 NALLSDINKGKKLKKTVTNDRSAPILD 32
Filament pfam00038
Intermediate filament protein;
206-335 7.14e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 38.75  E-value: 7.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765584  206 DIDKIRDDLQSTKQMLALELRNREAQDRE-------------NK-KLLAKIRTLETELE------REKSREKNLEYGSNV 265
Cdd:pfam00038  76 ELDNLRLAAEDFRQKYEDELNLRTSAENDlvglrkdldeatlARvDLEAKIESLKEELAflkknhEEEVRELQAQVSDTQ 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765584  266 IVATMDPTPTAEQTYV-NSLKREVED-ARKVSKEVEQNYQSTAEQLVE-----------AKTEIEEQRRQIQLLE----- 327
Cdd:pfam00038 156 VNVEMDAARKLDLTSAlAEIRAQYEEiAAKNREEAEEWYQSKLEELQQaaarngdalrsAKEEITELRRTIQSLEielqs 235


                  ....*....
gi 386765584  328 -RKLAAALQ 335
Cdd:pfam00038 236 lKKQKASLE 244
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 202-434 5.76e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 5.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765584   202 DELDDIDKIRDDLQSTKQMLALELRNREAQ------------------DRENKKLLAKIRTLETELEREKSREKNLEYGS 263
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQELEEKleelrlevseleeeieelQKELYALANEISRLEQQKQILRERLANLERQL 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765584   264 NVIVATMDPTPTAEQTY---VNSLKREVEDARKVSKEVEQNYQSTAEQLVEAKTEIEEQRRQIQLLERKLAAALQGGGSL 340
Cdd:TIGR02168  319 EELEAQLEELESKLDELaeeLAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765584   341 DGSRRPSDANFGR--DSSPELEPEVSE--SDPDEPEEKKVERRERRSGKELKILRSKLTKLKVKEEAAKKEKDALKQAMK 416
Cdd:TIGR02168  399 NNEIERLEARLERleDRRERLQQEIEEllKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478

                          250
                   ....*....|....*...
gi 386765584   417 KNQSILKEENKKFKKLEK 434
Cdd:TIGR02168  479 AAERELAQLQARLDSLER 496
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 276-442 5.13e-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: 5.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765584 276 AEQTYVNSLKREVEDARKVSKEVEQNYQSTAEQLVEAKTEIEEQRRQIQLLERKLAAALQgggSLDGSRRP----SDANF 351
Cdd:COG4942   38 ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA---ELEAQKEElaelLRALY 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765584 352 GRDSSPELEPEVSESDPDE------------PEEKKVERRERRSGKELKILRSKLT----KLKVKEEAAKKEKDALKQAM 415
Cdd:COG4942  115 RLGRQPPLALLLSPEDFLDavrrlqylkylaPARREQAEELRADLAELAALRAELEaeraELEALLAELEEERAALEALK 194

                        170       180
                 ....*....|....*....|....*..
gi 386765584 416 KKNQSILKEENKKFKKLEKEVQKMAAS 442
Cdd:COG4942  195 AERQKLLARLEKELAELAAELAELQQE 221
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 217-439 1.42e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765584   217 TKQMLALELRNREAQdRENKKLLAKIRTLETELEREKSREKNLEYGSNVIVATMDPTPTAEQTY---VNSLKREVEDARK 293
Cdd:TIGR02168  683 EEKIEELEEKIAELE-KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLeerIAQLSKELTELEA 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765584   294 VSKEVEQNYQSTAEQLVEAKTEIEEQRRQIQLLERKLAAALQGGGSLDG-----SRRPSDANFGRDSSpELEPEVSESDP 368
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAeltllNEEAANLRERLESL-ERRIAATERRL 840

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386765584   369 DEPEEKKVERRERRSG--KELKILRSKLTKLKVKEEAAKKEKDALKQAMKKNQSILKEENKKFKKLEKEVQKM 439
Cdd:TIGR02168  841 EDLEEQIEELSEDIESlaAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 219-441 2.00e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765584 219 QMLALELRNREAQDRENKkLLAKIRTLETELEREKSREKNLEygsnvivatmdptptAEQTyvnSLKREVEDARKVSKEV 298
Cdd:COG1196  275 ELEELELELEEAQAEEYE-LLAELARLEQDIARLEERRRELE---------------ERLE---ELEEELAELEEELEEL 335

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765584 299 EQNYQSTAEQLVEAKTEIEEQRRQIQLLERKLAAALQGGGSLDGSRRPSDANFGRDSSPELEPEVSESDPDEPEEKKVER 378
Cdd:COG1196  336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386765584 379 RERRSGKELKILRSKLTKLKVKEEAAKKEKDALKQAMKKNQSILKEENKKFKKLEKEVQKMAA 441
Cdd:COG1196  416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
199-420 3.04e-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: 3.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765584  199 ESPDELDDIDKIRDDLQSTKqmlalELRNREAQDRENKKLLAKIRTLETELEREKSREKNLEYgsnvIVATMDptPTAEQ 278
Cdd:COG4913   219 EEPDTFEAADALVEHFDDLE-----RAHEALEDAREQIELLEPIRELAERYAAARERLAELEY----LRAALR--LWFAQ 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765584  279 TYVNSLKREVEDARKVSKEVEQNYQSTAEQLVEAKTEIEEQRRQ--------IQLLERKLAAALQgggSLDGSRRPSDAN 350
Cdd:COG4913   288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgnggdrLEQLEREIERLER---ELEERERRRARL 364

