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Conserved domains on  [gi|1983980495|gb|QRN76687|]
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actin 5C [Tineola bisselliella]

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 ...
7-371 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: 939.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495   7 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 86
Cdd:cd10224     1 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  87 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 166
Cdd:cd10224    81 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 167 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDG 246
Cdd:cd10224   161 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 247 QVITIGNERFRCPEALFQPSFLGMEACGIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTM 326
Cdd:cd10224   241 QVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTM 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1983980495 327 KIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIV 371
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 ...
7-371 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: 939.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495   7 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 86
Cdd:cd10224     1 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  87 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 166
Cdd:cd10224    81 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 167 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDG 246
Cdd:cd10224   161 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 247 QVITIGNERFRCPEALFQPSFLGMEACGIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTM 326
Cdd:cd10224   241 QVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTM 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1983980495 327 KIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIV 371
Cdd:cd10224   321 KIKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIV 365
PTZ00281 PTZ00281
actin; Provisional
1-376 0e+00

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 775.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495   1 MCDEEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNW 80
Cdd:PTZ00281    1 MDGEDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  81 DDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGV 160
Cdd:PTZ00281   81 DDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 161 SHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKS 240
Cdd:PTZ00281  161 SHTVPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEMQTAASSSALEKS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 241 YELPDGQVITIGNERFRCPEALFQPSFLGMEACGIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITA 320
Cdd:PTZ00281  241 YELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELTA 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1983980495 321 LAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF 376
Cdd:PTZ00281  321 LAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIVHRKCF 376
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
6-376 0e+00

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 658.18  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495    6 VAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGmGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEK 85
Cdd:smart00268   1 VPAIVIDNGSGTIKAGFAGEDFPQVVFPSIVGRPKDGKGMVG-DAKDIFVGDEAQEKRGGLELKYPIENGIVENWDDMEK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495   86 IWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVP 165
Cdd:smart00268  80 IWDYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  166 IYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAAS---SSSLEKSYE 242
Cdd:smart00268 160 VVDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLAREsseSSKLEKTYE 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  243 LPDGQVITIGNERFRCPEALFQPSFLGMEACGIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALA 322
Cdd:smart00268 240 LPDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELKQLA 319
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1983980495  323 PSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF 376
Cdd:smart00268 320 PKKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERKCF 373
Actin pfam00022
Actin;
6-376 0e+00

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 578.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495   6 VAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGmgqKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEK 85
Cdd:pfam00022   1 VSALVIDNGSHTTRAGFAGEDAPKAVIPSCVGKPRGTKVEAA---NKYYVGDEALTYRPGMEVRSPVEDGIVVDWDAMEE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  86 IWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVP 165
Cdd:pfam00022  78 IWEHVLKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 166 IYEGYALPHAILRLDLAGRDLTDYLMKILTER------------------------------GYSFTTTAEREIVRDIKE 215
Cdd:pfam00022 158 VHDGYVLQKAIRRSDLGGDFLTDYLRELLRSRnieitprylikskkpgdpapavtkrelpdtTYSYKTYQERRVLEEIKE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 216 KLCYVALDFeqEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGME--------ACGIHETTYNSIMKCD 287
Cdd:pfam00022 238 SVCYVSDDP--FGDETTSSSIPTRVYELPDGSTIILGAERFRVPEILFNPSLIGSEselpppqtAVGIPELIVDAINACD 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 288 VDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPP---ERKYSVWIGGSILASLSTFQQMWISKQEYD 364
Cdd:pfam00022 316 VDLRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVKIIAPGntvERRYSAWIGGSILASLGTFQQMWVSKQEYE 395
                         410
                  ....*....|..
gi 1983980495 365 ESGPSIVHRKCF 376
Cdd:pfam00022 396 EHGASVVERKCK 407
COG5277 COG5277
Actin-related protein [Cytoskeleton];
10-366 2.46e-142

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 410.72  E-value: 2.46e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  10 VVDNGSGMCKAG-FAGDDAP-----RAVFPSIVGRPRHQGVMVGMGqKDSYVGDEAQS-----KRGILTLKYPIEHGIVT 78
Cdd:COG5277    12 GIDFGTSYVKYGpIALEEKPrviqtRGLFLRIVGESKLLGPMEGLS-RGLVVGDEVSKylssvRDAIRNLKYPLRDGIVR 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  79 -----NWDDMEKIWHHTFYNELRVAPEEHP--VLLTEAPLNPKANREKMTQIMFETF---NTPAMYVAIQAVLSLYASGR 148
Cdd:COG5277    91 rddedAWRVLKELLRYTFAQFLVVDPEFHGflVVVALSALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPLAVAIAEKA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 149 TTGIVLDSGDGVSHTVPIYEGyALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEReIVRDIKEKLCYVALDFEQEM 228
Cdd:COG5277   171 VTCVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSDTAREEY-VVRVVKEALGLVPRDLAKAI 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 229 -ATAASSSSLEKSYELPDGQV-ITIGN---ERFRCPEALFQPSFLGMEAC----------------------GIHETTYN 281
Cdd:COG5277   249 qKAASNPDSFEAKVRLPNPTVeIELGNyawERFLIGEILFNPNHEGFESYiqqgrlriedavigdvvlygemGLAEAIIN 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 282 SIMKCDVDIRKDLYANTVLSGGTTMY---PGIAD-------RMQKEITALAPsTMKIKIIAPPERKYSVWIGGSILASLS 351
Cdd:COG5277   329 SIMKCDVEIQDELYSNIILSGGAFNWsvpPGLEDvavdsvtRVQIELSELAP-ELKVNVRLVSDPQYSVWKGAIIYGYAL 407
                         410
                  ....*....|....*..
gi 1983980495 352 TFQQMW--ISKQEYDES 366
Cdd:COG5277   408 PFSVKWswITKEGWYFL 424
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
304-375 2.45e-35

