NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|113305|sp|P10993|]
View 

RecName: Full=Actin, cytoplasmic; AltName: Full=Actin, micronuclear

Protein Classification

actin( domain architecture ID 19021204)

actin is a ubiquitous protein involved in the formation of filaments that are major components of the cytoskeleton

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
8-371 0e+00

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: 833.55  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305     8 AIVIDNGSGMCKAGIAGDDAPRAAFPSIIGRPKMPGIMVGMDQKECYVGEEAQAKRGVLNLKYPIEHGIVTDYDDMEKIW 87
Cdd:cd10224   2 ALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIW 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    88 HHCFYNELRVTPEEHPCLLTEAPQNPKLNREKMTKTMFETFNVPSFYVAIQAVLSLYASGRTTGIVVDSGDGVTHTVSIY 167
Cdd:cd10224  82 HHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIY 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   168 EGYALPHAILRIDLAGRDLTEYCMKLLYEIGLNFSSTAEREIIRDIKEKLCYVALDYESELKAYKESSTNDKSYELPDGN 247
Cdd:cd10224 162 EGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDGQ 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   248 TITVQDQRFRCPELLFKPAFIGKEFPGIHELTFNSIMKCDVDVRKDLYNNIVLSGGTTMFPGIAERLSKEVSALAPSSMK 327
Cdd:cd10224 242 VITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTMK 321
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 113305   328 IKVVAPPERRYSVWIGGSILSSLSTFQTMWITKAEYDESGPSIV 371
Cdd:cd10224 322 IKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIV 365
 
Name Accession Description Interval E-value
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
8-371 0e+00

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: 833.55  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305     8 AIVIDNGSGMCKAGIAGDDAPRAAFPSIIGRPKMPGIMVGMDQKECYVGEEAQAKRGVLNLKYPIEHGIVTDYDDMEKIW 87
Cdd:cd10224   2 ALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIW 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    88 HHCFYNELRVTPEEHPCLLTEAPQNPKLNREKMTKTMFETFNVPSFYVAIQAVLSLYASGRTTGIVVDSGDGVTHTVSIY 167
Cdd:cd10224  82 HHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIY 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   168 EGYALPHAILRIDLAGRDLTEYCMKLLYEIGLNFSSTAEREIIRDIKEKLCYVALDYESELKAYKESSTNDKSYELPDGN 247
Cdd:cd10224 162 EGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDGQ 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   248 TITVQDQRFRCPELLFKPAFIGKEFPGIHELTFNSIMKCDVDVRKDLYNNIVLSGGTTMFPGIAERLSKEVSALAPSSMK 327
Cdd:cd10224 242 VITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTMK 321
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 113305   328 IKVVAPPERRYSVWIGGSILSSLSTFQTMWITKAEYDESGPSIV 371
Cdd:cd10224 322 IKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIV 365
PTZ00004 PTZ00004
actin-2; Provisional
1-376 0e+00

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 672.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305      1 MTDSDSPAIVIDNGSGMCKAGIAGDDAPRAAFPSIIGRPKMPGIMVGMDQKECYVGEEAQAKRGVLNLKYPIEHGIVTDY 80
Cdd:PTZ00004   1 MSVEETNAAVVDNGSGMVKAGFAGDDAPRCVFPSIVGRPKNPGIMVGMEEKDCYVGDEAQDKRGILTLKYPIEHGIVTNW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305     81 DDMEKIWHHCFYNELRVTPEEHPCLLTEAPQNPKLNREKMTKTMFETFNVPSFYVAIQAVLSLYASGRTTGIVVDSGDGV 160
Cdd:PTZ00004  81 DDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETHNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    161 THTVSIYEGYALPHAILRIDLAGRDLTEYCMKLLYEIGLNFSSTAEREIIRDIKEKLCYVALDYESELK-AYKESSTNDK 239
Cdd:PTZ00004 161 SHTVPIYEGYSLPHAIHRLDVAGRDLTEYMMKILHERGTTFTTTAEKEIVRDIKEKLCYIALDFDEEMGnSAGSSDKYEE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    240 SYELPDGNTITVQDQRFRCPELLFKPAFIGKEFP-GIHELTFNSIMKCDVDVRKDLYNNIVLSGGTTMFPGIAERLSKEV 318
Cdd:PTZ00004 241 SYELPDGTIITVGSERFRCPEALFQPSLIGKEEPpGIHELTFQSINKCDIDIRKDLYGNIVLSGGTTMYRGLPERLTKEL 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 113305    319 SALAPSSMKIKVVAPPERRYSVWIGGSILSSLSTFQTMWITKAEYDESGPSIVHRKCF 376
Cdd:PTZ00004 321 TTLAPSTMKIKVVAPPERKYSVWIGGSILSSLPTFQQMWVTKEEYDESGPSIVHRKCF 378
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
7-376 0e+00

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 605.79  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305        7 PAIVIDNGSGMCKAGIAGDDAPRAAFPSIIGRPKMPGIMVGmDQKECYVGEEAQAKRGVLNLKYPIEHGIVTDYDDMEKI 86
Cdd:smart00268   2 PAIVIDNGSGTIKAGFAGEDFPQVVFPSIVGRPKDGKGMVG-DAKDIFVGDEAQEKRGGLELKYPIENGIVENWDDMEKI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305       87 WHHCFYNELRVTPEEHPCLLTEAPQNPKLNREKMTKTMFETFNVPSFYVAIQAVLSLYASGRTTGIVVDSGDGVTHTVSI 166
Cdd:smart00268  81 WDYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVPV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305      167 YEGYALPHAILRIDLAGRDLTEYCMKLLYEIGLNFSSTAEREIIRDIKEKLCYVALDYESELKAYKE---SSTNDKSYEL 243
Cdd:smart00268 161 VDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLAREsseSSKLEKTYEL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305      244 PDGNTITVQDQRFRCPELLFKPAFIGKEFPGIHELTFNSIMKCDVDVRKDLYNNIVLSGGTTMFPGIAERLSKEVSALAP 323
Cdd:smart00268 241 PDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELKQLAP 320
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 113305      324 SSMKIKVVAPPERRYSVWIGGSILSSLSTFQTMWITKAEYDESGPSIVHRKCF 376
Cdd:smart00268 321 KKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERKCF 373
Actin pfam00022
Actin;
7-376 0e+00

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 518.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305       7 PAIVIDNGSGMCKAGIAGDDAPRAAFPSIIGRPKMPGimvGMDQKECYVGEEAQAKRGVLNLKYPIEHGIVTDYDDMEKI 86
Cdd:pfam00022   2 SALVIDNGSHTTRAGFAGEDAPKAVIPSCVGKPRGTK---VEAANKYYVGDEALTYRPGMEVRSPVEDGIVVDWDAMEEI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305      87 WHHCFYNELRVTPEEHPCLLTEAPQNPKLNREKMTKTMFETFNVPSFYVAIQAVLSLYASGRTTGIVVDSGDGVTHTVSI 166
Cdd:pfam00022  79 WEHVLKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVPV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305     167 YEGYALPHAILRIDLAGRDLTEYCMKLL------------------------------YEIGLNFSSTAEREIIRDIKEK 216
Cdd:pfam00022 159 HDGYVLQKAIRRSDLGGDFLTDYLRELLrsrnieitprylikskkpgdpapavtkrelPDTTYSYKTYQERRVLEEIKES 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305     217 LCYVALDYESelKAYKESSTNDKSYELPDGNTITVQDQRFRCPELLFKPAFIGKE--------FPGIHELTFNSIMKCDV 288
Cdd:pfam00022 239 VCYVSDDPFG--DETTSSSIPTRVYELPDGSTIILGAERFRVPEILFNPSLIGSEselpppqtAVGIPELIVDAINACDV 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305     289 DVRKDLYNNIVLSGGTTMFPGIAERLSKEVSALAPSSMKIKVVAPP---ERRYSVWIGGSILSSLSTFQTMWITKAEYDE 365
Cdd:pfam00022 317 DLRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVKIIAPGntvERRYSAWIGGSILASLGTFQQMWVSKQEYEE 396
                         410
                  ....*....|.
gi 113305     366 SGPSIVHRKCF 376
Cdd:pfam00022 397 HGASVVERKCK 407
COG5277 COG5277
Actin-related protein [Cytoskeleton];
6-366 8.53e-112

