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Conserved domains on  [gi|1207165482|ref|XP_021325769|]
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actin-related protein 3B isoform X3 [Danio rerio]

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: 711.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482   1 MEKFMEQVIFKYLRAEPEDHNFLMTEPPLNTPENREYLAEIMFETFNVPGLYIAVQAVLALAASWTSRQVGERTLTGIVI 80
Cdd:cd10221    83 MERFWEQCIFKYLRCEPEDHYFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQAVLALAASWTSRKVGERTLTGTVI 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  81 DSGDGVTHAIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREIGIPPEQSLETAKAVKERYCYICPDIVKEFTKYDMD 160
Cdd:cd10221   163 DSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREEGIPPEDSLEVAKRIKERYCYVCPDIVKEFAKYDSD 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 161 PGKWIKKYKGINAISKNEFQIDVGYERFLGPEIFFHPEFANPDFMQPISDVVDEVIQNCPIDVRRPLYKNIVLSGGSTMF 240
Cdd:cd10221   243 PAKYIKQYTGINSVTGKPYTVDVGYERFLAPEIFFNPEIASSDFTTPLPEVVDQVIQSCPIDTRRGLYKNIVLSGGSTMF 322
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 241 RDFGRRLQRDLKRVVDARLRLSEELSGGRIKPKPMEVQVISHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPRIC 320
Cdd:cd10221   323 KDFGRRLQRDVKRIVDARLKASEELSGGKLKPKPIDVNVISHPMQRYAVWFGGSMLASTPEFYTVCHTKAEYEEYGPSIC 402

                  ..
gi 1207165482 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: 711.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482   1 MEKFMEQVIFKYLRAEPEDHNFLMTEPPLNTPENREYLAEIMFETFNVPGLYIAVQAVLALAASWTSRQVGERTLTGIVI 80
Cdd:cd10221    83 MERFWEQCIFKYLRCEPEDHYFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQAVLALAASWTSRKVGERTLTGTVI 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  81 DSGDGVTHAIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREIGIPPEQSLETAKAVKERYCYICPDIVKEFTKYDMD 160
Cdd:cd10221   163 DSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREEGIPPEDSLEVAKRIKERYCYVCPDIVKEFAKYDSD 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 161 PGKWIKKYKGINAISKNEFQIDVGYERFLGPEIFFHPEFANPDFMQPISDVVDEVIQNCPIDVRRPLYKNIVLSGGSTMF 240
Cdd:cd10221   243 PAKYIKQYTGINSVTGKPYTVDVGYERFLAPEIFFNPEIASSDFTTPLPEVVDQVIQSCPIDTRRGLYKNIVLSGGSTMF 322
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 241 RDFGRRLQRDLKRVVDARLRLSEELSGGRIKPKPMEVQVISHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPRIC 320
Cdd:cd10221   323 KDFGRRLQRDVKRIVDARLKASEELSGGKLKPKPIDVNVISHPMQRYAVWFGGSMLASTPEFYTVCHTKAEYEEYGPSIC 402

                  ..
gi 1207165482 321 RH 322
Cdd:cd10221   403 RH 404
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
1-327 0e+00

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 592.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482   1 MEKFMEQVIFKYLRAEPEDHNFLMTEPPLNTPENREYLAEIMFETFNVPGLYIAVQAVLALAASWTSRQVGER--TLTGI 78
Cdd:PTZ00280   84 MEKFWEQCIFKYLRCEPEEHYFILTEPPMNPPENREYTAEIMFETFNVKGLYIAVQAVLALRASWTSKKAKELggTLTGT 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  79 VIDSGDGVTHAIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREIGIPPEQSLETAKAVKERYCYICPDIVKEFTKYD 158
Cdd:PTZ00280  164 VIDSGDGVTHVIPVVDGYVIGSSIKHIPLAGRDITNFIQQMLRERGEPIPAEDILLLAQRIKEKYCYVAPDIAKEFEKYD 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 159 MDPGKWIKKYKGINAISKNEFQIDVGYERFLGPEIFFHPEFANPDFMQPISDVVDEVIQNCPIDVRRPLYKNIVLSGGST 238
Cdd:PTZ00280  244 SDPKNHFKKYTAVNSVTKKPYTVDVGYERFLGPEMFFHPEIFSSEWTTPLPEVVDDAIQSCPIDCRRPLYKNIVLSGGST 323
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 239 MFRDFGRRLQRDLKRVVDARLRLSEELSGGRIKPKPMEVQVISHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPR 318
Cdd:PTZ00280  324 MFKGFDKRLQRDVRKRVDRRLKKAEELSGGKLKPIPIDVNVVSHPRQRYAVWYGGSMLASSPEFEKVCHTKAEYDEYGPS 403

                  ....*....
gi 1207165482 319 ICRHNPVFG 327
Cdd:PTZ00280  404 ICRYNNVFH 412
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
1-324 2.59e-124

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 361.19  E-value: 2.59e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482    1 MEKFMEQVIFKYLRAEPEDHNFLMTEPPLNTPENREYLAEIMFETFNVPGLYIAVQAVLALAASWTSrqvgertlTGIVI 80
Cdd:smart00268  77 MEKIWDYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRT--------TGLVI 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482   81 DSGDGVTHAIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREIGIPPEQSLETAKAVKERYCYICPDIVKEFTKYDMD 160
Cdd:smart00268 149 DSGDGVTHVVPVVDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLARES 228
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  161 pgkWIKKYKGINAISKNEFQIDVGYERFLGPEIFFHPEFANPDFMqPISDVVDEVIQNCPIDVRRPLYKNIVLSGGSTMF 240
Cdd:smart00268 229 ---SESSKLEKTYELPDGNTIKVGNERFRIPEILFSPELIGLEQK-GIHELVYESIQKCDIDVRKDLYENIVLSGGSTLI 304
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  241 RDFGRRLQRDLKRVVdarlrlseelsggrikPKPMEVQVISHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPRIC 320
Cdd:smart00268 305 PGFGERLEKELKQLA----------------PKKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIV 368

