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Conserved domains on  [gi|6671509|ref|NP_031419|]
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actin, cytoplasmic 1 [Mus musculus]

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: 938.33  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509    6 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 85
Cdd:cd10224   1 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   86 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPI 165
Cdd:cd10224  81 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  166 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDG 245
Cdd:cd10224 161 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  246 QVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTM 325
Cdd:cd10224 241 QVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTM 320
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 6671509  326 KIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIV 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: 938.33  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509    6 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 85
Cdd:cd10224   1 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   86 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPI 165
Cdd:cd10224  81 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  166 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDG 245
Cdd:cd10224 161 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  246 QVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTM 325
Cdd:cd10224 241 QVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTM 320
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 6671509  326 KIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIV 370
Cdd:cd10224 321 KIKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIV 365
PTZ00281 PTZ00281
actin; Provisional
1-375 0e+00

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 776.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509     1 MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWD 80
Cdd:PTZ00281   2 DGEDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509    81 DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVT 160
Cdd:PTZ00281  82 DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   161 HTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSY 240
Cdd:PTZ00281 162 HTVPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEMQTAASSSALEKSY 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   241 ELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITAL 320
Cdd:PTZ00281 242 ELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELTAL 321
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6671509   321 APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF 375
Cdd:PTZ00281 322 APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIVHRKCF 376
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
6-375 0e+00

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 658.56  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509       6 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGmGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 85
Cdd:smart00268   2 PAIVIDNGSGTIKAGFAGEDFPQVVFPSIVGRPKDGKGMVG-DAKDIFVGDEAQEKRGGLELKYPIENGIVENWDDMEKI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509      86 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPI 165
Cdd:smart00268  81 WDYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVPV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509     166 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAAS---SSSLEKSYEL 242
Cdd:smart00268 161 VDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLAREsseSSKLEKTYEL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509     243 PDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAP 322
Cdd:smart00268 241 PDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELKQLAP 320
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 6671509     323 STMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF 375
Cdd:smart00268 321 KKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERKCF 373
Actin pfam00022
Actin;
5-375 0e+00

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 578.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509      5 IAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGmgqKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEK 84
Cdd:pfam00022   1 VSALVIDNGSHTTRAGFAGEDAPKAVIPSCVGKPRGTKVEAA---NKYYVGDEALTYRPGMEVRSPVEDGIVVDWDAMEE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509     85 IWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVP 164
Cdd:pfam00022  78 IWEHVLKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509    165 IYEGYALPHAILRLDLAGRDLTDYLMKILTER------------------------------GYSFTTTAEREIVRDIKE 214
Cdd:pfam00022 158 VHDGYVLQKAIRRSDLGGDFLTDYLRELLRSRnieitprylikskkpgdpapavtkrelpdtTYSYKTYQERRVLEEIKE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509    215 KLCYVALDFeqEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMES--------CGIHETTFNSIMKCD 286
Cdd:pfam00022 238 SVCYVSDDP--FGDETTSSSIPTRVYELPDGSTIILGAERFRVPEILFNPSLIGSESelpppqtaVGIPELIVDAINACD 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509    287 VDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPP---ERKYSVWIGGSILASLSTFQQMWISKQEYD 363
Cdd:pfam00022 316 VDLRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVKIIAPGntvERRYSAWIGGSILASLGTFQQMWVSKQEYE 395
                         410
                  ....*....|..
gi 6671509    364 ESGPSIVHRKCF 375
Cdd:pfam00022 396 EHGASVVERKCK 407
COG5277 COG5277
Actin-related protein [Cytoskeleton];
9-365 1.99e-142

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 410.72  E-value: 1.99e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509    9 VVDNGSGMCKAG-FAGDDAP-----RAVFPSIVGRPRHQGVMVGMGqKDSYVGDEAQS-----KRGILTLKYPIEHGIVT 77
Cdd:COG5277  12 GIDFGTSYVKYGpIALEEKPrviqtRGLFLRIVGESKLLGPMEGLS-RGLVVGDEVSKylssvRDAIRNLKYPLRDGIVR 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   78 -----NWDDMEKIWHHTFYNELRVAPEEHP--VLLTEAPLNPKANREKMTQIMFETF---NTPAMYVAIQAVLSLYASGR 147
Cdd:COG5277  91 rddedAWRVLKELLRYTFAQFLVVDPEFHGflVVVALSALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPLAVAIAEKA 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  148 TTGIVMDSGDGVTHTVPIYEGyALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEReIVRDIKEKLCYVALDFEQEM 227
Cdd:COG5277 171 VTCVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSDTAREEY-VVRVVKEALGLVPRDLAKAI 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  228 -ATAASSSSLEKSYELPDGQV-ITIGN---ERFRCPEALFQPSFLGMESC----------------------GIHETTFN 280
Cdd:COG5277 249 qKAASNPDSFEAKVRLPNPTVeIELGNyawERFLIGEILFNPNHEGFESYiqqgrlriedavigdvvlygemGLAEAIIN 328
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  281 SIMKCDVDIRKDLYANTVLSGGTTMY---PGIAD-------RMQKEITALAPsTMKIKIIAPPERKYSVWIGGSILASLS 350
Cdd:COG5277 329 SIMKCDVEIQDELYSNIILSGGAFNWsvpPGLEDvavdsvtRVQIELSELAP-ELKVNVRLVSDPQYSVWKGAIIYGYAL 407
                       410
                ....*....|....*..
gi 6671509  351 TFQQMW--ISKQEYDES 365
Cdd:COG5277 408 PFSVKWswITKEGWYFL 424
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
303-374 2.59e-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: 125.86  E-value: 2.59e-35
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6671509   303 TTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKC 374
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 ...
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: 938.33  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509    6 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 85
Cdd:cd10224   1 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   86 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPI 165
Cdd:cd10224  81 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  166 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDG 245
Cdd:cd10224 161 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  246 QVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTM 325
Cdd:cd10224 241 QVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTM 320
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 6671509  326 KIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIV 370
Cdd:cd10224 321 KIKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIV 365
PTZ00281 PTZ00281
actin; Provisional
1-375 0e+00