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 332.91  E-value: 8.53e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305     6 SPAIVIDNGSGMCKAG-IAGDDAP-----RAAFPSIIGRPKMPGIMVGMDqKECYVGEEAQ-----AKRGVLNLKYPIEH 74
Cdd:COG5277   8 KYVIGIDFGTSYVKYGpIALEEKPrviqtRGLFLRIVGESKLLGPMEGLS-RGLVVGDEVSkylssVRDAIRNLKYPLRD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    75 GIVT-----DYDDMEKIWHHCFYNELRVTPEEHPCL--LTEAPQNPKLNREKMTKTMFETF---NVPSFYVAIQAVLSLY 144
Cdd:COG5277  87 GIVRrddedAWRVLKELLRYTFAQFLVVDPEFHGFLvvVALSALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPLAVAI 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   145 ASGRTTGIVVDSGDGVTHTVSIYEGyALPHAILRIDLAGRDLTEYCMKLLYEIGLNFSSTAEReIIRDIKEKLCYVALDY 224
Cdd:COG5277 167 AEKAVTCVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSDTAREEY-VVRVVKEALGLVPRDL 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   225 ESEL-KAYKESSTNDKSYELPDGNT-ITVQD---QRFRCPELLFKPAFIGKE----------------------FPGIHE 277
Cdd:COG5277 245 AKAIqKAASNPDSFEAKVRLPNPTVeIELGNyawERFLIGEILFNPNHEGFEsyiqqgrlriedavigdvvlygEMGLAE 324
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   278 LTFNSIMKCDVDVRKDLYNNIVLSGGTTMF---PGIAE-------RLSKEVSALAPsSMKIKVVAPPERRYSVWIGGSIL 347
Cdd:COG5277 325 AIINSIMKCDVEIQDELYSNIILSGGAFNWsvpPGLEDvavdsvtRVQIELSELAP-ELKVNVRLVSDPQYSVWKGAIIY 403
                       410       420
                ....*....|....*....|.
gi 113305   348 SSLSTFQTMW--ITKAEYDES 366
Cdd:COG5277 404 GYALPFSVKWswITKEGWYFL 424
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
304-375 1.02e-29

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: 111.22  E-value: 1.02e-29
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113305    304 TTMFPGIAERLSKEVSALAPSSMKIKVVAPPERRYSVWIGGSILSSLSTFQTMWITKAEYDESGPSIVHRKC 375
Cdd:NF040575  61 RVNESGFYEKLKKSITEKAPKGALIGMTLDPKPESAAWRGAAMYAASEGFVEMAITKQEYDESGPSIVHRKC 132
 
Name Accession Description Interval E-value
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
8-371 0e+00

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: 833.55  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305     8 AIVIDNGSGMCKAGIAGDDAPRAAFPSIIGRPKMPGIMVGMDQKECYVGEEAQAKRGVLNLKYPIEHGIVTDYDDMEKIW 87
Cdd:cd10224   2 ALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIW 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    88 HHCFYNELRVTPEEHPCLLTEAPQNPKLNREKMTKTMFETFNVPSFYVAIQAVLSLYASGRTTGIVVDSGDGVTHTVSIY 167
Cdd:cd10224  82 HHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIY 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   168 EGYALPHAILRIDLAGRDLTEYCMKLLYEIGLNFSSTAEREIIRDIKEKLCYVALDYESELKAYKESSTNDKSYELPDGN 247
Cdd:cd10224 162 EGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDGQ 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   248 TITVQDQRFRCPELLFKPAFIGKEFPGIHELTFNSIMKCDVDVRKDLYNNIVLSGGTTMFPGIAERLSKEVSALAPSSMK 327
Cdd:cd10224 242 VITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTMK 321
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 113305   328 IKVVAPPERRYSVWIGGSILSSLSTFQTMWITKAEYDESGPSIV 371
Cdd:cd10224 322 IKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIV 365
ASKHA_NBD_actin_Arp-T1-3 cd13397
nucleotide-binding domain (NBD) of actin, actin-related proteins T1-T3 (Arp-T1-3), and similar ...
7-367 0e+00

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: 717.43  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305     7 PAIVIDNGSGMCKAGIAGDDAPRAAFPSIIGRPKMPGIMVGMDQKECYVGEEAQAKRGVLNLKYPIEHGIVTDYDDMEKI 86
Cdd:cd13397   1 PAVVIDNGSGLIKAGFAGEDLPRAVFPSVVGRPKYKAVMLGAGQKEVYVGDEAQEKRGVLTLSYPIEHGIVTNWDDMEKI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    87 WHHCFYNELRVTPEEHPCLLTEAPQNPKLNREKMTKTMFETFNVPSFYVAIQAVLSLYASGRTTGIVVDSGDGVTHTVSI 166
Cdd:cd13397  81 WHHTFENELRVKPEEHPVLLTEAPLNPKQNREKMAEIMFETFGVPAFYVAIQAVLSLYSSGRTTGLVLDSGDGVTHTVPI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   167 YEGYALPHAILRIDLAGRDLTEYCMKLLYEIGLNFSSTAEREIIRDIKEKLCYVALDYESELKayKESSTNDKSYELPDG 246
Cdd:cd13397 161 YEGYALPHAVQRLDLAGRDLTEYLMKLLKERGHSFTTTAEREIVRDIKEKLCYVALDYEEELK--KKSEELEKEYTLPDG 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   247 NTITVQDQRFRCPELLFKPAFIGKEFPGIHELTFNSIMKCDVDVRKDLYNNIVLSGGTTMFPGIAERLSKEVSALAPSSM 326
Cdd:cd13397 239 QVIKIGSERFRCPEALFRPSLIGREAPGIHKLVYNSIMKCDIDIRKDLYSNIVLSGGSTMFPGLPERLQKELEALAPSST 318
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 113305   327 KIKVVAPPERRYSVWIGGSILSSLSTFQTMWITKAEYDESG 367
Cdd:cd13397 319 KVKVIAPPERKYSVWIGGSILASLSTFKSMWITRAEYDEFG 359
PTZ00004 PTZ00004
actin-2; Provisional
1-376 0e+00