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: 126.25  E-value: 2.45e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1983980495 304 TTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKC 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 ...
7-371 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: 939.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495   7 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 86
Cdd:cd10224     1 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  87 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 166
Cdd:cd10224    81 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 167 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDG 246
Cdd:cd10224   161 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 247 QVITIGNERFRCPEALFQPSFLGMEACGIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTM 326
Cdd:cd10224   241 QVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTM 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1983980495 327 KIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIV 371
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 ...
7-367 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: 776.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495   7 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 86
Cdd:cd13397     1 PAVVIDNGSGLIKAGFAGEDLPRAVFPSVVGRPKYKAVMLGAGQKEVYVGDEAQEKRGVLTLSYPIEHGIVTNWDDMEKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  87 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 166
Cdd:cd13397    81 WHHTFENELRVKPEEHPVLLTEAPLNPKQNREKMAEIMFETFGVPAFYVAIQAVLSLYSSGRTTGLVLDSGDGVTHTVPI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 167 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMatAASSSSLEKSYELPDG 246
Cdd:cd13397   161 YEGYALPHAVQRLDLAGRDLTEYLMKLLKERGHSFTTTAEREIVRDIKEKLCYVALDYEEEL--KKKSEELEKEYTLPDG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 247 QVITIGNERFRCPEALFQPSFLGMEACGIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTM 326
Cdd:cd13397   239 QVIKIGSERFRCPEALFRPSLIGREAPGIHKLVYNSIMKCDIDIRKDLYSNIVLSGGSTMFPGLPERLQKELEALAPSST 318
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1983980495 327 KIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESG 367
Cdd:cd13397   319 KVKVIAPPERKYSVWIGGSILASLSTFKSMWITRAEYDEFG 359
PTZ00281 PTZ00281
actin; Provisional
1-376 0e+00

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 775.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495   1 MCDEEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNW 80
Cdd:PTZ00281    1 MDGEDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  81 DDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGV 160
Cdd:PTZ00281   81 DDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 161 SHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKS 240
Cdd:PTZ00281  161 SHTVPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEMQTAASSSALEKS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 241 YELPDGQVITIGNERFRCPEALFQPSFLGMEACGIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITA 320
Cdd:PTZ00281  241 YELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELTA 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1983980495 321 LAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF 376
Cdd:PTZ00281  321 LAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIVHRKCF 376
PTZ00004 PTZ00004
actin-2; Provisional
1-376 0e+00

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 721.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495   1 MCDEEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNW 80
Cdd:PTZ00004    1 MSVEETNAAVVDNGSGMVKAGFAGDDAPRCVFPSIVGRPKNPGIMVGMEEKDCYVGDEAQDKRGILTLKYPIEHGIVTNW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  81 DDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGV 160
Cdd:PTZ00004   81 DDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETHNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 161 SHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSL-EK 239
Cdd:PTZ00004  161 SHTVPIYEGYSLPHAIHRLDVAGRDLTEYMMKILHERGTTFTTTAEKEIVRDIKEKLCYIALDFDEEMGNSAGSSDKyEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 240 SYELPDGQVITIGNERFRCPEALFQPSFLGMEAC-GIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEI 318
Cdd:PTZ00004  241 SYELPDGTIITVGSERFRCPEALFQPSLIGKEEPpGIHELTFQSINKCDIDIRKDLYGNIVLSGGTTMYRGLPERLTKEL 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1983980495 319 TALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF 376
Cdd:PTZ00004  321 TTLAPSTMKIKVVAPPERKYSVWIGGSILSSLPTFQQMWVTKEEYDESGPSIVHRKCF 378
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
6-376 0e+00

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 658.18  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495    6 VAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGmGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEK 85
Cdd:smart00268   1 VPAIVIDNGSGTIKAGFAGEDFPQVVFPSIVGRPKDGKGMVG-DAKDIFVGDEAQEKRGGLELKYPIENGIVENWDDMEK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495   86 IWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVP 165
Cdd:smart00268  80 IWDYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  166 IYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAAS---SSSLEKSYE 242
Cdd:smart00268 160 VVDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLAREsseSSKLEKTYE 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  243 LPDGQVITIGNERFRCPEALFQPSFLGMEACGIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALA 322
Cdd:smart00268 240 LPDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELKQLA 319
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1983980495  323 PSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF 376
Cdd:smart00268 320 PKKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERKCF 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: 631.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495   9 LVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWH 88
Cdd:cd10216     4 VVIDNGSGVIKAGFAGDDIPKVVFPSYVGRPKHVRVMAGALEGDVFVGPKAEEHRGLLKIRYPMEHGIVTDWNDMERIWQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  89 HTFYNE-LRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIY 167
Cdd:cd10216    84 YVYSKLqLNTFSEEHPVLLTEAPLNPRKNREKAAEVFFETFNVPALFVSMQAVLSLYASGRTTGVVLDSGDGVTHAVPIY 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 168 EGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFeQEMATAASSSSLEKSYELPDGQ 247
Cdd:cd10216   164 EGFALPHSIRRVDIAGRDVTEYLQLLLRKSGYNFHTSAEFEIVREIKEKACYVALNP-QKEEKLEEEKTEKAQYTLPDGS 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 248 VITIGNERFRCPEALFQPSFLGMEACGIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMK 327
Cdd:cd10216   243 TIEIGPERFRAPEILFNPELIGLEYPGVHEVLVDSIQKSDLDLRKTLYSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDVK 322
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1983980495 328 IKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKC 375
Cdd:cd10216   323 IRISAPPERLYSTWIGGSILASLSTFKKMWVSKKEYEEDGARILHRKT 370
Actin pfam00022
Actin;
6-376 0e+00

