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Conserved domains on  [gi|1906288369|ref|WP_189059937|]
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actin, partial [Deinococcus daejeonensis]

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

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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 ...
6-370 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: 932.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369   6 QALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 85
Cdd:cd10224     1 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  86 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 165
Cdd:cd10224    81 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 166 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYAFTTTAEREIVRDIKEKLCYIALDFEEEMQTAASSSSLEKSYELPDG 245
Cdd:cd10224   161 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 246 QVITIGNERFRCPEALFQPSFLGMEAAGVHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMYPGIADRMQKELTALAPSTM 325
Cdd:cd10224   241 QVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTM 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1906288369 326 KIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIV 370
Cdd:cd10224   321 KIKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIV 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 ...
6-370 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: 932.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369   6 QALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 85
Cdd:cd10224     1 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  86 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 165
Cdd:cd10224    81 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 166 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYAFTTTAEREIVRDIKEKLCYIALDFEEEMQTAASSSSLEKSYELPDG 245
Cdd:cd10224   161 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 246 QVITIGNERFRCPEALFQPSFLGMEAAGVHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMYPGIADRMQKELTALAPSTM 325
Cdd:cd10224   241 QVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTM 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1906288369 326 KIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIV 370
Cdd:cd10224   321 KIKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIV 365
PTZ00281 PTZ00281
actin; Provisional
1-370 0e+00

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 760.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369   1 MEDEVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWD 80
Cdd:PTZ00281    2 DGEDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  81 DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVS 160
Cdd:PTZ00281   82 DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 161 HTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYAFTTTAEREIVRDIKEKLCYIALDFEEEMQTAASSSSLEKSY 240
Cdd:PTZ00281  162 HTVPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEMQTAASSSALEKSY 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 241 ELPDGQVITIGNERFRCPEALFQPSFLGMEAAGVHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMYPGIADRMQKELTAL 320
Cdd:PTZ00281  242 ELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELTAL 321
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1906288369 321 APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIV 370
Cdd:PTZ00281  322 APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIV 371
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
5-370 0e+00

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 647.01  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369    5 VQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGmGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEK 84
Cdd:smart00268   1 VPAIVIDNGSGTIKAGFAGEDFPQVVFPSIVGRPKDGKGMVG-DAKDIFVGDEAQEKRGGLELKYPIENGIVENWDDMEK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369   85 IWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVP 164
Cdd:smart00268  80 IWDYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  165 IYEGYALPHAILRLDLAGRDLTDYLMKILTERGYAFTTTAEREIVRDIKEKLCYIALDFEEEMQTAAS---SSSLEKSYE 241
Cdd:smart00268 160 VVDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLAREsseSSKLEKTYE 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  242 LPDGQVITIGNERFRCPEALFQPSFLGMEAAGVHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMYPGIADRMQKELTALA 321
Cdd:smart00268 240 LPDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELKQLA 319
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1906288369  322 PSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIV 370
Cdd:smart00268 320 PKKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIV 368
Actin pfam00022
Actin;
5-370 0e+00

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 565.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369   5 VQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGmgqKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEK 84
Cdd:pfam00022   1 VSALVIDNGSHTTRAGFAGEDAPKAVIPSCVGKPRGTKVEAA---NKYYVGDEALTYRPGMEVRSPVEDGIVVDWDAMEE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  85 IWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVP 164
Cdd:pfam00022  78 IWEHVLKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 165 IYEGYALPHAILRLDLAGRDLTDYLMKILTER------------------------------GYAFTTTAEREIVRDIKE 214
Cdd:pfam00022 158 VHDGYVLQKAIRRSDLGGDFLTDYLRELLRSRnieitprylikskkpgdpapavtkrelpdtTYSYKTYQERRVLEEIKE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 215 KLCYIALDFeeEMQTAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGME--------AAGVHETTYNSIMKCD 286
Cdd:pfam00022 238 SVCYVSDDP--FGDETTSSSIPTRVYELPDGSTIILGAERFRVPEILFNPSLIGSEselpppqtAVGIPELIVDAINACD 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 287 VDIRKDLYGNVVLSGGTTMYPGIADRMQKELTALAPSTMKIKIIAPP---ERKYSVWIGGSILASLSTFQQMWISKEEYD 363
Cdd:pfam00022 316 VDLRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVKIIAPGntvERRYSAWIGGSILASLGTFQQMWVSKQEYE 395

                  ....*..
gi 1906288369 364 ESGPSIV 370
Cdd:pfam00022 396 EHGASVV 402
COG5277 COG5277
Actin-related protein [Cytoskeleton];
1-365 2.78e-140

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 405.33  E-value: 2.78e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369   1 MEDEVQA---LVIDNGSGMCKAG-FAGDDAP-----RAVFPSIVGRPRHTGVMVGMGqKDSYVGDEAQS-----KRGILT 66
Cdd:COG5277     1 MSDAYKLkyvIGIDFGTSYVKYGpIALEEKPrviqtRGLFLRIVGESKLLGPMEGLS-RGLVVGDEVSKylssvRDAIRN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  67 LKYPIEHGIVT-----NWDDMEKIWHHTFYNELRVAPEEHP--VLLTEAPLNPKANREKMTQIMFETF---NTPAMYVAI 136
Cdd:COG5277    80 LKYPLRDGIVRrddedAWRVLKELLRYTFAQFLVVDPEFHGflVVVALSALAPDYMRERLFDIHFEVFseeGAPAVTIIP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 137 QAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGyALPHAILRLDLAGRDLTDYLMKILTERGYAFTTTAEReIVRDIKEKL 216
Cdd:COG5277   160 QPLAVAIAEKAVTCVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSDTAREEY-VVRVVKEAL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 217 CYIALDFEEEMQTAASS-SSLEKSYELPDGQV-ITIGN---ERFRCPEALFQPSFLGMEA-------------------- 271
Cdd:COG5277   238 GLVPRDLAKAIQKAASNpDSFEAKVRLPNPTVeIELGNyawERFLIGEILFNPNHEGFESyiqqgrlriedavigdvvly 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 272 --AGVHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMY---PGIAD-------RMQKELTALAPsTMKIKIIAPPERKYSV 339
Cdd:COG5277   318 geMGLAEAIINSIMKCDVEIQDELYSNIILSGGAFNWsvpPGLEDvavdsvtRVQIELSELAP-ELKVNVRLVSDPQYSV 396
                         410       420
                  ....*....|....*....|....*...
gi 1906288369 340 WIGGSILASLSTFQQMW--ISKEEYDES 365
Cdd:COG5277   397 WKGAIIYGYALPFSVKWswITKEGWYFL 424
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
303-370 5.65e-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: 109.30  E-value: 5.65e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906288369 303 TTMYPGIADRMQKELTALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIV 370
Cdd:NF040575   61 RVNESGFYEKLKKSITEKAPKGALIGMTLDPKPESAAWRGAAMYAASEGFVEMAITKQEYDESGPSIV 128
 