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 672.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305      1 MTDSDSPAIVIDNGSGMCKAGIAGDDAPRAAFPSIIGRPKMPGIMVGMDQKECYVGEEAQAKRGVLNLKYPIEHGIVTDY 80
Cdd:PTZ00004   1 MSVEETNAAVVDNGSGMVKAGFAGDDAPRCVFPSIVGRPKNPGIMVGMEEKDCYVGDEAQDKRGILTLKYPIEHGIVTNW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305     81 DDMEKIWHHCFYNELRVTPEEHPCLLTEAPQNPKLNREKMTKTMFETFNVPSFYVAIQAVLSLYASGRTTGIVVDSGDGV 160
Cdd:PTZ00004  81 DDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETHNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    161 THTVSIYEGYALPHAILRIDLAGRDLTEYCMKLLYEIGLNFSSTAEREIIRDIKEKLCYVALDYESELK-AYKESSTNDK 239
Cdd:PTZ00004 161 SHTVPIYEGYSLPHAIHRLDVAGRDLTEYMMKILHERGTTFTTTAEKEIVRDIKEKLCYIALDFDEEMGnSAGSSDKYEE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    240 SYELPDGNTITVQDQRFRCPELLFKPAFIGKEFP-GIHELTFNSIMKCDVDVRKDLYNNIVLSGGTTMFPGIAERLSKEV 318
Cdd:PTZ00004 241 SYELPDGTIITVGSERFRCPEALFQPSLIGKEEPpGIHELTFQSINKCDIDIRKDLYGNIVLSGGTTMYRGLPERLTKEL 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 113305    319 SALAPSSMKIKVVAPPERRYSVWIGGSILSSLSTFQTMWITKAEYDESGPSIVHRKCF 376
Cdd:PTZ00004 321 TTLAPSTMKIKVVAPPERKYSVWIGGSILSSLPTFQQMWVTKEEYDESGPSIVHRKCF 378
PTZ00281 PTZ00281
actin; Provisional
1-376 0e+00

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 643.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305      1 MTDSDSPAIVIDNGSGMCKAGIAGDDAPRAAFPSIIGRPKMPGIMVGMDQKECYVGEEAQAKRGVLNLKYPIEHGIVTDY 80
Cdd:PTZ00281   1 MDGEDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305     81 DDMEKIWHHCFYNELRVTPEEHPCLLTEAPQNPKLNREKMTKTMFETFNVPSFYVAIQAVLSLYASGRTTGIVVDSGDGV 160
Cdd:PTZ00281  81 DDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    161 THTVSIYEGYALPHAILRIDLAGRDLTEYCMKLLYEIGLNFSSTAEREIIRDIKEKLCYVALDYESELKAYKESSTNDKS 240
Cdd:PTZ00281 161 SHTVPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEMQTAASSSALEKS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    241 YELPDGNTITVQDQRFRCPELLFKPAFIGKEFPGIHELTFNSIMKCDVDVRKDLYNNIVLSGGTTMFPGIAERLSKEVSA 320
Cdd:PTZ00281 241 YELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELTA 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 113305    321 LAPSSMKIKVVAPPERRYSVWIGGSILSSLSTFQTMWITKAEYDESGPSIVHRKCF 376
Cdd:PTZ00281 321 LAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIVHRKCF 376
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
7-376 0e+00

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 605.79  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305        7 PAIVIDNGSGMCKAGIAGDDAPRAAFPSIIGRPKMPGIMVGmDQKECYVGEEAQAKRGVLNLKYPIEHGIVTDYDDMEKI 86
Cdd:smart00268   2 PAIVIDNGSGTIKAGFAGEDFPQVVFPSIVGRPKDGKGMVG-DAKDIFVGDEAQEKRGGLELKYPIENGIVENWDDMEKI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305       87 WHHCFYNELRVTPEEHPCLLTEAPQNPKLNREKMTKTMFETFNVPSFYVAIQAVLSLYASGRTTGIVVDSGDGVTHTVSI 166
Cdd:smart00268  81 WDYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVPV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305      167 YEGYALPHAILRIDLAGRDLTEYCMKLLYEIGLNFSSTAEREIIRDIKEKLCYVALDYESELKAYKE---SSTNDKSYEL 243
Cdd:smart00268 161 VDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLAREsseSSKLEKTYEL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305      244 PDGNTITVQDQRFRCPELLFKPAFIGKEFPGIHELTFNSIMKCDVDVRKDLYNNIVLSGGTTMFPGIAERLSKEVSALAP 323
Cdd:smart00268 241 PDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELKQLAP 320
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 113305      324 SSMKIKVVAPPERRYSVWIGGSILSSLSTFQTMWITKAEYDESGPSIVHRKCF 376
Cdd:smart00268 321 KKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERKCF 373
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
9-375 0e+00

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: 591.06  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305     9 IVIDNGSGMCKAGIAGDDAPRAAFPSIIGRPKMPGIMVGMDQKECYVGEEAQAKRGVLNLKYPIEHGIVTDYDDMEKIWH 88
Cdd:cd10216   4 VVIDNGSGVIKAGFAGDDIPKVVFPSYVGRPKHVRVMAGALEGDVFVGPKAEEHRGLLKIRYPMEHGIVTDWNDMERIWQ 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    89 HCFYNE-LRVTPEEHPCLLTEAPQNPKLNREKMTKTMFETFNVPSFYVAIQAVLSLYASGRTTGIVVDSGDGVTHTVSIY 167
Cdd:cd10216  84 YVYSKLqLNTFSEEHPVLLTEAPLNPRKNREKAAEVFFETFNVPALFVSMQAVLSLYASGRTTGVVLDSGDGVTHAVPIY 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   168 EGYALPHAILRIDLAGRDLTEYCMKLLYEIGLNFSSTAEREIIRDIKEKLCYVALDYESELKAYKESSTNDkSYELPDGN 247
Cdd:cd10216 164 EGFALPHSIRRVDIAGRDVTEYLQLLLRKSGYNFHTSAEFEIVREIKEKACYVALNPQKEEKLEEEKTEKA-QYTLPDGS 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   248 TITVQDQRFRCPELLFKPAFIGKEFPGIHELTFNSIMKCDVDVRKDLYNNIVLSGGTTMFPGIAERLSKEVSALAPSSMK 327
Cdd:cd10216 243 TIEIGPERFRAPEILFNPELIGLEYPGVHEVLVDSIQKSDLDLRKTLYSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDVK 322
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 113305   328 IKVVAPPERRYSVWIGGSILSSLSTFQTMWITKAEYDESGPSIVHRKC 375
Cdd:cd10216 323 IRISAPPERLYSTWIGGSILASLSTFKKMWVSKKEYEEDGARILHRKT 370
Actin pfam00022
Actin;
7-376 0e+00

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 518.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305       7 PAIVIDNGSGMCKAGIAGDDAPRAAFPSIIGRPKMPGimvGMDQKECYVGEEAQAKRGVLNLKYPIEHGIVTDYDDMEKI 86
Cdd:pfam00022   2 SALVIDNGSHTTRAGFAGEDAPKAVIPSCVGKPRGTK---VEAANKYYVGDEALTYRPGMEVRSPVEDGIVVDWDAMEEI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305      87 WHHCFYNELRVTPEEHPCLLTEAPQNPKLNREKMTKTMFETFNVPSFYVAIQAVLSLYASGRTTGIVVDSGDGVTHTVSI 166
Cdd:pfam00022  79 WEHVLKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVPV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305     167 YEGYALPHAILRIDLAGRDLTEYCMKLL------------------------------YEIGLNFSSTAEREIIRDIKEK 216
Cdd:pfam00022 159 HDGYVLQKAIRRSDLGGDFLTDYLRELLrsrnieitprylikskkpgdpapavtkrelPDTTYSYKTYQERRVLEEIKES 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305     217 LCYVALDYESelKAYKESSTNDKSYELPDGNTITVQDQRFRCPELLFKPAFIGKE--------FPGIHELTFNSIMKCDV 288
Cdd:pfam00022 239 VCYVSDDPFG--DETTSSSIPTRVYELPDGSTIILGAERFRVPEILFNPSLIGSEselpppqtAVGIPELIVDAINACDV 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305     289 DVRKDLYNNIVLSGGTTMFPGIAERLSKEVSALAPSSMKIKVVAPP---ERRYSVWIGGSILSSLSTFQTMWITKAEYDE 365
Cdd:pfam00022 317 DLRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVKIIAPGntvERRYSAWIGGSILASLGTFQQMWVSKQEYEE 396
                         410
                  ....*....|.
gi 113305     366 SGPSIVHRKCF 376
Cdd:pfam00022 397 HGASVVERKCK 407
PTZ00452 PTZ00452
actin; Provisional
7-376 2.28e-177