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 776.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509     1 MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWD 80
Cdd:PTZ00281   2 DGEDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509    81 DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVT 160
Cdd:PTZ00281  82 DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   161 HTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSY 240
Cdd:PTZ00281 162 HTVPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEMQTAASSSALEKSY 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   241 ELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITAL 320
Cdd:PTZ00281 242 ELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELTAL 321
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6671509   321 APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF 375
Cdd:PTZ00281 322 APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIVHRKCF 376
ASKHA_NBD_actin_Arp-T1-3 cd13397
nucleotide-binding domain (NBD) of actin, actin-related proteins T1-T3 (Arp-T1-3), and similar ...
6-366 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: 775.59  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509    6 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 85
Cdd:cd13397   1 PAVVIDNGSGLIKAGFAGEDLPRAVFPSVVGRPKYKAVMLGAGQKEVYVGDEAQEKRGVLTLSYPIEHGIVTNWDDMEKI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   86 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPI 165
Cdd:cd13397  81 WHHTFENELRVKPEEHPVLLTEAPLNPKQNREKMAEIMFETFGVPAFYVAIQAVLSLYSSGRTTGLVLDSGDGVTHTVPI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  166 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMatAASSSSLEKSYELPDG 245
Cdd:cd13397 161 YEGYALPHAVQRLDLAGRDLTEYLMKLLKERGHSFTTTAEREIVRDIKEKLCYVALDYEEEL--KKKSEELEKEYTLPDG 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  246 QVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTM 325
Cdd:cd13397 239 QVIKIGSERFRCPEALFRPSLIGREAPGIHKLVYNSIMKCDIDIRKDLYSNIVLSGGSTMFPGLPERLQKELEALAPSST 318
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 6671509  326 KIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESG 366
Cdd:cd13397 319 KVKVIAPPERKYSVWIGGSILASLSTFKSMWITRAEYDEFG 359
PTZ00004 PTZ00004
actin-2; Provisional
1-375 0e+00

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 713.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509     1 MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWD 80
Cdd:PTZ00004   2 SVEETNAAVVDNGSGMVKAGFAGDDAPRCVFPSIVGRPKNPGIMVGMEEKDCYVGDEAQDKRGILTLKYPIEHGIVTNWD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509    81 DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVT 160
Cdd:PTZ00004  82 DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETHNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   161 HTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSL-EKS 239
Cdd:PTZ00004 162 HTVPIYEGYSLPHAIHRLDVAGRDLTEYMMKILHERGTTFTTTAEKEIVRDIKEKLCYIALDFDEEMGNSAGSSDKyEES 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   240 YELPDGQVITIGNERFRCPEALFQPSFLGMESC-GIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEIT 318
Cdd:PTZ00004 242 YELPDGTIITVGSERFRCPEALFQPSLIGKEEPpGIHELTFQSINKCDIDIRKDLYGNIVLSGGTTMYRGLPERLTKELT 321
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 6671509   319 ALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF 375
Cdd:PTZ00004 322 TLAPSTMKIKVVAPPERKYSVWIGGSILSSLPTFQQMWVTKEEYDESGPSIVHRKCF 378
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
6-375 0e+00

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 658.56  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509       6 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGmGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 85
Cdd:smart00268   2 PAIVIDNGSGTIKAGFAGEDFPQVVFPSIVGRPKDGKGMVG-DAKDIFVGDEAQEKRGGLELKYPIENGIVENWDDMEKI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509      86 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPI 165
Cdd:smart00268  81 WDYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVPV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509     166 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAAS---SSSLEKSYEL 242
Cdd:smart00268 161 VDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLAREsseSSKLEKTYEL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509     243 PDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAP 322
Cdd:smart00268 241 PDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELKQLAP 320
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 6671509     323 STMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF 375
Cdd:smart00268 321 KKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERKCF 373
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
8-374 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: 630.73  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509    8 LVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWH 87
Cdd:cd10216   4 VVIDNGSGVIKAGFAGDDIPKVVFPSYVGRPKHVRVMAGALEGDVFVGPKAEEHRGLLKIRYPMEHGIVTDWNDMERIWQ 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   88 HTFYNE-LRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIY 166
Cdd:cd10216  84 YVYSKLqLNTFSEEHPVLLTEAPLNPRKNREKAAEVFFETFNVPALFVSMQAVLSLYASGRTTGVVLDSGDGVTHAVPIY 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  167 EGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFeQEMATAASSSSLEKSYELPDGQ 246
Cdd:cd10216 164 EGFALPHSIRRVDIAGRDVTEYLQLLLRKSGYNFHTSAEFEIVREIKEKACYVALNP-QKEEKLEEEKTEKAQYTLPDGS 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  247 VITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMK 326
Cdd:cd10216 243 TIEIGPERFRAPEILFNPELIGLEYPGVHEVLVDSIQKSDLDLRKTLYSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDVK 322
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 6671509  327 IKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKC 374
Cdd:cd10216 323 IRISAPPERLYSTWIGGSILASLSTFKKMWVSKKEYEEDGARILHRKT 370
Actin pfam00022
Actin;
5-375 0e+00

