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Conserved domains on  [gi|9966913|ref|NP_065178|]
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actin-related protein 3B isoform 1 [Homo sapiens]

Protein Classification

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, ...
7-410 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: 870.73  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913    7 PCVVDCGTGYTKLGYAGNTEPQFIIPSCIAIRESAKVVDqAQRRVLRGVDDLDFFIGDEAIDK-PTYATKWPIRHGIIED 85
Cdd:cd10221   1 AVVIDNGTGYTKMGYAGNTEPQFIIPTVIAIKESAKVGD-GQRRSKKGIEDLDFYIGDEALANsPTYALKYPIRHGIVED 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   86 WDLMERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIAVQAVLALAASWTSRQVGERTLTG 165
Cdd:cd10221  80 WDLMERFWEQCIFKYLRCEPEDHYFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQAVLALAASWTSRKVGERTLTG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  166 IVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICPDIVKEFAKY 245
Cdd:cd10221 160 TVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREEGIPPEDSLEVAKRIKERYCYVCPDIVKEFAKY 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  246 DVDPRKWIKQYTGINAINQKKFVIDVGYERFLGPEIFFHPEFANPDFMESISDVVDEVIQNCPIDVRRPLYKNVVLSGGS 325
Cdd:cd10221 240 DSDPAKYIKQYTGINSVTGKPYTVDVGYERFLAPEIFFNPEIASSDFTTPLPEVVDQVIQSCPIDTRRGLYKNIVLSGGS 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  326 TMFRDFGRRLQRDLKRVVDARLRLSEELSGGRIKPKPVEVQVVTHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYGP 405
Cdd:cd10221 320 TMFKDFGRRLQRDVKRIVDARLKASEELSGGKLKPKPIDVNVISHPMQRYAVWFGGSMLASTPEFYTVCHTKAEYEEYGP 399

                ....*
gi 9966913  406 SICRH 410
Cdd:cd10221 400 SICRH 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, ...
7-410 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: 870.73  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913    7 PCVVDCGTGYTKLGYAGNTEPQFIIPSCIAIRESAKVVDqAQRRVLRGVDDLDFFIGDEAIDK-PTYATKWPIRHGIIED 85
Cdd:cd10221   1 AVVIDNGTGYTKMGYAGNTEPQFIIPTVIAIKESAKVGD-GQRRSKKGIEDLDFYIGDEALANsPTYALKYPIRHGIVED 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   86 WDLMERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIAVQAVLALAASWTSRQVGERTLTG 165
Cdd:cd10221  80 WDLMERFWEQCIFKYLRCEPEDHYFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQAVLALAASWTSRKVGERTLTG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  166 IVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICPDIVKEFAKY 245
Cdd:cd10221 160 TVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREEGIPPEDSLEVAKRIKERYCYVCPDIVKEFAKY 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  246 DVDPRKWIKQYTGINAINQKKFVIDVGYERFLGPEIFFHPEFANPDFMESISDVVDEVIQNCPIDVRRPLYKNVVLSGGS 325
Cdd:cd10221 240 DSDPAKYIKQYTGINSVTGKPYTVDVGYERFLAPEIFFNPEIASSDFTTPLPEVVDQVIQSCPIDTRRGLYKNIVLSGGS 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  326 TMFRDFGRRLQRDLKRVVDARLRLSEELSGGRIKPKPVEVQVVTHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYGP 405
Cdd:cd10221 320 TMFKDFGRRLQRDVKRIVDARLKASEELSGGKLKPKPIDVNVISHPMQRYAVWFGGSMLASTPEFYTVCHTKAEYEEYGP 399

                ....*
gi 9966913  406 SICRH 410
Cdd:cd10221 400 SICRH 404
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
2-417 0e+00

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 717.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913     2 AGSLPPCVVDCGTGYTKLGYAGNTEPQFIIPSCIAIRESAKVvdqaqRRVLRGVDDLDFFIGDEAIDKP-TYATKWPIRH 80
Cdd:PTZ00280   1 ASTLPVVVIDNGTGYTKMGYAGNTEPTYIIPTLIADNSKQSR-----RRSKKGFEDLDFYIGDEALAASkSYTLTYPMKH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913    81 GIIEDWDLMERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIAVQAVLALAASWTSRQVGE 160
Cdd:PTZ00280  76 GIVEDWDLMEKFWEQCIFKYLRCEPEEHYFILTEPPMNPPENREYTAEIMFETFNVKGLYIAVQAVLALRASWTSKKAKE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   161 R--TLTGIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICPDI 238
Cdd:PTZ00280 156 LggTLTGTVIDSGDGVTHVIPVVDGYVIGSSIKHIPLAGRDITNFIQQMLRERGEPIPAEDILLLAQRIKEKYCYVAPDI 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   239 VKEFAKYDVDPRKWIKQYTGINAINQKKFVIDVGYERFLGPEIFFHPEFANPDFMESISDVVDEVIQNCPIDVRRPLYKN 318
Cdd:PTZ00280 236 AKEFEKYDSDPKNHFKKYTAVNSVTKKPYTVDVGYERFLGPEMFFHPEIFSSEWTTPLPEVVDDAIQSCPIDCRRPLYKN 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   319 VVLSGGSTMFRDFGRRLQRDLKRVVDARLRLSEELSGGRIKPKPVEVQVVTHHMQRYAVWFGGSMLASTPEFFQVCHTKK 398
Cdd:PTZ00280 316 IVLSGGSTMFKGFDKRLQRDVRKRVDRRLKKAEELSGGKLKPIPIDVNVVSHPRQRYAVWYGGSMLASSPEFEKVCHTKA 395
                        410
                 ....*....|....*....
gi 9966913   399 DYEEYGPSICRHNPVFGVM 417
Cdd:PTZ00280 396 EYDEYGPSICRYNNVFHSV 414
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
6-412 6.46e-154

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 439.77  E-value: 6.46e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913       6 PPCVVDCGTGYTKLGYAGNTEPQFIIPSCIAiresakvvdQAQRRVLRGVDDLDFFIGDEAIDKPTYAT-KWPIRHGIIE 84
Cdd:smart00268   2 PAIVIDNGSGTIKAGFAGEDFPQVVFPSIVG---------RPKDGKGMVGDAKDIFVGDEAQEKRGGLElKYPIENGIVE 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913      85 DWDLMERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIAVQAVLALAASWTSrqvgertlT 164
Cdd:smart00268  73 NWDDMEKIWDYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRT--------T 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913     165 GIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICPDIVKEFAK 244
Cdd:smart00268 145 GLVIDSGDGVTHVVPVVDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKL 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913     245 YDvdpRKWIKQYTGINAINQKKFVIDVGYERFLGPEIFFHPEFANPDFmESISDVVDEVIQNCPIDVRRPLYKNVVLSGG 324
Cdd:smart00268 225 AR---ESSESSKLEKTYELPDGNTIKVGNERFRIPEILFSPELIGLEQ-KGIHELVYESIQKCDIDVRKDLYENIVLSGG 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913     325 STMFRDFGRRLQRDLKRVVdarlrlseelsggrikPKPVEVQVVTHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYG 404
Cdd:smart00268 301 STLIPGFGERLEKELKQLA----------------PKKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESG 364

                   ....*...
gi 9966913     405 PSICRHNP 412
Cdd:smart00268 365 SQIVERKC 372
Actin pfam00022
Actin;
6-409 1.11e-97