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 578.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495   6 VAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGmgqKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEK 85
Cdd:pfam00022   1 VSALVIDNGSHTTRAGFAGEDAPKAVIPSCVGKPRGTKVEAA---NKYYVGDEALTYRPGMEVRSPVEDGIVVDWDAMEE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  86 IWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVP 165
Cdd:pfam00022  78 IWEHVLKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 166 IYEGYALPHAILRLDLAGRDLTDYLMKILTER------------------------------GYSFTTTAEREIVRDIKE 215
Cdd:pfam00022 158 VHDGYVLQKAIRRSDLGGDFLTDYLRELLRSRnieitprylikskkpgdpapavtkrelpdtTYSYKTYQERRVLEEIKE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 216 KLCYVALDFeqEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGME--------ACGIHETTYNSIMKCD 287
Cdd:pfam00022 238 SVCYVSDDP--FGDETTSSSIPTRVYELPDGSTIILGAERFRVPEILFNPSLIGSEselpppqtAVGIPELIVDAINACD 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 288 VDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPP---ERKYSVWIGGSILASLSTFQQMWISKQEYD 364
Cdd:pfam00022 316 VDLRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVKIIAPGntvERRYSAWIGGSILASLGTFQQMWVSKQEYE 395
                         410
                  ....*....|..
gi 1983980495 365 ESGPSIVHRKCF 376
Cdd:pfam00022 396 EHGASVVERKCK 407
ASKHA_NBD_Arp2 cd10220
nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, ...
9-371 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: 528.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495   9 LVVDNGSGMCKAGFAGDDAPRAVFPSIVGRP--RHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 86
Cdd:cd10220     3 VVCDNGTGFVKCGFAGSNFPEHVFPSLVGRPilRAEEKVGDIEIKDIMVGDEASELRSMLEVTYPMENGIVRNWDDMEHL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  87 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 166
Cdd:cd10220    83 WDYTFGEKLKIDPRECKILLTEPPMNPTKNREKMVEVMFEKYGFAGVYVAIQAVLTLYAQGLLTGVVVDSGDGVTHIVPV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 167 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDG 246
Cdd:cd10220   163 YEGFSLPHLTRRLDVAGRDITRYLIKLLLLRGYAFNRTADFETVREIKEKLCYVAYDIELEQKLALETTVLVESYTLPDG 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 247 QVITIGNERFRCPEALFQPSFLGMEACGIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITAL----- 321
Cdd:cd10220   243 RVIKVGGERFEAPEALFQPHLIDVEGPGIAELLFNTIQAADIDTRPELYKHIVLSGGSTMYPGLPSRLEKEIKQLylerv 322
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1983980495 322 ------APSTMKIKIIAPPERKYSVWIGGSILASLSTFQ-QMWISKQEYDESGPSIV 371
Cdd:cd10220   323 lkgdteRLSKFKIRIEDPPRRKHMVFLGGAVLADIMKDKdEFWITRQEYEEQGVRVL 379
PTZ00466 PTZ00466
actin-like protein; Provisional
9-376 9.06e-178

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 499.08  E-value: 9.06e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495   9 LVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWH 88
Cdd:PTZ00466   15 IIIDNGTGYIKAGFAGEDVPNLVFPSYVGRPKYKRVMAGAVEGNIFVGNKAEEYRGLLKVTYPINHGIIENWNDMENIWI 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  89 HTfYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYE 168
Cdd:PTZ00466   95 HV-YNSMKINSEEHPVLLTEAPLNPQKNKEKIAEVFFETFNVPALFISIQAILSLYSCGKTNGTVLDCGDGVCHCVSIYE 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 169 GYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSlEKSYELPDGQV 248
Cdd:PTZ00466  174 GYSITNTITRTDVAGRDITTYLGYLLRKNGHLFNTSAEMEVVKNMKENCCYVSFNMNKEKNSSEKALT-TLPYILPDGSQ 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 249 ITIGNERFRCPEALFQPSFLGMEACGIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKI 328
Cdd:PTZ00466  253 ILIGSERYRAPEVLFNPSILGLEYLGLSELIVTSITRADMDLRRTLYSHIVLSGGTTMFHGFGDRLLNEIRKFAPKDITI 332
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1983980495 329 KIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF 376
Cdd:PTZ00466  333 RISAPPERKFSTFIGGSILASLATFKKIWISKQEFDEYGSVILHRKTF 380
PTZ00452 PTZ00452
actin; Provisional
8-376 1.05e-176

