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Conserved domains on  [gi|149062733|gb|EDM13156|]
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rCG47746, isoform CRA_a [Rattus norvegicus]

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 ...
8-372 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: 922.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733   8 TALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKI 87
Cdd:cd10224    1 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  88 WHHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPI 167
Cdd:cd10224   81 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 168 YEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDG 247
Cdd:cd10224  161 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 248 QVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTM 327
Cdd:cd10224  241 QVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTM 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 149062733 328 KIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIV 372
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 ...
8-372 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: 922.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733   8 TALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKI 87
Cdd:cd10224    1 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  88 WHHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPI 167
Cdd:cd10224   81 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 168 YEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDG 247
Cdd:cd10224  161 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 248 QVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTM 327
Cdd:cd10224  241 QVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTM 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 149062733 328 KIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIV 372
Cdd:cd10224  321 KIKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIV 365
PTZ00281 PTZ00281
actin; Provisional
3-377 0e+00

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 753.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733   3 EEEDSTALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWD 82
Cdd:PTZ00281   2 DGEDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  83 DMEKIWHHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVT 162
Cdd:PTZ00281  82 DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 163 HNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSY 242
Cdd:PTZ00281 162 HTVPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEMQTAASSSALEKSY 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 243 ELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITAL 322
Cdd:PTZ00281 242 ELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELTAL 321
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 149062733 323 APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKCF 377
Cdd:PTZ00281 322 APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIVHRKCF 376
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
8-377 0e+00

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 645.47  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733     8 TALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGmGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKI 87
Cdd:smart00268   2 PAIVIDNGSGTIKAGFAGEDFPQVVFPSIVGRPKDGKGMVG-DAKDIFVGDEAQEKRGGLELKYPIENGIVENWDDMEKI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733    88 WHHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPI 167
Cdd:smart00268  81 WDYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVPV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733   168 YEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAAS---SSSLEKSYEL 244
Cdd:smart00268 161 VDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLAREsseSSKLEKTYEL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733   245 PDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAP 324
Cdd:smart00268 241 PDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELKQLAP 320
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 149062733   325 STMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKCF 377
Cdd:smart00268 321 KKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERKCF 373
Actin pfam00022
Actin;
8-377 0e+00

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 570.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733    8 TALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGmgqKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKI 87
Cdd:pfam00022   2 SALVIDNGSHTTRAGFAGEDAPKAVIPSCVGKPRGTKVEAA---NKYYVGDEALTYRPGMEVRSPVEDGIVVDWDAMEEI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733   88 WHHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPI 167
Cdd:pfam00022  79 WEHVLKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVPV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  168 YEGYALPHAIMRLDLAGRDLTDYLMKILTER------------------------------GYSFVTTAEREIVRDIKEK 217
Cdd:pfam00022 159 HDGYVLQKAIRRSDLGGDFLTDYLRELLRSRnieitprylikskkpgdpapavtkrelpdtTYSYKTYQERRVLEEIKES 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  218 LCYVALDFenEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESA--------GIHETTYNSIMKCDI 289
Cdd:pfam00022 239 VCYVSDDP--FGDETTSSSIPTRVYELPDGSTIILGAERFRVPEILFNPSLIGSESElpppqtavGIPELIVDAINACDV 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  290 DIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPP---ERKYSVWIGGSILASLSTFQQMWISKQEYDE 366
Cdd:pfam00022 317 DLRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVKIIAPGntvERRYSAWIGGSILASLGTFQQMWVSKQEYEE 396
                         410
                  ....*....|.
gi 149062733  367 AGPSIVHRKCF 377
Cdd:pfam00022 397 HGASVVERKCK 407
COG5277 COG5277
Actin-related protein [Cytoskeleton];
13-366 2.83e-139

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 403.02  E-value: 2.83e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  13 DNGSGLCKAG-FAGDDAP-----RAVFPSIVGRPRHQGVMVGMGqKDSYVGDEAQS-----KRGILTLKYPIEHGIIT-- 79
Cdd:COG5277   14 DFGTSYVKYGpIALEEKPrviqtRGLFLRIVGESKLLGPMEGLS-RGLVVGDEVSKylssvRDAIRNLKYPLRDGIVRrd 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  80 ---NWDDMEKIWHHSFYNELRVAPEEHPTL--LTEAPLNPKANREKMTQIMFETF---NVPAMYVAIQAVLSLYASGRTT 151
Cdd:COG5277   93 dedAWRVLKELLRYTFAQFLVVDPEFHGFLvvVALSALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPLAVAIAEKAVT 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 152 GIVLDSGDGVTHNVPIYEGyALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEReIVRDIKEKLCYVALDFENEM-A 230
Cdd:COG5277  173 CVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSDTAREEY-VVRVVKEALGLVPRDLAKAIqK 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 231 TAASSSSLEKSYELPDGQV-ITIGN---ERFRCPETLFQPSFIGMES----------------------AGIHETTYNSI 284
Cdd:COG5277  251 AASNPDSFEAKVRLPNPTVeIELGNyawERFLIGEILFNPNHEGFESyiqqgrlriedavigdvvlygeMGLAEAIINSI 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 285 MKCDIDIRKDLYANNVLSGGTTMY---PGIAD-------RMQKEITALAPsTMKIKIIAPPERKYSVWIGGSILASLSTF 354
Cdd:COG5277  331 MKCDVEIQDELYSNIILSGGAFNWsvpPGLEDvavdsvtRVQIELSELAP-ELKVNVRLVSDPQYSVWKGAIIYGYALPF 409
                        410
                 ....*....|....
gi 149062733 355 QQMW--ISKQEYDE 366
Cdd:COG5277  410 SVKWswITKEGWYF 423
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
305-376 3.43e-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: 3.43e-35
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149062733 305 TTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKC 376
Cdd:NF040575  61 RVNESGFYEKLKKSITEKAPKGALIGMTLDPKPESAAWRGAAMYAASEGFVEMAITKQEYDESGPSIVHRKC 132
 