Name Accession Description Interval E-value
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
6-370 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: 932.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369   6 QALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 85
Cdd:cd10224     1 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  86 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 165
Cdd:cd10224    81 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 166 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYAFTTTAEREIVRDIKEKLCYIALDFEEEMQTAASSSSLEKSYELPDG 245
Cdd:cd10224   161 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 246 QVITIGNERFRCPEALFQPSFLGMEAAGVHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMYPGIADRMQKELTALAPSTM 325
Cdd:cd10224   241 QVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTM 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1906288369 326 KIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIV 370
Cdd:cd10224   321 KIKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIV 365
ASKHA_NBD_actin_Arp-T1-3 cd13397
nucleotide-binding domain (NBD) of actin, actin-related proteins T1-T3 (Arp-T1-3), and similar ...
7-366 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: 773.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369   7 ALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIW 86
Cdd:cd13397     2 AVVIDNGSGLIKAGFAGEDLPRAVFPSVVGRPKYKAVMLGAGQKEVYVGDEAQEKRGVLTLSYPIEHGIVTNWDDMEKIW 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  87 HHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIY 166
Cdd:cd13397    82 HHTFENELRVKPEEHPVLLTEAPLNPKQNREKMAEIMFETFGVPAFYVAIQAVLSLYSSGRTTGLVLDSGDGVTHTVPIY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 167 EGYALPHAILRLDLAGRDLTDYLMKILTERGYAFTTTAEREIVRDIKEKLCYIALDFEEEMQtaASSSSLEKSYELPDGQ 246
Cdd:cd13397   162 EGYALPHAVQRLDLAGRDLTEYLMKLLKERGHSFTTTAEREIVRDIKEKLCYVALDYEEELK--KKSEELEKEYTLPDGQ 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 247 VITIGNERFRCPEALFQPSFLGMEAAGVHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMYPGIADRMQKELTALAPSTMK 326
Cdd:cd13397   240 VIKIGSERFRCPEALFRPSLIGREAPGIHKLVYNSIMKCDIDIRKDLYSNIVLSGGSTMFPGLPERLQKELEALAPSSTK 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1906288369 327 IKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESG 366
Cdd:cd13397   320 VKVIAPPERKYSVWIGGSILASLSTFKSMWITRAEYDEFG 359
PTZ00281 PTZ00281
actin; Provisional
1-370 0e+00

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 760.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369   1 MEDEVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWD 80
Cdd:PTZ00281    2 DGEDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  81 DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVS 160
Cdd:PTZ00281   82 DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 161 HTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYAFTTTAEREIVRDIKEKLCYIALDFEEEMQTAASSSSLEKSY 240
Cdd:PTZ00281  162 HTVPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEMQTAASSSALEKSY 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 241 ELPDGQVITIGNERFRCPEALFQPSFLGMEAAGVHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMYPGIADRMQKELTAL 320
Cdd:PTZ00281  242 ELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELTAL 321
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1906288369 321 APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIV 370
Cdd:PTZ00281  322 APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIV 371
PTZ00004 PTZ00004
actin-2; Provisional
1-370 0e+00

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 705.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369   1 MEDEVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWD 80
Cdd:PTZ00004    2 SVEETNAAVVDNGSGMVKAGFAGDDAPRCVFPSIVGRPKNPGIMVGMEEKDCYVGDEAQDKRGILTLKYPIEHGIVTNWD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  81 DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVS 160
Cdd:PTZ00004   82 DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETHNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 161 HTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYAFTTTAEREIVRDIKEKLCYIALDFEEEMQTAASSSSL-EKS 239
Cdd:PTZ00004  162 HTVPIYEGYSLPHAIHRLDVAGRDLTEYMMKILHERGTTFTTTAEKEIVRDIKEKLCYIALDFDEEMGNSAGSSDKyEES 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 240 YELPDGQVITIGNERFRCPEALFQPSFLGM-EAAGVHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMYPGIADRMQKELT 318
Cdd:PTZ00004  242 YELPDGTIITVGSERFRCPEALFQPSLIGKeEPPGIHELTFQSINKCDIDIRKDLYGNIVLSGGTTMYRGLPERLTKELT 321
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1906288369 319 ALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIV 370
Cdd:PTZ00004  322 TLAPSTMKIKVVAPPERKYSVWIGGSILSSLPTFQQMWVTKEEYDESGPSIV 373
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
5-370 0e+00