actin; Provisional


Pssm-ID: 185631  Cd Length: 375  Bit Score: 496.20  E-value: 1.05e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495   8 ALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIW 87
Cdd:PTZ00452    7 AVVIDNGSGYCKIGIAGDDAPTSCFPAIVGRSKQNDGIFSTFNKEYYVGEEAQAKRGVLAIKEPIQNGIINSWDDIEIIW 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  88 HHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIY 167
Cdd:PTZ00452   87 HHAFYNELCMSPEDQPVFMTDAPMNSKFNRERMTQIMFETFNTPCLYISNEAVLSLYTSGKTIGLVVDSGEGVTHCVPVF 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 168 EGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQ 247
Cdd:PTZ00452  167 EGHQIPQAITKINLAGRLCTDYLTQILQELGYSLTEPHQRIIVKNIKERLCYTALDPQDEKRIYKESNSQDSPYKLPDGN 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 248 VITIGNERFRCPEALFQPSFLGMEACGIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMK 327
Cdd:PTZ00452  247 ILTIKSQKFRCSEILFQPKLIGLEVAGIHHLAYSSIKKCDLDLRQELCRNIVLSGGTTLFPGIANRLSNELTNLVPSQLK 326
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1983980495 328 IKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF 376
Cdd:PTZ00452  327 IQVAAPPDRRFSAWIGGSIQCTLSTQQPQWIKRQEYDEQGPSIVHRKCF 375
ASKHA_NBD_ACTL7 cd10214
nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ...
4-375 3.03e-173

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: 486.93  E-value: 3.03e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495   4 EEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDM 83
Cdd:cd10214     1 KETKAVIIDLGTGYCKAGFAGQPRPSYVISSTVGKPPQESAKTGDNRKETFVGKELANVEPPLKLVNPLRHGIVVDWDCV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  84 EKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHT 163
Cdd:cd10214    81 QDIWEYIFEKEMKILPEEHAVLVSDPPLSPTTNREKYAELMFETFSIPAMHIAYQSRLSLYSYGRTSGLVVESGHGVSYV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 164 VPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTaEREIVRDIKEKLCYVALDFEQEMATAASSSSLEksYEL 243
Cdd:cd10214   161 VPIHEGYNLPHITGRADYAGSDLTAYLMKLLNEAGNKFTDD-QLHIVEDIKKKCCYVALDFEEEMGLPPQEYTVD--YEL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 244 PDGQVITIGNERFRCPEALFQPSFLGMEACGIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAP 323
Cdd:cd10214   238 PDGHLITIGKERFRCPEMLFNPSLIGSKQPGLHTLTMNSLNKCDANLKKDLAKNILLCGGSTMFDGFPDRFQKELSKLCP 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1983980495 324 STMKIkIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKC 375
Cdd:cd10214   318 NDNPI-VAASPERKYSVWTGGSILASLKSFQQLWVRRREYEERGPFVIYRKC 368
ASKHA_NBD_actin-like cd10169
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ...
9-367 1.30e-162

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: 455.80  E-value: 1.30e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495   9 LVVDNGSGMCKAGFAGDDAPRAVFPsivgrprhqgvmvgmgqkdsyvgdeaqskrgiltlkypiehgivtnWDDMEKIWH 88
Cdd:cd10169     1 IVIDNGSGTIKAGFAGEDAPRLIFP----------------------------------------------WDDMEKIWE 34
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  89 HTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYE 168
Cdd:cd10169    35 HVFYNLLRVDPEEHPVLLTEPPLNPKANREKLAEILFETFNVPSLYIANQAVLSLYASGRTTGLVVDSGEGVTHIVPVYE 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 169 GYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLcyvaldfeqemataassssleksyelpdgqv 248
Cdd:cd10169   115 GYVLPHAVRRLDIGGRDLTDYLAKLLREKGYSFSTSAEREIVRDIKEKL------------------------------- 163
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 249 itignerfrcpealfqpsflgmeaCGIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKI 328
Cdd:cd10169   164 ------------------------CGLHELIYDSIMKCDIDLRKELYSNIVLSGGTTLFPGFAERLQKELSKLAPSSVKV 219
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1983980495 329 KIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESG 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 ...
4-367 5.99e-161

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: 457.41  E-value: 5.99e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495   4 EEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVG-RPRHQGVMVGMGQKDS-----YVGDEA-QSKRGILTLKYPIEHGI 76
Cdd:cd13395     2 DEVGALVLDIGSYSTRAGYAGEDTPKAVFPSVVGvVTDDDDAEDYVGGSGEkkrkyYIGTNSiGVPRPNMEVISPLKDGL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  77 VTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDS 156
Cdd:cd13395    82 IEDWDAFEKLWDHALKNRLRVDPSEHPLLLTEPSWNTRANREKLTELMFEKYNVPAFFLAKNAVLSAFANGRSTALVVDS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 157 GDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGY--------------------------------SFTTT 204
Cdd:cd13395   162 GATSTSVVPVHDGYVLQKAIVRSPLGGDFLTDQLLKLLESKNIeiiprymikskepveggapakytkkdlpnttsSYHRY 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 205 AEREIVRDIKEKLCYVALDFEQEmatAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFL---------GMEACGI 275
Cdd:cd13395   242 MVRRVLQDFKESVCQVSDSPFDE---SEAASIPTVSYELPDGYNIEFGAERFKIPELLFDPSLVkgipappseGNELLGL 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 276 HETTYNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPP---ERKYSVWIGGSILASLST 352
Cdd:cd13395   319 PQLVYTSIGSCDVDIRPELYGNVVLTGGNSLLPGFTDRLNRELSEKAPGSLKLKILASGntvERRFSSWIGGSILASLGS 398
                         410
                  ....*....|....*
gi 1983980495 353 FQQMWISKQEYDESG 367
Cdd:cd13395   399 FQQMWISKQEYEEHG 413
COG5277 COG5277
Actin-related protein [Cytoskeleton];
10-366 2.46e-142