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 297.68  E-value: 1.11e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913      6 PPCVVDCGTGYTKLGYAGNTEPQFIIPSCIAIRESAKVVDqaqrrvlrgvdDLDFFIGDEAIDK-PTYATKWPIRHGIIE 84
Cdd:pfam00022   2 SALVIDNGSHTTRAGFAGEDAPKAVIPSCVGKPRGTKVEA-----------ANKYYVGDEALTYrPGMEVRSPVEDGIVV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913     85 DWDLMERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIavqavlALAASWTSRQVGeRTlT 164
Cdd:pfam00022  71 DWDAMEEIWEHVLKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYL------AKNPVLSAFASG-RT-T 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913    165 GIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKA------------------ 226
Cdd:pfam00022 143 GLVVDSGAGVTSVVPVHDGYVLQKAIRRSDLGGDFLTDYLRELLRSRNIEITPRYLIKSKKPgdpapavtkrelpdttys 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913    227 ------------IKEKYCYICPDIVKEFAKYdvdprkwikqytgiNAINQKKFV------IDVGYERFLGPEIFFHPEFA 288
Cdd:pfam00022 223 yktyqerrvleeIKESVCYVSDDPFGDETTS--------------SSIPTRVYElpdgstIILGAERFRVPEILFNPSLI 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913    289 NPD-------FMESISDVVDEVIQNCPIDVRRPLYKNVVLSGGSTMFRDFGRRLQRDLKRVVdarlrlseeLSGGRIKPK 361
Cdd:pfam00022 289 GSEselpppqTAVGIPELIVDAINACDVDLRPSLLANIVVTGGNSLFPGFTERLEKELAQLA---------PPGVKVKII 359
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 9966913    362 PVEVQVVThhmqRYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPSICR 409
Cdd:pfam00022 360 APGNTVER----RYSAWIGGSILASLGTFQQMWVSKQEYEEHGASVVE 403
COG5277 COG5277
Actin-related protein [Cytoskeleton];
6-386 6.69e-39

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 144.55  E-value: 6.69e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913    6 PPCVVDCGTGYTKLG-YAGNTEPQFIIPSCIAIResakVVDQAQRRVLRGVDDLDFFIGDEAIDKP------TYATKWPI 78
Cdd:COG5277   9 YVIGIDFGTSYVKYGpIALEEKPRVIQTRGLFLR----IVGESKLLGPMEGLSRGLVVGDEVSKYLssvrdaIRNLKYPL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   79 RHGIIE-----DWDLMERFMEQVVFKYLRAEPEDHYFLM--TEPPLNTPENREYLAEIMFESF---NVPGLYIAVQAVLA 148
Cdd:COG5277  85 RDGIVRrddedAWRVLKELLRYTFAQFLVVDPEFHGFLVvvALSALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPLAV 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  149 LaaswtsrqVGERTLTGIVIDSGDGVTHVIPVAEGyVIGSCIKHIPIAGRDITYFIQQLLREREVG-IPPEQslETAKAI 227
Cdd:COG5277 165 A--------IAEKAVTCVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSdTAREE--YVVRVV 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  228 KEKYCYICPDIVKEFAKYDVDPRKWIKQYTGINAINQkkfvIDVG---YERFLGPEIFFHPEFanpDFMES--------- 295
Cdd:COG5277 234 KEALGLVPRDLAKAIQKAASNPDSFEAKVRLPNPTVE----IELGnyaWERFLIGEILFNPNH---EGFESyiqqgrlri 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  296 ---------------ISDVVDEVIQNCPIDVRRPLYKNVVLSGGSTMFrdfgrRLQRDLKRV-VDARLRLSEELSggRIK 359
Cdd:COG5277 307 edavigdvvlygemgLAEAIINSIMKCDVEIQDELYSNIILSGGAFNW-----SVPPGLEDVaVDSVTRVQIELS--ELA 379
                       410       420
                ....*....|....*....|....*..
gi 9966913  360 PKpVEVQVVTHHMQRYAVWFGGSMLAS 386
Cdd:COG5277 380 PE-LKVNVRLVSDPQYSVWKGAIIYGY 405
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
374-407 9.16e-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: 9.16e-06
                         10        20        30
                 ....*....|....*....|....*....|....
gi 9966913   374 RYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPSI 407
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, ...
7-410 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: 870.73  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913    7 PCVVDCGTGYTKLGYAGNTEPQFIIPSCIAIRESAKVVDqAQRRVLRGVDDLDFFIGDEAIDK-PTYATKWPIRHGIIED 85
Cdd:cd10221   1 AVVIDNGTGYTKMGYAGNTEPQFIIPTVIAIKESAKVGD-GQRRSKKGIEDLDFYIGDEALANsPTYALKYPIRHGIVED 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   86 WDLMERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIAVQAVLALAASWTSRQVGERTLTG 165
Cdd:cd10221  80 WDLMERFWEQCIFKYLRCEPEDHYFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQAVLALAASWTSRKVGERTLTG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  166 IVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICPDIVKEFAKY 245
Cdd:cd10221 160 TVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREEGIPPEDSLEVAKRIKERYCYVCPDIVKEFAKY 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  246 DVDPRKWIKQYTGINAINQKKFVIDVGYERFLGPEIFFHPEFANPDFMESISDVVDEVIQNCPIDVRRPLYKNVVLSGGS 325
Cdd:cd10221 240 DSDPAKYIKQYTGINSVTGKPYTVDVGYERFLAPEIFFNPEIASSDFTTPLPEVVDQVIQSCPIDTRRGLYKNIVLSGGS 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  326 TMFRDFGRRLQRDLKRVVDARLRLSEELSGGRIKPKPVEVQVVTHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYGP 405
Cdd:cd10221 320 TMFKDFGRRLQRDVKRIVDARLKASEELSGGKLKPKPIDVNVISHPMQRYAVWFGGSMLASTPEFYTVCHTKAEYEEYGP 399

                ....*
gi 9966913  406 SICRH 410
Cdd:cd10221 400 SICRH 404
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
2-417 0e+00

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 717.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913     2 AGSLPPCVVDCGTGYTKLGYAGNTEPQFIIPSCIAIRESAKVvdqaqRRVLRGVDDLDFFIGDEAIDKP-TYATKWPIRH 80
Cdd:PTZ00280   1 ASTLPVVVIDNGTGYTKMGYAGNTEPTYIIPTLIADNSKQSR-----RRSKKGFEDLDFYIGDEALAASkSYTLTYPMKH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913    81 GIIEDWDLMERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIAVQAVLALAASWTSRQVGE 160
Cdd:PTZ00280  76 GIVEDWDLMEKFWEQCIFKYLRCEPEEHYFILTEPPMNPPENREYTAEIMFETFNVKGLYIAVQAVLALRASWTSKKAKE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   161 R--TLTGIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICPDI 238
Cdd:PTZ00280 156 LggTLTGTVIDSGDGVTHVIPVVDGYVIGSSIKHIPLAGRDITNFIQQMLRERGEPIPAEDILLLAQRIKEKYCYVAPDI 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   239 VKEFAKYDVDPRKWIKQYTGINAINQKKFVIDVGYERFLGPEIFFHPEFANPDFMESISDVVDEVIQNCPIDVRRPLYKN 318
Cdd:PTZ00280 236 AKEFEKYDSDPKNHFKKYTAVNSVTKKPYTVDVGYERFLGPEMFFHPEIFSSEWTTPLPEVVDDAIQSCPIDCRRPLYKN 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   319 VVLSGGSTMFRDFGRRLQRDLKRVVDARLRLSEELSGGRIKPKPVEVQVVTHHMQRYAVWFGGSMLASTPEFFQVCHTKK 398
Cdd:PTZ00280 316 IVLSGGSTMFKGFDKRLQRDVRKRVDRRLKKAEELSGGKLKPIPIDVNVVSHPRQRYAVWYGGSMLASSPEFEKVCHTKA 395
                        410
                 ....*....|....*....
gi 9966913   399 DYEEYGPSICRHNPVFGVM 417
Cdd:PTZ00280 396 EYDEYGPSICRYNNVFHSV 414
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
6-412 6.46e-154