                   ....
gi 1207165482  321 RHNP 324
Cdd:smart00268 369 ERKC 372
Actin pfam00022
Actin;
1-321 8.57e-76

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 238.36  E-value: 8.57e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482   1 MEKFMEQVIFKYLRAEPEDHNFLMTEPPLNTPENREYLAEIMFETFNVPGLYIAVQAvlalaaSWTSRQVGeRTlTGIVI 80
Cdd:pfam00022  75 MEEIWEHVLKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNP------VLSAFASG-RT-TGLVV 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  81 DSGDGVTHAIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREIGIPPEQSLETAKA---------------------- 138
Cdd:pfam00022 147 DSGAGVTSVVPVHDGYVLQKAIRRSDLGGDFLTDYLRELLRSRNIEITPRYLIKSKKPgdpapavtkrelpdttysykty 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 139 --------VKERYCYICPDIVKEFTKYDMDPGKwikKYkginaisknEF----QIDVGYERFLGPEIFFHPEFANPD--- 203
Cdd:pfam00022 227 qerrvleeIKESVCYVSDDPFGDETTSSSIPTR---VY---------ELpdgsTIILGAERFRVPEILFNPSLIGSEsel 294
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 204 ----FMQPISDVVDEVIQNCPIDVRRPLYKNIVLSGGSTMFRDFGRRLQRDLKRVVdarlrlseeLSGGRIKpkpmevqV 279
Cdd:pfam00022 295 pppqTAVGIPELIVDAINACDVDLRPSLLANIVVTGGNSLFPGFTERLEKELAQLA---------PPGVKVK-------I 358
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1207165482 280 ISHHMQ---RYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPRICR 321
Cdd:pfam00022 359 IAPGNTverRYSAWIGGSILASLGTFQQMWVSKQEYEEHGASVVE 403
COG5277 COG5277
Actin-related protein [Cytoskeleton];
2-298 9.51e-32

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 122.98  E-value: 9.51e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482   2 EKFMEQVIFKYLRAEPEDHNFLM--TEPPLNTPENREYLAEIMFETF---NVPGLYIAVQAVLALaaswtsrqVGERTLT 76
Cdd:COG5277   101 KELLRYTFAQFLVVDPEFHGFLVvvALSALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPLAVA--------IAEKAVT 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  77 GIVIDSGDGVTHAIPVAEGyVIGSCIKHIPIAGRDITYFIQQLLREREIG-IPPEQslETAKAVKERYCYICPDIVKEFT 155
Cdd:COG5277   173 CVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSdTAREE--YVVRVVKEALGLVPRDLAKAIQ 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 156 KYDMDPGKWIKKYKGINAISKNEFQiDVGYERFLGPEIFFHPEF-----ANPDFMQPISDVV--DEV------------- 215
Cdd:COG5277   250 KAASNPDSFEAKVRLPNPTVEIELG-NYAWERFLIGEILFNPNHegfesYIQQGRLRIEDAVigDVVlygemglaeaiin 328
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 216 -IQNCPIDVRRPLYKNIVLSGGSTMFrdfgrRLQRDLKRV-VDARLRLSEELSggRIKPKpMEVQVISHHMQRYAVWFGG 293
Cdd:COG5277   329 sIMKCDVEIQDELYSNIILSGGAFNW-----SVPPGLEDVaVDSVTRVQIELS--ELAPE-LKVNVRLVSDPQYSVWKGA 400

                  ....*
gi 1207165482 294 SMLAS 298
Cdd:COG5277   401 IIYGY 405
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
272-319 2.63e-05

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: 43.43  E-value: 2.63e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1207165482 272 PKPMEVQVISHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPRI 319
Cdd:NF040575   80 PKGALIGMTLDPKPESAAWRGAAMYAASEGFVEMAITKQEYDESGPSI 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: 711.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482   1 MEKFMEQVIFKYLRAEPEDHNFLMTEPPLNTPENREYLAEIMFETFNVPGLYIAVQAVLALAASWTSRQVGERTLTGIVI 80
Cdd:cd10221    83 MERFWEQCIFKYLRCEPEDHYFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQAVLALAASWTSRKVGERTLTGTVI 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  81 DSGDGVTHAIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREIGIPPEQSLETAKAVKERYCYICPDIVKEFTKYDMD 160
Cdd:cd10221   163 DSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREEGIPPEDSLEVAKRIKERYCYVCPDIVKEFAKYDSD 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 161 PGKWIKKYKGINAISKNEFQIDVGYERFLGPEIFFHPEFANPDFMQPISDVVDEVIQNCPIDVRRPLYKNIVLSGGSTMF 240
Cdd:cd10221   243 PAKYIKQYTGINSVTGKPYTVDVGYERFLAPEIFFNPEIASSDFTTPLPEVVDQVIQSCPIDTRRGLYKNIVLSGGSTMF 322
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 241 RDFGRRLQRDLKRVVDARLRLSEELSGGRIKPKPMEVQVISHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPRIC 320
Cdd:cd10221   323 KDFGRRLQRDVKRIVDARLKASEELSGGKLKPKPIDVNVISHPMQRYAVWFGGSMLASTPEFYTVCHTKAEYEEYGPSIC 402

                  ..
gi 1207165482 321 RH 322
Cdd:cd10221   403 RH 404
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
1-327 0e+00