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 410.72  E-value: 2.46e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  10 VVDNGSGMCKAG-FAGDDAP-----RAVFPSIVGRPRHQGVMVGMGqKDSYVGDEAQS-----KRGILTLKYPIEHGIVT 78
Cdd:COG5277    12 GIDFGTSYVKYGpIALEEKPrviqtRGLFLRIVGESKLLGPMEGLS-RGLVVGDEVSKylssvRDAIRNLKYPLRDGIVR 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  79 -----NWDDMEKIWHHTFYNELRVAPEEHP--VLLTEAPLNPKANREKMTQIMFETF---NTPAMYVAIQAVLSLYASGR 148
Cdd:COG5277    91 rddedAWRVLKELLRYTFAQFLVVDPEFHGflVVVALSALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPLAVAIAEKA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 149 TTGIVLDSGDGVSHTVPIYEGyALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEReIVRDIKEKLCYVALDFEQEM 228
Cdd:COG5277   171 VTCVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSDTAREEY-VVRVVKEALGLVPRDLAKAI 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 229 -ATAASSSSLEKSYELPDGQV-ITIGN---ERFRCPEALFQPSFLGMEAC----------------------GIHETTYN 281
Cdd:COG5277   249 qKAASNPDSFEAKVRLPNPTVeIELGNyawERFLIGEILFNPNHEGFESYiqqgrlriedavigdvvlygemGLAEAIIN 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 282 SIMKCDVDIRKDLYANTVLSGGTTMY---PGIAD-------RMQKEITALAPsTMKIKIIAPPERKYSVWIGGSILASLS 351
Cdd:COG5277   329 SIMKCDVEIQDELYSNIILSGGAFNWsvpPGLEDvavdsvtRVQIELSELAP-ELKVNVRLVSDPQYSVWKGAIIYGYAL 407
                         410
                  ....*....|....*..
gi 1983980495 352 TFQQMW--ISKQEYDES 366
Cdd:COG5277   408 PFSVKWswITKEGWYFL 424
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
8-371 1.37e-123

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: 362.27  E-value: 1.37e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495   8 ALVVDNGSGMCKAGFAGDDAPRAVFPSIVG-------RPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNW 80
Cdd:cd10221     1 AVVIDNGTGYTKMGYAGNTEPQFIIPTVIAikesakvGDGQRRSKKGIEDLDFYIGDEALANSPTYALKYPIRHGIVEDW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  81 DDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRT--------TGI 152
Cdd:cd10221    81 DLMERFWEQCIFKYLRCEPEDHYFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQAVLALAASWTSrkvgertlTGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 153 VLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAA 232
Cdd:cd10221   161 VIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREEGIPPEDSLEVAKRIKERYCYVCPDIVKEFAKYD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 233 SS-SSLEKSYELPD---GQ--VITIGNERFRCPEALFQPSFLGMEAC-GIHETTYNSIMKCDVDIRKDLYANTVLSGGTT 305
Cdd:cd10221   241 SDpAKYIKQYTGINsvtGKpyTVDVGYERFLAPEIFFNPEIASSDFTtPLPEVVDQVIQSCPIDTRRGLYKNIVLSGGST 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 306 MYPGIADRMQKEITA----------------LAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPS 369
Cdd:cd10221   321 MFKDFGRRLQRDVKRivdarlkaseelsggkLKPKPIDVNVISHPMQRYAVWFGGSMLASTPEFYTVCHTKAEYEEYGPS 400

                  ..
gi 1983980495 370 IV 371
Cdd:cd10221   401 IC 402
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
8-373 4.85e-122

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 358.66  E-value: 4.85e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495   8 ALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMV---GMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDME 84
Cdd:PTZ00280    6 VVVIDNGTGYTKMGYAGNTEPTYIIPTLIADNSKQSRRRskkGFEDLDFYIGDEALAASKSYTLTYPMKHGIVEDWDLME 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  85 KIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYAS----------GRTTGIVL 154
Cdd:PTZ00280   86 KFWEQCIFKYLRCEPEEHYFILTEPPMNPPENREYTAEIMFETFNVKGLYIAVQAVLALRASwtskkakelgGTLTGTVI 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 155 DSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMAT---- 230
Cdd:PTZ00280  166 DSGDGVTHVIPVVDGYVIGSSIKHIPLAGRDITNFIQQMLRERGEPIPAEDILLLAQRIKEKYCYVAPDIAKEFEKydsd 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 231 --------AASSSSLEKSYElpdgqvITIGNERFRCPEALFQPSFLGME-ACGIHETTYNSIMKCDVDIRKDLYANTVLS 301
Cdd:PTZ00280  246 pknhfkkyTAVNSVTKKPYT------VDVGYERFLGPEMFFHPEIFSSEwTTPLPEVVDDAIQSCPIDCRRPLYKNIVLS 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 302 GGTTMYPGIADRMQKEITA----------------LAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDE 365
Cdd:PTZ00280  320 GGSTMFKGFDKRLQRDVRKrvdrrlkkaeelsggkLKPIPIDVNVVSHPRQRYAVWYGGSMLASSPEFEKVCHTKAEYDE 399