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 439.77  E-value: 6.46e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913       6 PPCVVDCGTGYTKLGYAGNTEPQFIIPSCIAiresakvvdQAQRRVLRGVDDLDFFIGDEAIDKPTYAT-KWPIRHGIIE 84
Cdd:smart00268   2 PAIVIDNGSGTIKAGFAGEDFPQVVFPSIVG---------RPKDGKGMVGDAKDIFVGDEAQEKRGGLElKYPIENGIVE 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913      85 DWDLMERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIAVQAVLALAASWTSrqvgertlT 164
Cdd:smart00268  73 NWDDMEKIWDYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRT--------T 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913     165 GIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICPDIVKEFAK 244
Cdd:smart00268 145 GLVIDSGDGVTHVVPVVDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKL 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913     245 YDvdpRKWIKQYTGINAINQKKFVIDVGYERFLGPEIFFHPEFANPDFmESISDVVDEVIQNCPIDVRRPLYKNVVLSGG 324
Cdd:smart00268 225 AR---ESSESSKLEKTYELPDGNTIKVGNERFRIPEILFSPELIGLEQ-KGIHELVYESIQKCDIDVRKDLYENIVLSGG 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913     325 STMFRDFGRRLQRDLKRVVdarlrlseelsggrikPKPVEVQVVTHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYG 404
Cdd:smart00268 301 STLIPGFGERLEKELKQLA----------------PKKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESG 364

                   ....*...
gi 9966913     405 PSICRHNP 412
Cdd:smart00268 365 SQIVERKC 372
ASKHA_NBD_actin_Arp-T1-3 cd13397
nucleotide-binding domain (NBD) of actin, actin-related proteins T1-T3 (Arp-T1-3), and similar ...
6-404 1.76e-106

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: 318.75  E-value: 1.76e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913    6 PPCVVDCGTGYTKLGYAGNTEPQFIIPSCIAiRESAKvvdqaqrRVLRGVDDLDFFIGDEAIDKPTYAT-KWPIRHGIIE 84
Cdd:cd13397   1 PAVVIDNGSGLIKAGFAGEDLPRAVFPSVVG-RPKYK-------AVMLGAGQKEVYVGDEAQEKRGVLTlSYPIEHGIVT 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   85 DWDLMERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIAVQAVLALAASwtsrqvGeRTlT 164
Cdd:cd13397  73 NWDDMEKIWHHTFENELRVKPEEHPVLLTEAPLNPKQNREKMAEIMFETFGVPAFYVAIQAVLSLYSS------G-RT-T 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  165 GIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICPDIVKEFAK 244
Cdd:cd13397 145 GLVLDSGDGVTHTVPIYEGYALPHAVQRLDLAGRDLTEYLMKLLKERGHSFTTTAEREIVRDIKEKLCYVALDYEEELKK 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  245 ydvDPRKWIKQYT---GInainqkkfVIDVGYERFLGPEIFFHPEFANPDfMESISDVVDEVIQNCPIDVRRPLYKNVVL 321
Cdd:cd13397 225 ---KSEELEKEYTlpdGQ--------VIKIGSERFRCPEALFRPSLIGRE-APGIHKLVYNSIMKCDIDIRKDLYSNIVL 292
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  322 SGGSTMFRDFGRRLQRDLKRVVdarlrlseelsggrikPKPVEVQVVTHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYE 401
Cdd:cd13397 293 SGGSTMFPGLPERLQKELEALA----------------PSSTKVKVIAPPERKYSVWIGGSILASLSTFKSMWITRAEYD 356

                ...
gi 9966913  402 EYG 404
Cdd:cd13397 357 EFG 359
Actin pfam00022
Actin;
6-409 1.11e-97

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 297.68  E-value: 1.11e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913      6 PPCVVDCGTGYTKLGYAGNTEPQFIIPSCIAIRESAKVVDqaqrrvlrgvdDLDFFIGDEAIDK-PTYATKWPIRHGIIE 84
Cdd:pfam00022   2 SALVIDNGSHTTRAGFAGEDAPKAVIPSCVGKPRGTKVEA-----------ANKYYVGDEALTYrPGMEVRSPVEDGIVV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913     85 DWDLMERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIavqavlALAASWTSRQVGeRTlT 164
Cdd:pfam00022  71 DWDAMEEIWEHVLKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYL------AKNPVLSAFASG-RT-T 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913    165 GIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKA------------------ 226
Cdd:pfam00022 143 GLVVDSGAGVTSVVPVHDGYVLQKAIRRSDLGGDFLTDYLRELLRSRNIEITPRYLIKSKKPgdpapavtkrelpdttys 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913    227 ------------IKEKYCYICPDIVKEFAKYdvdprkwikqytgiNAINQKKFV------IDVGYERFLGPEIFFHPEFA 288
Cdd:pfam00022 223 yktyqerrvleeIKESVCYVSDDPFGDETTS--------------SSIPTRVYElpdgstIILGAERFRVPEILFNPSLI 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913    289 NPD-------FMESISDVVDEVIQNCPIDVRRPLYKNVVLSGGSTMFRDFGRRLQRDLKRVVdarlrlseeLSGGRIKPK 361
Cdd:pfam00022 289 GSEselpppqTAVGIPELIVDAINACDVDLRPSLLANIVVTGGNSLFPGFTERLEKELAQLA---------PPGVKVKII 359
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 9966913    362 PVEVQVVThhmqRYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPSICR 409
Cdd:pfam00022 360 APGNTVER----RYSAWIGGSILASLGTFQQMWVSKQEYEEHGASVVE 403
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
7-411 4.32e-94

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: 287.13  E-value: 4.32e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913    7 PCVVDCGTGYTKLGYAGNTEPQFIIPSCIAireSAKVVdqaqrRVLRGVDDLDFFIGDEAID-KPTYATKWPIRHGIIED 85
Cdd:cd10216   3 PVVIDNGSGVIKAGFAGDDIPKVVFPSYVG---RPKHV-----RVMAGALEGDVFVGPKAEEhRGLLKIRYPMEHGIVTD 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   86 WDLMERfmeqvVFKY------LRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIavqavlalaaswtSRQV- 158
Cdd:cd10216  75 WNDMER-----IWQYvysklqLNTFSEEHPVLLTEAPLNPRKNREKAAEVFFETFNVPALFV-------------SMQAv 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  159 ------GeRTlTGIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLR----------EREVgippeqsle 222
Cdd:cd10216 137 lslyasG-RT-TGVVLDSGDGVTHAVPIYEGFALPHSIRRVDIAGRDVTEYLQLLLRksgynfhtsaEFEI--------- 205
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  223 tAKAIKEKYCYICPDIVKEFAKYDVDPRKwiKQYT---GInainqkkfVIDVGYERFLGPEIFFHPEFANPDFmESISDV 299
Cdd:cd10216 206 -VREIKEKACYVALNPQKEEKLEEEKTEK--AQYTlpdGS--------TIEIGPERFRAPEILFNPELIGLEY-PGVHEV 273
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  300 VDEVIQNCPIDVRRPLYKNVVLSGGSTMFRDFGRRLQRDLKRVV--DARLRLSeelsggrikpKPVEvqvvthhmQRYAV 377
Cdd:cd10216 274 LVDSIQKSDLDLRKTLYSNIVLSGGSTLFKGFGDRLLSEVKKLApkDVKIRIS----------APPE--------RLYST 335
                       410       420       430
                ....*....|....*....|....*....|....
gi 9966913  378 WFGGSMLASTPEFFQVCHTKKDYEEYGPSICRHN 411
Cdd:cd10216 336 WIGGSILASLSTFKKMWVSKKEYEEDGARILHRK 369
ASKHA_NBD_actin-like cd10169
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ...
9-404 2.37e-90