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 592.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482   1 MEKFMEQVIFKYLRAEPEDHNFLMTEPPLNTPENREYLAEIMFETFNVPGLYIAVQAVLALAASWTSRQVGER--TLTGI 78
Cdd:PTZ00280   84 MEKFWEQCIFKYLRCEPEEHYFILTEPPMNPPENREYTAEIMFETFNVKGLYIAVQAVLALRASWTSKKAKELggTLTGT 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  79 VIDSGDGVTHAIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREIGIPPEQSLETAKAVKERYCYICPDIVKEFTKYD 158
Cdd:PTZ00280  164 VIDSGDGVTHVIPVVDGYVIGSSIKHIPLAGRDITNFIQQMLRERGEPIPAEDILLLAQRIKEKYCYVAPDIAKEFEKYD 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 159 MDPGKWIKKYKGINAISKNEFQIDVGYERFLGPEIFFHPEFANPDFMQPISDVVDEVIQNCPIDVRRPLYKNIVLSGGST 238
Cdd:PTZ00280  244 SDPKNHFKKYTAVNSVTKKPYTVDVGYERFLGPEMFFHPEIFSSEWTTPLPEVVDDAIQSCPIDCRRPLYKNIVLSGGST 323
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 239 MFRDFGRRLQRDLKRVVDARLRLSEELSGGRIKPKPMEVQVISHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPR 318
Cdd:PTZ00280  324 MFKGFDKRLQRDVRKRVDRRLKKAEELSGGKLKPIPIDVNVVSHPRQRYAVWYGGSMLASSPEFEKVCHTKAEYDEYGPS 403

                  ....*....
gi 1207165482 319 ICRHNPVFG 327
Cdd:PTZ00280  404 ICRYNNVFH 412
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
1-324 2.59e-124

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 361.19  E-value: 2.59e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482    1 MEKFMEQVIFKYLRAEPEDHNFLMTEPPLNTPENREYLAEIMFETFNVPGLYIAVQAVLALAASWTSrqvgertlTGIVI 80
Cdd:smart00268  77 MEKIWDYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRT--------TGLVI 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482   81 DSGDGVTHAIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREIGIPPEQSLETAKAVKERYCYICPDIVKEFTKYDMD 160
Cdd:smart00268 149 DSGDGVTHVVPVVDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLARES 228
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  161 pgkWIKKYKGINAISKNEFQIDVGYERFLGPEIFFHPEFANPDFMqPISDVVDEVIQNCPIDVRRPLYKNIVLSGGSTMF 240
Cdd:smart00268 229 ---SESSKLEKTYELPDGNTIKVGNERFRIPEILFSPELIGLEQK-GIHELVYESIQKCDIDVRKDLYENIVLSGGSTLI 304
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  241 RDFGRRLQRDLKRVVdarlrlseelsggrikPKPMEVQVISHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPRIC 320
Cdd:smart00268 305 PGFGERLEKELKQLA----------------PKKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIV 368

                   ....
gi 1207165482  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 1.56e-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: 264.43  E-value: 1.56e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482   1 MEKFMEQVIFKYLRAEPEDHNFLMTEPPLNTPENREYLAEIMFETFNVPGLYIAVQAVLALAASwtsrqvGeRTlTGIVI 80
Cdd:cd13397    77 MEKIWHHTFENELRVKPEEHPVLLTEAPLNPKQNREKMAEIMFETFGVPAFYVAIQAVLSLYSS------G-RT-TGLVL 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  81 DSGDGVTHAIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREIGIPPEQSLETAKAVKERYCYICPDIVKEFTKydmD 160
Cdd:cd13397   149 DSGDGVTHTVPIYEGYALPHAVQRLDLAGRDLTEYLMKLLKERGHSFTTTAEREIVRDIKEKLCYVALDYEEELKK---K 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 161 PGKWIKKYK---GiNAISknefqidVGYERFLGPEIFFHPEFANPDfMQPISDVVDEVIQNCPIDVRRPLYKNIVLSGGS 237
Cdd:cd13397   226 SEELEKEYTlpdG-QVIK-------IGSERFRCPEALFRPSLIGRE-APGIHKLVYNSIMKCDIDIRKDLYSNIVLSGGS 296
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207165482 238 TMFRDFGRRLQRDLKRVVdarlrlseelsggrikPKPMEVQVISHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYG 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 7.33e-84

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: 253.95  E-value: 7.33e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482   1 MEKFMEQVIFKYLRAEPEDHNFLMTEPPLNTPENREYLAEIMFETFNVPGLYIavqavlalaaswtSRQ-------VGeR 73
Cdd:cd10169    29 MEKIWEHVFYNLLRVDPEEHPVLLTEPPLNPKANREKLAEILFETFNVPSLYI-------------ANQavlslyaSG-R 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  74 TlTGIVIDSGDGVTHAIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREIGIPPEQSLETAKAVKERYCyicpdivke 153
Cdd:cd10169    95 T-TGLVVDSGEGVTHIVPVYEGYVLPHAVRRLDIGGRDLTDYLAKLLREKGYSFSTSAEREIVRDIKEKLC--------- 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 154 ftkydmdpgkwikkykginaisknefqidvgyerflgpeiffhpefanpdfmqPISDVVDEVIQNCPIDVRRPLYKNIVL 233
Cdd:cd10169   165 -----------------------------------------------------GLHELIYDSIMKCDIDLRKELYSNIVL 191
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 234 SGGSTMFRDFGRRLQRDLKRVVdarlrlseelsggrikPKPMEVQVISHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYE 313
Cdd:cd10169   192 SGGTTLFPGFAERLQKELSKLA----------------PSSVKVKVIAPPERKYSAWIGGSILASLSTFQQMWITKEEYE 255

                  ...
gi 1207165482 314 EYG 316
Cdd:cd10169   256 EHG 258
Actin pfam00022
Actin;
1-321 8.57e-76

