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Conserved domains on  [gi|887239938|ref|NP_001297433|]
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actin-related protein 3B isoform 2 [Mus musculus]

Protein Classification

actin-related protein 3( domain architecture ID 19021160)

actin-related protein 3 (ACTR3) is an ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
1-322 0e+00

nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, also called actin-like protein 3, is the ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex is comprised of 7 proteins (Arp2, Arp3, and five conserved proteins, ARPC1-5). It generates cytoplasmic branched filaments networks, by promoting nucleation of actin filaments as 70 degrees branches on the side of older filaments. It is activated, by simultaneously binding to a pre-existing filament and a nucleation promoting factor plus an actin monomer. Daughter branches subsequently detach/debranch from the mother filament. Its Arp2 and Arp3 subunits must be loaded with ATP for it to initiate the assembly of branched actin filaments. ATP hydrolysis may be required for branch initiation or debranching. The Arp2/3 complex is also found in the nucleus where it plays a role in promoting de novo actin polymerization and in RNA polymerase II-dependent transcription. This may in part be through regulating nuclear actin polymerization in a way like its function in the cytoplasm. Human Arp3 and Arp3B are encoded by the ACTR3 and ACTR3B genes respectively. Arp3B is also known as actin-related protein Arp4.


:

Pssm-ID: 466822  Cd Length: 404  Bit Score: 713.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938   1 MERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIAVQAVLALAASWTSRQVGERTLTGIVI 80
Cdd:cd10221   83 MERFWEQCIFKYLRCEPEDHYFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQAVLALAASWTSRKVGERTLTGTVI 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  81 DSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICPDIVREFAKYDVD 160
Cdd:cd10221  163 DSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREEGIPPEDSLEVAKRIKERYCYVCPDIVKEFAKYDSD 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 161 PRKWIKQYTGINAINQKKFIIDVGYERFLGPEIFFHPEFANPDFMESISDVVDEVIQSCPIDVRRPLYKNVVLSGGSTMF 240
Cdd:cd10221  243 PAKYIKQYTGINSVTGKPYTVDVGYERFLAPEIFFNPEIASSDFTTPLPEVVDQVIQSCPIDTRRGLYKNIVLSGGSTMF 322
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 241 RDFGRRLQRDLKRVVDARLKLSQELSGGRIKPKPVEVQVVTHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPSIC 320
Cdd:cd10221  323 KDFGRRLQRDVKRIVDARLKASEELSGGKLKPKPIDVNVISHPMQRYAVWFGGSMLASTPEFYTVCHTKAEYEEYGPSIC 402

                 ..
gi 887239938 321 RH 322
Cdd:cd10221  403 RH 404
 
Name Accession Description Interval E-value
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
1-322 0e+00

nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, also called actin-like protein 3, is the ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex is comprised of 7 proteins (Arp2, Arp3, and five conserved proteins, ARPC1-5). It generates cytoplasmic branched filaments networks, by promoting nucleation of actin filaments as 70 degrees branches on the side of older filaments. It is activated, by simultaneously binding to a pre-existing filament and a nucleation promoting factor plus an actin monomer. Daughter branches subsequently detach/debranch from the mother filament. Its Arp2 and Arp3 subunits must be loaded with ATP for it to initiate the assembly of branched actin filaments. ATP hydrolysis may be required for branch initiation or debranching. The Arp2/3 complex is also found in the nucleus where it plays a role in promoting de novo actin polymerization and in RNA polymerase II-dependent transcription. This may in part be through regulating nuclear actin polymerization in a way like its function in the cytoplasm. Human Arp3 and Arp3B are encoded by the ACTR3 and ACTR3B genes respectively. Arp3B is also known as actin-related protein Arp4.


Pssm-ID: 466822  Cd Length: 404  Bit Score: 713.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938   1 MERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIAVQAVLALAASWTSRQVGERTLTGIVI 80
Cdd:cd10221   83 MERFWEQCIFKYLRCEPEDHYFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQAVLALAASWTSRKVGERTLTGTVI 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  81 DSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICPDIVREFAKYDVD 160
Cdd:cd10221  163 DSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREEGIPPEDSLEVAKRIKERYCYVCPDIVKEFAKYDSD 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 161 PRKWIKQYTGINAINQKKFIIDVGYERFLGPEIFFHPEFANPDFMESISDVVDEVIQSCPIDVRRPLYKNVVLSGGSTMF 240
Cdd:cd10221  243 PAKYIKQYTGINSVTGKPYTVDVGYERFLAPEIFFNPEIASSDFTTPLPEVVDQVIQSCPIDTRRGLYKNIVLSGGSTMF 322
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 241 RDFGRRLQRDLKRVVDARLKLSQELSGGRIKPKPVEVQVVTHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPSIC 320
Cdd:cd10221  323 KDFGRRLQRDVKRIVDARLKASEELSGGKLKPKPIDVNVISHPMQRYAVWFGGSMLASTPEFYTVCHTKAEYEEYGPSIC 402

                 ..
gi 887239938 321 RH 322
Cdd:cd10221  403 RH 404
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
1-329 0e+00

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 598.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938   1 MERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIAVQAVLALAASWTSRQVGER--TLTGI 78
Cdd:PTZ00280  84 MEKFWEQCIFKYLRCEPEEHYFILTEPPMNPPENREYTAEIMFETFNVKGLYIAVQAVLALRASWTSKKAKELggTLTGT 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  79 VIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICPDIVREFAKYD 158
Cdd:PTZ00280 164 VIDSGDGVTHVIPVVDGYVIGSSIKHIPLAGRDITNFIQQMLRERGEPIPAEDILLLAQRIKEKYCYVAPDIAKEFEKYD 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 159 VDPRKWIKQYTGINAINQKKFIIDVGYERFLGPEIFFHPEFANPDFMESISDVVDEVIQSCPIDVRRPLYKNVVLSGGST 238
Cdd:PTZ00280 244 SDPKNHFKKYTAVNSVTKKPYTVDVGYERFLGPEMFFHPEIFSSEWTTPLPEVVDDAIQSCPIDCRRPLYKNIVLSGGST 323
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 239 MFRDFGRRLQRDLKRVVDARLKLSQELSGGRIKPKPVEVQVVTHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPS 318
Cdd:PTZ00280 324 MFKGFDKRLQRDVRKRVDRRLKKAEELSGGKLKPIPIDVNVVSHPRQRYAVWYGGSMLASSPEFEKVCHTKAEYDEYGPS 403
                        330
                 ....*....|.
gi 887239938 319 ICRHNPVFGVM 329
Cdd:PTZ00280 404 ICRYNNVFHSV 414
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
1-324 5.30e-123

Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 357.72  E-value: 5.30e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938     1 MERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIAVQAVLALAASWTSrqvgertlTGIVI 80
Cdd:smart00268  77 MEKIWDYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRT--------TGLVI 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938    81 DSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICPDIVREFAKYDvd 160
Cdd:smart00268 149 DSGDGVTHVVPVVDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLAR-- 226
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938   161 pRKWIKQYTGINAINQKKFIIDVGYERFLGPEIFFHPEFANPDFmESISDVVDEVIQSCPIDVRRPLYKNVVLSGGSTMF 240
Cdd:smart00268 227 -ESSESSKLEKTYELPDGNTIKVGNERFRIPEILFSPELIGLEQ-KGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLI 304
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938   241 RDFGRRLQRDLKRVVdarlklsqelsggrikPKPVEVQVVTHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPSIC 320
Cdd:smart00268 305 PGFGERLEKELKQLA----------------PKKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIV 368

                   ....
gi 887239938   321 RHNP 324
Cdd:smart00268 369 ERKC 372
Actin pfam00022
Actin;
1-321 5.01e-74