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 578.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509      5 IAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGmgqKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEK 84
Cdd:pfam00022   1 VSALVIDNGSHTTRAGFAGEDAPKAVIPSCVGKPRGTKVEAA---NKYYVGDEALTYRPGMEVRSPVEDGIVVDWDAMEE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509     85 IWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVP 164
Cdd:pfam00022  78 IWEHVLKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509    165 IYEGYALPHAILRLDLAGRDLTDYLMKILTER------------------------------GYSFTTTAEREIVRDIKE 214
Cdd:pfam00022 158 VHDGYVLQKAIRRSDLGGDFLTDYLRELLRSRnieitprylikskkpgdpapavtkrelpdtTYSYKTYQERRVLEEIKE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509    215 KLCYVALDFeqEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMES--------CGIHETTFNSIMKCD 286
Cdd:pfam00022 238 SVCYVSDDP--FGDETTSSSIPTRVYELPDGSTIILGAERFRVPEILFNPSLIGSESelpppqtaVGIPELIVDAINACD 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509    287 VDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPP---ERKYSVWIGGSILASLSTFQQMWISKQEYD 363
Cdd:pfam00022 316 VDLRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVKIIAPGntvERRYSAWIGGSILASLGTFQQMWVSKQEYE 395
                         410
                  ....*....|..
gi 6671509    364 ESGPSIVHRKCF 375
Cdd:pfam00022 396 EHGASVVERKCK 407
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: 532.52  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509    8 LVVDNGSGMCKAGFAGDDAPRAVFPSIVGRP--RHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 85
Cdd:cd10220   3 VVCDNGTGFVKCGFAGSNFPEHVFPSLVGRPilRAEEKVGDIEIKDIMVGDEASELRSMLEVTYPMENGIVRNWDDMEHL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   86 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPI 165
Cdd:cd10220  83 WDYTFGEKLKIDPRECKILLTEPPMNPTKNREKMVEVMFEKYGFAGVYVAIQAVLTLYAQGLLTGVVVDSGDGVTHIVPV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  166 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDG 245
Cdd:cd10220 163 YEGFSLPHLTRRLDVAGRDITRYLIKLLLLRGYAFNRTADFETVREIKEKLCYVAYDIELEQKLALETTVLVESYTLPDG 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  246 QVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITAL----- 320
Cdd:cd10220 243 RVIKVGGERFEAPEALFQPHLIDVEGPGIAELLFNTIQAADIDTRPELYKHIVLSGGSTMYPGLPSRLEKEIKQLylerv 322
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6671509  321 ------APSTMKIKIIAPPERKYSVWIGGSILASLSTFQ-QMWISKQEYDESGPSIV 370
Cdd:cd10220 323 lkgdteRLSKFKIRIEDPPRRKHMVFLGGAVLADIMKDKdEFWITRQEYEEQGVRVL 379
PTZ00466 PTZ00466
actin-like protein; Provisional
8-375 6.49e-178

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 499.47  E-value: 6.49e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509     8 LVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWH 87
Cdd:PTZ00466  15 IIIDNGTGYIKAGFAGEDVPNLVFPSYVGRPKYKRVMAGAVEGNIFVGNKAEEYRGLLKVTYPINHGIIENWNDMENIWI 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509    88 HTfYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYE 167
Cdd:PTZ00466  95 HV-YNSMKINSEEHPVLLTEAPLNPQKNKEKIAEVFFETFNVPALFISIQAILSLYSCGKTNGTVLDCGDGVCHCVSIYE 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   168 GYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSlEKSYELPDGQV 247
Cdd:PTZ00466 174 GYSITNTITRTDVAGRDITTYLGYLLRKNGHLFNTSAEMEVVKNMKENCCYVSFNMNKEKNSSEKALT-TLPYILPDGSQ 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   248 ITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKI 327
Cdd:PTZ00466 253 ILIGSERYRAPEVLFNPSILGLEYLGLSELIVTSITRADMDLRRTLYSHIVLSGGTTMFHGFGDRLLNEIRKFAPKDITI 332
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 6671509   328 KIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF 375
Cdd:PTZ00466 333 RISAPPERKFSTFIGGSILASLATFKKIWISKQEFDEYGSVILHRKTF 380
PTZ00452 PTZ00452
actin; Provisional
1-375 1.61e-176