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 238.36  E-value: 8.57e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482   1 MEKFMEQVIFKYLRAEPEDHNFLMTEPPLNTPENREYLAEIMFETFNVPGLYIAVQAvlalaaSWTSRQVGeRTlTGIVI 80
Cdd:pfam00022  75 MEEIWEHVLKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNP------VLSAFASG-RT-TGLVV 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  81 DSGDGVTHAIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREIGIPPEQSLETAKA---------------------- 138
Cdd:pfam00022 147 DSGAGVTSVVPVHDGYVLQKAIRRSDLGGDFLTDYLRELLRSRNIEITPRYLIKSKKPgdpapavtkrelpdttysykty 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 139 --------VKERYCYICPDIVKEFTKYDMDPGKwikKYkginaisknEF----QIDVGYERFLGPEIFFHPEFANPD--- 203
Cdd:pfam00022 227 qerrvleeIKESVCYVSDDPFGDETTSSSIPTR---VY---------ELpdgsTIILGAERFRVPEILFNPSLIGSEsel 294
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 204 ----FMQPISDVVDEVIQNCPIDVRRPLYKNIVLSGGSTMFRDFGRRLQRDLKRVVdarlrlseeLSGGRIKpkpmevqV 279
Cdd:pfam00022 295 pppqTAVGIPELIVDAINACDVDLRPSLLANIVVTGGNSLFPGFTERLEKELAQLA---------PPGVKVK-------I 358
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1207165482 280 ISHHMQ---RYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPRICR 321
Cdd:pfam00022 359 IAPGNTverRYSAWIGGSILASLGTFQQMWVSKQEYEEHGASVVE 403
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
5-323 4.55e-74

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: 232.82  E-value: 4.55e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482   5 MEQvIFKY------LRAEPEDHNFLMTEPPLNTPENREYLAEIMFETFNVPGLYIavqavlalaaswtSRQV-------G 71
Cdd:cd10216    78 MER-IWQYvysklqLNTFSEEHPVLLTEAPLNPRKNREKAAEVFFETFNVPALFV-------------SMQAvlslyasG 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  72 eRTlTGIVIDSGDGVTHAIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLR----------EREIgippeqsletAKAVKE 141
Cdd:cd10216   144 -RT-TGVVLDSGDGVTHAVPIYEGFALPHSIRRVDIAGRDVTEYLQLLLRksgynfhtsaEFEI----------VREIKE 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 142 RYCYICPDIVKEFTKYDMDPGKwiKKYK---GInaisknefQIDVGYERFLGPEIFFHPEFANPDFMQpISDVVDEVIQN 218
Cdd:cd10216   212 KACYVALNPQKEEKLEEEKTEK--AQYTlpdGS--------TIEIGPERFRAPEILFNPELIGLEYPG-VHEVLVDSIQK 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 219 CPIDVRRPLYKNIVLSGGSTMFRDFGRRLQRDLKRVV--DARLRLSeelsggrikpKPMEvqvishhmQRYAVWFGGSML 296
Cdd:cd10216   281 SDLDLRKTLYSNIVLSGGSTLFKGFGDRLLSEVKKLApkDVKIRIS----------APPE--------RLYSTWIGGSIL 342
                         330       340
                  ....*....|....*....|....*..
gi 1207165482 297 ASTPEFFQVCHTKKDYEEYGPRICRHN 323
Cdd:cd10216   343 ASLSTFKKMWVSKKEYEEDGARILHRK 369
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
1-319 1.04e-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: 223.78  E-value: 1.04e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482   1 MEKFMEQVIFKYLRAEPEDHNFLMTEPPLNTPENREYLAEIMFETFNVPGLYIAVQAVLALAASwtsrqvgERTlTGIVI 80
Cdd:cd10224    77 MEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYAS-------GRT-TGIVL 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  81 DSGDGVTHAIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREIGIPPEQSLETAKAVKERYCYICPDIVKEftkydmd 160
Cdd:cd10224   149 DSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQE------- 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 161 pgkwIKKYKGINAISKN-EF----QIDVGYERFLGPEIFFHPEFANPDfMQPISDVVDEVIQNCPIDVRRPLYKNIVLSG 235
Cdd:cd10224   222 ----MQTAASSSSLEKSyELpdgqVITIGNERFRCPEALFQPSFLGME-AAGIHETTYNSIMKCDVDIRKDLYANIVLSG 296
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 236 GSTMFRDFGRRLQRDLKRVVdarlrlseelsggrikPKPMEVQVISHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEEY 315
Cdd:cd10224   297 GTTMFPGIADRMQKEITALA----------------PSTMKIKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDES 360

                  ....
gi 1207165482 316 GPRI 319
Cdd:cd10224   361 GPSI 364
PTZ00004 PTZ00004
actin-2; Provisional
1-319 3.34e-70

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 223.11  E-value: 3.34e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482   1 MEKFMEQVIFKYLRAEPEDHNFLMTEPPLNTPENREYLAEIMFETFNVPGLYIAVQAVLALAASwtsrqvgERTlTGIVI 80
Cdd:PTZ00004   83 MEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETHNVPAMYVAIQAVLSLYAS-------GRT-TGIVL 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  81 DSGDGVTHAIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREIGIPPEQSLETAKAVKERYCYICPDIVKEFTKYDMD 160
Cdd:PTZ00004  155 DSGDGVSHTVPIYEGYSLPHAIHRLDVAGRDLTEYMMKILHERGTTFTTTAEKEIVRDIKEKLCYIALDFDEEMGNSAGS 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 161 PGKWIKKYK---GiNAISknefqidVGYERFLGPEIFFHPEFANPDFMQPISDVVDEVIQNCPIDVRRPLYKNIVLSGGS 237
Cdd:PTZ00004  235 SDKYEESYElpdG-TIIT-------VGSERFRCPEALFQPSLIGKEEPPGIHELTFQSINKCDIDIRKDLYGNIVLSGGT 306
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 238 TMFRDFGRRLQRDLKRVVdarlrlseelsggrikPKPMEVQVISHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYGP 317
Cdd:PTZ00004  307 TMYRGLPERLTKELTTLA----------------PSTMKIKVVAPPERKYSVWIGGSILSSLPTFQQMWVTKEEYDESGP 370