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 233.74  E-value: 5.01e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938    1 MERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIavqavlALAASWTSRQVGeRTlTGIVI 80
Cdd:pfam00022  75 MEEIWEHVLKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYL------AKNPVLSAFASG-RT-TGLVV 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938   81 DSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKA---------------------- 138
Cdd:pfam00022 147 DSGAGVTSVVPVHDGYVLQKAIRRSDLGGDFLTDYLRELLRSRNIEITPRYLIKSKKPgdpapavtkrelpdttysykty 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  139 --------IKEKYCYICPDIVREFAKYdvdprkwikqytgiNAINQKKFI------IDVGYERFLGPEIFFHPEFANPD- 203
Cdd:pfam00022 227 qerrvleeIKESVCYVSDDPFGDETTS--------------SSIPTRVYElpdgstIILGAERFRVPEILFNPSLIGSEs 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  204 ------FMESISDVVDEVIQSCPIDVRRPLYKNVVLSGGSTMFRDFGRRLQRDLKRVVdarlklsqeLSGGRIKPKPVEV 277
Cdd:pfam00022 293 elpppqTAVGIPELIVDAINACDVDLRPSLLANIVVTGGNSLFPGFTERLEKELAQLA---------PPGVKVKIIAPGN 363
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 887239938  278 QVVThhmqRYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPSICR 321
Cdd:pfam00022 364 TVER----RYSAWIGGSILASLGTFQQMWVSKQEYEEHGASVVE 403
COG5277 COG5277
Actin-related protein [Cytoskeleton];
11-298 4.36e-28

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 112.96  E-value: 4.36e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  11 KYLRAEPEDHYFLM--TEPPLNTPENREYLAEIMFESF---NVPGLYIAVQAVLALaaswtsrqVGERTLTGIVIDSGDG 85
Cdd:COG5277  110 QFLVVDPEFHGFLVvvALSALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPLAVA--------IAEKAVTCVVVEAGHG 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  86 VTHVIPVAEGyVIGSCIKHIPIAGRDITYFIQQLLREREVG-IPPEQslETAKAIKEKYCYICPDIVREFAKYDVDPRKW 164
Cdd:COG5277  182 NSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSdTAREE--YVVRVVKEALGLVPRDLAKAIQKAASNPDSF 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 165 IKQYTGINAINQKKfIIDVGYERFLGPEIFFHPEFanpDFMES------------------------ISDVVDEVIQSCP 220
Cdd:COG5277  259 EAKVRLPNPTVEIE-LGNYAWERFLIGEILFNPNH---EGFESyiqqgrlriedavigdvvlygemgLAEAIINSIMKCD 334
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 887239938 221 IDVRRPLYKNVVLSGGSTMFrdfgrRLQRDLKRV-VDARLKLSQELSggRIKPKpVEVQVVTHHMQRYAVWFGGSMLAS 298
Cdd:COG5277  335 VEIQDELYSNIILSGGAFNW-----SVPPGLEDVaVDSVTRVQIELS--ELAPE-LKVNVRLVSDPQYSVWKGAIIYGY 405
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
286-319 6.83e-06

syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in the plant pathogen Pseudomonas syringae and related species. This model was created, in part, to clarify that the family is real and distinct, rather than an artifact of eukaryotic contamination of bacterial genomic sequence data. As of the creation of this HMM, the family is uncharacterized.


Pssm-ID: 468549 [Multi-domain]  Cd Length: 132  Bit Score: 44.97  E-value: 6.83e-06
                         10        20        30
                 ....*....|....*....|....*....|....
gi 887239938 286 RYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPSI 319
Cdd:NF040575  94 ESAAWRGAAMYAASEGFVEMAITKQEYDESGPSI 127
 
Name Accession Description Interval E-value
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
1-322 0e+00

nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, also called actin-like protein 3, is the ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex is comprised of 7 proteins (Arp2, Arp3, and five conserved proteins, ARPC1-5). It generates cytoplasmic branched filaments networks, by promoting nucleation of actin filaments as 70 degrees branches on the side of older filaments. It is activated, by simultaneously binding to a pre-existing filament and a nucleation promoting factor plus an actin monomer. Daughter branches subsequently detach/debranch from the mother filament. Its Arp2 and Arp3 subunits must be loaded with ATP for it to initiate the assembly of branched actin filaments. ATP hydrolysis may be required for branch initiation or debranching. The Arp2/3 complex is also found in the nucleus where it plays a role in promoting de novo actin polymerization and in RNA polymerase II-dependent transcription. This may in part be through regulating nuclear actin polymerization in a way like its function in the cytoplasm. Human Arp3 and Arp3B are encoded by the ACTR3 and ACTR3B genes respectively. Arp3B is also known as actin-related protein Arp4.


Pssm-ID: 466822  Cd Length: 404  Bit Score: 713.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938   1 MERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIAVQAVLALAASWTSRQVGERTLTGIVI 80
Cdd:cd10221   83 MERFWEQCIFKYLRCEPEDHYFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQAVLALAASWTSRKVGERTLTGTVI 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  81 DSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICPDIVREFAKYDVD 160
Cdd:cd10221  163 DSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREEGIPPEDSLEVAKRIKERYCYVCPDIVKEFAKYDSD 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 161 PRKWIKQYTGINAINQKKFIIDVGYERFLGPEIFFHPEFANPDFMESISDVVDEVIQSCPIDVRRPLYKNVVLSGGSTMF 240
Cdd:cd10221  243 PAKYIKQYTGINSVTGKPYTVDVGYERFLAPEIFFNPEIASSDFTTPLPEVVDQVIQSCPIDTRRGLYKNIVLSGGSTMF 322
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 241 RDFGRRLQRDLKRVVDARLKLSQELSGGRIKPKPVEVQVVTHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPSIC 320
Cdd:cd10221  323 KDFGRRLQRDVKRIVDARLKASEELSGGKLKPKPIDVNVISHPMQRYAVWFGGSMLASTPEFYTVCHTKAEYEEYGPSIC 402

                 ..
gi 887239938 321 RH 322
Cdd:cd10221  403 RH 404
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
1-329 0e+00

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 598.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938   1 MERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIAVQAVLALAASWTSRQVGER--TLTGI 78
Cdd:PTZ00280  84 MEKFWEQCIFKYLRCEPEEHYFILTEPPMNPPENREYTAEIMFETFNVKGLYIAVQAVLALRASWTSKKAKELggTLTGT 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  79 VIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICPDIVREFAKYD 158
Cdd:PTZ00280 164 VIDSGDGVTHVIPVVDGYVIGSSIKHIPLAGRDITNFIQQMLRERGEPIPAEDILLLAQRIKEKYCYVAPDIAKEFEKYD 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 159 VDPRKWIKQYTGINAINQKKFIIDVGYERFLGPEIFFHPEFANPDFMESISDVVDEVIQSCPIDVRRPLYKNVVLSGGST 238
Cdd:PTZ00280 244 SDPKNHFKKYTAVNSVTKKPYTVDVGYERFLGPEMFFHPEIFSSEWTTPLPEVVDDAIQSCPIDCRRPLYKNIVLSGGST 323
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 239 MFRDFGRRLQRDLKRVVDARLKLSQELSGGRIKPKPVEVQVVTHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPS 318
Cdd:PTZ00280 324 MFKGFDKRLQRDVRKRVDRRLKKAEELSGGKLKPIPIDVNVVSHPRQRYAVWYGGSMLASSPEFEKVCHTKAEYDEYGPS 403
                        330
                 ....*....|.
gi 887239938 319 ICRHNPVFGVM 329
Cdd:PTZ00280 404 ICRYNNVFHSV 414
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
1-324 5.30e-123

Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 357.72  E-value: 5.30e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938     1 MERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIAVQAVLALAASWTSrqvgertlTGIVI 80
Cdd:smart00268  77 MEKIWDYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRT--------TGLVI 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938    81 DSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICPDIVREFAKYDvd 160
Cdd:smart00268 149 DSGDGVTHVVPVVDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLAR-- 226
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938   161 pRKWIKQYTGINAINQKKFIIDVGYERFLGPEIFFHPEFANPDFmESISDVVDEVIQSCPIDVRRPLYKNVVLSGGSTMF 240
Cdd:smart00268 227 -ESSESSKLEKTYELPDGNTIKVGNERFRIPEILFSPELIGLEQ-KGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLI 304
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938   241 RDFGRRLQRDLKRVVdarlklsqelsggrikPKPVEVQVVTHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPSIC 320
Cdd:smart00268 305 PGFGERLEKELKQLA----------------PKKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIV 368

                   ....
gi 887239938   321 RHNP 324
Cdd:smart00268 369 ERKC 372
ASKHA_NBD_actin_Arp-T1-3 cd13397
nucleotide-binding domain (NBD) of actin, actin-related proteins T1-T3 (Arp-T1-3), and similar ...
1-316 3.70e-86

nucleotide-binding domain (NBD) of actin, actin-related proteins T1-T3 (Arp-T1-3), and similar proteins; The family includes actin and human actin-related proteins T1, T2, and T3. Actin is a ubiquitous protein involved in the formation of filaments that are major components of the cytoskeleton. It is a highly dynamic structural protein network involved in processes such as cell contraction, cell motility, vesicle trafficking, intracellular organization, cytokinesis, endocytosis and apoptosis. Arp-T1, encoded by ACTRT1/ARPT1 gene expressed in testis, negatively regulates the Hedgehog (SHH) signaling, binds to the promoter of the SHH signaling mediator, GLI1, and inhibits its expression. Arp-T2 (also called actin-related protein M2; encoded by ACTRT2/ARPM2 gene expressed in testis and various other cell types) and Arp-T3 (also called actin-related protein M1; encoded by ACTRT3/ARPM1 gene expressed in all tested human tissues) play general roles in the organization of the cytoskeleton like other cytoplasmic actin-related proteins.


Pssm-ID: 466848 [Multi-domain]  Cd Length: 359  Bit Score: 263.28  E-value: 3.70e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938   1 MERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIAVQAVLALAASwtsrqvGeRTlTGIVI 80
Cdd:cd13397   77 MEKIWHHTFENELRVKPEEHPVLLTEAPLNPKQNREKMAEIMFETFGVPAFYVAIQAVLSLYSS------G-RT-TGLVL 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  81 DSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICPDIVREFAKydvD 160
Cdd:cd13397  149 DSGDGVTHTVPIYEGYALPHAVQRLDLAGRDLTEYLMKLLKERGHSFTTTAEREIVRDIKEKLCYVALDYEEELKK---K 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 161 PRKWIKQYT---GInainqkkfIIDVGYERFLGPEIFFHPEFANPDfMESISDVVDEVIQSCPIDVRRPLYKNVVLSGGS 237
Cdd:cd13397  226 SEELEKEYTlpdGQ--------VIKIGSERFRCPEALFRPSLIGRE-APGIHKLVYNSIMKCDIDIRKDLYSNIVLSGGS 296
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 887239938 238 TMFRDFGRRLQRDLKRVVdarlklsqelsggrikPKPVEVQVVTHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYG 316
Cdd:cd13397  297 TMFPGLPERLQKELEALA----------------PSSTKVKVIAPPERKYSVWIGGSILASLSTFKSMWITRAEYDEFG 359
ASKHA_NBD_actin-like cd10169
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ...
1-316 1.89e-82

nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ubiquitous in eukaryotes, and the major component of the actin cytoskeleton; monomeric globular protein (G-actin) reversibly polymerizes to form filaments (F-actin). Each actin protomer binds one molecule of ATP and either calcium or magnesium ions. F-actin filaments form with the consequent hydrolysis of ATP. Some actin-related proteins (Arps) have roles in cytoskeletal functions, such as actin polymerization (Arp2/3) and dynein motor activity (Arp1). Both conventional actin and specific Arps have been implicated in chromatin remodeling and/or transcription regulation. The actin/ARP family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466810 [Multi-domain]  Cd Length: 258  Bit Score: 250.49  E-value: 1.89e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938   1 MERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIavqavlalaaswtSRQ-------VGeR 73
Cdd:cd10169   29 MEKIWEHVFYNLLRVDPEEHPVLLTEPPLNPKANREKLAEILFETFNVPSLYI-------------ANQavlslyaSG-R 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  74 TlTGIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCyicpdivre 153
Cdd:cd10169   95 T-TGLVVDSGEGVTHIVPVYEGYVLPHAVRRLDIGGRDLTDYLAKLLREKGYSFSTSAEREIVRDIKEKLC--------- 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 154 fakydvdprkwikqytginainqkkfiidvgyerflgpeiffhpefanpdfmeSISDVVDEVIQSCPIDVRRPLYKNVVL 233
Cdd:cd10169  165 -----------------------------------------------------GLHELIYDSIMKCDIDLRKELYSNIVL 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 234 SGGSTMFRDFGRRLQRDLKRVVdarlklsqelsggrikPKPVEVQVVTHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYE 313
Cdd:cd10169  192 SGGTTLFPGFAERLQKELSKLA----------------PSSVKVKVIAPPERKYSAWIGGSILASLSTFQQMWITKEEYE 255

                 ...
gi 887239938 314 EYG 316
Cdd:cd10169  256 EHG 258
Actin pfam00022
Actin;
1-321 5.01e-74

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 233.74  E-value: 5.01e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938    1 MERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIavqavlALAASWTSRQVGeRTlTGIVI 80
Cdd:pfam00022  75 MEEIWEHVLKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYL------AKNPVLSAFASG-RT-TGLVV 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938   81 DSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKA---------------------- 138
Cdd:pfam00022 147 DSGAGVTSVVPVHDGYVLQKAIRRSDLGGDFLTDYLRELLRSRNIEITPRYLIKSKKPgdpapavtkrelpdttysykty 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  139 --------IKEKYCYICPDIVREFAKYdvdprkwikqytgiNAINQKKFI------IDVGYERFLGPEIFFHPEFANPD- 203
Cdd:pfam00022 227 qerrvleeIKESVCYVSDDPFGDETTS--------------SSIPTRVYElpdgstIILGAERFRVPEILFNPSLIGSEs 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  204 ------FMESISDVVDEVIQSCPIDVRRPLYKNVVLSGGSTMFRDFGRRLQRDLKRVVdarlklsqeLSGGRIKPKPVEV 277
Cdd:pfam00022 293 elpppqTAVGIPELIVDAINACDVDLRPSLLANIVVTGGNSLFPGFTERLEKELAQLA---------PPGVKVKIIAPGN 363
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 887239938  278 QVVThhmqRYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPSICR 321
Cdd:pfam00022 364 TVER----RYSAWIGGSILASLGTFQQMWVSKQEYEEHGASVVE 403
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
5-323 5.05e-72

nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, also called centractin, actin-like protein, alpha-centractin, actin-RPV, or centrosome-associated actin homolog, may be a component of a multi-subunit centrosomal complex involved in microtubule-based vesicle motility. In yeast, actin-related protein is essential for viability and is associated with the centrosome. In vertebrates, Arp1 is a core component of the dynactin complex which assists cytoplasmic dynein by increasing its processivity and by regulation of its cargo binding. The dynactin complex is required for the spindle translocation late in anaphase and is involved in a cell wall synthesis checkpoint. ARP1 forms the backbone filament of the dynactin rod structure and serves as the scaffold for the remaining subunits. It is required for proper orientation of the mitotic spindle. Arp1 is the only actin-related protein known to form actin-like filaments. Human Arp1/centractin is encoded by the ACTR1A gene.