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 647.01  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369    5 VQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGmGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEK 84
Cdd:smart00268   1 VPAIVIDNGSGTIKAGFAGEDFPQVVFPSIVGRPKDGKGMVG-DAKDIFVGDEAQEKRGGLELKYPIENGIVENWDDMEK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369   85 IWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVP 164
Cdd:smart00268  80 IWDYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  165 IYEGYALPHAILRLDLAGRDLTDYLMKILTERGYAFTTTAEREIVRDIKEKLCYIALDFEEEMQTAAS---SSSLEKSYE 241
Cdd:smart00268 160 VVDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLAREsseSSKLEKTYE 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  242 LPDGQVITIGNERFRCPEALFQPSFLGMEAAGVHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMYPGIADRMQKELTALA 321
Cdd:smart00268 240 LPDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELKQLA 319
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1906288369  322 PSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIV 370
Cdd:smart00268 320 PKKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIV 368
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
6-370 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: 625.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369   6 QALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 85
Cdd:cd10216     2 QPVVIDNGSGVIKAGFAGDDIPKVVFPSYVGRPKHVRVMAGALEGDVFVGPKAEEHRGLLKIRYPMEHGIVTDWNDMERI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  86 WHHTFYNE-LRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVP 164
Cdd:cd10216    82 WQYVYSKLqLNTFSEEHPVLLTEAPLNPRKNREKAAEVFFETFNVPALFVSMQAVLSLYASGRTTGVVLDSGDGVTHAVP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 165 IYEGYALPHAILRLDLAGRDLTDYLMKILTERGYAFTTTAEREIVRDIKEKLCYIALDF--EEEMQTAASSSSlekSYEL 242
Cdd:cd10216   162 IYEGFALPHSIRRVDIAGRDVTEYLQLLLRKSGYNFHTSAEFEIVREIKEKACYVALNPqkEEKLEEEKTEKA---QYTL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 243 PDGQVITIGNERFRCPEALFQPSFLGMEAAGVHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMYPGIADRMQKELTALAP 322
Cdd:cd10216   239 PDGSTIEIGPERFRAPEILFNPELIGLEYPGVHEVLVDSIQKSDLDLRKTLYSNIVLSGGSTLFKGFGDRLLSEVKKLAP 318
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1906288369 323 STMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIV 370
Cdd:cd10216   319 KDVKIRISAPPERLYSTWIGGSILASLSTFKKMWVSKKEYEEDGARIL 366
Actin pfam00022
Actin;
5-370 0e+00

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 565.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369   5 VQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGmgqKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEK 84
Cdd:pfam00022   1 VSALVIDNGSHTTRAGFAGEDAPKAVIPSCVGKPRGTKVEAA---NKYYVGDEALTYRPGMEVRSPVEDGIVVDWDAMEE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  85 IWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVP 164
Cdd:pfam00022  78 IWEHVLKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 165 IYEGYALPHAILRLDLAGRDLTDYLMKILTER------------------------------GYAFTTTAEREIVRDIKE 214
Cdd:pfam00022 158 VHDGYVLQKAIRRSDLGGDFLTDYLRELLRSRnieitprylikskkpgdpapavtkrelpdtTYSYKTYQERRVLEEIKE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 215 KLCYIALDFeeEMQTAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGME--------AAGVHETTYNSIMKCD 286
Cdd:pfam00022 238 SVCYVSDDP--FGDETTSSSIPTRVYELPDGSTIILGAERFRVPEILFNPSLIGSEselpppqtAVGIPELIVDAINACD 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 287 VDIRKDLYGNVVLSGGTTMYPGIADRMQKELTALAPSTMKIKIIAPP---ERKYSVWIGGSILASLSTFQQMWISKEEYD 363
Cdd:pfam00022 316 VDLRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVKIIAPGntvERRYSAWIGGSILASLGTFQQMWVSKQEYE 395

                  ....*..
gi 1906288369 364 ESGPSIV 370
Cdd:pfam00022 396 EHGASVV 402
ASKHA_NBD_Arp2 cd10220
nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, ...
8-370 0e+00

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: 528.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369   8 LVIDNGSGMCKAGFAGDDAPRAVFPSIVGRP--RHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 85
Cdd:cd10220     3 VVCDNGTGFVKCGFAGSNFPEHVFPSLVGRPilRAEEKVGDIEIKDIMVGDEASELRSMLEVTYPMENGIVRNWDDMEHL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  86 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 165
Cdd:cd10220    83 WDYTFGEKLKIDPRECKILLTEPPMNPTKNREKMVEVMFEKYGFAGVYVAIQAVLTLYAQGLLTGVVVDSGDGVTHIVPV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 166 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYAFTTTAEREIVRDIKEKLCYIALDFEEEMQTAASSSSLEKSYELPDG 245
Cdd:cd10220   163 YEGFSLPHLTRRLDVAGRDITRYLIKLLLLRGYAFNRTADFETVREIKEKLCYVAYDIELEQKLALETTVLVESYTLPDG 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 246 QVITIGNERFRCPEALFQPSFLGMEAAGVHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMYPGIADRMQKELTAL----- 320
Cdd:cd10220   243 RVIKVGGERFEAPEALFQPHLIDVEGPGIAELLFNTIQAADIDTRPELYKHIVLSGGSTMYPGLPSRLEKEIKQLylerv 322
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1906288369 321 ------APSTMKIKIIAPPERKYSVWIGGSILASLSTFQ-QMWISKEEYDESGPSIV 370
Cdd:cd10220   323 lkgdteRLSKFKIRIEDPPRRKHMVFLGGAVLADIMKDKdEFWITRQEYEEQGVRVL 379
PTZ00466 PTZ00466
actin-like protein; Provisional
6-370 9.36e-174