Name Accession Description Interval E-value
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
8-372 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: 922.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733   8 TALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKI 87
Cdd:cd10224    1 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  88 WHHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPI 167
Cdd:cd10224   81 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 168 YEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDG 247
Cdd:cd10224  161 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 248 QVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTM 327
Cdd:cd10224  241 QVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTM 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 149062733 328 KIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIV 372
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 ...
8-368 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: 762.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733   8 TALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKI 87
Cdd:cd13397    1 PAVVIDNGSGLIKAGFAGEDLPRAVFPSVVGRPKYKAVMLGAGQKEVYVGDEAQEKRGVLTLSYPIEHGIVTNWDDMEKI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  88 WHHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPI 167
Cdd:cd13397   81 WHHTFENELRVKPEEHPVLLTEAPLNPKQNREKMAEIMFETFGVPAFYVAIQAVLSLYSSGRTTGLVLDSGDGVTHTVPI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 168 YEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMatAASSSSLEKSYELPDG 247
Cdd:cd13397  161 YEGYALPHAVQRLDLAGRDLTEYLMKLLKERGHSFTTTAEREIVRDIKEKLCYVALDYEEEL--KKKSEELEKEYTLPDG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 248 QVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTM 327
Cdd:cd13397  239 QVIKIGSERFRCPEALFRPSLIGREAPGIHKLVYNSIMKCDIDIRKDLYSNIVLSGGSTMFPGLPERLQKELEALAPSST 318
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 149062733 328 KIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAG 368
Cdd:cd13397  319 KVKVIAPPERKYSVWIGGSILASLSTFKSMWITRAEYDEFG 359
PTZ00281 PTZ00281
actin; Provisional
3-377 0e+00

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 753.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733   3 EEEDSTALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWD 82
Cdd:PTZ00281   2 DGEDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  83 DMEKIWHHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVT 162
Cdd:PTZ00281  82 DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 163 HNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSY 242
Cdd:PTZ00281 162 HTVPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEMQTAASSSALEKSY 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 243 ELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITAL 322
Cdd:PTZ00281 242 ELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELTAL 321
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 149062733 323 APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKCF 377
Cdd:PTZ00281 322 APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIVHRKCF 376
PTZ00004 PTZ00004
actin-2; Provisional
4-377 0e+00

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 707.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733   4 EEDSTALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDD 83
Cdd:PTZ00004   3 VEETNAAVVDNGSGMVKAGFAGDDAPRCVFPSIVGRPKNPGIMVGMEEKDCYVGDEAQDKRGILTLKYPIEHGIVTNWDD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  84 MEKIWHHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTH 163
Cdd:PTZ00004  83 MEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETHNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSH 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 164 NVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSL-EKSY 242
Cdd:PTZ00004 163 TVPIYEGYSLPHAIHRLDVAGRDLTEYMMKILHERGTTFTTTAEKEIVRDIKEKLCYIALDFDEEMGNSAGSSDKyEESY 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 243 ELPDGQVITIGNERFRCPETLFQPSFIGMESA-GIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITA 321
Cdd:PTZ00004 243 ELPDGTIITVGSERFRCPEALFQPSLIGKEEPpGIHELTFQSINKCDIDIRKDLYGNIVLSGGTTMYRGLPERLTKELTT 322
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 149062733 322 LAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKCF 377
Cdd:PTZ00004 323 LAPSTMKIKVVAPPERKYSVWIGGSILSSLPTFQQMWVTKEEYDESGPSIVHRKCF 378
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
8-377 0e+00

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 645.47  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733     8 TALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGmGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKI 87
Cdd:smart00268   2 PAIVIDNGSGTIKAGFAGEDFPQVVFPSIVGRPKDGKGMVG-DAKDIFVGDEAQEKRGGLELKYPIENGIVENWDDMEKI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733    88 WHHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPI 167
Cdd:smart00268  81 WDYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVPV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733   168 YEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAAS---SSSLEKSYEL 244
Cdd:smart00268 161 VDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLAREsseSSKLEKTYEL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733   245 PDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAP 324
Cdd:smart00268 241 PDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELKQLAP 320
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 149062733   325 STMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKCF 377
Cdd:smart00268 321 KKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERKCF 373
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
10-376 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 149062733  10 LVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWH 89
Cdd:cd10216    4 VVIDNGSGVIKAGFAGDDIPKVVFPSYVGRPKHVRVMAGALEGDVFVGPKAEEHRGLLKIRYPMEHGIVTDWNDMERIWQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  90 HSFYNE-LRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIY 168
Cdd:cd10216   84 YVYSKLqLNTFSEEHPVLLTEAPLNPRKNREKAAEVFFETFNVPALFVSMQAVLSLYASGRTTGVVLDSGDGVTHAVPIY 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 169 EGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEmATAASSSSLEKSYELPDGQ 248
Cdd:cd10216  164 EGFALPHSIRRVDIAGRDVTEYLQLLLRKSGYNFHTSAEFEIVREIKEKACYVALNPQKE-EKLEEEKTEKAQYTLPDGS 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 249 VITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMK 328
Cdd:cd10216  243 TIEIGPERFRAPEILFNPELIGLEYPGVHEVLVDSIQKSDLDLRKTLYSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDVK 322
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 149062733 329 IKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKC 376
Cdd:cd10216  323 IRISAPPERLYSTWIGGSILASLSTFKKMWVSKKEYEEDGARILHRKT 370
Actin pfam00022
Actin;
8-377 0e+00