Pssm-ID: 466820 [Multi-domain]  Cd Length: 370  Bit Score: 227.43  E-value: 5.05e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938   5 MEQVvFKY------LRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIAVQAVLALAASwtsrqvGeRTlTGI 78
Cdd:cd10216   78 MERI-WQYvysklqLNTFSEEHPVLLTEAPLNPRKNREKAAEVFFETFNVPALFVSMQAVLSLYAS------G-RT-TGV 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  79 VIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLR----------EREVgippeqsletAKAIKEKYCYICP 148
Cdd:cd10216  149 VLDSGDGVTHAVPIYEGFALPHSIRRVDIAGRDVTEYLQLLLRksgynfhtsaEFEI----------VREIKEKACYVAL 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 149 DIVREFAKYDVDPRKwiKQYT---GInainqkkfIIDVGYERFLGPEIFFHPEFANPDFmESISDVVDEVIQSCPIDVRR 225
Cdd:cd10216  219 NPQKEEKLEEEKTEK--AQYTlpdGS--------TIEIGPERFRAPEILFNPELIGLEY-PGVHEVLVDSIQKSDLDLRK 287
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 226 PLYKNVVLSGGSTMFRDFGRRLQRDLKRVV--DARLKLSqelsggrikpKPVEvqvvthhmQRYAVWFGGSMLASTPEFF 303
Cdd:cd10216  288 TLYSNIVLSGGSTLFKGFGDRLLSEVKKLApkDVKIRIS----------APPE--------RLYSTWIGGSILASLSTFK 349
                        330       340
                 ....*....|....*....|
gi 887239938 304 QVCHTKKDYEEYGPSICRHN 323
Cdd:cd10216  350 KMWVSKKEYEEDGARILHRK 369
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
1-319 2.95e-70

nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein involved in the formation of filaments that are major components of the cytoskeleton. It is a highly dynamic structural protein network involved in processes such as cell contraction, cell motility, vesicle trafficking, intracellular organization, cytokinesis, endocytosis and apoptosis. Actin is a monomeric globular protein (G-actin) that reversibly polymerizes to form filaments (F-actin). Each actin protomer binds one molecule of ATP and either calcium or magnesium ions. At low salt concentrations, actin exists as a monomer, and as the salt concentration rises F-actin forms, with the consequent hydrolysis of ATP. F-actin assembly is in constant flux with G-actin association occurring at the barbed end (+) and its disassociation at the pointed end (-). Actin monomers that have been released from the pointed end can be reused, if the ADP is exchanged for ATP. F-actin filaments can assemble into higher order structures, for example branched F-actin, and stress fibers. Actin binding proteins regulate actin filament dynamics by a range of functions including actin severing, depolymerizing, capping, stabilizing and de novo actin polymerization. Actins interaction with myosin is the basis of muscular contraction and many aspects of cell motility. In vertebrates there are three main groups of actin isoforms, alpha, beta and gamma. The alpha actins found in muscle tissues are a major constituent of the contractile apparatus. The beta and gamma actins co-exist in most cell types as components of the cytoskeleton and as mediators of internal cell motility. In plants there are many isoforms which are probably involved in a variety of functions such as cytoplasmic streaming, cell shape determination, tip growth, graviperception, cell wall deposition, etc.


Pssm-ID: 466823  Cd Length: 365  Bit Score: 222.63  E-value: 2.95e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938   1 MERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIAVQAVLALAASwtsrqvgERTlTGIVI 80
Cdd:cd10224   77 MEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYAS-------GRT-TGIVL 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  81 DSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICPDIVREFAKYDVD 160
Cdd:cd10224  149 DSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASS 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 161 PRkwikqytginaiNQKKF------IIDVGYERFLGPEIFFHPEFANpdfMES--ISDVVDEVIQSCPIDVRRPLYKNVV 232
Cdd:cd10224  229 SS------------LEKSYelpdgqVITIGNERFRCPEALFQPSFLG---MEAagIHETTYNSIMKCDVDIRKDLYANIV 293
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 233 LSGGSTMFRDFGRRLQRDLKRVVdarlklsqelsggrikPKPVEVQVVTHHMQRYAVWFGGSMLASTPEFFQVCHTKKDY 312
Cdd:cd10224  294 LSGGTTMFPGIADRMQKEITALA----------------PSTMKIKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEY 357

                 ....*..
gi 887239938 313 EEYGPSI 319
Cdd:cd10224  358 DESGPSI 364
PTZ00004 PTZ00004
actin-2; Provisional
1-319 3.03e-69

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 220.41  E-value: 3.03e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938   1 MERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIAVQAVLALAASwtsrqvgERTlTGIVI 80
Cdd:PTZ00004  83 MEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETHNVPAMYVAIQAVLSLYAS-------GRT-TGIVL 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  81 DSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICPDivrefakYDVD 160
Cdd:PTZ00004 155 DSGDGVSHTVPIYEGYSLPHAIHRLDVAGRDLTEYMMKILHERGTTFTTTAEKEIVRDIKEKLCYIALD-------FDEE 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 161 PrkwiKQYTGINAINQKKF------IIDVGYERFLGPEIFFHPEFANPDFMESISDVVDEVIQSCPIDVRRPLYKNVVLS 234
Cdd:PTZ00004 228 M----GNSAGSSDKYEESYelpdgtIITVGSERFRCPEALFQPSLIGKEEPPGIHELTFQSINKCDIDIRKDLYGNIVLS 303
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 235 GGSTMFRDFGRRLQRDLKRVVdarlklsqelsggrikPKPVEVQVVTHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEE 314
Cdd:PTZ00004 304 GGTTMYRGLPERLTKELTTLA----------------PSTMKIKVVAPPERKYSVWIGGSILSSLPTFQQMWVTKEEYDE 367

                 ....*
gi 887239938 315 YGPSI 319
Cdd:PTZ00004 368 SGPSI 372
ASKHA_NBD_Arp2 cd10220
nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, ...
13-321 1.34e-63

nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, also called actin-like protein 2, is the ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex is comprised of 7 proteins (Arp2, Arp3, and five conserved proteins, ARPC1-5). It generates cytoplasmic branched filaments networks, by promoting nucleation of actin filaments as 70 degrees branches on the side of older filaments. It is activated, by simultaneously binding to a pre-existing filament and a nucleation promoting factor plus an actin monomer. Daughter branches subsequently detach/debranch from the mother filament. Its Arp2 and Arp3 subunits must be loaded with ATP for it to initiate the assembly of branched actin filaments. ATP hydrolysis may be required for branch initiation or debranching. The Arp2/3 complex is also found in the nucleus where it plays a role in promoting de novo actin polymerization and in RNA polymerase II-dependent transcription. This may in part be through regulating nuclear actin polymerization in a way like its function in the cytoplasm. Human Arp2 is encoded by the ACTR2 gene.