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386765584  351 FGRDSSPELEPEVSESDPDEpEEKKVERRERRSGKELKILRSKLTKLKVKEEAAKKEKDALKQ---AMKKNQS 420
Cdd:COG4913   365 EALLAALGLPLPASAEEFAA-LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAeiaSLERRKS 436
WH2_WAS_WASL-1 cd22076
Wiskott Aldrich syndrome homology region 2 (WH2 motif) in WAS/WASL-interacting protein family ...
 113-139 6.33e-03

Wiskott Aldrich syndrome homology region 2 (WH2 motif) in WAS/WASL-interacting protein family member 1; This family contains the Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) in WAS/WASL-interacting protein family (WIPF, also known as WASP-interacting protein or WIP) member 1 (WIPF1). WIPF1 is a ubiquitously expressed proline-rich multidomain protein and is a binding partner and chaperone of WASP. It stabilizes actin filaments and regulates actin organization and polymerization which are associated with cell migration and invasion. Mutations in the WIPF1 binding site of WASP or in WIPF1 itself cause Wiskott-Aldrich syndrome (WAS), a rare X-linked recessive disease characterized by eczema, thrombocytopenia, immune deficiency, and bloody diarrhea. Aberrant expression of WIPF1 contributes to the invasion and metastasis of several malignancies such breast cancer, glioma and colorectal cancer; it has been identified as an oncoprotein in human pancreatic ductal adenocarcinoma (PDAC) and is associated with poor survival.


Pssm-ID: 409219 [Multi-domain]  Cd Length: 32  Bit Score: 34.56  E-value: 6.33e-03
                         10        20
                 ....*....|....*....|....*..
gi 386765584 113 NKLLKQIQGGIKLKPTKTNDRSKPVLD 139
Cdd:cd22076    6 NALLSDINKGKKLKKTVTNDRSAPILD 32
Filament pfam00038
Intermediate filament protein;
206-335 7.14e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 38.75  E-value: 7.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765584  206 DIDKIRDDLQSTKQMLALELRNREAQDRE-------------NK-KLLAKIRTLETELE------REKSREKNLEYGSNV 265
Cdd:pfam00038  76 ELDNLRLAAEDFRQKYEDELNLRTSAENDlvglrkdldeatlARvDLEAKIESLKEELAflkknhEEEVRELQAQVSDTQ 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765584  266 IVATMDPTPTAEQTYV-NSLKREVED-ARKVSKEVEQNYQSTAEQLVE-----------AKTEIEEQRRQIQLLE----- 327
Cdd:pfam00038 156 VNVEMDAARKLDLTSAlAEIRAQYEEiAAKNREEAEEWYQSKLEELQQaaarngdalrsAKEEITELRRTIQSLEielqs 235


                  ....*....
gi 386765584  328 -RKLAAALQ 335
Cdd:pfam00038 236 lKKQKASLE 244
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 212-438 9.06e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.90  E-value: 9.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765584   212 DDLQSTKQMLA--LELRNREAQDRENKKLLAKIRTLETELEREKSR--EKNLEYGSNVIV-----ATMDPTPTAEQTYVN 282
Cdd:TIGR02169  214 QALLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELEKLTEEisELEKRLEEIEQLleelnKKIKDLGEEEQLRVK 293

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765584   283 S------------------LKREVEDARKVSKEVEQNYQSTAEQLVEAKTEIEEQRRQ-------IQLLERKLAAALQGG 337
Cdd:TIGR02169  294 EkigeleaeiaslersiaeKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRrdklteeYAELKEELEDLRAEL 373

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765584   338 GSLDGSRRPSDANFgRDSSPELEPEVSESDPDEPEE-KKVERRERRSGK------ELKILRSKLTKLKVKEEAAKKEKDA 410
Cdd:TIGR02169  374 EEVDKEFAETRDEL-KDYREKLEKLKREINELKRELdRLQEELQRLSEEladlnaAIAGIEAKINELEEEKEDKALEIKK 452

                          250       260
                   ....*....|....*....|....*...
gi 386765584   411 LKQAMKKNQSILKEENKKFKKLEKEVQK 438
Cdd:TIGR02169  453 QEWKLEQLAADLSKYEQELYDLKEEYDR 480
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 307-436 9.19e-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: 39.17  E-value: 9.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765584  307 EQLVEAKTEIEEQRRQIQLLERKLAAALQGGGSLDGSRRPSdanfgRDSSPELEPEVSE---SDPDEPEEKKVERRERRS 383
Cdd:COG3096   991 ARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAK-----QQTLQELEQELEElgvQADAEAEERARIRRDELH 1065

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386765584  384 GkELKILRSKLTKLkvkeeaaKKEKDALKQAMKKNQSILKEENKKFKKLEKEV 436
Cdd:COG3096  1066 E-ELSQNRSRRSQL-------EKQLTRCEAEMDSLQKRLRKAERDYKQEREQV 1110
 
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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