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 570.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733    8 TALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGmgqKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKI 87
Cdd:pfam00022   2 SALVIDNGSHTTRAGFAGEDAPKAVIPSCVGKPRGTKVEAA---NKYYVGDEALTYRPGMEVRSPVEDGIVVDWDAMEEI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733   88 WHHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPI 167
Cdd:pfam00022  79 WEHVLKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVPV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  168 YEGYALPHAIMRLDLAGRDLTDYLMKILTER------------------------------GYSFVTTAEREIVRDIKEK 217
Cdd:pfam00022 159 HDGYVLQKAIRRSDLGGDFLTDYLRELLRSRnieitprylikskkpgdpapavtkrelpdtTYSYKTYQERRVLEEIKES 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  218 LCYVALDFenEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESA--------GIHETTYNSIMKCDI 289
Cdd:pfam00022 239 VCYVSDDP--FGDETTSSSIPTRVYELPDGSTIILGAERFRVPEILFNPSLIGSESElpppqtavGIPELIVDAINACDV 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  290 DIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPP---ERKYSVWIGGSILASLSTFQQMWISKQEYDE 366
Cdd:pfam00022 317 DLRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVKIIAPGntvERRYSAWIGGSILASLGTFQQMWVSKQEYEE 396
                         410
                  ....*....|.
gi 149062733  367 AGPSIVHRKCF 377
Cdd:pfam00022 397 HGASVVERKCK 407
ASKHA_NBD_Arp2 cd10220
nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, ...
10-372 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: 527.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  10 LVCDNGSGLCKAGFAGDDAPRAVFPSIVGRP--RHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKI 87
Cdd:cd10220    3 VVCDNGTGFVKCGFAGSNFPEHVFPSLVGRPilRAEEKVGDIEIKDIMVGDEASELRSMLEVTYPMENGIVRNWDDMEHL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  88 WHHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPI 167
Cdd:cd10220   83 WDYTFGEKLKIDPRECKILLTEPPMNPTKNREKMVEVMFEKYGFAGVYVAIQAVLTLYAQGLLTGVVVDSGDGVTHIVPV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 168 YEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDG 247
Cdd:cd10220  163 YEGFSLPHLTRRLDVAGRDITRYLIKLLLLRGYAFNRTADFETVREIKEKLCYVAYDIELEQKLALETTVLVESYTLPDG 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 248 QVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITAL----- 322
Cdd:cd10220  243 RVIKVGGERFEAPEALFQPHLIDVEGPGIAELLFNTIQAADIDTRPELYKHIVLSGGSTMYPGLPSRLEKEIKQLylerv 322
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 149062733 323 ------APSTMKIKIIAPPERKYSVWIGGSILASLSTFQ-QMWISKQEYDEAGPSIV 372
Cdd:cd10220  323 lkgdteRLSKFKIRIEDPPRRKHMVFLGGAVLADIMKDKdEFWITRQEYEEQGVRVL 379
PTZ00466 PTZ00466
actin-like protein; Provisional
10-377 2.63e-177

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 497.93  E-value: 2.63e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  10 LVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWH 89
Cdd:PTZ00466  15 IIIDNGTGYIKAGFAGEDVPNLVFPSYVGRPKYKRVMAGAVEGNIFVGNKAEEYRGLLKVTYPINHGIIENWNDMENIWI 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  90 HsFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYE 169
Cdd:PTZ00466  95 H-VYNSMKINSEEHPVLLTEAPLNPQKNKEKIAEVFFETFNVPALFISIQAILSLYSCGKTNGTVLDCGDGVCHCVSIYE 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 170 GYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSlEKSYELPDGQV 249
Cdd:PTZ00466 174 GYSITNTITRTDVAGRDITTYLGYLLRKNGHLFNTSAEMEVVKNMKENCCYVSFNMNKEKNSSEKALT-TLPYILPDGSQ 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 250 ITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKI 329
Cdd:PTZ00466 253 ILIGSERYRAPEVLFNPSILGLEYLGLSELIVTSITRADMDLRRTLYSHIVLSGGTTMFHGFGDRLLNEIRKFAPKDITI 332
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 149062733 330 KIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKCF 377
Cdd:PTZ00466 333 RISAPPERKFSTFIGGSILASLATFKKIWISKQEFDEYGSVILHRKTF 380
PTZ00452 PTZ00452
actin; Provisional
9-377 1.82e-175