Pssm-ID: 466821  Cd Length: 381  Bit Score: 205.88  E-value: 1.34e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  13 LRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIavqavlalaaswtSRQV-----GERTLTGIVIDSGDGVT 87
Cdd:cd10220   91 LKIDPRECKILLTEPPMNPTKNREKMVEVMFEKYGFAGVYV-------------AIQAvltlyAQGLLTGVVVDSGDGVT 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  88 HVIPVAEGYVIGSCIKHIPIAGRDIT-YFIQQLLRErevGIPPEQS--LETAKAIKEKYCYICPDIVREfAKYDVDPRKW 164
Cdd:cd10220  158 HIVPVYEGFSLPHLTRRLDVAGRDITrYLIKLLLLR---GYAFNRTadFETVREIKEKLCYVAYDIELE-QKLALETTVL 233
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 165 IKQYT---GinainqkkFIIDVGYERFLGPEIFFHPEFANpdfMES--ISDVVDEVIQSCPIDVRRPLYKNVVLSGGSTM 239
Cdd:cd10220  234 VESYTlpdG--------RVIKVGGERFEAPEALFQPHLID---VEGpgIAELLFNTIQAADIDTRPELYKHIVLSGGSTM 302
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 240 FRDFGRRLQRDLKrvvdaRLKLSQELSGGRIKPKPVEVQVVTHHMQRYAVWFGGSMLA----STPEFFQvchTKKDYEEY 315
Cdd:cd10220  303 YPGLPSRLEKEIK-----QLYLERVLKGDTERLSKFKIRIEDPPRRKHMVFLGGAVLAdimkDKDEFWI---TRQEYEEQ 374

                 ....*.
gi 887239938 316 GPSICR 321
Cdd:cd10220  375 GVRVLD 380
PTZ00281 PTZ00281
actin; Provisional
1-319 1.67e-60

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 198.00  E-value: 1.67e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938   1 MERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIAVQAVLALAASwtsrqvgERTlTGIVI 80
Cdd:PTZ00281  83 MEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYAS-------GRT-TGIVM 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  81 DSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICPDIVREFakydvd 160
Cdd:PTZ00281 155 DSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEM------ 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 161 prkwikQYTGINAINQKKF------IIDVGYERFLGPEIFFHPEFANpdfMES--ISDVVDEVIQSCPIDVRRPLYKNVV 232
Cdd:PTZ00281 229 ------QTAASSSALEKSYelpdgqVITIGNERFRCPEALFQPSFLG---MESagIHETTYNSIMKCDVDIRKDLYGNVV 299
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 233 LSGGSTMFRDFGRRLQRDLKrvvdarlklsqelsggRIKPKPVEVQVVTHHMQRYAVWFGGSMLASTPEFFQVCHTKKDY 312
Cdd:PTZ00281 300 LSGGTTMFPGIADRMNKELT----------------ALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEY 363

                 ....*..
gi 887239938 313 EEYGPSI 319
Cdd:PTZ00281 364 DESGPSI 370
PTZ00466 PTZ00466
actin-like protein; Provisional
5-319 3.26e-58

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 192.08  E-value: 3.26e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938   5 MEQV---VFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIAVQAVLALAASWTSrqvgertlTGIVID 81
Cdd:PTZ00466  89 MENIwihVYNSMKINSEEHPVLLTEAPLNPQKNKEKIAEVFFETFNVPALFISIQAILSLYSCGKT--------NGTVLD 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  82 SGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICPDIVREFAKYDvdp 161
Cdd:PTZ00466 161 CGDGVCHCVSIYEGYSITNTITRTDVAGRDITTYLGYLLRKNGHLFNTSAEMEVVKNMKENCCYVSFNMNKEKNSSE--- 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 162 rkwiKQYTGINAINQKKFIIDVGYERFLGPEIFFHPEFANPDFMeSISDVVDEVIQSCPIDVRRPLYKNVVLSGGSTMFR 241
Cdd:PTZ00466 238 ----KALTTLPYILPDGSQILIGSERYRAPEVLFNPSILGLEYL-GLSELIVTSITRADMDLRRTLYSHIVLSGGTTMFH 312
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 887239938 242 DFGRRLQRDLKrvvdarlklsqelsggRIKPKPVEVQVVTHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPSI 319
Cdd:PTZ00466 313 GFGDRLLNEIR----------------KFAPKDITIRISAPPERKFSTFIGGSILASLATFKKIWISKQEFDEYGSVI 374
ASKHA_NBD_Arp4_ACTL6-like cd13395
nucleotide-binding domain (NBD) of the actin-related protein 4 (Arp4)-like subfamily; The ...
1-316 2.31e-57

nucleotide-binding domain (NBD) of the actin-related protein 4 (Arp4)-like subfamily; The Arp4-like subfamily includes Arp4, also called actin-like protein 4, from fungi and plants. Saccharomyces cerevisiae Arp4 acts synergistically with Arp8 to depolymerize F-actin; it binds ATP, but unlike conventional actin, does not form filaments. It is a component of the NuA4 histone acetyltransferase complex, the chromatin-remodeling INO80 complex and the SWR1 chromatin remodeling complex. Arabidopsis thaliana Arp4 is involved in several developmental processes including organization of plant organs, flowering time, anther development, flower senescence and fertility, probably by regulating the chromatin structure. This family also includes human homologs of yeast and plant, which are actin-like protein 6A (encoded by the ACTL6A gene; also known as ArpNbeta, 53 kDa BRG1-associated factor A/BRG1-associated factor 53A/BAF35A, and INO80 complex subunit K/INO80K) and actin-like protein 6B (encoded by the ACTL6B gene; also known as ArpNalpha, 53 kDa BRG1-associated factor B/BRG1-associated factor 53B/BAF35B). ACTL6A and ACTL6B are involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). They are components of numerous complexes with chromatin remodeling and histone acetyltransferase activity. ACTL6A is also a putative core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. Schizosaccharomyces pombe actin-related protein 42 (Arp42) is also included in this family. It is also a component of SWI/SNF and RSC complexes.


Pssm-ID: 466846 [Multi-domain]  Cd Length: 413  Bit Score: 190.85  E-value: 2.31e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938   1 MERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIavqavlalaaswtSRQ-------VGeR 73
Cdd:cd13395   88 FEKLWDHALKNRLRVDPSEHPLLLTEPSWNTRANREKLTELMFEKYNVPAFFL-------------AKNavlsafaNG-R 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  74 TlTGIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSL---------ETAKAIKEKYC 144
Cdd:cd13395  154 S-TALVVDSGATSTSVVPVHDGYVLQKAIVRSPLGGDFLTDQLLKLLESKNIEIIPRYMIkskepveggAPAKYTKKDLP 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 145 --------YICPDIVREFAK--YDVDPRKWIKQYTGinAINQKKF------IIDVGYERFLGPEIFFHPEFANPDF---- 204
Cdd:cd13395  233 nttssyhrYMVRRVLQDFKEsvCQVSDSPFDESEAA--SIPTVSYelpdgyNIEFGAERFKIPELLFDPSLVKGIPapps 310
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 205 ----MESISDVVDEVIQSCPIDVRRPLYKNVVLSGGSTMFRDFGRRLQRDLKRvvdarlKLSQELsggRIK----PKPVE 276
Cdd:cd13395  311 egneLLGLPQLVYTSIGSCDVDIRPELYGNVVLTGGNSLLPGFTDRLNRELSE------KAPGSL---KLKilasGNTVE 381
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 887239938 277 vqvvthhmQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYG 316
Cdd:cd13395  382 --------RRFSSWIGGSILASLGSFQQMWISKQEYEEHG 413
ASKHA_NBD_ACTL7 cd10214
nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ...
6-319 4.77e-56

nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ACTL7-like family includes ACTL7A, ACTL7B and ACTL9 (also known as ACTL7C). In mammalian, ACTL7A is expressed in a wide variety of adult tissues, while the ACTL7B is expressed in spermatids through the elongation phase of spermatid development. ACTL7A, also called actin-like-7-alpha, or T-ACTIN-2 in mouse, may play an important role in formation and fusion of Golgi-derived vesicles during acrosome biogenesis. ACTL7B, also called actin-like-7-beta, acts as a key regulator of spermiogenesis that is required for male fertility. ACTL9 is a testis-specific protein that plays an important role in fusion of proacrosomal vesicles and perinuclear theca formation.