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: 273.60  E-value: 2.37e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913    9 VVDCGTGYTKLGYAGNTEPQFIIPsciairesakvvdqaqrrvlrgvddldffigdeaidkptyatkwpirhgiiedWDL 88
Cdd:cd10169   2 VIDNGSGTIKAGFAGEDAPRLIFP-----------------------------------------------------WDD 28
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   89 MERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIavqavlalaaswtSRQ-------VGeR 161
Cdd:cd10169  29 MEKIWEHVFYNLLRVDPEEHPVLLTEPPLNPKANREKLAEILFETFNVPSLYI-------------ANQavlslyaSG-R 94
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  162 TlTGIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCyicpdivke 241
Cdd:cd10169  95 T-TGLVVDSGEGVTHIVPVYEGYVLPHAVRRLDIGGRDLTDYLAKLLREKGYSFSTSAEREIVRDIKEKLC--------- 164
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  242 fakydvdprkwikqytginainqkkfvidvgyerflgpeiffhpefanpdfmeSISDVVDEVIQNCPIDVRRPLYKNVVL 321
Cdd:cd10169 165 -----------------------------------------------------GLHELIYDSIMKCDIDLRKELYSNIVL 191
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  322 SGGSTMFRDFGRRLQRDLKRVVdarlrlseelsggrikPKPVEVQVVTHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYE 401
Cdd:cd10169 192 SGGTTLFPGFAERLQKELSKLA----------------PSSVKVKVIAPPERKYSAWIGGSILASLSTFQQMWITKEEYE 255

                ...
gi 9966913  402 EYG 404
Cdd:cd10169 256 EHG 258
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
7-407 1.08e-89

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: 275.78  E-value: 1.08e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913    7 PCVVDCGTGYTKLGYAGNTEPQFIIPSCIAIREsakvvdqaQRRVLRGVDDLDFFIGDEAIDKPTYAT-KWPIRHGIIED 85
Cdd:cd10224   2 ALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPR--------HQGVMVGMGQKDSYVGDEAQSKRGILTlKYPIEHGIVTN 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   86 WDLMERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIAVQAVLALAASwtsrqvgERTlTG 165
Cdd:cd10224  74 WDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYAS-------GRT-TG 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  166 IVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICPDIVKEFAKY 245
Cdd:cd10224 146 IVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTA 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  246 DVDPRkwikqytginaiNQKKF------VIDVGYERFLGPEIFFHPEFANpdfMES--ISDVVDEVIQNCPIDVRRPLYK 317
Cdd:cd10224 226 ASSSS------------LEKSYelpdgqVITIGNERFRCPEALFQPSFLG---MEAagIHETTYNSIMKCDVDIRKDLYA 290
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  318 NVVLSGGSTMFRDFGRRLQRDLKRVVdarlrlseelsggrikPKPVEVQVVTHHMQRYAVWFGGSMLASTPEFFQVCHTK 397
Cdd:cd10224 291 NIVLSGGTTMFPGIADRMQKEITALA----------------PSTMKIKIVAPPERKYSVWIGGSILASLSTFQQMWISK 354
                       410
                ....*....|
gi 9966913  398 KDYEEYGPSI 407
Cdd:cd10224 355 QEYDESGPSI 364
PTZ00004 PTZ00004
actin-2; Provisional
9-407 3.71e-89

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 275.11  E-value: 3.71e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913     9 VVDCGTGYTKLGYAGNTEPQFIIPSCiairesakVVDQAQRRVLRGVDDLDFFIGDEAIDK-PTYATKWPIRHGIIEDWD 87
Cdd:PTZ00004  10 VVDNGSGMVKAGFAGDDAPRCVFPSI--------VGRPKNPGIMVGMEEKDCYVGDEAQDKrGILTLKYPIEHGIVTNWD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913    88 LMERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIAVQAVLALAASwtsrqvgERTlTGIV 167
Cdd:PTZ00004  82 DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETHNVPAMYVAIQAVLSLYAS-------GRT-TGIV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   168 IDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICPDIVKEfakydv 247
Cdd:PTZ00004 154 LDSGDGVSHTVPIYEGYSLPHAIHRLDVAGRDLTEYMMKILHERGTTFTTTAEKEIVRDIKEKLCYIALDFDEE------ 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   248 dprkwIKQYTGINAINQKKF------VIDVGYERFLGPEIFFHPEFANPDFMESISDVVDEVIQNCPIDVRRPLYKNVVL 321
Cdd:PTZ00004 228 -----MGNSAGSSDKYEESYelpdgtIITVGSERFRCPEALFQPSLIGKEEPPGIHELTFQSINKCDIDIRKDLYGNIVL 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   322 SGGSTMFRDFGRRLQRDLKRVVdarlrlseelsggrikPKPVEVQVVTHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYE 401
Cdd:PTZ00004 303 SGGTTMYRGLPERLTKELTTLA----------------PSTMKIKVVAPPERKYSVWIGGSILSSLPTFQQMWVTKEEYD 366

                 ....*.
gi 9966913   402 EYGPSI 407
Cdd:PTZ00004 367 ESGPSI 372
ASKHA_NBD_Arp2 cd10220
nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, ...
7-409 1.02e-81

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: 255.95  E-value: 1.02e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913    7 PCVVDCGTGYTKLGYAGNTEPQFIIPSCIA---IRESAKVVDQAqrrvlrgVDDLdfFIGDEAIDKPTY-ATKWPIRHGI 82
Cdd:cd10220   2 VVVCDNGTGFVKCGFAGSNFPEHVFPSLVGrpiLRAEEKVGDIE-------IKDI--MVGDEASELRSMlEVTYPMENGI 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   83 IEDWDLMERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIavqavlalaaswtSRQV---- 158
Cdd:cd10220  73 VRNWDDMEHLWDYTFGEKLKIDPRECKILLTEPPMNPTKNREKMVEVMFEKYGFAGVYV-------------AIQAvltl 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  159 -GERTLTGIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDIT-YFIQQLLRErevGIPPEQS--LETAKAIKEKYCYI 234
Cdd:cd10220 140 yAQGLLTGVVVDSGDGVTHIVPVYEGFSLPHLTRRLDVAGRDITrYLIKLLLLR---GYAFNRTadFETVREIKEKLCYV 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  235 CPDIVKEfAKYDVDPRKWIKQYT---GinainqkkFVIDVGYERFLGPEIFFHPEFANpdfMES--ISDVVDEVIQNCPI 309
Cdd:cd10220 217 AYDIELE-QKLALETTVLVESYTlpdG--------RVIKVGGERFEAPEALFQPHLID---VEGpgIAELLFNTIQAADI 284
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  310 DVRRPLYKNVVLSGGSTMFRDFGRRLQRDLKrvvdaRLRLSEELSGGRIKPKPVEVQVVTHHMQRYAVWFGGSMLA---- 385
Cdd:cd10220 285 DTRPELYKHIVLSGGSTMYPGLPSRLEKEIK-----QLYLERVLKGDTERLSKFKIRIEDPPRRKHMVFLGGAVLAdimk 359
                       410       420
                ....*....|....*....|....
gi 9966913  386 STPEFFQvchTKKDYEEYGPSICR 409
Cdd:cd10220 360 DKDEFWI---TRQEYEEQGVRVLD 380
PTZ00281 PTZ00281
actin; Provisional
9-407 1.51e-77