actin; Provisional


Pssm-ID: 185631  Cd Length: 375  Bit Score: 495.81  E-value: 1.61e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509     1 MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWD 80
Cdd:PTZ00452   1 MQAQYPAVVIDNGSGYCKIGIAGDDAPTSCFPAIVGRSKQNDGIFSTFNKEYYVGEEAQAKRGVLAIKEPIQNGIINSWD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509    81 DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVT 160
Cdd:PTZ00452  81 DIEIIWHHAFYNELCMSPEDQPVFMTDAPMNSKFNRERMTQIMFETFNTPCLYISNEAVLSLYTSGKTIGLVVDSGEGVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   161 HTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSY 240
Cdd:PTZ00452 161 HCVPVFEGHQIPQAITKINLAGRLCTDYLTQILQELGYSLTEPHQRIIVKNIKERLCYTALDPQDEKRIYKESNSQDSPY 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   241 ELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITAL 320
Cdd:PTZ00452 241 KLPDGNILTIKSQKFRCSEILFQPKLIGLEVAGIHHLAYSSIKKCDLDLRQELCRNIVLSGGTTLFPGIANRLSNELTNL 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6671509   321 APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF 375
Cdd:PTZ00452 321 VPSQLKIQVAAPPDRRFSAWIGGSIQCTLSTQQPQWIKRQEYDEQGPSIVHRKCF 375
ASKHA_NBD_ACTL7 cd10214
nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ...
5-374 1.00e-172

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: 485.77  E-value: 1.00e-172
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509    5 IAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEK 84
Cdd:cd10214   3 TKAVIIDLGTGYCKAGFAGQPRPSYVISSTVGKPPQESAKTGDNRKETFVGKELANVEPPLKLVNPLRHGIVVDWDCVQD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   85 IWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVP 164
Cdd:cd10214  83 IWEYIFEKEMKILPEEHAVLVSDPPLSPTTNREKYAELMFETFSIPAMHIAYQSRLSLYSYGRTSGLVVESGHGVSYVVP 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  165 IYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTaEREIVRDIKEKLCYVALDFEQEMATAASSSSLEksYELPD 244
Cdd:cd10214 163 IHEGYNLPHITGRADYAGSDLTAYLMKLLNEAGNKFTDD-QLHIVEDIKKKCCYVALDFEEEMGLPPQEYTVD--YELPD 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  245 GQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPST 324
Cdd:cd10214 240 GHLITIGKERFRCPEMLFNPSLIGSKQPGLHTLTMNSLNKCDANLKKDLAKNILLCGGSTMFDGFPDRFQKELSKLCPND 319
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 6671509  325 MKIkIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKC 374
Cdd:cd10214 320 NPI-VAASPERKYSVWTGGSILASLKSFQQLWVRRREYEERGPFVIYRKC 368
ASKHA_NBD_actin-like cd10169
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ...
8-366 2.75e-161

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: 452.33  E-value: 2.75e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509    8 LVVDNGSGMCKAGFAGDDAPRAVFPsivgrprhqgvmvgmgqkdsyvgdeaqskrgiltlkypiehgivtnWDDMEKIWH 87
Cdd:cd10169   1 IVIDNGSGTIKAGFAGEDAPRLIFP----------------------------------------------WDDMEKIWE 34
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   88 HTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYE 167
Cdd:cd10169  35 HVFYNLLRVDPEEHPVLLTEPPLNPKANREKLAEILFETFNVPSLYIANQAVLSLYASGRTTGLVVDSGEGVTHIVPVYE 114
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  168 GYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLcyvaldfeqemataassssleksyelpdgqv 247
Cdd:cd10169 115 GYVLPHAVRRLDIGGRDLTDYLAKLLREKGYSFSTSAEREIVRDIKEKL------------------------------- 163
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  248 itignerfrcpealfqpsflgmesCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKI 327
Cdd:cd10169 164 ------------------------CGLHELIYDSIMKCDIDLRKELYSNIVLSGGTTLFPGFAERLQKELSKLAPSSVKV 219
                       330       340       350
                ....*....|....*....|....*....|....*....
gi 6671509  328 KIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESG 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 2.49e-160

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: 455.87  E-value: 2.49e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509    3 DDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVG-RPRHQGVMVGMGQKDS-----YVGDEA-QSKRGILTLKYPIEHGI 75
Cdd:cd13395   2 DEVGALVLDIGSYSTRAGYAGEDTPKAVFPSVVGvVTDDDDAEDYVGGSGEkkrkyYIGTNSiGVPRPNMEVISPLKDGL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   76 VTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDS 155
Cdd:cd13395  82 IEDWDAFEKLWDHALKNRLRVDPSEHPLLLTEPSWNTRANREKLTELMFEKYNVPAFFLAKNAVLSAFANGRSTALVVDS 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  156 GDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGY--------------------------------SFTTT 203
Cdd:cd13395 162 GATSTSVVPVHDGYVLQKAIVRSPLGGDFLTDQLLKLLESKNIeiiprymikskepveggapakytkkdlpnttsSYHRY 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  204 AEREIVRDIKEKLCYVALDFEQEmatAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFL---------GMESCGI 274
Cdd:cd13395 242 MVRRVLQDFKESVCQVSDSPFDE---SEAASIPTVSYELPDGYNIEFGAERFKIPELLFDPSLVkgipappseGNELLGL 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  275 HETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPP---ERKYSVWIGGSILASLST 351
Cdd:cd13395 319 PQLVYTSIGSCDVDIRPELYGNVVLTGGNSLLPGFTDRLNRELSEKAPGSLKLKILASGntvERRFSSWIGGSILASLGS 398
                       410
                ....*....|....*
gi 6671509  352 FQQMWISKQEYDESG 366
Cdd:cd13395 399 FQQMWISKQEYEEHG 413
COG5277 COG5277
Actin-related protein [Cytoskeleton];
9-365 1.99e-142