Pssm-ID: 466819 [Multi-domain]  Cd Length: 368  Bit Score: 186.09  E-value: 4.77e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938   6 EQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIavqavlaLAASWTSRQVGERTlTGIVIDSGDG 85
Cdd:cd10214   85 EYIFEKEMKILPEEHAVLVSDPPLSPTTNREKYAELMFETFSIPAMHI-------AYQSRLSLYSYGRT-SGLVVESGHG 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  86 VTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLreREVGIP-PEQSLETAKAIKEKYCYICPDIVREFAkydVDPRKW 164
Cdd:cd10214  157 VSYVVPIHEGYNLPHITGRADYAGSDLTAYLMKLL--NEAGNKfTDDQLHIVEDIKKKCCYVALDFEEEMG---LPPQEY 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 165 IKQYTGINAinqkkFIIDVGYERFLGPEIFFHPEFAnPDFMESISDVVDEVIQSCPIDVRRPLYKNVVLSGGSTMFRDFG 244
Cdd:cd10214  232 TVDYELPDG-----HLITIGKERFRCPEMLFNPSLI-GSKQPGLHTLTMNSLNKCDANLKKDLAKNILLCGGSTMFDGFP 305
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 887239938 245 RRLQRDLKRVVdarlklsqelsggrikpkPVEVQVVTHHMQR-YAVWFGGSMLASTPEFFQVCHTKKDYEEYGPSI 319
Cdd:cd10214  306 DRFQKELSKLC------------------PNDNPIVAASPERkYSVWTGGSILASLKSFQQLWVRRREYEERGPFV 363
ASKHA_NBD_Arp6 cd10210
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ...
6-316 2.13e-45

nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, also called actin-like protein 6, is required for formation and/or maintenance of proper nucleolar structure and function, plays a dual role in the regulation of ribosomal DNA (rDNA) transcription. In the presence of high glucose, Arp6 maintains active rDNA transcription through H2A.Z deposition and under glucose starvation, it is required for the repression of rDNA transcription, and this function may be independent of H2A.Z. Arp6 is also required for telomere silencing in both fission and budding yeast. It is a component of the budding yeast and Arabidopsis SWR1 complex (SWR1C) and the human SWI2/SNF2-related CBP activator protein (SRCAP) chromatin remodeling complexes which catalyze the exchange of the histone H2A with the H2AZ. Drosophila Arp6 colocalizes with HP1 (heterochromatin protein 1) in the pericentric heterochromatin, and vertebrate Arp6 also interacts with HP1. Human Arp6 is encoded by the ACTR6 gene. Arabidopsis thaliana ACTIN RELATED PROTEIN 6/EARLY IN SHORT DAYS 1/SUPPRESSOR OF FRIGIDA 3 (encoded by ARP6/ESD1/SUF3) participates in regulating several leaf and flower development stages. It is needed for Flowering locus C (FLC, the master repressor of flowering) and FLC-like gene expression in the shoot and root apex, and for the activity of the floral repressor pathway.


Pssm-ID: 466816 [Multi-domain]  Cd Length: 389  Bit Score: 158.87  E-value: 2.13e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938   6 EQVVFKYL------RAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIA------VQAVLALAASWTSRqvgeR 73
Cdd:cd10210   70 QRQIWDHLfgklllNVDPSDTALVLTEPPFNPPSIQEAMDEIVFEEYGFQSLYRTtaaalsAFAYLADSEQSSSS----S 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  74 TLTGIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLetAKAIKEKYCYICPDIVRE 153
Cdd:cd10210  146 SQCCLVVDSGFSFTHIVPFFDGKPVKRAVRRIDVGGKLLTNYLKEIISYRQLNVMDETYL--VNQIKEDLCFVSTDFYED 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 154 FAKYDVDPRK-WIKQ------YTGINainqKKFIIDVGY-----------------ERFLGPEIFFHPEFANPDFMeSIS 209
Cdd:cd10210  224 LEIAKKKGKEnTIRRdyvlpdYTTSK----RGYVRDPEEpnrgklkedeqvlrlnnERFTVPELLFHPSDIGIQQA-GIA 298
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 210 DVVDEVIQSCPIDVRRPLYKNVVLSGGSTMFRDFGRRLQRDLKRVVdarlklsqelsggrikPKPVEVQVVTHHMQRYAV 289
Cdd:cd10210  299 EAIVQSINACPEELQPLLYANIVLTGGNALFPGFRERLEAELRSLA----------------PDDYDVNVTLPEDPITYA 362
                        330       340
                 ....*....|....*....|....*..
gi 887239938 290 WFGGSMLASTPEFFQVCHTKKDYEEYG 316
Cdd:cd10210  363 WEGGSLLAQSPEFEELAVTRAEYEEHG 389
PTZ00452 PTZ00452
actin; Provisional
1-319 3.61e-41

actin; Provisional


Pssm-ID: 185631  Cd Length: 375  Bit Score: 147.59  E-value: 3.61e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938   1 MERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIAVQAVLALAASWTSrqvgertlTGIVI 80
Cdd:PTZ00452  82 IEIIWHHAFYNELCMSPEDQPVFMTDAPMNSKFNRERMTQIMFETFNTPCLYISNEAVLSLYTSGKT--------IGLVV 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  81 DSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICpdivrefakydVD 160
Cdd:PTZ00452 154 DSGEGVTHCVPVFEGHQIPQAITKINLAGRLCTDYLTQILQELGYSLTEPHQRIIVKNIKERLCYTA-----------LD 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 161 PRKWIKQYTGINAINQ-----KKFIIDVGYERFLGPEIFFHPEFANPDfMESISDVVDEVIQSCPIDVRRPLYKNVVLSG 235
Cdd:PTZ00452 223 PQDEKRIYKESNSQDSpyklpDGNILTIKSQKFRCSEILFQPKLIGLE-VAGIHHLAYSSIKKCDLDLRQELCRNIVLSG 301
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 236 GSTMFRDFGRRLQRDLKRVVDARLKlsqelsggrikpkpveVQVVTHHMQRYAVWFGGSMLAS----TPEFFQvchtKKD 311
Cdd:PTZ00452 302 GTTLFPGIANRLSNELTNLVPSQLK----------------IQVAAPPDRRFSAWIGGSIQCTlstqQPQWIK----RQE 361

                 ....*...
gi 887239938 312 YEEYGPSI 319
Cdd:PTZ00452 362 YDEQGPSI 369
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
5-317 1.90e-35

nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, also called actin-like protein 5, may act as a core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. It is involved in DNA double-strand break repair and UV-damage excision repair. Human Arp5 is encoded by the ACTR5 gene. Arabidopsis thaliana ARP5 (AtARp5) is a ubiquitously expressed nuclear protein involved in DNA repair and required for multicellular development of all organs. AtARp5 may be part of other chromatin remodeling machines in addition to INO80.