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 244.99  E-value: 1.51e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913     9 VVDCGTGYTKLGYAGNTEPQFIIPSCIA-IRESAKVVDQAQRrvlrgvddlDFFIGDEAIDKPTYAT-KWPIRHGIIEDW 86
Cdd:PTZ00281  10 VIDNGSGMCKAGFAGDDAPRAVFPSIVGrPRHTGVMVGMGQK---------DSYVGDEAQSKRGILTlKYPIEHGIVTNW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913    87 DLMERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIAVQAVLALAASwtsrqvgERTlTGI 166
Cdd:PTZ00281  81 DDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYAS-------GRT-TGI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   167 VIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICPDIVKEFakyd 246
Cdd:PTZ00281 153 VMDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEM---- 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   247 vdprkwikQYTGINAINQKKF------VIDVGYERFLGPEIFFHPEFANpdfMES--ISDVVDEVIQNCPIDVRRPLYKN 318
Cdd:PTZ00281 229 --------QTAASSSALEKSYelpdgqVITIGNERFRCPEALFQPSFLG---MESagIHETTYNSIMKCDVDIRKDLYGN 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   319 VVLSGGSTMFRDFGRRLQRDLKrvvdarlrlseelsggRIKPKPVEVQVVTHHMQRYAVWFGGSMLASTPEFFQVCHTKK 398
Cdd:PTZ00281 298 VVLSGGTTMFPGIADRMNKELT----------------ALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKE 361

                 ....*....
gi 9966913   399 DYEEYGPSI 407
Cdd:PTZ00281 362 EYDESGPSI 370
ASKHA_NBD_Arp4_ACTL6-like cd13395
nucleotide-binding domain (NBD) of the actin-related protein 4 (Arp4)-like subfamily; The ...
9-404 1.70e-76

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: 243.24  E-value: 1.70e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913    9 VVDCGTGYTKLGYAGNTEPQFIIPSCIAIRESAKVVDQAQRRVLRGVddLDFFIGDEAIDKPT--YATKWPIRHGIIEDW 86
Cdd:cd13395   8 VLDIGSYSTRAGYAGEDTPKAVFPSVVGVVTDDDDAEDYVGGSGEKK--RKYYIGTNSIGVPRpnMEVISPLKDGLIEDW 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   87 DLMERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIavqavlalaaswtSRQ-------VG 159
Cdd:cd13395  86 DAFEKLWDHALKNRLRVDPSEHPLLLTEPSWNTRANREKLTELMFEKYNVPAFFL-------------AKNavlsafaNG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  160 eRTlTGIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSL---------ETAKAIKEK 230
Cdd:cd13395 153 -RS-TALVVDSGATSTSVVPVHDGYVLQKAIVRSPLGGDFLTDQLLKLLESKNIEIIPRYMIkskepveggAPAKYTKKD 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  231 YC--------YICPDIVKEFAK--YDVDPRKWIKQYTGinAINQKKF------VIDVGYERFLGPEIFFHPEFANPDF-- 292
Cdd:cd13395 231 LPnttssyhrYMVRRVLQDFKEsvCQVSDSPFDESEAA--SIPTVSYelpdgyNIEFGAERFKIPELLFDPSLVKGIPap 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  293 ------MESISDVVDEVIQNCPIDVRRPLYKNVVLSGGSTMFRDFGRRLQRDlkrvvdarlrLSEELSGG-RIK----PK 361
Cdd:cd13395 309 psegneLLGLPQLVYTSIGSCDVDIRPELYGNVVLTGGNSLLPGFTDRLNRE----------LSEKAPGSlKLKilasGN 378
                       410       420       430       440
                ....*....|....*....|....*....|....*....|...
gi 9966913  362 PVEvqvvthhmQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYG 404
Cdd:cd13395 379 TVE--------RRFSSWIGGSILASLGSFQQMWISKQEYEEHG 413
PTZ00466 PTZ00466
actin-like protein; Provisional
7-407 2.68e-76

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 241.77  E-value: 2.68e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913     7 PCVVDCGTGYTKLGYAGNTEPQFIIPSCIAiRESAKvvdqaqrRVLRGVDDLDFFIGDEA-----IDKPTYatkwPIRHG 81
Cdd:PTZ00466  14 PIIIDNGTGYIKAGFAGEDVPNLVFPSYVG-RPKYK-------RVMAGAVEGNIFVGNKAeeyrgLLKVTY----PINHG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913    82 IIEDWDLMERFMEQVvFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIAVQAVLALAASWTSrqvger 161
Cdd:PTZ00466  82 IIENWNDMENIWIHV-YNSMKINSEEHPVLLTEAPLNPQKNKEKIAEVFFETFNVPALFISIQAILSLYSCGKT------ 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   162 tlTGIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICPDIVKE 241
Cdd:PTZ00466 155 --NGTVLDCGDGVCHCVSIYEGYSITNTITRTDVAGRDITTYLGYLLRKNGHLFNTSAEMEVVKNMKENCCYVSFNMNKE 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   242 FAKYDvdprkwiKQYTGINAINQKKFVIDVGYERFLGPEIFFHPEFANPDFMeSISDVVDEVIQNCPIDVRRPLYKNVVL 321
Cdd:PTZ00466 233 KNSSE-------KALTTLPYILPDGSQILIGSERYRAPEVLFNPSILGLEYL-GLSELIVTSITRADMDLRRTLYSHIVL 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   322 SGGSTMFRDFGRRLQRDLKrvvdarlrlseelsggRIKPKPVEVQVVTHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYE 401
Cdd:PTZ00466 305 SGGTTMFHGFGDRLLNEIR----------------KFAPKDITIRISAPPERKFSTFIGGSILASLATFKKIWISKQEFD 368

                 ....*.
gi 9966913   402 EYGPSI 407
Cdd:PTZ00466 369 EYGSVI 374
ASKHA_NBD_ACTL7 cd10214
nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ...
7-407 2.52e-75

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: 238.86  E-value: 2.52e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913    7 PCVVDCGTGYTKLGYAGNTEPQFIIPSCIAIR--ESAKVVDQAQRRvlrgvddldfFIGDEAID-KPTYATKWPIRHGII 83
Cdd:cd10214   5 AVIIDLGTGYCKAGFAGQPRPSYVISSTVGKPpqESAKTGDNRKET----------FVGKELANvEPPLKLVNPLRHGIV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   84 EDWDLMERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIavqavlaLAASWTSRQVGERTl 163
Cdd:cd10214  75 VDWDCVQDIWEYIFEKEMKILPEEHAVLVSDPPLSPTTNREKYAELMFETFSIPAMHI-------AYQSRLSLYSYGRT- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  164 TGIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLreREVGIP-PEQSLETAKAIKEKYCYICPDIVKEF 242
Cdd:cd10214 147 SGLVVESGHGVSYVVPIHEGYNLPHITGRADYAGSDLTAYLMKLL--NEAGNKfTDDQLHIVEDIKKKCCYVALDFEEEM 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  243 AkydVDPRKWIKQYTGINAinqkkFVIDVGYERFLGPEIFFHPEFAnPDFMESISDVVDEVIQNCPIDVRRPLYKNVVLS 322
Cdd:cd10214 225 G---LPPQEYTVDYELPDG-----HLITIGKERFRCPEMLFNPSLI-GSKQPGLHTLTMNSLNKCDANLKKDLAKNILLC 295
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  323 GGSTMFRDFGRRLQRDLKRVVdarlrlseelsggrikpkPVEVQVVTHHMQR-YAVWFGGSMLASTPEFFQVCHTKKDYE 401
Cdd:cd10214 296 GGSTMFDGFPDRFQKELSKLC------------------PNDNPIVAASPERkYSVWTGGSILASLKSFQQLWVRRREYE 357