                  ..
gi 1207165482 318 RI 319
Cdd:PTZ00004  371 SI 372
ASKHA_NBD_Arp2 cd10220
nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, ...
1-321 3.25e-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: 205.11  E-value: 3.25e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482   1 MEKFMEQVIFKYLRAEPEDHNFLMTEPPLNTPENREYLAEIMFETFNVPGLYIavqavlalaaswtSRQV-----GERTL 75
Cdd:cd10220    79 MEHLWDYTFGEKLKIDPRECKILLTEPPMNPTKNREKMVEVMFEKYGFAGVYV-------------AIQAvltlyAQGLL 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  76 TGIVIDSGDGVTHAIPVAEGYVIGSCIKHIPIAGRDIT-YFIQQLLREreiGIPPEQS--LETAKAVKERYCYICPDIVK 152
Cdd:cd10220   146 TGVVVDSGDGVTHIVPVYEGFSLPHLTRRLDVAGRDITrYLIKLLLLR---GYAFNRTadFETVREIKEKLCYVAYDIEL 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 153 E----------FTKYDMDPGKWIKkykginaisknefqidVGYERFLGPEIFFHPEFANPDfmQP-ISDVVDEVIQNCPI 221
Cdd:cd10220   223 EqklalettvlVESYTLPDGRVIK----------------VGGERFEAPEALFQPHLIDVE--GPgIAELLFNTIQAADI 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 222 DVRRPLYKNIVLSGGSTMFRDFGRRLQRDLKrvvdaRLRLSEELSGGRIKPKPMEVQVISHHMQRYAVWFGGSMLA---- 297
Cdd:cd10220   285 DTRPELYKHIVLSGGSTMYPGLPSRLEKEIK-----QLYLERVLKGDTERLSKFKIRIEDPPRRKHMVFLGGAVLAdimk 359
                         330       340
                  ....*....|....*....|....
gi 1207165482 298 STPEFFQvchTKKDYEEYGPRICR 321
Cdd:cd10220   360 DKDEFWI---TRQEYEEQGVRVLD 380
PTZ00466 PTZ00466
actin-like protein; Provisional
5-319 1.82e-59

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 195.55  E-value: 1.82e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482   5 MEQV---IFKYLRAEPEDHNFLMTEPPLNTPENREYLAEIMFETFNVPGLYIAVQAVLALAASWTSrqvgertlTGIVID 81
Cdd:PTZ00466   89 MENIwihVYNSMKINSEEHPVLLTEAPLNPQKNKEKIAEVFFETFNVPALFISIQAILSLYSCGKT--------NGTVLD 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  82 SGDGVTHAIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREIGIPPEQSLETAKAVKERYCYICPDIVKEFTKYDmdp 161
Cdd:PTZ00466  161 CGDGVCHCVSIYEGYSITNTITRTDVAGRDITTYLGYLLRKNGHLFNTSAEMEVVKNMKENCCYVSFNMNKEKNSSE--- 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 162 gkwiKKYKGINAISKNEFQIDVGYERFLGPEIFFHPEFANPDFMQpISDVVDEVIQNCPIDVRRPLYKNIVLSGGSTMFR 241
Cdd:PTZ00466  238 ----KALTTLPYILPDGSQILIGSERYRAPEVLFNPSILGLEYLG-LSELIVTSITRADMDLRRTLYSHIVLSGGTTMFH 312
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207165482 242 DFGRRLQRDLKrvvdarlrlseelsggRIKPKPMEVQVISHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPRI 319
Cdd:PTZ00466  313 GFGDRLLNEIR----------------KFAPKDITIRISAPPERKFSTFIGGSILASLATFKKIWISKQEFDEYGSVI 374
PTZ00281 PTZ00281
actin; Provisional
1-319 2.26e-59

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 194.92  E-value: 2.26e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482   1 MEKFMEQVIFKYLRAEPEDHNFLMTEPPLNTPENREYLAEIMFETFNVPGLYIAVQAVLALAASwtsrqvgERTlTGIVI 80
Cdd:PTZ00281   83 MEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYAS-------GRT-TGIVM 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  81 DSGDGVTHAIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREIGIPPEQSLETAKAVKERYCYICPDIVKEFtKYDMD 160
Cdd:PTZ00281  155 DSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEM-QTAAS 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 161 PGKWIKKYKGINAISknefqIDVGYERFLGPEIFFHPEFANPDfMQPISDVVDEVIQNCPIDVRRPLYKNIVLSGGSTMF 240
Cdd:PTZ00281  234 SSALEKSYELPDGQV-----ITIGNERFRCPEALFQPSFLGME-SAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMF 307
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207165482 241 RDFGRRLQRDLKrvvdarlrlseelsggRIKPKPMEVQVISHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPRI 319
Cdd:PTZ00281  308 PGIADRMNKELT----------------ALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSI 370
ASKHA_NBD_Arp4_ACTL6-like cd13395
nucleotide-binding domain (NBD) of the actin-related protein 4 (Arp4)-like subfamily; The ...
1-316 6.25e-58