actin; Provisional


Pssm-ID: 185631  Cd Length: 375  Bit Score: 493.12  E-value: 1.82e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733   9 ALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIW 88
Cdd:PTZ00452   7 AVVIDNGSGYCKIGIAGDDAPTSCFPAIVGRSKQNDGIFSTFNKEYYVGEEAQAKRGVLAIKEPIQNGIINSWDDIEIIW 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  89 HHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIY 168
Cdd:PTZ00452  87 HHAFYNELCMSPEDQPVFMTDAPMNSKFNRERMTQIMFETFNTPCLYISNEAVLSLYTSGKTIGLVVDSGEGVTHCVPVF 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 169 EGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQ 248
Cdd:PTZ00452 167 EGHQIPQAITKINLAGRLCTDYLTQILQELGYSLTEPHQRIIVKNIKERLCYTALDPQDEKRIYKESNSQDSPYKLPDGN 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 249 VITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMK 328
Cdd:PTZ00452 247 ILTIKSQKFRCSEILFQPKLIGLEVAGIHHLAYSSIKKCDLDLRQELCRNIVLSGGTTLFPGIANRLSNELTNLVPSQLK 326
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 149062733 329 IKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKCF 377
Cdd:PTZ00452 327 IQVAAPPDRRFSAWIGGSIQCTLSTQQPQWIKRQEYDEQGPSIVHRKCF 375
ASKHA_NBD_ACTL7 cd10214
nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ...
9-376 3.53e-168

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: 474.22  E-value: 3.53e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733   9 ALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIW 88
Cdd:cd10214    5 AVIIDLGTGYCKAGFAGQPRPSYVISSTVGKPPQESAKTGDNRKETFVGKELANVEPPLKLVNPLRHGIVVDWDCVQDIW 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  89 HHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIY 168
Cdd:cd10214   85 EYIFEKEMKILPEEHAVLVSDPPLSPTTNREKYAELMFETFSIPAMHIAYQSRLSLYSYGRTSGLVVESGHGVSYVVPIH 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 169 EGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFvTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEksYELPDGQ 248
Cdd:cd10214  165 EGYNLPHITGRADYAGSDLTAYLMKLLNEAGNKF-TDDQLHIVEDIKKKCCYVALDFEEEMGLPPQEYTVD--YELPDGH 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 249 VITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMK 328
Cdd:cd10214  242 LITIGKERFRCPEMLFNPSLIGSKQPGLHTLTMNSLNKCDANLKKDLAKNILLCGGSTMFDGFPDRFQKELSKLCPNDNP 321
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 149062733 329 IkIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKC 376
Cdd:cd10214  322 I-VAASPERKYSVWTGGSILASLKSFQQLWVRRREYEERGPFVIYRKC 368
ASKHA_NBD_actin-like cd10169
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ...
10-368 1.75e-158

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: 445.40  E-value: 1.75e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  10 LVCDNGSGLCKAGFAGDDAPRAVFPsivgrprhqgvmvgmgqkdsyvgdeaqskrgiltlkypiehgiitnWDDMEKIWH 89
Cdd:cd10169    1 IVIDNGSGTIKAGFAGEDAPRLIFP----------------------------------------------WDDMEKIWE 34
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  90 HSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYE 169
Cdd:cd10169   35 HVFYNLLRVDPEEHPVLLTEPPLNPKANREKLAEILFETFNVPSLYIANQAVLSLYASGRTTGLVVDSGEGVTHIVPVYE 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 170 GYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCyvaldfenemataassssleksyelpdgqv 249
Cdd:cd10169  115 GYVLPHAVRRLDIGGRDLTDYLAKLLREKGYSFSTSAEREIVRDIKEKLC------------------------------ 164
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 250 itignerfrcpetlfqpsfigmesaGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKI 329
Cdd:cd10169  165 -------------------------GLHELIYDSIMKCDIDLRKELYSNIVLSGGTTLFPGFAERLQKELSKLAPSSVKV 219
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 149062733 330 KIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAG 368
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 ...
9-368 4.32e-158

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: 450.48  E-value: 4.32e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733   9 ALVCDNGSGLCKAGFAGDDAPRAVFPSIVG-RPRHQGVMVGMGQKDS-----YVGDEA-QSKRGILTLKYPIEHGIITNW 81
Cdd:cd13395    6 ALVLDIGSYSTRAGYAGEDTPKAVFPSVVGvVTDDDDAEDYVGGSGEkkrkyYIGTNSiGVPRPNMEVISPLKDGLIEDW 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  82 DDMEKIWHHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGV 161
Cdd:cd13395   86 DAFEKLWDHALKNRLRVDPSEHPLLLTEPSWNTRANREKLTELMFEKYNVPAFFLAKNAVLSAFANGRSTALVVDSGATS 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 162 THNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFV--------------------------TT------AERE 209
Cdd:cd13395  166 TSVVPVHDGYVLQKAIVRSPLGGDFLTDQLLKLLESKNIEIIprymikskepveggapakytkkdlpnTTssyhryMVRR 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 210 IVRDIKEKLCYVALDFENEmatAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFI---------GMESAGIHETT 280
Cdd:cd13395  246 VLQDFKESVCQVSDSPFDE---SEAASIPTVSYELPDGYNIEFGAERFKIPELLFDPSLVkgipappseGNELLGLPQLV 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 281 YNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPP---ERKYSVWIGGSILASLSTFQQM 357
Cdd:cd13395  323 YTSIGSCDVDIRPELYGNVVLTGGNSLLPGFTDRLNRELSEKAPGSLKLKILASGntvERRFSSWIGGSILASLGSFQQM 402
                        410
                 ....*....|.
gi 149062733 358 WISKQEYDEAG 368
Cdd:cd13395  403 WISKQEYEEHG 413
COG5277 COG5277
Actin-related protein [Cytoskeleton];
13-366 2.83e-139