                ....*.
gi 9966913  402 EYGPSI 407
Cdd:cd10214 358 ERGPFV 363
PTZ00452 PTZ00452
actin; Provisional
1-407 4.65e-57

actin; Provisional


Pssm-ID: 185631  Cd Length: 375  Bit Score: 191.89  E-value: 4.65e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913     1 MAGSLPPCVVDCGTGYTKLGYAGNTEPQFIIPSCIAiresakvvDQAQRRVLRGVDDLDFFIGDEA-IDKPTYATKWPIR 79
Cdd:PTZ00452   1 MQAQYPAVVIDNGSGYCKIGIAGDDAPTSCFPAIVG--------RSKQNDGIFSTFNKEYYVGEEAqAKRGVLAIKEPIQ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913    80 HGIIEDWDLMERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIAVQAVLALAASWTSrqvg 159
Cdd:PTZ00452  73 NGIINSWDDIEIIWHHAFYNELCMSPEDQPVFMTDAPMNSKFNRERMTQIMFETFNTPCLYISNEAVLSLYTSGKT---- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   160 ertlTGIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICpdiv 239
Cdd:PTZ00452 149 ----IGLVVDSGEGVTHCVPVFEGHQIPQAITKINLAGRLCTDYLTQILQELGYSLTEPHQRIIVKNIKERLCYTA---- 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   240 kefakydVDPRKWIKQYTGINAINQKKFVID-----VGYERFLGPEIFFHPEFANPDfMESISDVVDEVIQNCPIDVRRP 314
Cdd:PTZ00452 221 -------LDPQDEKRIYKESNSQDSPYKLPDgniltIKSQKFRCSEILFQPKLIGLE-VAGIHHLAYSSIKKCDLDLRQE 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   315 LYKNVVLSGGSTMFRDFGRRLQRDLKRVVdarlrlseelsggrikPKPVEVQVVTHHMQRYAVWFGGSMLAS----TPEF 390
Cdd:PTZ00452 293 LCRNIVLSGGTTLFPGIANRLSNELTNLV----------------PSQLKIQVAAPPDRRFSAWIGGSIQCTlstqQPQW 356
                        410
                 ....*....|....*..
gi 9966913   391 FQvchtKKDYEEYGPSI 407
Cdd:PTZ00452 357 IK----RQEYDEQGPSI 369
ASKHA_NBD_Arp6 cd10210
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ...
9-404 2.92e-54

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: 184.68  E-value: 2.92e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913    9 VVDCGTGYTKLGYAGNTEPqFIIPSCIAiresaKVVDQaqRRVLRGVDDLDffigdEAIDKPTYATKWPIRHGIIEDWDL 88
Cdd:cd10210   3 VLDNGAYTIKAGFASDDPP-RVIPNCIA-----KPKSE--RRRLFGDDQLD-----ECKDLSGLFYRRPFERGYLVNWDL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   89 merfmEQVVFKYL------RAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIA------VQAVLALAASWTSR 156
Cdd:cd10210  70 -----QRQIWDHLfgklllNVDPSDTALVLTEPPFNPPSIQEAMDEIVFEEYGFQSLYRTtaaalsAFAYLADSEQSSSS 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  157 qvgeRTLTGIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLetAKAIKEKYCYICP 236
Cdd:cd10210 145 ----SSQCCLVVDSGFSFTHIVPFFDGKPVKRAVRRIDVGGKLLTNYLKEIISYRQLNVMDETYL--VNQIKEDLCFVST 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  237 DIVKEFAKYDVDPRK-WIKQ------YTGINainqKKFVIDVGY-----------------ERFLGPEIFFHPEFANPDF 292
Cdd:cd10210 219 DFYEDLEIAKKKGKEnTIRRdyvlpdYTTSK----RGYVRDPEEpnrgklkedeqvlrlnnERFTVPELLFHPSDIGIQQ 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  293 MeSISDVVDEVIQNCPIDVRRPLYKNVVLSGGSTMFRDFGRRLQRDLkrvvdaRLRLSEELsggrikpkpvEVQVVTHHM 372
Cdd:cd10210 295 A-GIAEAIVQSINACPEELQPLLYANIVLTGGNALFPGFRERLEAEL------RSLAPDDY----------DVNVTLPED 357
                       410       420       430
                ....*....|....*....|....*....|..
gi 9966913  373 QRYAVWFGGSMLASTPEFFQVCHTKKDYEEYG 404
Cdd:cd10210 358 PITYAWEGGSLLAQSPEFEELAVTRAEYEEHG 389
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
8-407 3.02e-44

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: 157.55  E-value: 3.02e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913    8 CVVDCGTGYTKLGYAGNT-EPQFIIPSciairesakvvdqAQRRVLRGVDDLDFFIGDEAIDkptyatkwPIRHGIIEDW 86
Cdd:cd10209   1 VVIDAGSRLLKAGYAYPDrEPSVVEPT-------------RVTPAVEDGEESDTVVEGNTVS--------PIRRGRIEDW 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   87 DLMERFMEQVVFKYLRAEPEDH-YFLMTEPPLNTPENREYLAEIMFESFNVPGLYIavqavlalaaswtSRQ-------V 158
Cdd:cd10209  60 DALEALLRYVFYTGLGWEEGNEgQVLIAEPLLTSKAERERLTQLMFETFNVSGLYA-------------SEQavlslyaV 126
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  159 GErtLTGIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIppEQSLETAKAIKEKYCYiCPDI 238
Cdd:cd10209 127 GR--ISGCVVDVGHGKIDIAPVWEGAIQHNAVRRFEIGGRDLTELLAAELGKSNPKV--KLDRSIVERLKEAVAW-SADD 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  239 VKEFAKYDVDPRkwIKQYTGINAInqkkfVIDVGYERFLGPEIFFHPEfANPDFMESISDVVDEVIQNCPIDVRRPLYKN 318
Cdd:cd10209 202 EEAYEKKVLTCS--PETYTLPDGR-----VISVGKERYCVGEALFRPS-ILGIEEYGIVEQLVRAVSTSPSENRRQLLEN 273
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  319 VVLSGGSTMFRDFGRRLQRdlkrvvDARLRLSEELSGGRIKPkPvevQVVTHHMQRYAVWFGGSMLASTpEFFQVCH-TK 397
Cdd:cd10209 274 IVLCGGTSSVPGLEARLQK------EIRLLSSPSSRPALVKP-P---EYMPENTLRYSAWIGGAILAKV-VFPQNQHvTK 342
                       410
                ....*....|
gi 9966913  398 KDYEEYGPSI 407
Cdd:cd10209 343 ADYDETGPSV 352
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
7-405 1.07e-43

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: 155.81  E-value: 1.07e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913    7 PCVVDCGTGYTKLGYAGNTEPQFIIPSCIA-IRESAKvvdqaqrrvlrgvDDLDFFIGDEAIDKPtyATKWPIR----HG 81
Cdd:cd10211   1 PIVIDNGSYQCRAGWAGDKEPRLVFRNLVAkPRDRKK-------------GITVTLVGNDILNDE--AVRSHLRspfdRN 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   82 IIEDWDLMERFMEQVvFKYLRAEPE---DHYFLMTEPPLNTPENREYLAEIMFESFNVP-------GLYiavqavlalaa 151
Cdd:cd10211  66 VVTNFDLQEQILDYI-FSHLGINSEgsvDHPIVLTEALCNPNYSRQLMSELLFECYGVPsvaygidSLF----------- 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  152 SWTSRQVGERTLTGIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKY 231
Cdd:cd10211 134 SYYHNQPQGDPSDGLVISSGYSTTHVIPVLNGRLDLSQCKRINLGGFHATDYLQRLLQLKYPTHPSAITLSRAEELVHEH 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  232 CYICPDivkefakYDVDPRKWikqytginainqkkfvidvgyerflgpeiffhpefANPDFMES----------ISDVVD 301
Cdd:cd10211 214 CYVAED-------YDEELKKW-----------------------------------EDPEYYEEnvrkiqlpfgLVETIE 251
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  302 EVIQNCPIDVRRPLYKNVVLSGGSTMFRDFGRRLQRDLKrvvdarlrlseelsggRIKPKPVEVQVVTHHMQRYAVWFGG 381
Cdd:cd10211 252 FVLKRYPAEQQDRLVQNVFLTGGNALFPGLKERLEKELR----------------AIRPFGSPFNVVRAKDPVLDAWRGA 315
                       410       420
                ....*....|....*....|....
gi 9966913  382 SMLASTPEFFQVCHTKKDYEEYGP 405
Cdd:cd10211 316 AKWALDSTFEKVWITKQEYEEKGG 339
ASKHA_NBD_Arp10 cd10207
nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins; ...
9-404 2.61e-43