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 410.72  E-value: 1.99e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509    9 VVDNGSGMCKAG-FAGDDAP-----RAVFPSIVGRPRHQGVMVGMGqKDSYVGDEAQS-----KRGILTLKYPIEHGIVT 77
Cdd:COG5277  12 GIDFGTSYVKYGpIALEEKPrviqtRGLFLRIVGESKLLGPMEGLS-RGLVVGDEVSKylssvRDAIRNLKYPLRDGIVR 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   78 -----NWDDMEKIWHHTFYNELRVAPEEHP--VLLTEAPLNPKANREKMTQIMFETF---NTPAMYVAIQAVLSLYASGR 147
Cdd:COG5277  91 rddedAWRVLKELLRYTFAQFLVVDPEFHGflVVVALSALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPLAVAIAEKA 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  148 TTGIVMDSGDGVTHTVPIYEGyALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEReIVRDIKEKLCYVALDFEQEM 227
Cdd:COG5277 171 VTCVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSDTAREEY-VVRVVKEALGLVPRDLAKAI 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  228 -ATAASSSSLEKSYELPDGQV-ITIGN---ERFRCPEALFQPSFLGMESC----------------------GIHETTFN 280
Cdd:COG5277 249 qKAASNPDSFEAKVRLPNPTVeIELGNyawERFLIGEILFNPNHEGFESYiqqgrlriedavigdvvlygemGLAEAIIN 328
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  281 SIMKCDVDIRKDLYANTVLSGGTTMY---PGIAD-------RMQKEITALAPsTMKIKIIAPPERKYSVWIGGSILASLS 350
Cdd:COG5277 329 SIMKCDVEIQDELYSNIILSGGAFNWsvpPGLEDvavdsvtRVQIELSELAP-ELKVNVRLVSDPQYSVWKGAIIYGYAL 407
                       410
                ....*....|....*..
gi 6671509  351 TFQQMW--ISKQEYDES 365
Cdd:COG5277 408 PFSVKWswITKEGWYFL 424
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
7-370 5.13e-124

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: 363.43  E-value: 5.13e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509    7 ALVVDNGSGMCKAGFAGDDAPRAVFPSIVG-------RPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNW 79
Cdd:cd10221   1 AVVIDNGTGYTKMGYAGNTEPQFIIPTVIAikesakvGDGQRRSKKGIEDLDFYIGDEALANSPTYALKYPIRHGIVEDW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   80 DDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRT--------TGI 151
Cdd:cd10221  81 DLMERFWEQCIFKYLRCEPEDHYFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQAVLALAASWTSrkvgertlTGT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  152 VMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAA 231
Cdd:cd10221 161 VIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREEGIPPEDSLEVAKRIKERYCYVCPDIVKEFAKYD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  232 SS-SSLEKSYELPD---GQ--VITIGNERFRCPEALFQPSFLGMESC-GIHETTFNSIMKCDVDIRKDLYANTVLSGGTT 304
Cdd:cd10221 241 SDpAKYIKQYTGINsvtGKpyTVDVGYERFLAPEIFFNPEIASSDFTtPLPEVVDQVIQSCPIDTRRGLYKNIVLSGGST 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  305 MYPGIADRMQKEITA----------------LAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPS 368
Cdd:cd10221 321 MFKDFGRRLQRDVKRivdarlkaseelsggkLKPKPIDVNVISHPMQRYAVWFGGSMLASTPEFYTVCHTKAEYEEYGPS 400

                ..
gi 6671509  369 IV 370
Cdd:cd10221 401 IC 402
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
7-372 9.04e-123

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 360.59  E-value: 9.04e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509     7 ALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMV---GMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDME 83
Cdd:PTZ00280   6 VVVIDNGTGYTKMGYAGNTEPTYIIPTLIADNSKQSRRRskkGFEDLDFYIGDEALAASKSYTLTYPMKHGIVEDWDLME 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509    84 KIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYAS----------GRTTGIVM 153
Cdd:PTZ00280  86 KFWEQCIFKYLRCEPEEHYFILTEPPMNPPENREYTAEIMFETFNVKGLYIAVQAVLALRASwtskkakelgGTLTGTVI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   154 DSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMAT---- 229
Cdd:PTZ00280 166 DSGDGVTHVIPVVDGYVIGSSIKHIPLAGRDITNFIQQMLRERGEPIPAEDILLLAQRIKEKYCYVAPDIAKEFEKydsd 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   230 --------AASSSSLEKSYElpdgqvITIGNERFRCPEALFQPSFLGME-SCGIHETTFNSIMKCDVDIRKDLYANTVLS 300
Cdd:PTZ00280 246 pknhfkkyTAVNSVTKKPYT------VDVGYERFLGPEMFFHPEIFSSEwTTPLPEVVDDAIQSCPIDCRRPLYKNIVLS 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   301 GGTTMYPGIADRMQKEITA----------------LAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDE 364
Cdd:PTZ00280 320 GGSTMFKGFDKRLQRDVRKrvdrrlkkaeelsggkLKPIPIDVNVVSHPRQRYAVWYGGSMLASSPEFEKVCHTKAEYDE 399