                  ....*...
gi 1983980495 366 SGPSIVHR 373
Cdd:PTZ00280  400 YGPSICRY 407
ASKHA_NBD_Arp6 cd10210
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ...
9-367 4.05e-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: 301.78  E-value: 4.05e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495   9 LVVDNGSGMCKAGFAGDDAPRaVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQskrgiLTLKYPIEHGIVTNWDDMEKIWH 88
Cdd:cd10210     2 LVLDNGAYTIKAGFASDDPPR-VIPNCIAKPKSERRRLFGDDQLDECKDLSG-----LFYRRPFERGYLVNWDLQRQIWD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  89 HTFYNE-LRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYA----------SGRTTGIVLDSG 157
Cdd:cd10210    76 HLFGKLlLNVDPSDTALVLTEPPFNPPSIQEAMDEIVFEEYGFQSLYRTTAAALSAFAyladseqsssSSSQCCLVVDSG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 158 DGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFtttaERE--IVRDIKEKLCYVALDFEQEMATAAS-- 233
Cdd:cd10210   156 FSFTHIVPFFDGKPVKRAVRRIDVGGKLLTNYLKEIISYRQLNV----MDEtyLVNQIKEDLCFVSTDFYEDLEIAKKkg 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 234 -SSSLEKSYELPDG-----------------------QVITIGNERFRCPEALFQPSFLGMEACGIHETTYNSIMKCDVD 289
Cdd:cd10210   232 kENTIRRDYVLPDYttskrgyvrdpeepnrgklkedeQVLRLNNERFTVPELLFHPSDIGIQQAGIAEAIVQSINACPEE 311
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1983980495 290 IRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESG 367
Cdd:cd10210   312 LQPLLYANIVLTGGNALFPGFRERLEAELRSLAPDDYDVNVTLPEDPITYAWEGGSLLAQSPEFEELAVTRAEYEEHG 389
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
9-372 3.81e-89

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: 272.73  E-value: 3.81e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495   9 LVVDNGSGMCKAGFAGDDApravFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSkrgiltlkyPIEHGIVTNWDDMEKIWH 88
Cdd:cd10209     1 VVIDAGSRLLKAGYAYPDR----EPSVVEPTRVTPAVEDGEESDTVVEGNTVS---------PIRRGRIEDWDALEALLR 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  89 HTFYNELR-VAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIY 167
Cdd:cd10209    68 YVFYTGLGwEEGNEGQVLIAEPLLTSKAERERLTQLMFETFNVSGLYASEQAVLSLYAVGRISGCVVDVGHGKIDIAPVW 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 168 EGYALPHAILRLDLAGRDLTDYLMKILTERGYSftTTAEREIVRDIKEKLCYVALDFEQEMATAASSSslEKSYELPDGQ 247
Cdd:cd10209   148 EGAIQHNAVRRFEIGGRDLTELLAAELGKSNPK--VKLDRSIVERLKEAVAWSADDEEAYEKKVLTCS--PETYTLPDGR 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 248 VITIGNERFRCPEALFQPSFLGMEACGIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMK 327
Cdd:cd10209   224 VISVGKERYCVGEALFRPSILGIEEYGIVEQLVRAVSTSPSENRRQLLENIVLCGGTSSVPGLEARLQKEIRLLSSPSSR 303
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1983980495 328 IKIIAPPE------RKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVH 372
Cdd:cd10209   304 PALVKPPEympentLRYSAWIGGAILAKVVFPQNQHVTKADYDETGPSVVH 354
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
8-368 1.81e-74

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: 234.39  E-value: 1.81e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495   8 ALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQgvmvGMGQKDSYVGDEA---QSKRGilTLKYPIEHGIVTNWDDME 84
Cdd:cd10211     1 PIVIDNGSYQCRAGWAGDKEPRLVFRNLVAKPRDR----KKGITVTLVGNDIlndEAVRS--HLRSPFDRNVVTNFDLQE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  85 KIWHHTFyNELRVAPE---EHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRT----TGIVLDSG 157
Cdd:cd10211    75 QILDYIF-SHLGINSEgsvDHPIVLTEALCNPNYSRQLMSELLFECYGVPSVAYGIDSLFSYYHNQPQgdpsDGLVISSG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 158 DGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTT--TAEReiVRDIKEKLCYVALDFEQEMATAASSS 235
Cdd:cd10211   154 YSTTHVIPVLNGRLDLSQCKRINLGGFHATDYLQRLLQLKYPTHPSaiTLSR--AEELVHEHCYVAEDYDEELKKWEDPE 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 236 SLEKSyelpdgqvitigNERFRCPealFqpsflgmeacGIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQ 315
Cdd:cd10211   232 YYEEN------------VRKIQLP---F----------GLVETIEFVLKRYPAEQQDRLVQNVFLTGGNALFPGLKERLE 286
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1983980495 316 KEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGP 368
Cdd:cd10211   287 KELRAIRPFGSPFNVVRAKDPVLDAWRGAAKWALDSTFEKVWITKQEYEEKGG 339
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
39-374 1.43e-57