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 488.68  E-value: 9.36e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369   6 QALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 85
Cdd:PTZ00466   13 QPIIIDNGTGYIKAGFAGEDVPNLVFPSYVGRPKYKRVMAGAVEGNIFVGNKAEEYRGLLKVTYPINHGIIENWNDMENI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  86 WHHTfYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 165
Cdd:PTZ00466   93 WIHV-YNSMKINSEEHPVLLTEAPLNPQKNKEKIAEVFFETFNVPALFISIQAILSLYSCGKTNGTVLDCGDGVCHCVSI 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 166 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYAFTTTAEREIVRDIKEKLCYIALDFEEEmQTAASSSSLEKSYELPDG 245
Cdd:PTZ00466  172 YEGYSITNTITRTDVAGRDITTYLGYLLRKNGHLFNTSAEMEVVKNMKENCCYVSFNMNKE-KNSSEKALTTLPYILPDG 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 246 QVITIGNERFRCPEALFQPSFLGMEAAGVHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMYPGIADRMQKELTALAPSTM 325
Cdd:PTZ00466  251 SQILIGSERYRAPEVLFNPSILGLEYLGLSELIVTSITRADMDLRRTLYSHIVLSGGTTMFHGFGDRLLNEIRKFAPKDI 330
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1906288369 326 KIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIV 370
Cdd:PTZ00466  331 TIRISAPPERKFSTFIGGSILASLATFKKIWISKQEFDEYGSVIL 375
PTZ00452 PTZ00452
actin; Provisional
1-370 2.77e-173

actin; Provisional


Pssm-ID: 185631  Cd Length: 375  Bit Score: 487.34  E-value: 2.77e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369   1 MEDEVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWD 80
Cdd:PTZ00452    1 MQAQYPAVVIDNGSGYCKIGIAGDDAPTSCFPAIVGRSKQNDGIFSTFNKEYYVGEEAQAKRGVLAIKEPIQNGIINSWD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  81 DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVS 160
Cdd:PTZ00452   81 DIEIIWHHAFYNELCMSPEDQPVFMTDAPMNSKFNRERMTQIMFETFNTPCLYISNEAVLSLYTSGKTIGLVVDSGEGVT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 161 HTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYAFTTTAEREIVRDIKEKLCYIALDFEEEMQTAASSSSLEKSY 240
Cdd:PTZ00452  161 HCVPVFEGHQIPQAITKINLAGRLCTDYLTQILQELGYSLTEPHQRIIVKNIKERLCYTALDPQDEKRIYKESNSQDSPY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 241 ELPDGQVITIGNERFRCPEALFQPSFLGMEAAGVHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMYPGIADRMQKELTAL 320
Cdd:PTZ00452  241 KLPDGNILTIKSQKFRCSEILFQPKLIGLEVAGIHHLAYSSIKKCDLDLRQELCRNIVLSGGTTLFPGIANRLSNELTNL 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1906288369 321 APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIV 370
Cdd:PTZ00452  321 VPSQLKIQVAAPPDRRFSAWIGGSIQCTLSTQQPQWIKRQEYDEQGPSIV 370
ASKHA_NBD_ACTL7 cd10214
nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ...
4-370 3.86e-171

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: 481.54  E-value: 3.86e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369   4 EVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDME 83
Cdd:cd10214     2 ETKAVIIDLGTGYCKAGFAGQPRPSYVISSTVGKPPQESAKTGDNRKETFVGKELANVEPPLKLVNPLRHGIVVDWDCVQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  84 KIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTV 163
Cdd:cd10214    82 DIWEYIFEKEMKILPEEHAVLVSDPPLSPTTNREKYAELMFETFSIPAMHIAYQSRLSLYSYGRTSGLVVESGHGVSYVV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 164 PIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYAFTTTaEREIVRDIKEKLCYIALDFEEEMqtAASSSSLEKSYELP 243
Cdd:cd10214   162 PIHEGYNLPHITGRADYAGSDLTAYLMKLLNEAGNKFTDD-QLHIVEDIKKKCCYVALDFEEEM--GLPPQEYTVDYELP 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 244 DGQVITIGNERFRCPEALFQPSFLGMEAAGVHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMYPGIADRMQKELTALAPS 323
Cdd:cd10214   239 DGHLITIGKERFRCPEMLFNPSLIGSKQPGLHTLTMNSLNKCDANLKKDLAKNILLCGGSTMFDGFPDRFQKELSKLCPN 318
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1906288369 324 TMKIkIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIV 370
Cdd:cd10214   319 DNPI-VAASPERKYSVWTGGSILASLKSFQQLWVRRREYEERGPFVI 364
ASKHA_NBD_actin-like cd10169
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ...
8-366 3.85e-164

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: 459.26  E-value: 3.85e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369   8 LVIDNGSGMCKAGFAGDDAPRAVFPsivgrprhtgvmvgmgqkdsyvgdeaqskrgiltlkypiehgivtnWDDMEKIWH 87
Cdd:cd10169     1 IVIDNGSGTIKAGFAGEDAPRLIFP----------------------------------------------WDDMEKIWE 34
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  88 HTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYE 167
Cdd:cd10169    35 HVFYNLLRVDPEEHPVLLTEPPLNPKANREKLAEILFETFNVPSLYIANQAVLSLYASGRTTGLVVDSGEGVTHIVPVYE 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 168 GYALPHAILRLDLAGRDLTDYLMKILTERGYAFTTTAEREIVRDIKEKLCyialdfeeemqtaassssleksyelpdgqv 247
Cdd:cd10169   115 GYVLPHAVRRLDIGGRDLTDYLAKLLREKGYSFSTSAEREIVRDIKEKLC------------------------------ 164
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 248 itignerfrcpealfqpsflgmeaaGVHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMYPGIADRMQKELTALAPSTMKI 327
Cdd:cd10169   165 -------------------------GLHELIYDSIMKCDIDLRKELYSNIVLSGGTTLFPGFAERLQKELSKLAPSSVKV 219
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1906288369 328 KIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESG 366
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 ...
3-366 1.17e-163