                 ....*...
gi 6671509   365 SGPSIVHR 372
Cdd:PTZ00280 400 YGPSICRY 407
ASKHA_NBD_Arp6 cd10210
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ...
8-366 6.97e-101

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: 303.70  E-value: 6.97e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509    8 LVVDNGSGMCKAGFAGDDAPRaVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQskrgiLTLKYPIEHGIVTNWDDMEKIWH 87
Cdd:cd10210   2 LVLDNGAYTIKAGFASDDPPR-VIPNCIAKPKSERRRLFGDDQLDECKDLSG-----LFYRRPFERGYLVNWDLQRQIWD 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   88 HTFYNE-LRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYA----------SGRTTGIVMDSG 156
Cdd:cd10210  76 HLFGKLlLNVDPSDTALVLTEPPFNPPSIQEAMDEIVFEEYGFQSLYRTTAAALSAFAyladseqsssSSSQCCLVVDSG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  157 DGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFtttaERE--IVRDIKEKLCYVALDFEQEMATAAS-- 232
Cdd:cd10210 156 FSFTHIVPFFDGKPVKRAVRRIDVGGKLLTNYLKEIISYRQLNV----MDEtyLVNQIKEDLCFVSTDFYEDLEIAKKkg 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  233 -SSSLEKSYELPDG-----------------------QVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVD 288
Cdd:cd10210 232 kENTIRRDYVLPDYttskrgyvrdpeepnrgklkedeQVLRLNNERFTVPELLFHPSDIGIQQAGIAEAIVQSINACPEE 311
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6671509  289 IRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESG 366
Cdd:cd10210 312 LQPLLYANIVLTGGNALFPGFRERLEAELRSLAPDDYDVNVTLPEDPITYAWEGGSLLAQSPEFEELAVTRAEYEEHG 389
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
8-371 4.56e-90

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: 275.04  E-value: 4.56e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509    8 LVVDNGSGMCKAGFAGDDApravFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSkrgiltlkyPIEHGIVTNWDDMEKIWH 87
Cdd:cd10209   1 VVIDAGSRLLKAGYAYPDR----EPSVVEPTRVTPAVEDGEESDTVVEGNTVS---------PIRRGRIEDWDALEALLR 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   88 HTFYNELR-VAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIY 166
Cdd:cd10209  68 YVFYTGLGwEEGNEGQVLIAEPLLTSKAERERLTQLMFETFNVSGLYASEQAVLSLYAVGRISGCVVDVGHGKIDIAPVW 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  167 EGYALPHAILRLDLAGRDLTDYLMKILTERGYSftTTAEREIVRDIKEKLCYVALDFEQEMATAASSSslEKSYELPDGQ 246
Cdd:cd10209 148 EGAIQHNAVRRFEIGGRDLTELLAAELGKSNPK--VKLDRSIVERLKEAVAWSADDEEAYEKKVLTCS--PETYTLPDGR 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  247 VITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMK 326
Cdd:cd10209 224 VISVGKERYCVGEALFRPSILGIEEYGIVEQLVRAVSTSPSENRRQLLENIVLCGGTSSVPGLEARLQKEIRLLSSPSSR 303
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 6671509  327 IKIIAPPE------RKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVH 371
Cdd:cd10209 304 PALVKPPEympentLRYSAWIGGAILAKVVFPQNQHVTKADYDETGPSVVH 354
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
7-367 2.48e-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: 234.00  E-value: 2.48e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509    7 ALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQgvmvGMGQKDSYVGDEA---QSKRGilTLKYPIEHGIVTNWDDME 83
Cdd:cd10211   1 PIVIDNGSYQCRAGWAGDKEPRLVFRNLVAKPRDR----KKGITVTLVGNDIlndEAVRS--HLRSPFDRNVVTNFDLQE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   84 KIWHHTFyNELRVAPE---EHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRT----TGIVMDSG 156
Cdd:cd10211  75 QILDYIF-SHLGINSEgsvDHPIVLTEALCNPNYSRQLMSELLFECYGVPSVAYGIDSLFSYYHNQPQgdpsDGLVISSG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  157 DGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTT--TAEReiVRDIKEKLCYVALDFEQEMATAASSS 234
Cdd:cd10211 154 YSTTHVIPVLNGRLDLSQCKRINLGGFHATDYLQRLLQLKYPTHPSaiTLSR--AEELVHEHCYVAEDYDEELKKWEDPE 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  235 SLEKSyelpdgqvitigNERFRCPealFqpsflgmescGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQ 314
Cdd:cd10211 232 YYEEN------------VRKIQLP---F----------GLVETIEFVLKRYPAEQQDRLVQNVFLTGGNALFPGLKERLE 286
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 6671509  315 KEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGP 367
Cdd:cd10211 287 KELRAIRPFGSPFNVVRAKDPVLDAWRGAAKWALDSTFEKVWITKQEYEEKGG 339
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
38-373 1.93e-58