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: 155.49  E-value: 2.61e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913    9 VVDCGTGYTKLGYAGNTEPQFIIPSciairesaKVVDQAQRRVLRGvddldffigdeaidkptyatkWPIRHGIIEDW-D 87
Cdd:cd10207   2 VLDIGSAYTKCGFAGESAPRCIIPS--------EVKLPGGKKVIRV---------------------VDQRSGNEEELyE 52
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   88 LMERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPG-LYIavqavlalaaswTSRQVGERTL--- 163
Cdd:cd10207  53 ALKEFLHELYFKHLLVNPKDRRVVVVESVLCPTPFRETLAKVLFKHFEVPSvLFA------------PSHLLSLLTLgir 120
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  164 TGIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQ------------SLETAKAIKEKY 231
Cdd:cd10207 121 TALVVDCGYRETRVLPVYEGVPLLSAWQSTPLGGKALHKRLKKLLLEHATVVTGDNkgqllssvdsllSEEVLEDIKVRA 200
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  232 CYICP-DIVKEFAKYDVDPRKWIKQY---TGINAINQKKFVIdVGYERFLGPEIFFhpEFANPDfmESISDVVDEVIQNC 307
Cdd:cd10207 201 CFVTSlERGKTLQSATEEGSTEEPSPpppVDYPLDGEKILIV-PGSIRESAEELLF--EGDNEE--KSLPTLILDSLLKC 275
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  308 PIDVRRPLYKNVVLSGGSTMFRDFGRRLQRDLKRVVDARlRLSEELSGGRIKPkpveVQVVTHHMQRYAVWFGGSMLAST 387
Cdd:cd10207 276 PIDVRKQLAENIVVIGGTSMLPGFKHRLLEELRALLRKP-KYFEELAPKTFRF----HTPPSVFKPNYLAWLGGSIFGAL 350
                       410
                ....*....|....*..
gi 9966913  388 PEFFQVCHTKKDYEEYG 404
Cdd:cd10207 351 ESILGRSLSREAYLQTG 367
COG5277 COG5277
Actin-related protein [Cytoskeleton];
6-386 6.69e-39

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 144.55  E-value: 6.69e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913    6 PPCVVDCGTGYTKLG-YAGNTEPQFIIPSCIAIResakVVDQAQRRVLRGVDDLDFFIGDEAIDKP------TYATKWPI 78
Cdd:COG5277   9 YVIGIDFGTSYVKYGpIALEEKPRVIQTRGLFLR----IVGESKLLGPMEGLSRGLVVGDEVSKYLssvrdaIRNLKYPL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   79 RHGIIE-----DWDLMERFMEQVVFKYLRAEPEDHYFLM--TEPPLNTPENREYLAEIMFESF---NVPGLYIAVQAVLA 148
Cdd:COG5277  85 RDGIVRrddedAWRVLKELLRYTFAQFLVVDPEFHGFLVvvALSALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPLAV 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  149 LaaswtsrqVGERTLTGIVIDSGDGVTHVIPVAEGyVIGSCIKHIPIAGRDITYFIQQLLREREVG-IPPEQslETAKAI 227
Cdd:COG5277 165 A--------IAEKAVTCVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSdTAREE--YVVRVV 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  228 KEKYCYICPDIVKEFAKYDVDPRKWIKQYTGINAINQkkfvIDVG---YERFLGPEIFFHPEFanpDFMES--------- 295
Cdd:COG5277 234 KEALGLVPRDLAKAIQKAASNPDSFEAKVRLPNPTVE----IELGnyaWERFLIGEILFNPNH---EGFESyiqqgrlri 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  296 ---------------ISDVVDEVIQNCPIDVRRPLYKNVVLSGGSTMFrdfgrRLQRDLKRV-VDARLRLSEELSggRIK 359
Cdd:COG5277 307 edavigdvvlygemgLAEAIINSIMKCDVEIQDELYSNIILSGGAFNW-----SVPPGLEDVaVDSVTRVQIELS--ELA 379
                       410       420
                ....*....|....*....|....*..
gi 9966913  360 PKpVEVQVVTHHMQRYAVWFGGSMLAS 386
Cdd:COG5277 380 PE-LKVNVRLVSDPQYSVWKGAIIYGY 405
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
76-407 2.84e-31

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: 122.42  E-value: 2.84e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   76 WPIRHGIIEDWDLMERFMEQVVFKYL--RAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIavqavlalaasw 153
Cdd:cd10208  37 WPIQDGRVVDWDALEALWRHILFSLLsiPRPTNNSPVLLSVPPSWSKSDLELLTQLFFERLNVPAFAI------------ 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  154 tsrqvGERTL---------TGIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQS---- 220
Cdd:cd10208 105 -----LEAPLaalyaagatSGIVVDIGHEKTDITPIVDSQVVPHALVSIPIGGQDCTAHLAQLLKSDEPELKSQAEsgee 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  221 --LETAKAIKEKycyicpDIVkEFAKYDVDPrkwikqytginainQKKFVIDVGYERFLGPEIFFHPEF---ANPDFMES 295
Cdd:cd10208 180 atLDLAEALKKS------PIC-EVLSDGADL--------------ASGTEITVGKERFRACEPLFKPSSlrvDLLIAAIA 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  296 ISDVVDEViqnCPIDVRRPLYKNVVLSGGSTMFRDFGRRLQRDLKrvvdARLRLSEELSGG------RIKPKPVEVQVVT 369
Cdd:cd10208 239 GALVLNAS---DEPDKRPALWENIIIVGGGSRIRGLKEALLSELQ----QFHLISETSASPqqpriiRLAKIPDYFPEWK 311
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 9966913  370 HHMQRYAVWFGGSMLA------STPEFFQvchTKKDYEEYGPSI 407
Cdd:cd10208 312 KSGYEEAAFLGASIVAklvfndPSSKHYI---SKVDYNEKGPAA 352
ASKHA_NBD_AtArp8-like cd13396
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and ...
158-400 4.48e-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: 78.74  E-value: 4.48e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  158 VGERTlTGIVIDSGDGVTHVIPVAEGYV---IGscIKHIPIAGRDITYFIQQLLREREVGIPpeqSLETAKAIKEKYCYI 234
Cdd:cd13396 111 AANRT-SGIVVNIGFRVTTIVPVYRGRVmhdIG--VEVVGQGALRLTGFLKELMQQNGIRFP---SLYTVRTIKEKLCYV 184
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  235 CPDIVKEFAK-----YDVDPRKWikqytginainqkkFVIdvGYERFLGPEIFFHPEFANPDFMeSISDVVDEVIQNCPI 309
Cdd:cd13396 185 AEDYEAELAKdtqasCEVAGEGW--------------FTL--SNERFKTGEILFQPGLGGMRAM-GLHQAVALCMDHCAL 247
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  310 DVR---RPLYKNVVLSGGSTMFRDFGRRLQRDLKRVVDARLrlseeLSGGRIKPKPVEVqvvthhmqrYAVWFGGSMLAS 386
Cdd:cd13396 248 VHSqgdDGWFKTIVLSGGSACLPGLSERLERELRKLLPKSL-----SEGIRIIPPPLGP---------DSAWQGAKLISN 313
                       250
                ....*....|....*
gi 9966913  387 TPEFFQV-CHTKKDY 400
Cdd:cd13396 314 LSNFPDGwCITKKQF 328
ASKHA_NBD_Arp8-like cd10206
nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The ...
164-410 7.53e-08