actin; Provisional


Pssm-ID: 185631  Cd Length: 375  Bit Score: 497.74  E-value: 2.28e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305      7 PAIVIDNGSGMCKAGIAGDDAPRAAFPSIIGRPKMPGIMVGMDQKECYVGEEAQAKRGVLNLKYPIEHGIVTDYDDMEKI 86
Cdd:PTZ00452   6 PAVVIDNGSGYCKIGIAGDDAPTSCFPAIVGRSKQNDGIFSTFNKEYYVGEEAQAKRGVLAIKEPIQNGIINSWDDIEII 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305     87 WHHCFYNELRVTPEEHPCLLTEAPQNPKLNREKMTKTMFETFNVPSFYVAIQAVLSLYASGRTTGIVVDSGDGVTHTVSI 166
Cdd:PTZ00452  86 WHHAFYNELCMSPEDQPVFMTDAPMNSKFNRERMTQIMFETFNTPCLYISNEAVLSLYTSGKTIGLVVDSGEGVTHCVPV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    167 YEGYALPHAILRIDLAGRDLTEYCMKLLYEIGLNFSSTAEREIIRDIKEKLCYVALDYESELKAYKESSTNDKSYELPDG 246
Cdd:PTZ00452 166 FEGHQIPQAITKINLAGRLCTDYLTQILQELGYSLTEPHQRIIVKNIKERLCYTALDPQDEKRIYKESNSQDSPYKLPDG 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    247 NTITVQDQRFRCPELLFKPAFIGKEFPGIHELTFNSIMKCDVDVRKDLYNNIVLSGGTTMFPGIAERLSKEVSALAPSSM 326
Cdd:PTZ00452 246 NILTIKSQKFRCSEILFQPKLIGLEVAGIHHLAYSSIKKCDLDLRQELCRNIVLSGGTTLFPGIANRLSNELTNLVPSQL 325
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 113305    327 KIKVVAPPERRYSVWIGGSILSSLSTFQTMWITKAEYDESGPSIVHRKCF 376
Cdd:PTZ00452 326 KIQVAAPPDRRFSAWIGGSIQCTLSTQQPQWIKRQEYDEQGPSIVHRKCF 375
ASKHA_NBD_Arp2 cd10220
nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, ...
9-371 7.14e-167

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: 471.28  E-value: 7.14e-167
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305     9 IVIDNGSGMCKAGIAGDDAPRAAFPSIIGRP------KMPGIMVgmdqKECYVGEEAQAKRGVLNLKYPIEHGIVTDYDD 82
Cdd:cd10220   3 VVCDNGTGFVKCGFAGSNFPEHVFPSLVGRPilraeeKVGDIEI----KDIMVGDEASELRSMLEVTYPMENGIVRNWDD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    83 MEKIWHHCFYNELRVTPEEHPCLLTEAPQNPKLNREKMTKTMFETFNVPSFYVAIQAVLSLYASGRTTGIVVDSGDGVTH 162
Cdd:cd10220  79 MEHLWDYTFGEKLKIDPRECKILLTEPPMNPTKNREKMVEVMFEKYGFAGVYVAIQAVLTLYAQGLLTGVVVDSGDGVTH 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   163 TVSIYEGYALPHAILRIDLAGRDLTEYCMKLLYEIGLNFSSTAEREIIRDIKEKLCYVALDYESELKAYKESSTNDKSYE 242
Cdd:cd10220 159 IVPVYEGFSLPHLTRRLDVAGRDITRYLIKLLLLRGYAFNRTADFETVREIKEKLCYVAYDIELEQKLALETTVLVESYT 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   243 LPDGNTITVQDQRFRCPELLFKPAFIGKEFPGIHELTFNSIMKCDVDVRKDLYNNIVLSGGTTMFPGIAERLSKEVSAL- 321
Cdd:cd10220 239 LPDGRVIKVGGERFEAPEALFQPHLIDVEGPGIAELLFNTIQAADIDTRPELYKHIVLSGGSTMYPGLPSRLEKEIKQLy 318
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 113305   322 ----------APSSMKIKVVAPPERRYSVWIGGSILSSLSTFQT-MWITKAEYDESGPSIV 371
Cdd:cd10220 319 lervlkgdteRLSKFKIRIEDPPRRKHMVFLGGAVLADIMKDKDeFWITRQEYEEQGVRVL 379
PTZ00466 PTZ00466
actin-like protein; Provisional
9-376 7.18e-162

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 458.64  E-value: 7.18e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305      9 IVIDNGSGMCKAGIAGDDAPRAAFPSIIGRPKMPGIMVGMDQKECYVGEEAQAKRGVLNLKYPIEHGIVTDYDDMEKIWH 88
Cdd:PTZ00466  15 IIIDNGTGYIKAGFAGEDVPNLVFPSYVGRPKYKRVMAGAVEGNIFVGNKAEEYRGLLKVTYPINHGIIENWNDMENIWI 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305     89 HCfYNELRVTPEEHPCLLTEAPQNPKLNREKMTKTMFETFNVPSFYVAIQAVLSLYASGRTTGIVVDSGDGVTHTVSIYE 168
Cdd:PTZ00466  95 HV-YNSMKINSEEHPVLLTEAPLNPQKNKEKIAEVFFETFNVPALFISIQAILSLYSCGKTNGTVLDCGDGVCHCVSIYE 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    169 GYALPHAILRIDLAGRDLTEYCMKLLYEIGLNFSSTAEREIIRDIKEKLCYVALDYESElKAYKESSTNDKSYELPDGNT 248
Cdd:PTZ00466 174 GYSITNTITRTDVAGRDITTYLGYLLRKNGHLFNTSAEMEVVKNMKENCCYVSFNMNKE-KNSSEKALTTLPYILPDGSQ 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    249 ITVQDQRFRCPELLFKPAFIGKEFPGIHELTFNSIMKCDVDVRKDLYNNIVLSGGTTMFPGIAERLSKEVSALAPSSMKI 328
Cdd:PTZ00466 253 ILIGSERYRAPEVLFNPSILGLEYLGLSELIVTSITRADMDLRRTLYSHIVLSGGTTMFHGFGDRLLNEIRKFAPKDITI 332
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 113305    329 KVVAPPERRYSVWIGGSILSSLSTFQTMWITKAEYDESGPSIVHRKCF 376
Cdd:PTZ00466 333 RISAPPERKFSTFIGGSILASLATFKKIWISKQEFDEYGSVILHRKTF 380
ASKHA_NBD_ACTL7 cd10214
nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ...
8-375 5.84e-155