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: 193.29  E-value: 1.93e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   38 PRHQGVMVGMGQKDSYVGD--EAQSKRGILtlkYPIEHGIVTNWDDMEKIWHHTFYNEL--RVAPEEHPVLLTEAPLNPK 113
Cdd:cd10208   7 PGSQTTRAGLGLGELLTPPtiEIPTRVEII---WPIQDGRVVDWDALEALWRHILFSLLsiPRPTNNSPVLLSVPPSWSK 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  114 ANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKIL 193
Cdd:cd10208  84 SDLELLTQLFFERLNVPAFAILEAPLAALYAAGATSGIVVDIGHEKTDITPIVDSQVVPHALVSIPIGGQDCTAHLAQLL 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  194 TER--GYSFTTTAEREIVRDIKEKLcyvaldFEQEMATAASSSSleksyELPDGQVITIGNERFRCPEALFQPSFLGM-- 269
Cdd:cd10208 164 KSDepELKSQAESGEEATLDLAEAL------KKSPICEVLSDGA-----DLASGTEITVGKERFRACEPLFKPSSLRVdl 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  270 --ESCGIHETTFNSimkCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITAL-----------APSTMKIKIIaP---P 333
Cdd:cd10208 233 liAAIAGALVLNAS---DEPDKRPALWENIIIVGGGSRIRGLKEALLSELQQFhlisetsaspqQPRIIRLAKI-PdyfP 308
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 6671509  334 ERK-----YSVWIGGSILASLsTF----QQMWISKQEYDESGPSIVHRK 373
Cdd:cd10208 309 EWKksgyeEAAFLGASIVAKL-VFndpsSKHYISKVDYNEKGPAAIHTK 356
ASKHA_NBD_Arp10 cd10207
nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins; ...
9-366 4.28e-51

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: 174.75  E-value: 4.28e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509    9 VVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRhqgvmvgmGQKDSYVGDeaqsKRGILTLKypiehgivtnWDDM-EKIWH 87
Cdd:cd10207   2 VLDIGSAYTKCGFAGESAPRCIIPSEVKLPG--------GKKVIRVVD----QRSGNEEE----------LYEAlKEFLH 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   88 HTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYE 167
Cdd:cd10207  60 ELYFKHLLVNPKDRRVVVVESVLCPTPFRETLAKVLFKHFEVPSVLFAPSHLLSLLTLGIRTALVVDCGYRETRVLPVYE 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  168 GYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAER------------EIVRDIKEKLCYVA-LDFEQEMATAASSS 234
Cdd:cd10207 140 GVPLLSAWQSTPLGGKALHKRLKKLLLEHATVVTGDNKGqllssvdsllseEVLEDIKVRACFVTsLERGKTLQSATEEG 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  235 SLEKS-------YELPDGQVITIGNERFRCPEALFqpsFLGMESC-GIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMY 306
Cdd:cd10207 220 STEEPsppppvdYPLDGEKILIVPGSIRESAEELL---FEGDNEEkSLPTLILDSLLKCPIDVRKQLAENIVVIGGTSML 296
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6671509  307 PGIADRMQKEITA----------LAPSTMKI---KIIAPPErkYSVWIGGSILASLSTFQQMWISKQEYDESG 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 5.37e-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: 165.41  E-value: 5.37e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   89 TFYNELRVAPEEHPVLLTEaPL-------NPKANREKMTQIMFETF---NTPAMYVAIQAVLSLYASGRTTGIVMDSGDG 158
Cdd:cd13396  47 TIMTRMQVKPSRQPVVVSL-PLchsddteSAAASRRQLRGTIFNVLfdmNVPAVCAVDQAVLALYAANRTSGIVVNIGFR 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  159 VTHTVPIYEGYALPH-AILRLDLAGRDLTDYLMKILTERGYSFTTTAereIVRDIKEKLCYVALDFEQEMAtaassSSLE 237
Cdd:cd13396 126 VTTIVPVYRGRVMHDiGVEVVGQGALRLTGFLKELMQQNGIRFPSLY---TVRTIKEKLCYVAEDYEAELA-----KDTQ 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  238 KSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIR---KDLYANTVLSGGTTMYPGIADRMQ 314
Cdd:cd13396 198 ASCEVAGEGWFTLSNERFKTGEILFQPGLGGMRAMGLHQAVALCMDHCALVHSqgdDGWFKTIVLSGGSACLPGLSERLE 277
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6671509  315 KEITALAPSTMK--IKIIAPPERKYSVWIGGSILASLSTFQQMW-ISKQEYDESG 366
Cdd:cd13396 278 RELRKLLPKSLSegIRIIPPPLGPDSAWQGAKLISNLSNFPDGWcITKKQFRNKP 332
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
303-374 2.59e-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: 125.86  E-value: 2.59e-35
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6671509   303 TTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKC 374
Cdd:NF040575  61 RVNESGFYEKLKKSITEKAPKGALIGMTLDPKPESAAWRGAAMYAASEGFVEMAITKQEYDESGPSIVHRKC 132
ASKHA_NBD_Arp8-like cd10206
nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The ...
48-369 1.16e-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: 113.10  E-value: 1.16e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   48 GQKDSYVGDEAQ--SKRGILTLKYPIEHGiVTNW-----------DDMEKIWHHTFYNELRVAPEEHP----VLLTEAPL 110
Cdd:cd10206 118 DYPDFLVGEEALrlPPSEEYNLHWPIRRG-RLNVhsdggsltavlDDLEDIWSHALEEKLEIPRKDLKnyraVLVIPDLF 196
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  111 NpKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLM 190
Cdd:cd10206 197 D-RRHVKELVDLLLRRLGFSSVFVHQESVCATFGAGLSSACVVDIGAQKTSVACVEDGLSIPNSRIRLPYGGDDITRCFL 275
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  191 KILTERGY-----SFTTTAEREIVRDIKEKLCYValdfeqemataassssleksyelpDGQVITIGNERF--RCPealFQ 263
Cdd:cd10206 276 WLLRRSGFpyrecNLNSPLDFLLLERLKETYCTL------------------------DQDDIGVQLHEFyvREP---GQ 328
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  264 PSFL-GMESCGIHETTFNSIMKC-DVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMK----IKIIAPPERK- 336
Cdd:cd10206 329 PTLKyQFKLLPLDEAIVQSILSCaSDELKRKMYSSILLVGGGAKIPGLAEALEDRLLIKIPSLFEavetVEVLPPPKDMd 408
                       330       340       350
                ....*....|....*....|....*....|....*
gi 6671509  337 --YSVWIGGSILASLSTFQQMWISKQEYDESGPSI 369
Cdd:cd10206 409 psLLAWKGGAVLACLDSAQELWITRKEWQRLGVRA 443
ASKHA_NBD_ScArp7-like cd10212
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and ...
8-363 1.20e-19