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: 192.40  E-value: 6.25e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482   1 MEKFMEQVIFKYLRAEPEDHNFLMTEPPLNTPENREYLAEIMFETFNVPGLYIavqavlalaaswtSRQ-------VGeR 73
Cdd:cd13395    88 FEKLWDHALKNRLRVDPSEHPLLLTEPSWNTRANREKLTELMFEKYNVPAFFL-------------AKNavlsafaNG-R 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  74 TlTGIVIDSGDGVTHAIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREIGIPPEQSL---------ETAKAVKE--- 141
Cdd:cd13395   154 S-TALVVDSGATSTSVVPVHDGYVLQKAIVRSPLGGDFLTDQLLKLLESKNIEIIPRYMIkskepveggAPAKYTKKdlp 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 142 -------RYCyiCPDIVKEF---------TKYDMDpgkwikKYKGINAISKnEF----QIDVGYERFLGPEIFFHPEFAN 201
Cdd:cd13395   233 nttssyhRYM--VRRVLQDFkesvcqvsdSPFDES------EAASIPTVSY-ELpdgyNIEFGAERFKIPELLFDPSLVK 303
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 202 PDF--------MQPISDVVDEVIQNCPIDVRRPLYKNIVLSGGSTMFRDFGRRLQRDlkrvvdarlrLSEELSGG-RIK- 271
Cdd:cd13395   304 GIPappsegneLLGLPQLVYTSIGSCDVDIRPELYGNVVLTGGNSLLPGFTDRLNRE----------LSEKAPGSlKLKi 373
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1207165482 272 ---PKPMEvqvishhmQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYG 316
Cdd:cd13395   374 lasGNTVE--------RRFSSWIGGSILASLGSFQQMWISKQEYEEHG 413
ASKHA_NBD_ACTL7 cd10214
nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ...
7-319 6.78e-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: 185.70  E-value: 6.78e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482   7 QVIFKY-----LRAEPEDHNFLMTEPPLNTPENREYLAEIMFETFNVPGLYIavqavlaLAASWTSRQVGERTlTGIVID 81
Cdd:cd10214    81 QDIWEYifekeMKILPEEHAVLVSDPPLSPTTNREKYAELMFETFSIPAMHI-------AYQSRLSLYSYGRT-SGLVVE 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  82 SGDGVTHAIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLreREIGIP-PEQSLETAKAVKERYCYICPDIVKEFTkydMD 160
Cdd:cd10214   153 SGHGVSYVVPIHEGYNLPHITGRADYAGSDLTAYLMKLL--NEAGNKfTDDQLHIVEDIKKKCCYVALDFEEEMG---LP 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 161 PGKWIKKYKginaiSKNEFQIDVGYERFLGPEIFFHPEFANpdFMQP-ISDVVDEVIQNCPIDVRRPLYKNIVLSGGSTM 239
Cdd:cd10214   228 PQEYTVDYE-----LPDGHLITIGKERFRCPEMLFNPSLIG--SKQPgLHTLTMNSLNKCDANLKKDLAKNILLCGGSTM 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 240 FRDFGRRLQRDLKRVVdarlrlseelsggrikpkPMEVQVISHHMQR-YAVWFGGSMLASTPEFFQVCHTKKDYEEYGPR 318
Cdd:cd10214   301 FDGFPDRFQKELSKLC------------------PNDNPIVAASPERkYSVWTGGSILASLKSFQQLWVRRREYEERGPF 362

                  .
gi 1207165482 319 I 319
Cdd:cd10214   363 V 363
ASKHA_NBD_Arp6 cd10210
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ...
6-316 8.35e-46

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: 160.02  E-value: 8.35e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482   6 EQVIFKYL------RAEPEDHNFLMTEPPLNTPENREYLAEIMFETFNVPGLYIA------VQAVLALAASWTSRqvgeR 73
Cdd:cd10210    70 QRQIWDHLfgklllNVDPSDTALVLTEPPFNPPSIQEAMDEIVFEEYGFQSLYRTtaaalsAFAYLADSEQSSSS----S 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  74 TLTGIVIDSGDGVTHAIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREIGIPPEQSLetAKAVKERYC--------- 144
Cdd:cd10210   146 SQCCLVVDSGFSFTHIVPFFDGKPVKRAVRRIDVGGKLLTNYLKEIISYRQLNVMDETYL--VNQIKEDLCfvstdfyed 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 145 ----------------YICPDIVKEFTKYDMDPGKWIkkykgiNAISKNEFQI-DVGYERFLGPEIFFHPEFANPDFMQp 207
Cdd:cd10210   224 leiakkkgkentirrdYVLPDYTTSKRGYVRDPEEPN------RGKLKEDEQVlRLNNERFTVPELLFHPSDIGIQQAG- 296
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 208 ISDVVDEVIQNCPIDVRRPLYKNIVLSGGSTMFRDFGRRLQRDLKRVVdarlrlseelsggrikPKPMEVQVI-SHHMQR 286
Cdd:cd10210   297 IAEAIVQSINACPEELQPLLYANIVLTGGNALFPGFRERLEAELRSLA----------------PDDYDVNVTlPEDPIT 360
                         330       340       350
                  ....*....|....*....|....*....|
gi 1207165482 287 YAvWFGGSMLASTPEFFQVCHTKKDYEEYG 316
Cdd:cd10210   361 YA-WEGGSLLAQSPEFEELAVTRAEYEEHG 389
PTZ00452 PTZ00452
actin; Provisional
1-319 5.43e-41

actin; Provisional


Pssm-ID: 185631  Cd Length: 375  Bit Score: 146.82  E-value: 5.43e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482   1 MEKFMEQVIFKYLRAEPEDHNFLMTEPPLNTPENREYLAEIMFETFNVPGLYIAVQAVLALAASWTSrqvgertlTGIVI 80
Cdd:PTZ00452   82 IEIIWHHAFYNELCMSPEDQPVFMTDAPMNSKFNRERMTQIMFETFNTPCLYISNEAVLSLYTSGKT--------IGLVV 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  81 DSGDGVTHAIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREIGIPPEQSLETAKAVKERYCYICpdivkeftkydMD 160
Cdd:PTZ00452  154 DSGEGVTHCVPVFEGHQIPQAITKINLAGRLCTDYLTQILQELGYSLTEPHQRIIVKNIKERLCYTA-----------LD 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 161 PGKWIKKYKGINAiSKNEFQIDVG------YERFLGPEIFFHPEFANPDfMQPISDVVDEVIQNCPIDVRRPLYKNIVLS 234
Cdd:PTZ00452  223 PQDEKRIYKESNS-QDSPYKLPDGniltikSQKFRCSEILFQPKLIGLE-VAGIHHLAYSSIKKCDLDLRQELCRNIVLS 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 235 GGSTMFRDFGRRLQRDLKRVVdarlrlseelsggrikPKPMEVQVISHHMQRYAVWFGGSMLAS----TPEFFQvchtKK 310
Cdd:PTZ00452  301 GGTTLFPGIANRLSNELTNLV----------------PSQLKIQVAAPPDRRFSAWIGGSIQCTlstqQPQWIK----RQ 360

                  ....*....
gi 1207165482 311 DYEEYGPRI 319
Cdd:PTZ00452  361 EYDEQGPSI 369
ASKHA_NBD_Arp10 cd10207
nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins; ...
2-316 1.66e-33