Pssm-ID: 466817 [Multi-domain]  Cd Length: 345  Bit Score: 131.54  E-value: 1.90e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938   5 MEQV---VFKYLRAEPE---DHYFLMTEPPLNTPENREYLAEIMFESFNVP-------GLYiavqavlalaaSWTSRQVG 71
Cdd:cd10211   73 QEQIldyIFSHLGINSEgsvDHPIVLTEALCNPNYSRQLMSELLFECYGVPsvaygidSLF-----------SYYHNQPQ 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  72 ERTLTGIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICPDIV 151
Cdd:cd10211  142 GDPSDGLVISSGYSTTHVIPVLNGRLDLSQCKRINLGGFHATDYLQRLLQLKYPTHPSAITLSRAEELVHEHCYVAEDYD 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 152 REFAKYDvDPRKWikqytginaiNQKKFIIDVGYerflgpeiffhpefanpdfmeSISDVVDEVIQSCPIDVRRPLYKNV 231
Cdd:cd10211  222 EELKKWE-DPEYY----------EENVRKIQLPF---------------------GLVETIEFVLKRYPAEQQDRLVQNV 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 232 VLSGGSTMFRDFGRRLQRDLKrvvdarlklsqelsggRIKPKPVEVQVVTHHMQRYAVWFGGSMLASTPEFFQVCHTKKD 311
Cdd:cd10211  270 FLTGGNALFPGLKERLEKELR----------------AIRPFGSPFNVVRAKDPVLDAWRGAAKWALDSTFEKVWITKQE 333

                 ....*.
gi 887239938 312 YEEYGP 317
Cdd:cd10211  334 YEEKGG 339
ASKHA_NBD_Arp10 cd10207
nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins; ...
2-316 4.85e-35

nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins; Arp10, also known as actin-related protein 11 (Arp11), is a subunit of the cargo-binding portion of the dynein activator, dynactin. It, together with dynactin4 (p62), -5(p25), and -6(p27), forms a heterotetrameric complex located at the pointed end of Arp1. Arp1 forms a mini-filament of uniform size, with proteins bound along its length and at both ends. Human Arp10 is encoded by the ACTR10 gene.


Pssm-ID: 466813 [Multi-domain]  Cd Length: 375  Bit Score: 130.84  E-value: 4.85e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938   2 ERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPG-LYIavqavlalaaswTSRQVGERTL---TG 77
Cdd:cd10207   55 KEFLHELYFKHLLVNPKDRRVVVVESVLCPTPFRETLAKVLFKHFEVPSvLFA------------PSHLLSLLTLgirTA 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  78 IVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQ------------SLETAKAIKEKYCY 145
Cdd:cd10207  123 LVVDCGYRETRVLPVYEGVPLLSAWQSTPLGGKALHKRLKKLLLEHATVVTGDNkgqllssvdsllSEEVLEDIKVRACF 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 146 ICP-DIVREFAKYDVDPRKWIKQY---TGINAINQKKFIIdVGYERFLGPEIFFhpEFANPDfmESISDVVDEVIQSCPI 221
Cdd:cd10207  203 VTSlERGKTLQSATEEGSTEEPSPpppVDYPLDGEKILIV-PGSIRESAEELLF--EGDNEE--KSLPTLILDSLLKCPI 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 222 DVRRPLYKNVVLSGGSTMFRDFGRRLQRDLKRVVDARlKLSQELSGGRIKPkpveVQVVTHHMQRYAVWFGGSMLASTPE 301
Cdd:cd10207  278 DVRKQLAENIVVIGGTSMLPGFKHRLLEELRALLRKP-KYFEELAPKTFRF----HTPPSVFKPNYLAWLGGSIFGALES 352
                        330
                 ....*....|....*
gi 887239938 302 FFQVCHTKKDYEEYG 316
Cdd:cd10207  353 ILGRSLSREAYLQTG 367
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
1-319 1.69e-31

nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar proteins; Arabidopsis thaliana ARP7 is an essential nuclear protein, ubiquitously expressed in all cell types. It is needed for normal embryogenesis, plant architecture, and floral organ abscission. It may play a role in regulating various phases of plant development through chromatin-mediated gene regulation.


Pssm-ID: 466815 [Multi-domain]  Cd Length: 354  Bit Score: 120.96  E-value: 1.69e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938   1 MERFMEQVVFKYLRAEPEDH-YFLMTEPPLNTPENREYLAEIMFESFNVPGLYIavqavlalaaswtSRQ-------VGE 72
Cdd:cd10209   62 LEALLRYVFYTGLGWEEGNEgQVLIAEPLLTSKAERERLTQLMFETFNVSGLYA-------------SEQavlslyaVGR 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  73 rtLTGIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIppEQSLETAKAIKEKYCYiCPDIVR 152
Cdd:cd10209  129 --ISGCVVDVGHGKIDIAPVWEGAIQHNAVRRFEIGGRDLTELLAAELGKSNPKV--KLDRSIVERLKEAVAW-SADDEE 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 153 EFAKYDVDPRkwIKQYTGINAinQKkfiIDVGYERFLGPEIFFHPEfANPDFMESISDVVDEVIQSCPIDVRRPLYKNVV 232
Cdd:cd10209  204 AYEKKVLTCS--PETYTLPDG--RV---ISVGKERYCVGEALFRPS-ILGIEEYGIVEQLVRAVSTSPSENRRQLLENIV 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 233 LSGGSTMFRDFGRRLQRdlkrvvDARLKLSQELSGGRIKPkPvevQVVTHHMQRYAVWFGGSMLASTpEFFQVCH-TKKD 311
Cdd:cd10209  276 LCGGTSSVPGLEARLQK------EIRLLSSPSSRPALVKP-P---EYMPENTLRYSAWIGGAILAKV-VFPQNQHvTKAD 344

                 ....*...
gi 887239938 312 YEEYGPSI 319
Cdd:cd10209  345 YDETGPSV 352
COG5277 COG5277
Actin-related protein [Cytoskeleton];
11-298 4.36e-28

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 112.96  E-value: 4.36e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  11 KYLRAEPEDHYFLM--TEPPLNTPENREYLAEIMFESF---NVPGLYIAVQAVLALaaswtsrqVGERTLTGIVIDSGDG 85
Cdd:COG5277  110 QFLVVDPEFHGFLVvvALSALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPLAVA--------IAEKAVTCVVVEAGHG 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  86 VTHVIPVAEGyVIGSCIKHIPIAGRDITYFIQQLLREREVG-IPPEQslETAKAIKEKYCYICPDIVREFAKYDVDPRKW 164
Cdd:COG5277  182 NSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSdTAREE--YVVRVVKEALGLVPRDLAKAIQKAASNPDSF 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 165 IKQYTGINAINQKKfIIDVGYERFLGPEIFFHPEFanpDFMES------------------------ISDVVDEVIQSCP 220
Cdd:COG5277  259 EAKVRLPNPTVEIE-LGNYAWERFLIGEILFNPNH---EGFESyiqqgrlriedavigdvvlygemgLAEAIINSIMKCD 334
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 887239938 221 IDVRRPLYKNVVLSGGSTMFrdfgrRLQRDLKRV-VDARLKLSQELSggRIKPKpVEVQVVTHHMQRYAVWFGGSMLAS 298
Cdd:COG5277  335 VEIQDELYSNIILSGGAFNW-----SVPPGLEDVaVDSVTRVQIELS--ELAPE-LKVNVRLVSDPQYSVWKGAIIYGY 405
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
2-319 6.76e-25

nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and similar proteins; Saccharomyces cerevisiae Arp9, also called actin-like protein 9, chromatin structure-remodeling complex protein ARP9, or SWI/SNF complex component ARP9, is a component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. It is also part of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, which is required for the positive and negative regulation of gene expression of many genes. Arp9 forms a stable heterodimer with Arp7 protein in both the RSC and SWI/SNF chromatin-remodeling complexes. It has been suggested that this dimer functions as a module with DNA bending proteins, to achieve correct architecture and facilitate complex-complex interactions. Fission yeast SWI/SNF and RSC complexes do not contain Arp7 and Arp8, but instead contain Arp9 and Arp42.