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 403.02  E-value: 2.83e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  13 DNGSGLCKAG-FAGDDAP-----RAVFPSIVGRPRHQGVMVGMGqKDSYVGDEAQS-----KRGILTLKYPIEHGIIT-- 79
Cdd:COG5277   14 DFGTSYVKYGpIALEEKPrviqtRGLFLRIVGESKLLGPMEGLS-RGLVVGDEVSKylssvRDAIRNLKYPLRDGIVRrd 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  80 ---NWDDMEKIWHHSFYNELRVAPEEHPTL--LTEAPLNPKANREKMTQIMFETF---NVPAMYVAIQAVLSLYASGRTT 151
Cdd:COG5277   93 dedAWRVLKELLRYTFAQFLVVDPEFHGFLvvVALSALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPLAVAIAEKAVT 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 152 GIVLDSGDGVTHNVPIYEGyALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEReIVRDIKEKLCYVALDFENEM-A 230
Cdd:COG5277  173 CVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSDTAREEY-VVRVVKEALGLVPRDLAKAIqK 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 231 TAASSSSLEKSYELPDGQV-ITIGN---ERFRCPETLFQPSFIGMES----------------------AGIHETTYNSI 284
Cdd:COG5277  251 AASNPDSFEAKVRLPNPTVeIELGNyawERFLIGEILFNPNHEGFESyiqqgrlriedavigdvvlygeMGLAEAIINSI 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 285 MKCDIDIRKDLYANNVLSGGTTMY---PGIAD-------RMQKEITALAPsTMKIKIIAPPERKYSVWIGGSILASLSTF 354
Cdd:COG5277  331 MKCDVEIQDELYSNIILSGGAFNWsvpPGLEDvavdsvtRVQIELSELAP-ELKVNVRLVSDPQYSVWKGAIIYGYALPF 409
                        410
                 ....*....|....
gi 149062733 355 QQMW--ISKQEYDE 366
Cdd:COG5277  410 SVKWswITKEGWYF 423
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
9-372 2.70e-125

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: 366.51  E-value: 2.70e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733   9 ALVCDNGSGLCKAGFAGDDAPRAVFPSIVG-------RPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNW 81
Cdd:cd10221    1 AVVIDNGTGYTKMGYAGNTEPQFIIPTVIAikesakvGDGQRRSKKGIEDLDFYIGDEALANSPTYALKYPIRHGIVEDW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  82 DDMEKIWHHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRT--------TGI 153
Cdd:cd10221   81 DLMERFWEQCIFKYLRCEPEDHYFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQAVLALAASWTSrkvgertlTGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 154 VLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAA 233
Cdd:cd10221  161 VIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREEGIPPEDSLEVAKRIKERYCYVCPDIVKEFAKYD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 234 SS-SSLEKSYELPD---GQ--VITIGNERFRCPETLFQPSFIGME-SAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTT 306
Cdd:cd10221  241 SDpAKYIKQYTGINsvtGKpyTVDVGYERFLAPEIFFNPEIASSDfTTPLPEVVDQVIQSCPIDTRRGLYKNIVLSGGST 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 307 MYPGIADRMQKEITA----------------LAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPS 370
Cdd:cd10221  321 MFKDFGRRLQRDVKRivdarlkaseelsggkLKPKPIDVNVISHPMQRYAVWFGGSMLASTPEFYTVCHTKAEYEEYGPS 400

                 ..
gi 149062733 371 IV 372
Cdd:cd10221  401 IC 402
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
9-374 2.56e-122

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 359.43  E-value: 2.56e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733   9 ALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMV---GMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDME 85
Cdd:PTZ00280   6 VVVIDNGTGYTKMGYAGNTEPTYIIPTLIADNSKQSRRRskkGFEDLDFYIGDEALAASKSYTLTYPMKHGIVEDWDLME 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  86 KIWHHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYAS----------GRTTGIVL 155
Cdd:PTZ00280  86 KFWEQCIFKYLRCEPEEHYFILTEPPMNPPENREYTAEIMFETFNVKGLYIAVQAVLALRASwtskkakelgGTLTGTVI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 156 DSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMAT---- 231
Cdd:PTZ00280 166 DSGDGVTHVIPVVDGYVIGSSIKHIPLAGRDITNFIQQMLRERGEPIPAEDILLLAQRIKEKYCYVAPDIAKEFEKydsd 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 232 --------AASSSSLEKSYElpdgqvITIGNERFRCPETLFQPSFIGME-SAGIHETTYNSIMKCDIDIRKDLYANNVLS 302
Cdd:PTZ00280 246 pknhfkkyTAVNSVTKKPYT------VDVGYERFLGPEMFFHPEIFSSEwTTPLPEVVDDAIQSCPIDCRRPLYKNIVLS 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 303 GGTTMYPGIADRMQKEITA----------------LAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDE 366
Cdd:PTZ00280 320 GGSTMFKGFDKRLQRDVRKrvdrrlkkaeelsggkLKPIPIDVNVVSHPRQRYAVWYGGSMLASSPEFEKVCHTKAEYDE 399

                 ....*...
gi 149062733 367 AGPSIVHR 374
Cdd:PTZ00280 400 YGPSICRY 407
ASKHA_NBD_Arp6 cd10210
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ...
10-368 5.53e-99