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: 463.96  E-value: 1.17e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369   3 DEVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVG-RPRHTGVMVGMGQKDS-----YVGDEA-QSKRGILTLKYPIEHGI 75
Cdd:cd13395     2 DEVGALVLDIGSYSTRAGYAGEDTPKAVFPSVVGvVTDDDDAEDYVGGSGEkkrkyYIGTNSiGVPRPNMEVISPLKDGL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  76 VTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDS 155
Cdd:cd13395    82 IEDWDAFEKLWDHALKNRLRVDPSEHPLLLTEPSWNTRANREKLTELMFEKYNVPAFFLAKNAVLSAFANGRSTALVVDS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 156 GDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYAFT--------------------------TT------ 203
Cdd:cd13395   162 GATSTSVVPVHDGYVLQKAIVRSPLGGDFLTDQLLKLLESKNIEIIprymikskepveggapakytkkdlpnTTssyhry 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 204 AEREIVRDIKEKLCYIALDFEEEmQTAASSSSleKSYELPDGQVITIGNERFRCPEALFQPSFL---------GMEAAGV 274
Cdd:cd13395   242 MVRRVLQDFKESVCQVSDSPFDE-SEAASIPT--VSYELPDGYNIEFGAERFKIPELLFDPSLVkgipappseGNELLGL 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 275 HETTYNSIMKCDVDIRKDLYGNVVLSGGTTMYPGIADRMQKELTALAPSTMKIKIIAPP---ERKYSVWIGGSILASLST 351
Cdd:cd13395   319 PQLVYTSIGSCDVDIRPELYGNVVLTGGNSLLPGFTDRLNRELSEKAPGSLKLKILASGntvERRFSSWIGGSILASLGS 398
                         410
                  ....*....|....*
gi 1906288369 352 FQQMWISKEEYDESG 366
Cdd:cd13395   399 FQQMWISKQEYEEHG 413
COG5277 COG5277
Actin-related protein [Cytoskeleton];
1-365 2.78e-140

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 405.33  E-value: 2.78e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369   1 MEDEVQA---LVIDNGSGMCKAG-FAGDDAP-----RAVFPSIVGRPRHTGVMVGMGqKDSYVGDEAQS-----KRGILT 66
Cdd:COG5277     1 MSDAYKLkyvIGIDFGTSYVKYGpIALEEKPrviqtRGLFLRIVGESKLLGPMEGLS-RGLVVGDEVSKylssvRDAIRN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  67 LKYPIEHGIVT-----NWDDMEKIWHHTFYNELRVAPEEHP--VLLTEAPLNPKANREKMTQIMFETF---NTPAMYVAI 136
Cdd:COG5277    80 LKYPLRDGIVRrddedAWRVLKELLRYTFAQFLVVDPEFHGflVVVALSALAPDYMRERLFDIHFEVFseeGAPAVTIIP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 137 QAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGyALPHAILRLDLAGRDLTDYLMKILTERGYAFTTTAEReIVRDIKEKL 216
Cdd:COG5277   160 QPLAVAIAEKAVTCVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSDTAREEY-VVRVVKEAL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 217 CYIALDFEEEMQTAASS-SSLEKSYELPDGQV-ITIGN---ERFRCPEALFQPSFLGMEA-------------------- 271
Cdd:COG5277   238 GLVPRDLAKAIQKAASNpDSFEAKVRLPNPTVeIELGNyawERFLIGEILFNPNHEGFESyiqqgrlriedavigdvvly 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 272 --AGVHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMY---PGIAD-------RMQKELTALAPsTMKIKIIAPPERKYSV 339
Cdd:COG5277   318 geMGLAEAIINSIMKCDVEIQDELYSNIILSGGAFNWsvpPGLEDvavdsvtRVQIELSELAP-ELKVNVRLVSDPQYSV 396
                         410       420
                  ....*....|....*....|....*...
gi 1906288369 340 WIGGSILASLSTFQQMW--ISKEEYDES 365
Cdd:COG5277   397 WKGAIIYGYALPFSVKWswITKEGWYFL 424
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
7-370 1.98e-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: 359.19  E-value: 1.98e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369   7 ALVIDNGSGMCKAGFAGDDAPRAVFPSIVG-------RPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNW 79
Cdd:cd10221     1 AVVIDNGTGYTKMGYAGNTEPQFIIPTVIAikesakvGDGQRRSKKGIEDLDFYIGDEALANSPTYALKYPIRHGIVEDW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  80 DDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRT--------TGI 151
Cdd:cd10221    81 DLMERFWEQCIFKYLRCEPEDHYFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQAVLALAASWTSrkvgertlTGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 152 VLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYAFTTTAEREIVRDIKEKLCYIALDFEEEMQTAA 231
Cdd:cd10221   161 VIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREEGIPPEDSLEVAKRIKERYCYVCPDIVKEFAKYD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 232 SS-SSLEKSYELPD---GQ--VITIGNERFRCPEALFQPSFLGMEA-AGVHETTYNSIMKCDVDIRKDLYGNVVLSGGTT 304
Cdd:cd10221   241 SDpAKYIKQYTGINsvtGKpyTVDVGYERFLAPEIFFNPEIASSDFtTPLPEVVDQVIQSCPIDTRRGLYKNIVLSGGST 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 305 MYPGIADRMQKELTA----------------LAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPS 368
Cdd:cd10221   321 MFKDFGRRLQRDVKRivdarlkaseelsggkLKPKPIDVNVISHPMQRYAVWFGGSMLASTPEFYTVCHTKAEYEEYGPS 400

                  ..
gi 1906288369 369 IV 370
Cdd:cd10221   401 IC 402
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
7-370 9.36e-121