Pssm-ID: 466814  Cd Length: 356  Bit Score: 103.16  E-value: 6.76e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938   2 ERFMEQVVFKYL--RAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIavqavlalaaswtsrqvGERTL---- 75
Cdd:cd10208   51 EALWRHILFSLLsiPRPTNNSPVLLSVPPSWSKSDLELLTQLFFERLNVPAFAI-----------------LEAPLaaly 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  76 -----TGIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQS------LETAKAIKEKyc 144
Cdd:cd10208  114 aagatSGIVVDIGHEKTDITPIVDSQVVPHALVSIPIGGQDCTAHLAQLLKSDEPELKSQAEsgeeatLDLAEALKKS-- 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 145 yicpDIVrEFAKYDVDPRKWIKqytginainqkkfiIDVGYERFLGPEIFFHPEF---ANPDFMESISDVvdeVIQSCPI 221
Cdd:cd10208  192 ----PIC-EVLSDGADLASGTE--------------ITVGKERFRACEPLFKPSSlrvDLLIAAIAGALV---LNASDEP 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 222 DVRRPLYKNVVLSGGSTMFRDFGRRLQRDLKRVVdarlkLSQELSGGRIKP---KPVEV----QVVTHHMQRYAVWFGGS 294
Cdd:cd10208  250 DKRPALWENIIIVGGGSRIRGLKEALLSELQQFH-----LISETSASPQQPriiRLAKIpdyfPEWKKSGYEEAAFLGAS 324
                        330       340       350
                 ....*....|....*....|....*....|.
gi 887239938 295 MLA------STPEFFQvchTKKDYEEYGPSI 319
Cdd:cd10208  325 IVAklvfndPSSKHYI---SKVDYNEKGPAA 352
ASKHA_NBD_AtArp8-like cd13396
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and ...
70-312 6.08e-16

nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and similar proteins; Arabidopsis thaliana ARP8, also called F-box protein ARP8, is an F-Box protein localized to the nucleolus. It is ubiquitously expressed in all organs and cell types and has a cell cycle-dependent subcellular pattern of distribution: it is localized to the nucleolus in interphase cells and dispersed in the cytoplasm in mitotic cells.


Pssm-ID: 466847  Cd Length: 332  Bit Score: 77.20  E-value: 6.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  70 VGERTlTGIVIDSGDGVTHVIPVAEGYV---IGscIKHIPIAGRDITYFIQQLLREREVGIPpeqSLETAKAIKEKYCYI 146
Cdd:cd13396  111 AANRT-SGIVVNIGFRVTTIVPVYRGRVmhdIG--VEVVGQGALRLTGFLKELMQQNGIRFP---SLYTVRTIKEKLCYV 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 147 CPDIVREFAK-----YDVDPRKWikqytginainqkkFIIdvGYERFLGPEIFFHPEFANPDFMeSISDVVDEVIQSCPI 221
Cdd:cd13396  185 AEDYEAELAKdtqasCEVAGEGW--------------FTL--SNERFKTGEILFQPGLGGMRAM-GLHQAVALCMDHCAL 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 222 DVR---RPLYKNVVLSGGSTMFRDFGRRLQRDLKRVVDARLklsqeLSGGRIKPKPVEVqvvthhmqrYAVWFGGSMLAS 298
Cdd:cd13396  248 VHSqgdDGWFKTIVLSGGSACLPGLSERLERELRKLLPKSL-----SEGIRIIPPPLGP---------DSAWQGAKLISN 313
                        250
                 ....*....|....*
gi 887239938 299 TPEFFQV-CHTKKDY 312
Cdd:cd13396  314 LSNFPDGwCITKKQF 328
ASKHA_NBD_Arp8-like cd10206
nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The ...
76-322 2.23e-07

nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The Arp8-like family includes Arp8, also called actin-like protein 8, from vertebrates and fungi. Human Arp8 is encoded by the ACTR8 gene and is also known as INO80 complex subunit N. It plays an important role in the functional organization of mitotic chromosomes. Arp8 exhibits low basal ATPase activity, and is unable to polymerize. It is probably a core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication, and probably DNA repair. it is required for the recruitment of INO80 (and probably the INO80 complex) to sites of DNA damage. Arp8 strongly prefers nucleosomes and H3-H4 tetramers over H2A-H2B dimers, suggesting it may act as a nucleosome recognition module within the complex. This subfamily also contains Arabidopsis thaliana Arp9.


Pssm-ID: 466812 [Multi-domain]  Cd Length: 447  Bit Score: 51.86  E-value: 2.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  76 TGIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLreREVGIPPE-------QSLETAKAIKEKYCYICP 148
Cdd:cd10206  234 SACVVDIGAQKTSVACVEDGLSIPNSRIRLPYGGDDITRCFLWLL--RRSGFPYRecnlnspLDFLLLERLKETYCTLDQ 311
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 149 DI--VREfakYDVDPRKWIKQytginainQKKFIIdvgyeRFLGpeiffhpefanpdfmesISDVVDEVIQSCP-IDVRR 225
Cdd:cd10206  312 DDigVQL---HEFYVREPGQP--------TLKYQF-----KLLP-----------------LDEAIVQSILSCAsDELKR 358
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 226 PLYKNVVLSGGSTMFRDFGRRLQRDLKRVVDARLKLSQElsggrikpkpVEVQVVTHHMQ-RYAVWFGGSMLA---STPE 301
Cdd:cd10206  359 KMYSSILLVGGGAKIPGLAEALEDRLLIKIPSLFEAVET----------VEVLPPPKDMDpSLLAWKGGAVLAcldSAQE 428
                        250       260
                 ....*....|....*....|.
gi 887239938 302 FFQvchTKKDYEEYGPSICRH 322
Cdd:cd10206  429 LWI---TRKEWQRLGVRALRE 446
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
286-319 6.83e-06

syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in the plant pathogen Pseudomonas syringae and related species. This model was created, in part, to clarify that the family is real and distinct, rather than an artifact of eukaryotic contamination of bacterial genomic sequence data. As of the creation of this HMM, the family is uncharacterized.


Pssm-ID: 468549 [Multi-domain]  Cd Length: 132  Bit Score: 44.97  E-value: 6.83e-06
                         10        20        30
                 ....*....|....*....|....*....|....
gi 887239938 286 RYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPSI 319
Cdd:NF040575  94 ESAAWRGAAMYAASEGFVEMAITKQEYDESGPSI 127
ASKHA_NBD_FtsA cd24048
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ...
72-237 9.78e-04

nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. FtsA binds ATP. FtsA interacts with FtsZ. This interaction plays an essential role in cell division.


Pssm-ID: 466898 [Multi-domain]  Cd Length: 372  Bit Score: 40.59  E-value: 9.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938  72 ERTLTGIVIDSGDGVTHVIPVAEGYVIgsCIKHIPIAGRDITYFIQQLLRerevgIPpeqsLETAKAIKEKY--CYICPD 149
Cdd:cd24048  195 EKELGVALIDIGGGTTDIAVFKNGSLR--YTAVIPVGGNHITNDIAIGLN-----TP----FEEAERLKIKYgsALSEEA 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887239938 150 IVREFAKYDVDPRKWIKQYTginainqKKFIIDVGYERFLgpEIFfhpefanpdfmesiSDVVDEVIQScpiDVRRPLYK 229
Cdd:cd24048  264 DEDEIIEIPGVGGREPREVS-------RRELAEIIEARVE--EIL--------------ELVKKELKES---GYEDLLPG 317

                 ....*...
gi 887239938 230 NVVLSGGS 237
Cdd:cd24048  318 GIVLTGGG 325
ASKHA_NBD_PilM-like cd24004
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ...
72-143 6.85e-03

nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes type IV pilus inner membrane component PilM, cell division protein FtsA, and ethanolamine utilization protein EutJ. PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity. Members in PilM-like family belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466854 [Multi-domain]  Cd Length: 282  Bit Score: 37.66  E-value: 6.85e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 887239938  72 ERTLTGIVIDSGDGVTHVIPVAEGYVIGscIKHIPIAGRDITYFIQQllrerEVGIppeqSLETAKAIKEKY 143
Cdd:cd24004  111 MRDLNIALVDIGAGTTDIALIRNGGIEA--YRMVPLGGDDFTKAIAE-----GFLI----SFEEAEKIKRTY 171
 
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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