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: 191.37  E-value: 1.43e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  39 PRHQGVMVGMGQKDSYVGD--EAQSKRGILtlkYPIEHGIVTNWDDMEKIWHHTFYNEL--RVAPEEHPVLLTEAPLNPK 114
Cdd:cd10208     7 PGSQTTRAGLGLGELLTPPtiEIPTRVEII---WPIQDGRVVDWDALEALWRHILFSLLsiPRPTNNSPVLLSVPPSWSK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 115 ANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKIL 194
Cdd:cd10208    84 SDLELLTQLFFERLNVPAFAILEAPLAALYAAGATSGIVVDIGHEKTDITPIVDSQVVPHALVSIPIGGQDCTAHLAQLL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 195 TER--GYSFTTTAEREIVRDIKEKLcyvaldFEQEMATAASSSSleksyELPDGQVITIGNERFRCPEALFQPSFLGM-- 270
Cdd:cd10208   164 KSDepELKSQAESGEEATLDLAEAL------KKSPICEVLSDGA-----DLASGTEITVGKERFRACEPLFKPSSLRVdl 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 271 --EACGIHETTYNSimkCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITAL-----------APSTMKIKIIaP---P 334
Cdd:cd10208   233 liAAIAGALVLNAS---DEPDKRPALWENIIIVGGGSRIRGLKEALLSELQQFhlisetsaspqQPRIIRLAKI-PdyfP 308
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1983980495 335 ERK-----YSVWIGGSILASLsTF----QQMWISKQEYDESGPSIVHRK 374
Cdd:cd10208   309 EWKksgyeEAAFLGASIVAKL-VFndpsSKHYISKVDYNEKGPAAIHTK 356
ASKHA_NBD_Arp10 cd10207
nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins; ...
10-367 2.59e-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: 172.82  E-value: 2.59e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  10 VVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRhqgvmvgmGQKDSYVGDeaqsKRGILTLKypiehgivtnWDDM-EKIWH 88
Cdd:cd10207     2 VLDIGSAYTKCGFAGESAPRCIIPSEVKLPG--------GKKVIRVVD----QRSGNEEE----------LYEAlKEFLH 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  89 HTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYE 168
Cdd:cd10207    60 ELYFKHLLVNPKDRRVVVVESVLCPTPFRETLAKVLFKHFEVPSVLFAPSHLLSLLTLGIRTALVVDCGYRETRVLPVYE 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 169 GYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAER------------EIVRDIKEKLCYVA-LDFEQEMATAASSS 235
Cdd:cd10207   140 GVPLLSAWQSTPLGGKALHKRLKKLLLEHATVVTGDNKGqllssvdsllseEVLEDIKVRACFVTsLERGKTLQSATEEG 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 236 SLEKS-------YELPDGQVITIGNERFRCPEALFqpsFLGMEAC-GIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMY 307
Cdd:cd10207   220 STEEPsppppvdYPLDGEKILIVPGSIRESAEELL---FEGDNEEkSLPTLILDSLLKCPIDVRKQLAENIVVIGGTSML 296
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1983980495 308 PGIADRMQKEITA----------LAPSTMKI---KIIAPPErkYSVWIGGSILASLSTFQQMWISKQEYDESG 367
Cdd:cd10207   297 PGFKHRLLEELRAllrkpkyfeeLAPKTFRFhtpPSVFKPN--YLAWLGGSIFGALESILGRSLSREAYLQTG 367
ASKHA_NBD_AtArp8-like cd13396
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and ...
90-367 4.65e-48

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: 165.80  E-value: 4.65e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  90 TFYNELRVAPEEHPVLLTEaPL-------NPKANREKMTQIMFETF---NTPAMYVAIQAVLSLYASGRTTGIVLDSGDG 159
Cdd:cd13396    47 TIMTRMQVKPSRQPVVVSL-PLchsddteSAAASRRQLRGTIFNVLfdmNVPAVCAVDQAVLALYAANRTSGIVVNIGFR 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 160 VSHTVPIYEGYALPH-AILRLDLAGRDLTDYLMKILTERGYSFTTTAereIVRDIKEKLCYVALDFEQEMAtaassSSLE 238
Cdd:cd13396   126 VTTIVPVYRGRVMHDiGVEVVGQGALRLTGFLKELMQQNGIRFPSLY---TVRTIKEKLCYVAEDYEAELA-----KDTQ 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 239 KSYELPDGQVITIGNERFRCPEALFQPSFLGMEACGIHETTYNSIMKCDVDIR---KDLYANTVLSGGTTMYPGIADRMQ 315
Cdd:cd13396   198 ASCEVAGEGWFTLSNERFKTGEILFQPGLGGMRAMGLHQAVALCMDHCALVHSqgdDGWFKTIVLSGGSACLPGLSERLE 277
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1983980495 316 KEITALAPSTMK--IKIIAPPERKYSVWIGGSILASLSTFQQMW-ISKQEYDESG 367
Cdd:cd13396   278 RELRKLLPKSLSegIRIIPPPLGPDSAWQGAKLISNLSNFPDGWcITKKQFRNKP 332
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
304-375 2.45e-35