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: 126.98  E-value: 1.66e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482   2 EKFMEQVIFKYLRAEPEDHNFLMTEPPLNTPENREYLAEIMFETFNVPG-LYIavqavlalaaswTSRQVGERTL---TG 77
Cdd:cd10207    55 KEFLHELYFKHLLVNPKDRRVVVVESVLCPTPFRETLAKVLFKHFEVPSvLFA------------PSHLLSLLTLgirTA 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  78 IVIDSGDGVTHAIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREReIGIPPEQSLETAKAVKEryCYICPDIVKEF-TK 156
Cdd:cd10207   123 LVVDCGYRETRVLPVYEGVPLLSAWQSTPLGGKALHKRLKKLLLEH-ATVVTGDNKGQLLSSVD--SLLSEEVLEDIkVR 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 157 Y----DMDPGKWIKKYKGINAISKNEFQIDVGY----ERFLGP---------EIFFhpEFANPDfmQPISDVVDEVIQNC 219
Cdd:cd10207   200 AcfvtSLERGKTLQSATEEGSTEEPSPPPPVDYpldgEKILIVpgsiresaeELLF--EGDNEE--KSLPTLILDSLLKC 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 220 PIDVRRPLYKNIVLSGGSTMFRDFGRRLQRDLKRVVDARlRLSEELSGGRIKPkpmeVQVISHHMQRYAVWFGGSMLAST 299
Cdd:cd10207   276 PIDVRKQLAENIVVIGGTSMLPGFKHRLLEELRALLRKP-KYFEELAPKTFRF----HTPPSVFKPNYLAWLGGSIFGAL 350
                         330
                  ....*....|....*..
gi 1207165482 300 PEFFQVCHTKKDYEEYG 316
Cdd:cd10207   351 ESILGRSLSREAYLQTG 367
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
5-317 2.47e-33

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: 125.76  E-value: 2.47e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482   5 MEQV---IFKYLRAEPE---DHNFLMTEPPLNTPENREYLAEIMFETFNVP-------GLYiavqavlalaaSWTSRQVG 71
Cdd:cd10211    73 QEQIldyIFSHLGINSEgsvDHPIVLTEALCNPNYSRQLMSELLFECYGVPsvaygidSLF-----------SYYHNQPQ 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  72 ERTLTGIVIDSGDGVTHAIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREIGIPPEQSLETAKAVKERYCYICPDiv 151
Cdd:cd10211   142 GDPSDGLVISSGYSTTHVIPVLNGRLDLSQCKRINLGGFHATDYLQRLLQLKYPTHPSAITLSRAEELVHEHCYVAED-- 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 152 keftkydmdpgkwikkykginaisknefqidvgYERFLgpEIFFHPEFA--NPDFMQ-P--ISDVVDEVIQNCPIDVRRP 226
Cdd:cd10211   220 ---------------------------------YDEEL--KKWEDPEYYeeNVRKIQlPfgLVETIEFVLKRYPAEQQDR 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 227 LYKNIVLSGGSTMFRDFGRRLQRDLKrvvdarlrlseelsggRIKPKPMEVQVISHHMQRYAVWFGGSMLASTPEFFQVC 306
Cdd:cd10211   265 LVQNVFLTGGNALFPGLKERLEKELR----------------AIRPFGSPFNVVRAKDPVLDAWRGAAKWALDSTFEKVW 328
                         330
                  ....*....|.
gi 1207165482 307 HTKKDYEEYGP 317
Cdd:cd10211   329 ITKQEYEEKGG 339
COG5277 COG5277
Actin-related protein [Cytoskeleton];
2-298 9.51e-32

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 122.98  E-value: 9.51e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482   2 EKFMEQVIFKYLRAEPEDHNFLM--TEPPLNTPENREYLAEIMFETF---NVPGLYIAVQAVLALaaswtsrqVGERTLT 76
Cdd:COG5277   101 KELLRYTFAQFLVVDPEFHGFLVvvALSALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPLAVA--------IAEKAVT 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  77 GIVIDSGDGVTHAIPVAEGyVIGSCIKHIPIAGRDITYFIQQLLREREIG-IPPEQslETAKAVKERYCYICPDIVKEFT 155
Cdd:COG5277   173 CVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSdTAREE--YVVRVVKEALGLVPRDLAKAIQ 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 156 KYDMDPGKWIKKYKGINAISKNEFQiDVGYERFLGPEIFFHPEF-----ANPDFMQPISDVV--DEV------------- 215
Cdd:COG5277   250 KAASNPDSFEAKVRLPNPTVEIELG-NYAWERFLIGEILFNPNHegfesYIQQGRLRIEDAVigDVVlygemglaeaiin 328
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 216 -IQNCPIDVRRPLYKNIVLSGGSTMFrdfgrRLQRDLKRV-VDARLRLSEELSggRIKPKpMEVQVISHHMQRYAVWFGG 293
Cdd:COG5277   329 sIMKCDVEIQDELYSNIILSGGAFNW-----SVPPGLEDVaVDSVTRVQIELS--ELAPE-LKVNVRLVSDPQYSVWKGA 400