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 355.19  E-value: 9.36e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369   7 ALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMV---GMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDME 83
Cdd:PTZ00280    6 VVVIDNGTGYTKMGYAGNTEPTYIIPTLIADNSKQSRRRskkGFEDLDFYIGDEALAASKSYTLTYPMKHGIVEDWDLME 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  84 KIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYAS----------GRTTGIVL 153
Cdd:PTZ00280   86 KFWEQCIFKYLRCEPEEHYFILTEPPMNPPENREYTAEIMFETFNVKGLYIAVQAVLALRASwtskkakelgGTLTGTVI 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 154 DSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYAFTTTAEREIVRDIKEKLCYIALDFEEEMQT---- 229
Cdd:PTZ00280  166 DSGDGVTHVIPVVDGYVIGSSIKHIPLAGRDITNFIQQMLRERGEPIPAEDILLLAQRIKEKYCYVAPDIAKEFEKydsd 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 230 --------AASSSSLEKSYElpdgqvITIGNERFRCPEALFQPSFLGME-AAGVHETTYNSIMKCDVDIRKDLYGNVVLS 300
Cdd:PTZ00280  246 pknhfkkyTAVNSVTKKPYT------VDVGYERFLGPEMFFHPEIFSSEwTTPLPEVVDDAIQSCPIDCRRPLYKNIVLS 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 301 GGTTMYPGIADRMQKELTA----------------LAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDE 364
Cdd:PTZ00280  320 GGSTMFKGFDKRLQRDVRKrvdrrlkkaeelsggkLKPIPIDVNVVSHPRQRYAVWYGGSMLASSPEFEKVCHTKAEYDE 399

                  ....*.
gi 1906288369 365 SGPSIV 370
Cdd:PTZ00280  400 YGPSIC 405
ASKHA_NBD_Arp6 cd10210
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ...
8-366 2.14e-100

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: 302.16  E-value: 2.14e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369   8 LVIDNGSGMCKAGFAGDDAPRaVFPSIVGRPRHtgvmvgmgQKDSYVGDEAQSK---RGILTLKYPIEHGIVTNWDDMEK 84
Cdd:cd10210     2 LVLDNGAYTIKAGFASDDPPR-VIPNCIAKPKS--------ERRRLFGDDQLDEckdLSGLFYRRPFERGYLVNWDLQRQ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  85 IWHHTFYNE-LRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYA----------SGRTTGIVL 153
Cdd:cd10210    73 IWDHLFGKLlLNVDPSDTALVLTEPPFNPPSIQEAMDEIVFEEYGFQSLYRTTAAALSAFAyladseqsssSSSQCCLVV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 154 DSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYafttTAERE--IVRDIKEKLCYIALDFEEEMQTAA 231
Cdd:cd10210   153 DSGFSFTHIVPFFDGKPVKRAVRRIDVGGKLLTNYLKEIISYRQL----NVMDEtyLVNQIKEDLCFVSTDFYEDLEIAK 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 232 S---SSSLEKSYELPDG-----------------------QVITIGNERFRCPEALFQPSFLGMEAAGVHETTYNSIMKC 285
Cdd:cd10210   229 KkgkENTIRRDYVLPDYttskrgyvrdpeepnrgklkedeQVLRLNNERFTVPELLFHPSDIGIQQAGIAEAIVQSINAC 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 286 DVDIRKDLYGNVVLSGGTTMYPGIADRMQKELTALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDES 365
Cdd:cd10210   309 PEELQPLLYANIVLTGGNALFPGFRERLEAELRSLAPDDYDVNVTLPEDPITYAWEGGSLLAQSPEFEELAVTRAEYEEH 388

                  .
gi 1906288369 366 G 366
Cdd:cd10210   389 G 389
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
8-370 2.46e-86

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: 265.02  E-value: 2.46e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369   8 LVIDNGSGMCKAGFAGDDApravFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSkrgiltlkyPIEHGIVTNWDDMEKIWH 87
Cdd:cd10209     1 VVIDAGSRLLKAGYAYPDR----EPSVVEPTRVTPAVEDGEESDTVVEGNTVS---------PIRRGRIEDWDALEALLR 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  88 HTFYNELR-VAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIY 166
Cdd:cd10209    68 YVFYTGLGwEEGNEGQVLIAEPLLTSKAERERLTQLMFETFNVSGLYASEQAVLSLYAVGRISGCVVDVGHGKIDIAPVW 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 167 EGYALPHAILRLDLAGRDLTDYLMKILTERGYafTTTAEREIVRDIKEKlCYIALDFEEEMQTAASSSSLEkSYELPDGQ 246
Cdd:cd10209   148 EGAIQHNAVRRFEIGGRDLTELLAAELGKSNP--KVKLDRSIVERLKEA-VAWSADDEEAYEKKVLTCSPE-TYTLPDGR 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 247 VITIGNERFRCPEALFQPSFLGMEAAGVHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMYPGIADRMQKELTALAPSTMK 326
Cdd:cd10209   224 VISVGKERYCVGEALFRPSILGIEEYGIVEQLVRAVSTSPSENRRQLLENIVLCGGTSSVPGLEARLQKEIRLLSSPSSR 303
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1906288369 327 IKIIAPPE------RKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIV 370
Cdd:cd10209   304 PALVKPPEympentLRYSAWIGGAILAKVVFPQNQHVTKADYDETGPSVV 353
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
7-367 1.17e-76

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: 240.17  E-value: 1.17e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369   7 ALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTgvmvGMGQKDSYVGDEA---QSKRGilTLKYPIEHGIVTNWDDME 83
Cdd:cd10211     1 PIVIDNGSYQCRAGWAGDKEPRLVFRNLVAKPRDR----KKGITVTLVGNDIlndEAVRS--HLRSPFDRNVVTNFDLQE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  84 KIWHHTFyNELRVAPE---EHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRT----TGIVLDSG 156
Cdd:cd10211    75 QILDYIF-SHLGINSEgsvDHPIVLTEALCNPNYSRQLMSELLFECYGVPSVAYGIDSLFSYYHNQPQgdpsDGLVISSG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 157 DGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYAFTT--TAEReiVRDIKEKLCYIALDFEEEMQTAASSS 234
Cdd:cd10211   154 YSTTHVIPVLNGRLDLSQCKRINLGGFHATDYLQRLLQLKYPTHPSaiTLSR--AEELVHEHCYVAEDYDEELKKWEDPE 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 235 SLEKSyelpdgqvitigNERFRCPealfqpsflgmeaAGVHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMYPGIADRMQ 314
Cdd:cd10211   232 YYEEN------------VRKIQLP-------------FGLVETIEFVLKRYPAEQQDRLVQNVFLTGGNALFPGLKERLE 286
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1906288369 315 KELTALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGP 367
Cdd:cd10211   287 KELRAIRPFGSPFNVVRAKDPVLDAWRGAAKWALDSTFEKVWITKQEYEEKGG 339
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
38-370 5.53e-59

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: 194.83  E-value: 5.53e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  38 PRHTGVMVGMGQKDSYVGD--EAQSKRGILtlkYPIEHGIVTNWDDMEKIWHHTFYNEL--RVAPEEHPVLLTEAPLNPK 113
Cdd:cd10208     7 PGSQTTRAGLGLGELLTPPtiEIPTRVEII---WPIQDGRVVDWDALEALWRHILFSLLsiPRPTNNSPVLLSVPPSWSK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 114 ANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKIL 193
Cdd:cd10208    84 SDLELLTQLFFERLNVPAFAILEAPLAALYAAGATSGIVVDIGHEKTDITPIVDSQVVPHALVSIPIGGQDCTAHLAQLL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 194 TErgyaftttaEREIVRDIKEKLCYIALDFEEEMQTAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGM---- 269
Cdd:cd10208   164 KS---------DEPELKSQAESGEEATLDLAEALKKSPICEVLSDGADLASGTEITVGKERFRACEPLFKPSSLRVdlli 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 270 EAAGVHETTYNSimkCDVDIRKDLYGNVVLSGGTTMYPGIADRMQKELTAL-----------APSTMKIKIIaP---PER 335
Cdd:cd10208   235 AAIAGALVLNAS---DEPDKRPALWENIIIVGGGSRIRGLKEALLSELQQFhlisetsaspqQPRIIRLAKI-PdyfPEW 310
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1906288369 336 K-----YSVWIGGSILASLsTF----QQMWISKEEYDESGPSIV 370
Cdd:cd10208   311 KksgyeEAAFLGASIVAKL-VFndpsSKHYISKVDYNEKGPAAI 353
ASKHA_NBD_Arp10 cd10207
nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins; ...
9-366 1.20e-50

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: 173.59  E-value: 1.20e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369   9 VIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRhtgvmvgmGQKDSYVGDeaqsKRGILTLKypiehgivtnWDDM-EKIWH 87
Cdd:cd10207     2 VLDIGSAYTKCGFAGESAPRCIIPSEVKLPG--------GKKVIRVVD----QRSGNEEE----------LYEAlKEFLH 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  88 HTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYE 167
Cdd:cd10207    60 ELYFKHLLVNPKDRRVVVVESVLCPTPFRETLAKVLFKHFEVPSVLFAPSHLLSLLTLGIRTALVVDCGYRETRVLPVYE 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 168 GYALPHAILRLDLAGRDLTDYLMKILTERGYAFTTTAER------------EIVRDIKEKLCYIA-LDFEEEMQTAASSS 234
Cdd:cd10207   140 GVPLLSAWQSTPLGGKALHKRLKKLLLEHATVVTGDNKGqllssvdsllseEVLEDIKVRACFVTsLERGKTLQSATEEG 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 235 SLEKS-------YELPDGQVITIGNERFRCPEALFqpsFLGM-EAAGVHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMY 306
Cdd:cd10207   220 STEEPsppppvdYPLDGEKILIVPGSIRESAEELL---FEGDnEEKSLPTLILDSLLKCPIDVRKQLAENIVVIGGTSML 296
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906288369 307 PGIADRMQKELTA----------LAPSTMKI---KIIAPPErkYSVWIGGSILASLSTFQQMWISKEEYDESG 366
Cdd:cd10207   297 PGFKHRLLEELRAllrkpkyfeeLAPKTFRFhtpPSVFKPN--YLAWLGGSIFGALESILGRSLSREAYLQTG 367
ASKHA_NBD_AtArp8-like cd13396
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and ...
89-366 3.28e-49

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: 168.49  E-value: 3.28e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  89 TFYNELRVAPEEHPVLLTEaPL-------NPKANREKMTQIMFETF---NTPAMYVAIQAVLSLYASGRTTGIVLDSGDG 158
Cdd:cd13396    47 TIMTRMQVKPSRQPVVVSL-PLchsddteSAAASRRQLRGTIFNVLfdmNVPAVCAVDQAVLALYAANRTSGIVVNIGFR 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 159 VSHTVPIYEGYALPH-AILRLDLAGRDLTDYLMKILTERGYAFTTTAereIVRDIKEKLCYIALDFEEEMqtaasSSSLE 237
Cdd:cd13396   126 VTTIVPVYRGRVMHDiGVEVVGQGALRLTGFLKELMQQNGIRFPSLY---TVRTIKEKLCYVAEDYEAEL-----AKDTQ 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 238 KSYELPDGQVITIGNERFRCPEALFQPSFLGMEAAGVHETTYNSIMKCDVDIR---KDLYGNVVLSGGTTMYPGIADRMQ 314
Cdd:cd13396   198 ASCEVAGEGWFTLSNERFKTGEILFQPGLGGMRAMGLHQAVALCMDHCALVHSqgdDGWFKTIVLSGGSACLPGLSERLE 277
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1906288369 315 KELTALAPSTMK--IKIIAPPERKYSVWIGGSILASLSTFQQMW-ISKEEYDESG 366
Cdd:cd13396   278 RELRKLLPKSLSegIRIIPPPLGPDSAWQGAKLISNLSNFPDGWcITKKQFRNKP 332
ASKHA_NBD_Arp8-like cd10206
nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The ...
48-369 2.60e-29