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: 126.25  E-value: 2.45e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1983980495 304 TTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKC 375
Cdd:NF040575   61 RVNESGFYEKLKKSITEKAPKGALIGMTLDPKPESAAWRGAAMYAASEGFVEMAITKQEYDESGPSIVHRKC 132
ASKHA_NBD_Arp8-like cd10206
nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The ...
49-370 3.20e-27

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: 111.95  E-value: 3.20e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  49 GQKDSYVGDEAQ--SKRGILTLKYPIEHGiVTNW-----------DDMEKIWHHTFYNELRVAPEEHP----VLLTEAPL 111
Cdd:cd10206   118 DYPDFLVGEEALrlPPSEEYNLHWPIRRG-RLNVhsdggsltavlDDLEDIWSHALEEKLEIPRKDLKnyraVLVIPDLF 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 112 NpKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLM 191
Cdd:cd10206   197 D-RRHVKELVDLLLRRLGFSSVFVHQESVCATFGAGLSSACVVDIGAQKTSVACVEDGLSIPNSRIRLPYGGDDITRCFL 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 192 KILTERGY-----SFTTTAEREIVRDIKEKLCYValdfeqemataassssleksyelpDGQVITIGNERF--RCPealFQ 264
Cdd:cd10206   276 WLLRRSGFpyrecNLNSPLDFLLLERLKETYCTL------------------------DQDDIGVQLHEFyvREP---GQ 328
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 265 PSFL-GMEACGIHETTYNSIMKC-DVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMK----IKIIAPPERK- 337
Cdd:cd10206   329 PTLKyQFKLLPLDEAIVQSILSCaSDELKRKMYSSILLVGGGAKIPGLAEALEDRLLIKIPSLFEavetVEVLPPPKDMd 408
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1983980495 338 --YSVWIGGSILASLSTFQQMWISKQEYDESGPSI 370
Cdd:cd10206   409 psLLAWKGGAVLACLDSAQELWITRKEWQRLGVRA 443
ASKHA_NBD_ScArp7-like cd10212
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and ...
9-364 8.82e-20

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: 90.16  E-value: 8.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495   9 LVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGvmvgmGQKDSYVG-----DEAQSKR-GILTLKYPIEHGIVTNWDD 82
Cdd:cd10212     6 VVIHNGSHRTVAGFSNVELPQCIIPSSYIKRTDEG-----GEAEFIFGtynmiDAAAEKRnGDEVYTLVDSQGLPYNWDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  83 MEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANR---EKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDG 159
Cdd:cd10212    81 LEMQWRYLYDTQLKVSPEELPLVITMPATNGKPDMailERYYELAFDKLNVPVFQIVIEPLAIALSMGKSSAFVIDIGAS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 160 VSHTVPIYEGYALPHAILRLDLAGrDLTDYLM---------------------KILTERGYSFTT--------------- 203
Cdd:cd10212   161 GCNVTPIIDGIVVKNAVVRSKFGG-DFLDFQVherlaplikeendmenmadeqKRSTDVWYEASTwiqqfkstmlqvsek 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 204 ----------------TAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKsyelPDGQVITIG-NERFRCPEALFQPS 266
Cdd:cd10212   240 dlfeleryykeqadiyAKQQEQLKQMDQQLQYTALTGSPNNPLVQKKNFLFK----PLNKTLTLDlKECYQFAEYLFKPQ 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 267 FLGMEAC---GIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAP----STMKIKIIAppERKYS 339
Cdd:cd10212   316 LISDKFSpedGLGPLMAKSVKKAPEQVYSLLLTNVIITGSTSLIEGMEQRIIKELSIRFPqyklTTFANQVMM--DRKIQ 393
                         410       420
                  ....*....|....*....|....*.
gi 1983980495 340 VWIGGSILASLSTFQ-QMWISKQEYD 364
Cdd:cd10212   394 GWLGALTMANLPSWSlGKWYSKEDYE 419
ASKHA_NBD_MamK cd24009
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ...
16-317 2.10e-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: 58.38  E-value: 2.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  16 GMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGqKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDmekiwhhtfyNEL 95
Cdd:cd24009     9 GTSRSAVVTSRGKRFSFRSVVGYPKDIIARKLLG-KEVLFGDEALENRLALDLRRPLEDGVIKEGDD----------RDL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495  96 RVAPE--EHPVLLTEAPLNPK-------------ANREKMTQIMFETFNTPAMYVAIQAVlsLYASGRTTG-IVLDSGDG 159
Cdd:cd24009    78 EAAREllQHLIELALPGPDDEiyavigvparasaENKQALLEIARELVDGVMVVSEPFAV--AYGLDRLDNsLIVDIGAG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 160 VSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTER--GYSFTttaeREIVRDIKEKLCYValdfeqemataaSSSSL 237
Cdd:cd24009   156 TTDLCRMKGTIPTEEDQITLPKAGDYIDEELVDLIKERypEVQLT----LNMARRWKEKYGFV------------GDASE 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980495 238 EKSYELP-DGQVIT--IGNE-RFRCpEALFQPsflgmeacgIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADR 313
Cdd:cd24009   220 PVKVELPvDGKPVTydITEElRIAC-ESLVPD---------IVEGIKKLIASFDPEFQEELRNNIVLAGGGSRIRGLDTY 289

                  ....
gi 1983980495 314 MQKE 317
Cdd:cd24009   290 IEKA 293
 
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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