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: 440.71  E-value: 5.84e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305     8 AIVIDNGSGMCKAGIAGDDAPRAAFPSIIGRPKMPGIMVGMDQKECYVGEEAQAKRGVLNLKYPIEHGIVTDYDDMEKIW 87
Cdd:cd10214   5 AVIIDLGTGYCKAGFAGQPRPSYVISSTVGKPPQESAKTGDNRKETFVGKELANVEPPLKLVNPLRHGIVVDWDCVQDIW 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    88 HHCFYNELRVTPEEHPCLLTEAPQNPKLNREKMTKTMFETFNVPSFYVAIQAVLSLYASGRTTGIVVDSGDGVTHTVSIY 167
Cdd:cd10214  85 EYIFEKEMKILPEEHAVLVSDPPLSPTTNREKYAELMFETFSIPAMHIAYQSRLSLYSYGRTSGLVVESGHGVSYVVPIH 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   168 EGYALPHAILRIDLAGRDLTEYCMKLLYEIGLNFSSTaEREIIRDIKEKLCYVALDYESELKAYKESSTNDksYELPDGN 247
Cdd:cd10214 165 EGYNLPHITGRADYAGSDLTAYLMKLLNEAGNKFTDD-QLHIVEDIKKKCCYVALDFEEEMGLPPQEYTVD--YELPDGH 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   248 TITVQDQRFRCPELLFKPAFIGKEFPGIHELTFNSIMKCDVDVRKDLYNNIVLSGGTTMFPGIAERLSKEVSALAPSSMK 327
Cdd:cd10214 242 LITIGKERFRCPEMLFNPSLIGSKQPGLHTLTMNSLNKCDANLKKDLAKNILLCGGSTMFDGFPDRFQKELSKLCPNDNP 321
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 113305   328 IkVVAPPERRYSVWIGGSILSSLSTFQTMWITKAEYDESGPSIVHRKC 375
Cdd:cd10214 322 I-VAASPERKYSVWTGGSILASLKSFQQLWVRRREYEERGPFVIYRKC 368
ASKHA_NBD_actin-like cd10169
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ...
9-367 4.48e-154

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: 433.84  E-value: 4.48e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305     9 IVIDNGSGMCKAGIAGDDAPRAAFPsiigrpkmpgimvgmdqkecyvgeeaqakrgvlnlkypiehgivtdYDDMEKIWH 88
Cdd:cd10169   1 IVIDNGSGTIKAGFAGEDAPRLIFP----------------------------------------------WDDMEKIWE 34
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    89 HCFYNELRVTPEEHPCLLTEAPQNPKLNREKMTKTMFETFNVPSFYVAIQAVLSLYASGRTTGIVVDSGDGVTHTVSIYE 168
Cdd:cd10169  35 HVFYNLLRVDPEEHPVLLTEPPLNPKANREKLAEILFETFNVPSLYIANQAVLSLYASGRTTGLVVDSGEGVTHIVPVYE 114
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   169 GYALPHAILRIDLAGRDLTEYCMKLLYEIGLNFSSTAEREIIRDIKEKLCyvaldyeselkaykesstndksyelpdgnt 248
Cdd:cd10169 115 GYVLPHAVRRLDIGGRDLTDYLAKLLREKGYSFSTSAEREIVRDIKEKLC------------------------------ 164
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   249 itvqdqrfrcpellfkpafigkefpGIHELTFNSIMKCDVDVRKDLYNNIVLSGGTTMFPGIAERLSKEVSALAPSSMKI 328
Cdd:cd10169 165 -------------------------GLHELIYDSIMKCDIDLRKELYSNIVLSGGTTLFPGFAERLQKELSKLAPSSVKV 219
                       330       340       350
                ....*....|....*....|....*....|....*....
gi 113305   329 KVVAPPERRYSVWIGGSILSSLSTFQTMWITKAEYDESG 367
Cdd:cd10169 220 KVIAPPERKYSAWIGGSILASLSTFQQMWITKEEYEEHG 258
ASKHA_NBD_Arp4_ACTL6-like cd13395
nucleotide-binding domain (NBD) of the actin-related protein 4 (Arp4)-like subfamily; The ...
7-367 6.92e-149

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: 426.98  E-value: 6.92e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305     7 PAIVIDNGSGMCKAGIAGDDAPRAAFPSIIG-RPKMPGIMVGMD-----QKECYVGEEA-QAKRGVLNLKYPIEHGIVTD 79
Cdd:cd13395   5 GALVLDIGSYSTRAGYAGEDTPKAVFPSVVGvVTDDDDAEDYVGgsgekKRKYYIGTNSiGVPRPNMEVISPLKDGLIED 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    80 YDDMEKIWHHCFYNELRVTPEEHPCLLTEAPQNPKLNREKMTKTMFETFNVPSFYVAIQAVLSLYASGRTTGIVVDSGDG 159
Cdd:cd13395  85 WDAFEKLWDHALKNRLRVDPSEHPLLLTEPSWNTRANREKLTELMFEKYNVPAFFLAKNAVLSAFANGRSTALVVDSGAT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   160 VTHTVSIYEGYALPHAILRIDLAGRDLTEYCMKLL----------YEI---------------GLNFSST-------AER 207
Cdd:cd13395 165 STSVVPVHDGYVLQKAIVRSPLGGDFLTDQLLKLLesknieiiprYMIkskepveggapakytKKDLPNTtssyhryMVR 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   208 EIIRDIKEKLCYVAldyESELKAYKESSTNDKSYELPDGNTITVQDQRFRCPELLFKPAFI---------GKEFPGIHEL 278
Cdd:cd13395 245 RVLQDFKESVCQVS---DSPFDESEAASIPTVSYELPDGYNIEFGAERFKIPELLFDPSLVkgipappseGNELLGLPQL 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   279 TFNSIMKCDVDVRKDLYNNIVLSGGTTMFPGIAERLSKEVSALAPSSMKIKVVAPP---ERRYSVWIGGSILSSLSTFQT 355
Cdd:cd13395 322 VYTSIGSCDVDIRPELYGNVVLTGGNSLLPGFTDRLNRELSEKAPGSLKLKILASGntvERRFSSWIGGSILASLGSFQQ 401
                       410
                ....*....|..
gi 113305   356 MWITKAEYDESG 367
Cdd:cd13395 402 MWISKQEYEEHG 413
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
4-373 5.87e-123

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 360.97  E-value: 5.87e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305      4 SDSPAIVIDNGSGMCKAGIAGDDAPRAAFPSIIG-RPKMPGIMV--GMDQKECYVGEEAQAKRGVLNLKYPIEHGIVTDY 80
Cdd:PTZ00280   2 STLPVVVIDNGTGYTKMGYAGNTEPTYIIPTLIAdNSKQSRRRSkkGFEDLDFYIGDEALAASKSYTLTYPMKHGIVEDW 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305     81 DDMEKIWHHCFYNELRVTPEEHPCLLTEAPQNPKLNREKMTKTMFETFNVPSFYVAIQAVLSLYAS----------GRTT 150
Cdd:PTZ00280  82 DLMEKFWEQCIFKYLRCEPEEHYFILTEPPMNPPENREYTAEIMFETFNVKGLYIAVQAVLALRASwtskkakelgGTLT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    151 GIVVDSGDGVTHTVSIYEGYALPHAILRIDLAGRDLTEYCMKLLYEIGLNFSSTAEREIIRDIKEKLCYVALD------- 223
Cdd:PTZ00280 162 GTVIDSGDGVTHVIPVVDGYVIGSSIKHIPLAGRDITNFIQQMLRERGEPIPAEDILLLAQRIKEKYCYVAPDiakefek 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    224 YESEL-----KAYKESSTNDKSYelpdgnTITVQDQRFRCPELLFKPAFIGKEF-PGIHELTFNSIMKCDVDVRKDLYNN 297
Cdd:PTZ00280 242 YDSDPknhfkKYTAVNSVTKKPY------TVDVGYERFLGPEMFFHPEIFSSEWtTPLPEVVDDAIQSCPIDCRRPLYKN 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    298 IVLSGGTTMFPGIAERLSKEV----------------SALAPSSMKIKVVAPPERRYSVWIGGSILSSLSTFQTMWITKA 361
Cdd:PTZ00280 316 IVLSGGSTMFKGFDKRLQRDVrkrvdrrlkkaeelsgGKLKPIPIDVNVVSHPRQRYAVWYGGSMLASSPEFEKVCHTKA 395
                        410
                 ....*....|..
gi 113305    362 EYDESGPSIVHR 373
Cdd:PTZ00280 396 EYDEYGPSICRY 407
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
8-371 7.86e-122