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: 89.78  E-value: 1.20e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509    8 LVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGvmvgmGQKDSYVG-----DEAQSKR-GILTLKYPIEHGIVTNWDD 81
Cdd:cd10212   6 VVIHNGSHRTVAGFSNVELPQCIIPSSYIKRTDEG-----GEAEFIFGtynmiDAAAEKRnGDEVYTLVDSQGLPYNWDA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   82 MEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANR---EKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDG 158
Cdd:cd10212  81 LEMQWRYLYDTQLKVSPEELPLVITMPATNGKPDMailERYYELAFDKLNVPVFQIVIEPLAIALSMGKSSAFVIDIGAS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  159 VTHTVPIYEGYALPHAILRLDLAGrDLTDYLM---------------------KILTERGYSFTT--------------- 202
Cdd:cd10212 161 GCNVTPIIDGIVVKNAVVRSKFGG-DFLDFQVherlaplikeendmenmadeqKRSTDVWYEASTwiqqfkstmlqvsek 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  203 ----------------TAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKsyelPDGQVITIG-NERFRCPEALFQPS 265
Cdd:cd10212 240 dlfeleryykeqadiyAKQQEQLKQMDQQLQYTALTGSPNNPLVQKKNFLFK----PLNKTLTLDlKECYQFAEYLFKPQ 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  266 FLGMESC---GIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAP----STMKIKIIAppERKYS 338
Cdd:cd10212 316 LISDKFSpedGLGPLMAKSVKKAPEQVYSLLLTNVIITGSTSLIEGMEQRIIKELSIRFPqyklTTFANQVMM--DRKIQ 393
                       410       420
                ....*....|....*....|....*.
gi 6671509  339 VWIGGSILASLSTFQ-QMWISKQEYD 363
Cdd:cd10212 394 GWLGALTMANLPSWSlGKWYSKEDYE 419
ASKHA_NBD_MamK cd24009
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ...
15-316 5.34e-10

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: 59.92  E-value: 5.34e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   15 GMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGqKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDmekiwhhtfyNEL 94
Cdd:cd24009   9 GTSRSAVVTSRGKRFSFRSVVGYPKDIIARKLLG-KEVLFGDEALENRLALDLRRPLEDGVIKEGDD----------RDL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509   95 RVAPE--EHPVLLTEAPLNPK-------------ANREKMTQIMFETFNTPAMYVAIQAVlsLYASGRTTG-IVMDSGDG 158
Cdd:cd24009  78 EAAREllQHLIELALPGPDDEiyavigvparasaENKQALLEIARELVDGVMVVSEPFAV--AYGLDRLDNsLIVDIGAG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  159 VTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTER--GYSFTttaeREIVRDIKEKLCYValdfeqemataaSSSSL 236
Cdd:cd24009 156 TTDLCRMKGTIPTEEDQITLPKAGDYIDEELVDLIKERypEVQLT----LNMARRWKEKYGFV------------GDASE 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671509  237 EKSYELP-DGQVIT--IGNE-RFRCpEALFQPsflgmescgIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADR 312
Cdd:cd24009 220 PVKVELPvDGKPVTydITEElRIAC-ESLVPD---------IVEGIKKLIASFDPEFQEELRNNIVLAGGGSRIRGLDTY 289

                ....
gi 6671509  313 MQKE 316
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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