                  ....*
gi 1207165482 294 SMLAS 298
Cdd:COG5277   401 IIYGY 405
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
1-319 9.00e-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: 119.03  E-value: 9.00e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482   1 MEKFMEQVIFKYLRAEPEDH-NFLMTEPPLNTPENREYLAEIMFETFNVPGLYIavqavlalaaswtSRQ-------VGE 72
Cdd:cd10209    62 LEALLRYVFYTGLGWEEGNEgQVLIAEPLLTSKAERERLTQLMFETFNVSGLYA-------------SEQavlslyaVGR 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  73 rtLTGIVIDSGDGVTHAIPVAEGYVIGSCIKHIPIAGRDIT-YFIQQLLREREIGIPPEQSLETAKAVkeryCYICPDiv 151
Cdd:cd10209   129 --ISGCVVDVGHGKIDIAPVWEGAIQHNAVRRFEIGGRDLTeLLAAELGKSNPKVKLDRSIVERLKEA----VAWSAD-- 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 152 keftkydmDPGKWIKKYKGINAIS---KNEFQIDVGYERFLGPEIFFHPEfanpDFMQPISDVVDEV---IQNCPIDVRR 225
Cdd:cd10209   201 --------DEEAYEKKVLTCSPETytlPDGRVISVGKERYCVGEALFRPS----ILGIEEYGIVEQLvraVSTSPSENRR 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 226 PLYKNIVLSGGSTMFRDFGRRLQRdlkrvvDARLRLSEELSGGRIKPkPmevQVISHHMQRYAVWFGGSMLASTPeFFQV 305
Cdd:cd10209   269 QLLENIVLCGGTSSVPGLEARLQK------EIRLLSSPSSRPALVKP-P---EYMPENTLRYSAWIGGAILAKVV-FPQN 337
                         330
                  ....*....|....*
gi 1207165482 306 CH-TKKDYEEYGPRI 319
Cdd:cd10209   338 QHvTKADYDETGPSV 352
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
2-317 2.88e-24

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: 101.23  E-value: 2.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482   2 EKFMEQVIFKYLRAEPEDHNF--LMTEPPLNTPENREYLAEIMFETFNVPGLYIavqavlalaaswtsrqvGERTL---- 75
Cdd:cd10208    51 EALWRHILFSLLSIPRPTNNSpvLLSVPPSWSKSDLELLTQLFFERLNVPAFAI-----------------LEAPLaaly 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  76 -----TGIVIDSGDGVTHAIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREIGIPPEQS------LETAKAVKeryc 144
Cdd:cd10208   114 aagatSGIVVDIGHEKTDITPIVDSQVVPHALVSIPIGGQDCTAHLAQLLKSDEPELKSQAEsgeeatLDLAEALK---- 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 145 yiCPDIVkEFTKYDMDPgkwikkYKGInaisknefQIDVGYERFLGPEIFFHPEFANPDFMQPISDVVDEVIQNCPIDVR 224
Cdd:cd10208   190 --KSPIC-EVLSDGADL------ASGT--------EITVGKERFRACEPLFKPSSLRVDLLIAAIAGALVLNASDEPDKR 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 225 RPLYKNIVLSGGSTMFRDFGRRLQRDLKrvvdARLRLSEELSGG------RIKPKPMEVQVISHHMQRYAVWFGGSMLA- 297
Cdd:cd10208   253 PALWENIIIVGGGSRIRGLKEALLSELQ----QFHLISETSASPqqpriiRLAKIPDYFPEWKKSGYEEAAFLGASIVAk 328
                         330       340
                  ....*....|....*....|....*
gi 1207165482 298 -----STPEFFQvchTKKDYEEYGP 317
Cdd:cd10208   329 lvfndPSSKHYI---SKVDYNEKGP 350
ASKHA_NBD_AtArp8-like cd13396
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and ...
70-312 1.94e-14

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: 72.96  E-value: 1.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  70 VGERTlTGIVIDSGDGVTHAIPVAEGYV---IGscIKHIPIAGRDITYFIQQLLREREIGIPpeqSLETAKAVKERYCYI 146
Cdd:cd13396   111 AANRT-SGIVVNIGFRVTTIVPVYRGRVmhdIG--VEVVGQGALRLTGFLKELMQQNGIRFP---SLYTVRTIKEKLCYV 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 147 CPDIVKEFTK-----YDMDPGKWIKkykginaisknefqidVGYERFLGPEIFFHPEFANPDFMQpISDVVDEVIQNCPI 221
Cdd:cd13396   185 AEDYEAELAKdtqasCEVAGEGWFT----------------LSNERFKTGEILFQPGLGGMRAMG-LHQAVALCMDHCAL 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 222 DVR---RPLYKNIVLSGGSTMFRDFGRRLQRDLKRVVDARLrlseeLSGGRIKPKPMEVqvishhmqrYAVWFGGSMLAS 298
Cdd:cd13396   248 VHSqgdDGWFKTIVLSGGSACLPGLSERLERELRKLLPKSL-----SEGIRIIPPPLGP---------DSAWQGAKLISN 313
                         250
                  ....*....|....*
gi 1207165482 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 3.00e-11

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: 63.80  E-value: 3.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482  76 TGIVIDSGDGVTHAIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLRE-----REIGIPPEQSLETAKAVKERYCYICPDI 150
Cdd:cd10206   234 SACVVDIGAQKTSVACVEDGLSIPNSRIRLPYGGDDITRCFLWLLRRsgfpyRECNLNSPLDFLLLERLKETYCTLDQDD 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 151 --VKEFTKYDMDPGKWIKKYKginaiskneFQIdvgyerflgpeiffhpefanpdfmQPISDVVDEVIQNCP-IDVRRPL 227
Cdd:cd10206   314 igVQLHEFYVREPGQPTLKYQ---------FKL------------------------LPLDEAIVQSILSCAsDELKRKM 360
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207165482 228 YKNIVLSGGSTMFRDFGRRLQRDLKRVVDARLRLSEELSggrIKPKPMEVQvishhmQRYAVWFGGSMLA---STPEFFQ 304
Cdd:cd10206   361 YSSILLVGGGAKIPGLAEALEDRLLIKIPSLFEAVETVE---VLPPPKDMD------PSLLAWKGGAVLAcldSAQELWI 431
                         250
                  ....*....|....*...
gi 1207165482 305 vchTKKDYEEYGPRICRH 322
Cdd:cd10206   432 ---TRKEWQRLGVRALRE 446
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
272-319 2.63e-05

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: 43.43  E-value: 2.63e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1207165482 272 PKPMEVQVISHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPRI 319
Cdd:NF040575   80 PKGALIGMTLDPKPESAAWRGAAMYAASEGFVEMAITKQEYDESGPSI 127
 
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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