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: 357.65  E-value: 7.86e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305     8 AIVIDNGSGMCKAGIAGDDAPRAAFPSIIG-------RPKMPGIMVGMDQKECYVGEEAQAKRGVLNLKYPIEHGIVTDY 80
Cdd:cd10221   1 AVVIDNGTGYTKMGYAGNTEPQFIIPTVIAikesakvGDGQRRSKKGIEDLDFYIGDEALANSPTYALKYPIRHGIVEDW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    81 DDMEKIWHHCFYNELRVTPEEHPCLLTEAPQNPKLNREKMTKTMFETFNVPSFYVAIQAVLSLYASGRT--------TGI 152
Cdd:cd10221  81 DLMERFWEQCIFKYLRCEPEDHYFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQAVLALAASWTSrkvgertlTGT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   153 VVDSGDGVTHTVSIYEGYALPHAILRIDLAGRDLTEYCMKLLYEIGLNFSSTAEREIIRDIKEKLCYVALDYESELKAY- 231
Cdd:cd10221 161 VIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREEGIPPEDSLEVAKRIKERYCYVCPDIVKEFAKYd 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   232 KESSTNDKSYELPDGNT-----ITVQDQRFRCPELLFKPAFIGKEF-PGIHELTFNSIMKCDVDVRKDLYNNIVLSGGTT 305
Cdd:cd10221 241 SDPAKYIKQYTGINSVTgkpytVDVGYERFLAPEIFFNPEIASSDFtTPLPEVVDQVIQSCPIDTRRGLYKNIVLSGGST 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   306 MFPGIAERLSKEV----------------SALAPSSMKIKVVAPPERRYSVWIGGSILSSLSTFQTMWITKAEYDESGPS 369
Cdd:cd10221 321 MFKDFGRRLQRDVkrivdarlkaseelsgGKLKPKPIDVNVISHPMQRYAVWFGGSMLASTPEFYTVCHTKAEYEEYGPS 400

                ..
gi 113305   370 IV 371
Cdd:cd10221 401 IC 402
COG5277 COG5277
Actin-related protein [Cytoskeleton];
6-366 8.53e-112

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 332.91  E-value: 8.53e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305     6 SPAIVIDNGSGMCKAG-IAGDDAP-----RAAFPSIIGRPKMPGIMVGMDqKECYVGEEAQ-----AKRGVLNLKYPIEH 74
Cdd:COG5277   8 KYVIGIDFGTSYVKYGpIALEEKPrviqtRGLFLRIVGESKLLGPMEGLS-RGLVVGDEVSkylssVRDAIRNLKYPLRD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    75 GIVT-----DYDDMEKIWHHCFYNELRVTPEEHPCL--LTEAPQNPKLNREKMTKTMFETF---NVPSFYVAIQAVLSLY 144
Cdd:COG5277  87 GIVRrddedAWRVLKELLRYTFAQFLVVDPEFHGFLvvVALSALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPLAVAI 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   145 ASGRTTGIVVDSGDGVTHTVSIYEGyALPHAILRIDLAGRDLTEYCMKLLYEIGLNFSSTAEReIIRDIKEKLCYVALDY 224
Cdd:COG5277 167 AEKAVTCVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSDTAREEY-VVRVVKEALGLVPRDL 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   225 ESEL-KAYKESSTNDKSYELPDGNT-ITVQD---QRFRCPELLFKPAFIGKE----------------------FPGIHE 277
Cdd:COG5277 245 AKAIqKAASNPDSFEAKVRLPNPTVeIELGNyawERFLIGEILFNPNHEGFEsyiqqgrlriedavigdvvlygEMGLAE 324
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   278 LTFNSIMKCDVDVRKDLYNNIVLSGGTTMF---PGIAE-------RLSKEVSALAPsSMKIKVVAPPERRYSVWIGGSIL 347
Cdd:COG5277 325 AIINSIMKCDVEIQDELYSNIILSGGAFNWsvpPGLEDvavdsvtRVQIELSELAP-ELKVNVRLVSDPQYSVWKGAIIY 403
                       410       420
                ....*....|....*....|.
gi 113305   348 SSLSTFQTMW--ITKAEYDES 366
Cdd:COG5277 404 GYALPFSVKWswITKEGWYFL 424
ASKHA_NBD_Arp6 cd10210
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ...
9-367 2.12e-86

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: 266.72  E-value: 2.12e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305     9 IVIDNGSGMCKAGIAGDDAPRAaFPSIIGRPKmpgimvgmDQKECYVGEEAQAK---RGVLNLKYPIEHGIVTDYDDMEK 85
Cdd:cd10210   2 LVLDNGAYTIKAGFASDDPPRV-IPNCIAKPK--------SERRRLFGDDQLDEckdLSGLFYRRPFERGYLVNWDLQRQ 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    86 IWHHCFYNE-LRVTPEEHPCLLTEAPQNPKLNREKMTKTMFETFNVPSFYVAIQAVLSLYA----------SGRTTGIVV 154
Cdd:cd10210  73 IWDHLFGKLlLNVDPSDTALVLTEPPFNPPSIQEAMDEIVFEEYGFQSLYRTTAAALSAFAyladseqsssSSSQCCLVV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   155 DSGDGVTHTVSIYEGYALPHAILRIDLAGRDLTEYcmklLYEI----GLNFSStaEREIIRDIKEKLCYVALDYESELKA 230
Cdd:cd10210 153 DSGFSFTHIVPFFDGKPVKRAVRRIDVGGKLLTNY----LKEIisyrQLNVMD--ETYLVNQIKEDLCFVSTDFYEDLEI 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   231 YK---ESSTNDKSYELPDGNTI----------------TVQDQ-------RFRCPELLFKPAFIGKEFPGIHELTFNSIM 284
Cdd:cd10210 227 AKkkgKENTIRRDYVLPDYTTSkrgyvrdpeepnrgklKEDEQvlrlnneRFTVPELLFHPSDIGIQQAGIAEAIVQSIN 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   285 KCDVDVRKDLYNNIVLSGGTTMFPGIAERLSKEVSALAPSSMKIKVVAPPERRYSVWIGGSILSSLSTFQTMWITKAEYD 364
Cdd:cd10210 307 ACPEELQPLLYANIVLTGGNALFPGFRERLEAELRSLAPDDYDVNVTLPEDPITYAWEGGSLLAQSPEFEELAVTRAEYE 386

                ...
gi 113305   365 ESG 367
Cdd:cd10210 387 EHG 389
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
9-372 5.03e-83

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: 256.93  E-value: 5.03e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305     9 IVIDNGSGMCKAGIAGDDApraaFPSIIgrpkMPGIMVGMDQkecyvGEEAQAKRGVLNLKYPIEHGIVTDYDDMEKIWH 88
Cdd:cd10209   1 VVIDAGSRLLKAGYAYPDR----EPSVV----EPTRVTPAVE-----DGEESDTVVEGNTVSPIRRGRIEDWDALEALLR 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    89 HCFYNELR-VTPEEHPCLLTEAPQNPKLNREKMTKTMFETFNVPSFYVAIQAVLSLYASGRTTGIVVDSGDGVTHTVSIY 167
Cdd:cd10209  68 YVFYTGLGwEEGNEGQVLIAEPLLTSKAERERLTQLMFETFNVSGLYASEQAVLSLYAVGRISGCVVDVGHGKIDIAPVW 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   168 EGYALPHAILRIDLAGRDLTEYCMKLLYEigLNFSSTAEREIIRDIKEKLCYVAldyESELKAYKESST-NDKSYELPDG 246
Cdd:cd10209 148 EGAIQHNAVRRFEIGGRDLTELLAAELGK--SNPKVKLDRSIVERLKEAVAWSA---DDEEAYEKKVLTcSPETYTLPDG 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   247 NTITVQDQRFRCPELLFKPAFIGKEFPGIHELTFNSIMKCDVDVRKDLYNNIVLSGGTTMFPGIAERLSKEVSALAPSSM 326
Cdd:cd10209 223 RVISVGKERYCVGEALFRPSILGIEEYGIVEQLVRAVSTSPSENRRQLLENIVLCGGTSSVPGLEARLQKEIRLLSSPSS 302
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 113305   327 KIKVVAPPE------RRYSVWIGGSILSSLSTFQTMWITKAEYDESGPSIVH 372
Cdd:cd10209 303 RPALVKPPEympentLRYSAWIGGAILAKVVFPQNQHVTKADYDETGPSVVH 354
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
8-368 1.54e-68