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: 299.08  E-value: 5.53e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  10 LVCDNGSGLCKAGFAGDDAPRaVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQskrgiLTLKYPIEHGIITNWDDMEKIWH 89
Cdd:cd10210    2 LVLDNGAYTIKAGFASDDPPR-VIPNCIAKPKSERRRLFGDDQLDECKDLSG-----LFYRRPFERGYLVNWDLQRQIWD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  90 HSFYNE-LRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYA----------SGRTTGIVLDSG 158
Cdd:cd10210   76 HLFGKLlLNVDPSDTALVLTEPPFNPPSIQEAMDEIVFEEYGFQSLYRTTAAALSAFAyladseqsssSSSQCCLVVDSG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 159 DGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFvttaERE--IVRDIKEKLCYVALDFENEMATAAS-- 234
Cdd:cd10210  156 FSFTHIVPFFDGKPVKRAVRRIDVGGKLLTNYLKEIISYRQLNV----MDEtyLVNQIKEDLCFVSTDFYEDLEIAKKkg 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 235 -SSSLEKSYELPDG-----------------------QVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDID 290
Cdd:cd10210  232 kENTIRRDYVLPDYttskrgyvrdpeepnrgklkedeQVLRLNNERFTVPELLFHPSDIGIQQAGIAEAIVQSINACPEE 311
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 149062733 291 IRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAG 368
Cdd:cd10210  312 LQPLLYANIVLTGGNALFPGFRERLEAELRSLAPDDYDVNVTLPEDPITYAWEGGSLLAQSPEFEELAVTRAEYEEHG 389
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
10-373 3.18e-88

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: 270.41  E-value: 3.18e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  10 LVCDNGSGLCKAGFAGDDApravFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSkrgiltlkyPIEHGIITNWDDMEKIWH 89
Cdd:cd10209    1 VVIDAGSRLLKAGYAYPDR----EPSVVEPTRVTPAVEDGEESDTVVEGNTVS---------PIRRGRIEDWDALEALLR 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  90 HSFYNELR-VAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIY 168
Cdd:cd10209   68 YVFYTGLGwEEGNEGQVLIAEPLLTSKAERERLTQLMFETFNVSGLYASEQAVLSLYAVGRISGCVVDVGHGKIDIAPVW 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 169 EGYALPHAIMRLDLAGRDLTDYLMKILTERGYSfvTTAEREIVRDIKEKLCYVAldfENEMATAASSSSLEK-SYELPDG 247
Cdd:cd10209  148 EGAIQHNAVRRFEIGGRDLTELLAAELGKSNPK--VKLDRSIVERLKEAVAWSA---DDEEAYEKKVLTCSPeTYTLPDG 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 248 QVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTM 327
Cdd:cd10209  223 RVISVGKERYCVGEALFRPSILGIEEYGIVEQLVRAVSTSPSENRRQLLENIVLCGGTSSVPGLEARLQKEIRLLSSPSS 302
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 149062733 328 KIKIIAPPE------RKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVH 373
Cdd:cd10209  303 RPALVKPPEympentLRYSAWIGGAILAKVVFPQNQHVTKADYDETGPSVVH 354
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
9-369 5.15e-72

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: 228.23  E-value: 5.15e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733   9 ALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQgvmvGMGQKDSYVGDEA---QSKRGilTLKYPIEHGIITNWDDME 85
Cdd:cd10211    1 PIVIDNGSYQCRAGWAGDKEPRLVFRNLVAKPRDR----KKGITVTLVGNDIlndEAVRS--HLRSPFDRNVVTNFDLQE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  86 KIWHHSFyNELRVAPE---EHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRT----TGIVLDSG 158
Cdd:cd10211   75 QILDYIF-SHLGINSEgsvDHPIVLTEALCNPNYSRQLMSELLFECYGVPSVAYGIDSLFSYYHNQPQgdpsDGLVISSG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 159 DGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVT--TAEReiVRDIKEKLCYVALDFENEMATAASSS 236
Cdd:cd10211  154 YSTTHVIPVLNGRLDLSQCKRINLGGFHATDYLQRLLQLKYPTHPSaiTLSR--AEELVHEHCYVAEDYDEELKKWEDPE 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 237 SLEKSyelpdgqvitigNERFRCPetlfqpsfigmesAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQ 316
Cdd:cd10211  232 YYEEN------------VRKIQLP-------------FGLVETIEFVLKRYPAEQQDRLVQNVFLTGGNALFPGLKERLE 286
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 149062733 317 KEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGP 369
Cdd:cd10211  287 KELRAIRPFGSPFNVVRAKDPVLDAWRGAAKWALDSTFEKVWITKQEYEEKGG 339
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
40-375 7.91e-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: 191.75  E-value: 7.91e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  40 PRHQGVMVGMGQKDSYVGD--EAQSKRGILtlkYPIEHGIITNWDDMEKIWHHSFYNEL--RVAPEEHPTLLTEAPLNPK 115
Cdd:cd10208    7 PGSQTTRAGLGLGELLTPPtiEIPTRVEII---WPIQDGRVVDWDALEALWRHILFSLLsiPRPTNNSPVLLSVPPSWSK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 116 ANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKIL 195
Cdd:cd10208   84 SDLELLTQLFFERLNVPAFAILEAPLAALYAAGATSGIVVDIGHEKTDITPIVDSQVVPHALVSIPIGGQDCTAHLAQLL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 196 TER--GYSFVTTAEREIVRDIKEKLcyvaldFENEMATAASSSSleksyELPDGQVITIGNERFRCPETLFQPSFIGM-- 271
Cdd:cd10208  164 KSDepELKSQAESGEEATLDLAEAL------KKSPICEVLSDGA-----DLASGTEITVGKERFRACEPLFKPSSLRVdl 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 272 --ESAGIHETTYNSimkCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITAL-----------APSTMKIKIIaP---P 335
Cdd:cd10208  233 liAAIAGALVLNAS---DEPDKRPALWENIIIVGGGSRIRGLKEALLSELQQFhlisetsaspqQPRIIRLAKI-PdyfP 308
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 149062733 336 ERK-----YSVWIGGSILASLsTF----QQMWISKQEYDEAGPSIVHRK 375
Cdd:cd10208  309 EWKksgyeEAAFLGASIVAKL-VFndpsSKHYISKVDYNEKGPAAIHTK 356
ASKHA_NBD_Arp10 cd10207
nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins; ...
11-368 1.16e-49

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: 171.28  E-value: 1.16e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  11 VCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRhqgvmvgmGQKDSYVGDeaqsKRGILTLKypiehgiitnWDDM-EKIWH 89
Cdd:cd10207    2 VLDIGSAYTKCGFAGESAPRCIIPSEVKLPG--------GKKVIRVVD----QRSGNEEE----------LYEAlKEFLH 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  90 HSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYE 169
Cdd:cd10207   60 ELYFKHLLVNPKDRRVVVVESVLCPTPFRETLAKVLFKHFEVPSVLFAPSHLLSLLTLGIRTALVVDCGYRETRVLPVYE 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 170 GYALPHAIMRLDLAGRDLTDYLMKILTERGySFVTTAER-------------EIVRDIKEKLCYVA-LDFENEMATAASS 235
Cdd:cd10207  140 GVPLLSAWQSTPLGGKALHKRLKKLLLEHA-TVVTGDNKgqllssvdsllseEVLEDIKVRACFVTsLERGKTLQSATEE 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 236 SSLEKS-------YELPDGQVITIGNERFRCPETLFQPSFIGMESagIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMY 308
Cdd:cd10207  219 GSTEEPsppppvdYPLDGEKILIVPGSIRESAEELLFEGDNEEKS--LPTLILDSLLKCPIDVRKQLAENIVVIGGTSML 296
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 149062733 309 PGIADRMQKEITA----------LAPSTMKI---KIIAPPErkYSVWIGGSILASLSTFQQMWISKQEYDEAG 368
Cdd:cd10207  297 PGFKHRLLEELRAllrkpkyfeeLAPKTFRFhtpPSVFKPN--YLAWLGGSIFGALESILGRSLSREAYLQTG 367
ASKHA_NBD_AtArp8-like cd13396
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and ...
93-368 1.22e-45

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: 159.25  E-value: 1.22e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  93 YNELRVAPEEHPTLLTEaPL-------NPKANREKMTQIMFETF---NVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVT 162
Cdd:cd13396   49 MTRMQVKPSRQPVVVSL-PLchsddteSAAASRRQLRGTIFNVLfdmNVPAVCAVDQAVLALYAANRTSGIVVNIGFRVT 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 163 HNVPIYEGYALPH-AIMRLDLAGRDLTDYLMKILTERGYSFVTTAereIVRDIKEKLCYVALDFENEMAtaassSSLEKS 241
Cdd:cd13396  128 TIVPVYRGRVMHDiGVEVVGQGALRLTGFLKELMQQNGIRFPSLY---TVRTIKEKLCYVAEDYEAELA-----KDTQAS 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 242 YELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIR---KDLYANNVLSGGTTMYPGIADRMQKE 318
Cdd:cd13396  200 CEVAGEGWFTLSNERFKTGEILFQPGLGGMRAMGLHQAVALCMDHCALVHSqgdDGWFKTIVLSGGSACLPGLSERLERE 279
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 149062733 319 ITALAPSTMK--IKIIAPPERKYSVWIGGSILASLSTFQQMW-ISKQEYDEAG 368
Cdd:cd13396  280 LRKLLPKSLSegIRIIPPPLGPDSAWQGAKLISNLSNFPDGWcITKKQFRNKP 332
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
305-376 3.43e-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: 3.43e-35
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149062733 305 TTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKC 376
Cdd:NF040575  61 RVNESGFYEKLKKSITEKAPKGALIGMTLDPKPESAAWRGAAMYAASEGFVEMAITKQEYDESGPSIVHRKC 132
ASKHA_NBD_Arp8-like cd10206
nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The ...
50-371 1.02e-26

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: 110.41  E-value: 1.02e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  50 GQKDSYVGDEAQ--SKRGILTLKYPIEHGIItNW-----------DDMEKIWHHSFYNELRVAPEEHPtllteaplNPKA 116
Cdd:cd10206  118 DYPDFLVGEEALrlPPSEEYNLHWPIRRGRL-NVhsdggsltavlDDLEDIWSHALEEKLEIPRKDLK--------NYRA 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 117 --------NR---EKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGR 185
Cdd:cd10206  189 vlvipdlfDRrhvKELVDLLLRRLGFSSVFVHQESVCATFGAGLSSACVVDIGAQKTSVACVEDGLSIPNSRIRLPYGGD 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 186 DLTDYLMKILteRGYSFVTTA-------EREIVRDIKEKLCYVALDFENemataassssleksyelpdGQVITIGNERFR 258
Cdd:cd10206  269 DITRCFLWLL--RRSGFPYREcnlnsplDFLLLERLKETYCTLDQDDIG-------------------VQLHEFYVREPG 327
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 259 CPETLFQpsfigMESAGIHETTYNSIMKC-DIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMK----IKIIA 333
Cdd:cd10206  328 QPTLKYQ-----FKLLPLDEAIVQSILSCaSDELKRKMYSSILLVGGGAKIPGLAEALEDRLLIKIPSLFEavetVEVLP 402
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 149062733 334 PPERK---YSVWIGGSILASLSTFQQMWISKQEYDEAGPSI 371
Cdd:cd10206  403 PPKDMdpsLLAWKGGAVLACLDSAQELWITRKEWQRLGVRA 443
ASKHA_NBD_ScArp7-like cd10212
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and ...
10-365 1.36e-18

nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and similar proteins; Saccharomyces cerevisiae Arp7, also called actin-like protein 7, is a component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. It is also part of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, which is required for the positive and negative regulation of gene expression of many genes. Arp7 forms a stable heterodimer with Arp9 protein in both the RSC and SWI/SNF chromatin-remodeling complexes. It has been suggested that this dimer functions as a module with DNA bending proteins, to achieve correct architecture and facilitate complex-complex interactions. Fission yeast SWI/SNF and RSC complexes do not contain Arp7 and Arp8, but instead contain Arp9 and Arp42.


Pssm-ID: 466818 [Multi-domain]  Cd Length: 424  Bit Score: 86.70  E-value: 1.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  10 LVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGvmvgmGQKDSYVG-----DEAQSKR-GILTLKYPIEHGIITNWDD 83
Cdd:cd10212    6 VVIHNGSHRTVAGFSNVELPQCIIPSSYIKRTDEG-----GEAEFIFGtynmiDAAAEKRnGDEVYTLVDSQGLPYNWDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  84 MEKIWHHSFYNELRVAPEEHPTLLTEAPLNPKANR---EKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDG 160
Cdd:cd10212   81 LEMQWRYLYDTQLKVSPEELPLVITMPATNGKPDMailERYYELAFDKLNVPVFQIVIEPLAIALSMGKSSAFVIDIGAS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 161 VTHNVPIYEGYALPHAIMRLDLAGrDLTDY--------LMK--------------------------------------- 193
Cdd:cd10212  161 GCNVTPIIDGIVVKNAVVRSKFGG-DFLDFqvherlapLIKeendmenmadeqkrstdvwyeastwiqqfkstmlqvsek 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 194 --ILTERGY---SFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKsyelPDGQVITIG-NERFRCPETLFQPS 267
Cdd:cd10212  240 dlFELERYYkeqADIYAKQQEQLKQMDQQLQYTALTGSPNNPLVQKKNFLFK----PLNKTLTLDlKECYQFAEYLFKPQ 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 268 FIGMESA---GIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAP----STMKIKIIAppERKYS 340
Cdd:cd10212  316 LISDKFSpedGLGPLMAKSVKKAPEQVYSLLLTNVIITGSTSLIEGMEQRIIKELSIRFPqyklTTFANQVMM--DRKIQ 393
                        410       420
                 ....*....|....*....|....*.
gi 149062733 341 VWIGGSILASLSTFQ-QMWISKQEYD 365
Cdd:cd10212  394 GWLGALTMANLPSWSlGKWYSKEDYE 419
ASKHA_NBD_MamK cd24009
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ...
24-318 1.60e-07

nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called magnetosome cytoskeleton protein MamK, is a protein with ATPase activity which forms dynamic cytoplasmic filaments (probably with paralog MamK-like) that may organize magnetosomes into long chains running parallel to the long axis of the cell. Turnover of MamK filaments is probably promoted by MamK-like (e.g.. MamJ and/or LimJ), which provides a monomer pool. MamK forms twisted filaments in the presence of ATP or GTP. It serves to close gaps between magnetosomes in the chain. Interaction with MCP10 is involved in controlling the response to magnetic fields, possibly by controlling flagellar rotation. The MamK family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466859 [Multi-domain]  Cd Length: 328  Bit Score: 52.60  E-value: 1.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733  24 AGDDAPRAVFPSIVGRPRHQGVMVGMGqKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDmekiwhhsfyNELRVAPE-- 101
Cdd:cd24009   16 VTSRGKRFSFRSVVGYPKDIIARKLLG-KEVLFGDEALENRLALDLRRPLEDGVIKEGDD----------RDLEAAREll 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 102 EHptLLTEAPLNPKA---------------NREKMTQIMFETFN----VPAMY-VAiqavlslYASGRTTG-IVLDSGDG 160
Cdd:cd24009   85 QH--LIELALPGPDDeiyavigvparasaeNKQALLEIARELVDgvmvVSEPFaVA-------YGLDRLDNsLIVDIGAG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 161 VTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERgY--SFVTtaeREIVRDIKEKLCYVALDFENEMAtaassssl 238
Cdd:cd24009  156 TTDLCRMKGTIPTEEDQITLPKAGDYIDEELVDLIKER-YpeVQLT---LNMARRWKEKYGFVGDASEPVKV-------- 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149062733 239 eksyELP-DGQVIT--IGNE-RFRCpETLFQPsfigmesagIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADR 314
Cdd:cd24009  224 ----ELPvDGKPVTydITEElRIAC-ESLVPD---------IVEGIKKLIASFDPEFQEELRNNIVLAGGGSRIRGLDTY 289

                 ....
gi 149062733 315 MQKE 318
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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