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: 54.17  E-value: 7.53e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  164 TGIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLreREVGIPPE-------QSLETAKAIKEKYCYICP 236
Cdd:cd10206 234 SACVVDIGAQKTSVACVEDGLSIPNSRIRLPYGGDDITRCFLWLL--RRSGFPYRecnlnspLDFLLLERLKETYCTLDQ 311
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  237 DIVKEfAKYDVDPRKWIKQytginainQKKFVIdvgyeRFLGpeiffhpefanpdfmesISDVVDEVIQNCP-IDVRRPL 315
Cdd:cd10206 312 DDIGV-QLHEFYVREPGQP--------TLKYQF-----KLLP-----------------LDEAIVQSILSCAsDELKRKM 360
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  316 YKNVVLSGGSTMFRDFGRRLQRDLKRVVDARLRLSEElsggrikpkpVEVQVVTHHMQ-RYAVWFGGSMLA---STPEFF 391
Cdd:cd10206 361 YSSILLVGGGAKIPGLAEALEDRLLIKIPSLFEAVET----------VEVLPPPKDMDpSLLAWKGGAVLAcldSAQELW 430
                       250
                ....*....|....*....
gi 9966913  392 QvchTKKDYEEYGPSICRH 410
Cdd:cd10206 431 I---TRKEWQRLGVRALRE 446
ASKHA_NBD_MamK cd24009
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ...
59-352 4.13e-07

nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called magnetosome cytoskeleton protein MamK, is a protein with ATPase activity which forms dynamic cytoplasmic filaments (probably with paralog MamK-like) that may organize magnetosomes into long chains running parallel to the long axis of the cell. Turnover of MamK filaments is probably promoted by MamK-like (e.g.. MamJ and/or LimJ), which provides a monomer pool. MamK forms twisted filaments in the presence of ATP or GTP. It serves to close gaps between magnetosomes in the chain. Interaction with MCP10 is involved in controlling the response to magnetic fields, possibly by controlling flagellar rotation. The MamK 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: 466859 [Multi-domain]  Cd Length: 328  Bit Score: 51.44  E-value: 4.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   59 DFFIGDEAIDKPTY-ATKWPIRHGIIEDWD---------LMERFMEQvvfkyLRAEPEDH-YFLMTEPPLNTPENREYLA 127
Cdd:cd24009  44 EVLFGDEALENRLAlDLRRPLEDGVIKEGDdrdleaareLLQHLIEL-----ALPGPDDEiYAVIGVPARASAENKQALL 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  128 EIMFESFN----VPGLYIAVQavlalaaswtsrqvGERTLTG-IVIDSGDGVTHV------IPVAEgyvigSCIkHIPIA 196
Cdd:cd24009 119 EIARELVDgvmvVSEPFAVAY--------------GLDRLDNsLIVDIGAGTTDLcrmkgtIPTEE-----DQI-TLPKA 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  197 GRDITYFIQQLLRER--EVGIPPEQsletAKAIKEKYCYIcpdivkefakydVDPRKWIKQYTGINAINQKkfvIDVGye 274
Cdd:cd24009 179 GDYIDEELVDLIKERypEVQLTLNM----ARRWKEKYGFV------------GDASEPVKVELPVDGKPVT---YDIT-- 237
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9966913  275 rflgPEIFFHPEFANPDFMESIsdvvDEVIQNCPIDVRRPLYKNVVLSGGSTMFRDFGRRLQRDLKRVVDARLRLSEE 352
Cdd:cd24009 238 ----EELRIACESLVPDIVEGI----KKLIASFDPEFQEELRNNIVLAGGGSRIRGLDTYIEKALKEYGGGKVTCVDD 307
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
374-407 9.16e-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: 9.16e-06
                         10        20        30
                 ....*....|....*....|....*....|....
gi 9966913   374 RYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPSI 407
Cdd:NF040575  94 ESAAWRGAAMYAASEGFVEMAITKQEYDESGPSI 127
ASKHA_NBD_ParM-like cd10227
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ...
9-89 2.78e-03

nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ParM is a plasmid-encoded bacterial homolog of actin, which polymerizes into filaments similar to F-actin, and plays a vital role in plasmid segregation. ParM filaments segregate plasmids paired at midcell into the individual daughter cells. This subfamily also contains Thermoplasma acidophilum Ta0583, an active ATPase at physiological temperatures, which has a propensity to form filaments. ParM-like proteins 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: 466825 [Multi-domain]  Cd Length: 263  Bit Score: 39.43  E-value: 2.78e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913    9 VVDCGTGYTKLGYAGNTEpqFIIPSCIA-IRESAKVVDQAQRRVLRGVDDLDFFIGDEAIDKPTYATKWPIRHGIIEDWD 87
Cdd:cd10227   2 GIDIGNGNTKVVTGGGKE--FKFPSAVAeARESSLDDGLLEDDIIVEYNGKRYLVGELALREGGGGRSTGDDKKKSEDAL 79

                ..
gi 9966913   88 LM 89
Cdd:cd10227  80 LL 81
ASKHA_NBD_FtsA cd24048
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ...
160-241 4.34e-03

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: 39.05  E-value: 4.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  160 ERTLTGIVIDSGDGVTHVIPVAEGYVIgsCIKHIPIAGRDITYFIQQLLRerevgIPpeqsLETAKAIKEKYCYICPDIV 239
Cdd:cd24048 195 EKELGVALIDIGGGTTDIAVFKNGSLR--YTAVIPVGGNHITNDIAIGLN-----TP----FEEAERLKIKYGSALSEEA 263

                ..
gi 9966913  240 KE 241
Cdd:cd24048 264 DE 265
ASKHA_NBD_ScArp7-like cd10212
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and ...
9-401 6.50e-03

nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and similar proteins; Saccharomyces cerevisiae Arp7, also called actin-like protein 7, 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. Arp7 forms a stable heterodimer with Arp9 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: 466818 [Multi-domain]  Cd Length: 424  Bit Score: 38.55  E-value: 6.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913    9 VVDCGTGYTKLGYAGNTEPQFIIPSCIAIResakvVDQAqrrvlrgvDDLDFFIG-----DEAIDKPTYATKWPI--RHG 81
Cdd:cd10212   7 VIHNGSHRTVAGFSNVELPQCIIPSSYIKR-----TDEG--------GEAEFIFGtynmiDAAAEKRNGDEVYTLvdSQG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913   82 IIEDWDLMERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLA---EIMFESFNVPGLYIAVQAVLALAASWTSrqv 158
Cdd:cd10212  74 LPYNWDALEMQWRYLYDTQLKVSPEELPLVITMPATNGKPDMAILEryyELAFDKLNVPVFQIVIEPLAIALSMGKS--- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  159 gertlTGIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQ----LLRER------------------EVGIP 216
Cdd:cd10212 151 -----SAFVIDIGASGCNVTPIIDGIVVKNAVVRSKFGGDFLDFQVHErlapLIKEEndmenmadeqkrstdvwyEASTW 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  217 PEQSLETAKAIKEKYCYICPDIVKEFAKYDVDPRKWIK------QYTGI-----NAINQKK----------FVIDVGyER 275
Cdd:cd10212 226 IQQFKSTMLQVSEKDLFELERYYKEQADIYAKQQEQLKqmdqqlQYTALtgspnNPLVQKKnflfkplnktLTLDLK-EC 304
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966913  276 FLGPEIFFHPEFANPDFM--ESISDVVDEVIQNCPIDVRRPLYKNVVLSGGSTMFRDFGRRLQRDLKrvvdarLRLSEel 353
Cdd:cd10212 305 YQFAEYLFKPQLISDKFSpeDGLGPLMAKSVKKAPEQVYSLLLTNVIITGSTSLIEGMEQRIIKELS------IRFPQ-- 376
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*....
gi 9966913  354 sggrIKPKPVEVQVVTHhmQRYAVWFGGSMLASTPEF-FQVCHTKKDYE 401
Cdd:cd10212 377 ----YKLTTFANQVMMD--RKIQGWLGALTMANLPSWsLGKWYSKEDYE 419
 
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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