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: 219.37  E-value: 1.54e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305     8 AIVIDNGSGMCKAGIAGDDAPRAAFPSIIGRPK-----MPGIMVGMDqkecyVGEEAQAKrgvLNLKYPIEHGIVTDYDD 82
Cdd:cd10211   1 PIVIDNGSYQCRAGWAGDKEPRLVFRNLVAKPRdrkkgITVTLVGND-----ILNDEAVR---SHLRSPFDRNVVTNFDL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    83 MEKIWHHCFY-----NELRVtpeEHPCLLTEAPQNPKLNREKMTKTMFETFNVPSFYVAIQAVLSLYASGRT----TGIV 153
Cdd:cd10211  73 QEQILDYIFShlginSEGSV---DHPIVLTEALCNPNYSRQLMSELLFECYGVPSVAYGIDSLFSYYHNQPQgdpsDGLV 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   154 VDSGDGVTHTVSIYEGYALPHAILRIDLAGRDLTEYCMKLL-----YEIGLNFSSTAEreiirDIKEKLCYVALDYESEL 228
Cdd:cd10211 150 ISSGYSTTHVIPVLNGRLDLSQCKRINLGGFHATDYLQRLLqlkypTHPSAITLSRAE-----ELVHEHCYVAEDYDEEL 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   229 KAYKesstNDKSYElpdGNTITVQdqrfrcpellfkpafigkeFP-GIHELTFNSIMKCDVDVRKDLYNNIVLSGGTTMF 307
Cdd:cd10211 225 KKWE----DPEYYE---ENVRKIQ-------------------LPfGLVETIEFVLKRYPAEQQDRLVQNVFLTGGNALF 278
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 113305   308 PGIAERLSKEVSALAPSSMKIKVVAPPERRYSVWIGGSILSSLSTFQTMWITKAEYDESGP 368
Cdd:cd10211 279 PGLKERLEKELRAIRPFGSPFNVVRAKDPVLDAWRGAAKWALDSTFEKVWITKQEYEEKGG 339
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
70-374 1.99e-54

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: 182.89  E-value: 1.99e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    70 YPIEHGIVTDYDDMEKIWHHCFYNEL--RVTPEEHPCLLTEAPQNPKLNREKMTKTMFETFNVPSFYVAIQAVLSLYASG 147
Cdd:cd10208  37 WPIQDGRVVDWDALEALWRHILFSLLsiPRPTNNSPVLLSVPPSWSKSDLELLTQLFFERLNVPAFAILEAPLAALYAAG 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   148 RTTGIVVDSGDGVTHTVSIYEGYALPHAILRIDLAGRDLTEYCMKLL--YEIGLNFSSTAEREIIRDIKEKL-----CYV 220
Cdd:cd10208 117 ATSGIVVDIGHEKTDITPIVDSQVVPHALVSIPIGGQDCTAHLAQLLksDEPELKSQAESGEEATLDLAEALkkspiCEV 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   221 ALDyeselkaykesstndkSYELPDGNTITVQDQRFRCPELLFKPAFIGKEfpGIHELTFNSIMK---CDVDVRKDLYNN 297
Cdd:cd10208 197 LSD----------------GADLASGTEITVGKERFRACEPLFKPSSLRVD--LLIAAIAGALVLnasDEPDKRPALWEN 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   298 IVLSGGTTMFPGIAERLSKEVSA-LAPSSMKIKVVAPPERR-----------------YSVWIGGSILSSLsTF----QT 355
Cdd:cd10208 259 IIIVGGGSRIRGLKEALLSELQQfHLISETSASPQQPRIIRlakipdyfpewkksgyeEAAFLGASIVAKL-VFndpsSK 337
                       330
                ....*....|....*....
gi 113305   356 MWITKAEYDESGPSIVHRK 374
Cdd:cd10208 338 HYISKVDYNEKGPAAIHTK 356
ASKHA_NBD_Arp10 cd10207
nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins; ...
9-367 1.53e-47

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: 165.50  E-value: 1.53e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305     9 IVIDNGSGMCKAGIAGDDAPRAAFPSIIGRPKMPGIMVGMDQKecYVGEEaqakrgvlnlkypiehgivtDYDDM-EKIW 87
Cdd:cd10207   1 VVLDIGSAYTKCGFAGESAPRCIIPSEVKLPGGKKVIRVVDQR--SGNEE--------------------ELYEAlKEFL 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    88 HHCFYNELRVTPEEHPCLLTEAPQNPKLNREKMTKTMFETFNVPSFYVAIQAVLSLYASGRTTGIVVDSGDGVTHTVSIY 167
Cdd:cd10207  59 HELYFKHLLVNPKDRRVVVVESVLCPTPFRETLAKVLFKHFEVPSVLFAPSHLLSLLTLGIRTALVVDCGYRETRVLPVY 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   168 EGYALPHAILRIDLAGRDLTEYCMKLLYEIGLNFSSTAER------------EIIRDIKEKLCYVA-LDYESELKAYKES 234
Cdd:cd10207 139 EGVPLLSAWQSTPLGGKALHKRLKKLLLEHATVVTGDNKGqllssvdsllseEVLEDIKVRACFVTsLERGKTLQSATEE 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   235 ST-------NDKSYELPDGNTITVQ-DQRFRCPELLFKPAfigKEFPGIHELTFNSIMKCDVDVRKDLYNNIVLSGGTTM 306
Cdd:cd10207 219 GSteepsppPPVDYPLDGEKILIVPgSIRESAEELLFEGD---NEEKSLPTLILDSLLKCPIDVRKQLAENIVVIGGTSM 295
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113305   307 FPGIAERLSKEV----------SALAPSSMKIKVVAPP-ERRYSVWIGGSILSSLSTFQTMWITKAEYDESG 367
Cdd:cd10207 296 LPGFKHRLLEELrallrkpkyfEELAPKTFRFHTPPSVfKPNYLAWLGGSIFGALESILGRSLSREAYLQTG 367
ASKHA_NBD_AtArp8-like cd13396
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and ...
92-367 1.20e-44