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: 117.34  E-value: 2.60e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  48 GQKDSYVGDEAQ--SKRGILTLKYPIEHGiVTNW-----------DDMEKIWHHTFYNELRVAPEEHP----VLLTEAPL 110
Cdd:cd10206   118 DYPDFLVGEEALrlPPSEEYNLHWPIRRG-RLNVhsdggsltavlDDLEDIWSHALEEKLEIPRKDLKnyraVLVIPDLF 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 111 NpKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLM 190
Cdd:cd10206   197 D-RRHVKELVDLLLRRLGFSSVFVHQESVCATFGAGLSSACVVDIGAQKTSVACVEDGLSIPNSRIRLPYGGDDITRCFL 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 191 KILTERGYAFT-----TTAEREIVRDIKEKLCYIALDFeeemqtaassssleksyelpDGQVITIGNERFRC-PEALFQP 264
Cdd:cd10206   276 WLLRRSGFPYRecnlnSPLDFLLLERLKETYCTLDQDD--------------------IGVQLHEFYVREPGqPTLKYQF 335
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 265 SFLGMEAAGVHettynSIMKC-DVDIRKDLYGNVVLSGGTTMYPGIADRMQKELTALAPSTMK----IKIIAPPERK--- 336
Cdd:cd10206   336 KLLPLDEAIVQ-----SILSCaSDELKRKMYSSILLVGGGAKIPGLAEALEDRLLIKIPSLFEavetVEVLPPPKDMdps 410
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1906288369 337 YSVWIGGSILASLSTFQQMWISKEEYDESGPSI 369
Cdd:cd10206   411 LLAWKGGAVLACLDSAQELWITRKEWQRLGVRA 443
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
303-370 5.65e-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: 109.30  E-value: 5.65e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906288369 303 TTMYPGIADRMQKELTALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIV 370
Cdd:NF040575   61 RVNESGFYEKLKKSITEKAPKGALIGMTLDPKPESAAWRGAAMYAASEGFVEMAITKQEYDESGPSIV 128
ASKHA_NBD_ScArp7-like cd10212
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and ...
6-363 1.76e-21

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: 95.17  E-value: 1.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369   6 QALVIDNGSGMCKAGFAGDDAPRAVFPS-IVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEK 84
Cdd:cd10212     4 KCVVIHNGSHRTVAGFSNVELPQCIIPSsYIKRTDEGGEAEFIFGTYNMIDAAAEKRNGDEVYTLVDSQGLPYNWDALEM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  85 IWHHTFYNELRVAPEEHPVLLTEAPLNPKANR---EKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSH 161
Cdd:cd10212    84 QWRYLYDTQLKVSPEELPLVITMPATNGKPDMailERYYELAFDKLNVPVFQIVIEPLAIALSMGKSSAFVIDIGASGCN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 162 TVPIYEGYALPHAILRLDLAGrDLTDYLM---------------------KILTERGYAFTTTAER-------------- 206
Cdd:cd10212   164 VTPIIDGIVVKNAVVRSKFGG-DFLDFQVherlaplikeendmenmadeqKRSTDVWYEASTWIQQfkstmlqvsekdlf 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 207 EIVRDIKEKLCYIALDFE------EEMQTAASSSS-----LEKSYEL--PDGQVITIG-NERFRCPEALFQPSFLGMEAA 272
Cdd:cd10212   243 ELERYYKEQADIYAKQQEqlkqmdQQLQYTALTGSpnnplVQKKNFLfkPLNKTLTLDlKECYQFAEYLFKPQLISDKFS 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 273 ---GVHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMYPGIADRMQKELTALAP----STMKIKIIAppERKYSVWIGGSI 345
Cdd:cd10212   323 pedGLGPLMAKSVKKAPEQVYSLLLTNVIITGSTSLIEGMEQRIIKELSIRFPqyklTTFANQVMM--DRKIQGWLGALT 400
                         410
                  ....*....|....*....
gi 1906288369 346 LASLSTFQ-QMWISKEEYD 363
Cdd:cd10212   401 MANLPSWSlGKWYSKEDYE 419
ASKHA_NBD_MamK cd24009
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ...
15-317 1.49e-09

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: 58.76  E-value: 1.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  15 GMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGqKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDmekiwhhtfyNEL 94
Cdd:cd24009     9 GTSRSAVVTSRGKRFSFRSVVGYPKDIIARKLLG-KEVLFGDEALENRLALDLRRPLEDGVIKEGDD----------RDL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369  95 RVAPE--EHPVLLTEAPLNPK-------------ANREKMTQIMFETFNTPAMYVAIQAVlsLYASGRTTG-IVLDSGDG 158
Cdd:cd24009    78 EAAREllQHLIELALPGPDDEiyavigvparasaENKQALLEIARELVDGVMVVSEPFAV--AYGLDRLDNsLIVDIGAG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 159 VSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTER--GYAFTttaeREIVRDIKEKLCYIaldfeeemqtaaSSSSL 236
Cdd:cd24009   156 TTDLCRMKGTIPTEEDQITLPKAGDYIDEELVDLIKERypEVQLT----LNMARRWKEKYGFV------------GDASE 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906288369 237 EKSYELP-DGQVIT--IGNE-RFRCpEALFQPsflgmeaagVHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMYPGIADR 312
Cdd:cd24009   220 PVKVELPvDGKPVTydITEElRIAC-ESLVPD---------IVEGIKKLIASFDPEFQEELRNNIVLAGGGSRIRGLDTY 289

                  ....*
gi 1906288369 313 MQKEL 317
Cdd:cd24009   290 IEKAL 294
 
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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