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: 156.94  E-value: 1.20e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    92 YNELRVTPEEHPCLLTEA------PQNPKLNREKMTKTMFETF---NVPSFYVAIQAVLSLYASGRTTGIVVDSGDGVTH 162
Cdd:cd13396  49 MTRMQVKPSRQPVVVSLPlchsddTESAAASRRQLRGTIFNVLfdmNVPAVCAVDQAVLALYAANRTSGIVVNIGFRVTT 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   163 TVSIYEGYALPH-AILRIDLAGRDLTEYCMKLLYEIGLNFSSTAereIIRDIKEKLCYVALDYESELKayKESStndKSY 241
Cdd:cd13396 129 IVPVYRGRVMHDiGVEVVGQGALRLTGFLKELMQQNGIRFPSLY---TVRTIKEKLCYVAEDYEAELA--KDTQ---ASC 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   242 ELPDGNTITVQDQRFRCPELLFKPAFIGKEFPGIHELTFNSIMKCDVDVR---KDLYNNIVLSGGTTMFPGIAERLSKEV 318
Cdd:cd13396 201 EVAGEGWFTLSNERFKTGEILFQPGLGGMRAMGLHQAVALCMDHCALVHSqgdDGWFKTIVLSGGSACLPGLSERLEREL 280
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 113305   319 SALAPSSMK--IKVVAPPERRYSVWIGGSILSSLSTFQTMW-ITKAEYDESG 367
Cdd:cd13396 281 RKLLPKSLSegIRIIPPPLGPDSAWQGAKLISNLSNFPDGWcITKKQFRNKP 332
ASKHA_NBD_Arp8-like cd10206
nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The ...
49-370 4.22e-34

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: 130.82  E-value: 4.22e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    49 DQKECYVGEEAQ--AKRGVLNLKYPIEHG---IVTDY-------DDMEKIWHHCFYNELRVTPEEHP---CLLTEapqnP 113
Cdd:cd10206 118 DYPDFLVGEEALrlPPSEEYNLHWPIRRGrlnVHSDGgsltavlDDLEDIWSHALEEKLEIPRKDLKnyrAVLVI----P 193
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   114 KL-NR---EKMTKTMFETFNVPSFYVAIQAVLSLYASGRTTGIVVDSGDGVTHTVSIYEGYALPHAILRIDLAGRDLTEY 189
Cdd:cd10206 194 DLfDRrhvKELVDLLLRRLGFSSVFVHQESVCATFGAGLSSACVVDIGAQKTSVACVEDGLSIPNSRIRLPYGGDDITRC 273
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   190 CMKLLYEIG-----LNFSSTAEREIIRDIKEKLCYVALDyeselkaykESSTNDKSYELPDGNTITVqdqRFRcpellFK 264
Cdd:cd10206 274 FLWLLRRSGfpyreCNLNSPLDFLLLERLKETYCTLDQD---------DIGVQLHEFYVREPGQPTL---KYQ-----FK 336
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   265 pafigkeFPGIHELTFNSIMKC-DVDVRKDLYNNIVLSGGTTMFPGIAE----RLSKEVSALAPSSMKIKVVAPPE---R 336
Cdd:cd10206 337 -------LLPLDEAIVQSILSCaSDELKRKMYSSILLVGGGAKIPGLAEaledRLLIKIPSLFEAVETVEVLPPPKdmdP 409
                       330       340       350
                ....*....|....*....|....*....|....
gi 113305   337 RYSVWIGGSILSSLSTFQTMWITKAEYDESGPSI 370
Cdd:cd10206 410 SLLAWKGGAVLACLDSAQELWITRKEWQRLGVRA 443
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
304-375 1.02e-29

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: 111.22  E-value: 1.02e-29
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113305    304 TTMFPGIAERLSKEVSALAPSSMKIKVVAPPERRYSVWIGGSILSSLSTFQTMWITKAEYDESGPSIVHRKC 375
Cdd:NF040575  61 RVNESGFYEKLKKSITEKAPKGALIGMTLDPKPESAAWRGAAMYAASEGFVEMAITKQEYDESGPSIVHRKC 132
ASKHA_NBD_ScArp7-like cd10212
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and ...
9-364 6.49e-18

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: 84.77  E-value: 6.49e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305     9 IVIDNGSGMCKAGIAGDDAPRAAFPS-IIGRPKMPGIMVGMDQKECYVGEEAQAKRGVLNLKYPIEHGIVTDYDDMEKIW 87
Cdd:cd10212   6 VVIHNGSHRTVAGFSNVELPQCIIPSsYIKRTDEGGEAEFIFGTYNMIDAAAEKRNGDEVYTLVDSQGLPYNWDALEMQW 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    88 HHCFYNELRVTPEEHPCLLTEAPQNPKLNR---EKMTKTMFETFNVPSFYVAIQAVLSLYASGRTTGIVVDSGDGVTHTV 164
Cdd:cd10212  86 RYLYDTQLKVSPEELPLVITMPATNGKPDMailERYYELAFDKLNVPVFQIVIEPLAIALSMGKSSAFVIDIGASGCNVT 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   165 SIYEGYALPHAILRIDLAG------------------------RDLTEYCMKLLYEIGL---NFSST----AER---EII 210
Cdd:cd10212 166 PIIDGIVVKNAVVRSKFGGdfldfqvherlaplikeendmenmADEQKRSTDVWYEASTwiqQFKSTmlqvSEKdlfELE 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   211 RDIKEKLCYVA--------LDYESELKAYKESSTN----DKSYEL-PDGNTITVQ-DQRFRCPELLFKPAFIGKEFP--- 273
Cdd:cd10212 246 RYYKEQADIYAkqqeqlkqMDQQLQYTALTGSPNNplvqKKNFLFkPLNKTLTLDlKECYQFAEYLFKPQLISDKFSped 325
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   274 GIHELTFNSIMKCDVDVRKDLYNNIVLSGGTTMFPGIAERLSKEVSALAPsSMKIKVVAPP---ERRYSVWIGGSILSSL 350
Cdd:cd10212 326 GLGPLMAKSVKKAPEQVYSLLLTNVIITGSTSLIEGMEQRIIKELSIRFP-QYKLTTFANQvmmDRKIQGWLGALTMANL 404
                       410
                ....*....|....*
gi 113305   351 STFQT-MWITKAEYD 364
Cdd:cd10212 405 PSWSLgKWYSKEDYE 419
ASKHA_NBD_MamK cd24009
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ...
16-335 1.84e-12

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: 67.62  E-value: 1.84e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    16 GMCKAGIAGDDAPRAAFPSIIGRPK-MPGIMVGmdQKECYVGEEAQAKRGVLNLKYPIEHGIVTDYD--DMEKIWHHC-- 90
Cdd:cd24009   9 GTSRSAVVTSRGKRFSFRSVVGYPKdIIARKLL--GKEVLFGDEALENRLALDLRRPLEDGVIKEGDdrDLEAARELLqh 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305    91 FYNELRVTPEEHPCLLTEAP-----QNPKLNREkMTKTMFETFNVPS--FYVAiqavlslYASGRTTG-IVVDSGDGVTH 162
Cdd:cd24009  87 LIELALPGPDDEIYAVIGVParasaENKQALLE-IARELVDGVMVVSepFAVA-------YGLDRLDNsLIVDIGAGTTD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   163 TVSIYEGYALPHAILRIDLAGRDLTEYCMKLLYEI--GLNFSstaeREIIRDIKEKLCYVaLDYESELKAykESSTNDKS 240
Cdd:cd24009 159 LCRMKGTIPTEEDQITLPKAGDYIDEELVDLIKERypEVQLT----LNMARRWKEKYGFV-GDASEPVKV--ELPVDGKP 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113305   241 YELpdgnTITvQDQRFRCPELLfkPAFIgkefPGIHELtfnsIMKCDVDVRKDLYNNIVLSGGTTMFPGIAERLSKEVSA 320
Cdd:cd24009 232 VTY----DIT-EELRIACESLV--PDIV----EGIKKL----IASFDPEFQEELRNNIVLAGGGSRIRGLDTYIEKALKE 296
                       330
                ....*....|....*
gi 113305   321 LAPSsmKIKVVAPPE 335
Cdd:cd24009 297 YGGG--KVTCVDDPV 309
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH