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Conserved domains on  [gi|15229955|ref|NP_187818|]
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actin-11 [Arabidopsis thaliana]

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: 912.90  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955   8 QPLVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDMEKI 87
Cdd:cd10224   1 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  88 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 167
Cdd:cd10224  81 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 168 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTSAEREIVRDVKEKLAYIALDYEQEMETANTSSSVEKSYELPDG 247
Cdd:cd10224 161 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 248 QVITIGGERFRCPEVLFQPSLVGMEAAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMSKEITALAPSSM 327
Cdd:cd10224 241 QVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTM 320
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 15229955 328 KIKVVAPPERKYSVWIGGSILASLSTFQQMWIAKAEYDESGPSIV 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: 912.90  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955   8 QPLVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDMEKI 87
Cdd:cd10224   1 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  88 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 167
Cdd:cd10224  81 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 168 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTSAEREIVRDVKEKLAYIALDYEQEMETANTSSSVEKSYELPDG 247
Cdd:cd10224 161 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 248 QVITIGGERFRCPEVLFQPSLVGMEAAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMSKEITALAPSSM 327
Cdd:cd10224 241 QVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTM 320
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 15229955 328 KIKVVAPPERKYSVWIGGSILASLSTFQQMWIAKAEYDESGPSIV 372
Cdd:cd10224 321 KIKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIV 365
PTZ00281 PTZ00281
actin; Provisional
5-377 0e+00

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 739.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955    5 EDIQPLVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDM 84
Cdd:PTZ00281   4 EDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955   85 EKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHT 164
Cdd:PTZ00281  84 EKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVSHT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  165 VPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTSAEREIVRDVKEKLAYIALDYEQEMETANTSSSVEKSYEL 244
Cdd:PTZ00281 164 VPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEMQTAASSSALEKSYEL 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  245 PDGQVITIGGERFRCPEVLFQPSLVGMEAAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMSKEITALAP 324
Cdd:PTZ00281 244 PDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELTALAP 323
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15229955  325 SSMKIKVVAPPERKYSVWIGGSILASLSTFQQMWIAKAEYDESGPSIVHRKCF 377
Cdd:PTZ00281 324 STMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIVHRKCF 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: 638.53  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955      8 QPLVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGmGQKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDMEKI 87
Cdd:smart00268   2 PAIVIDNGSGTIKAGFAGEDFPQVVFPSIVGRPKDGKGMVG-DAKDIFVGDEAQEKRGGLELKYPIENGIVENWDDMEKI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955     88 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 167
Cdd:smart00268  81 WDYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVPV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955    168 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTSAEREIVRDVKEKLAYIALDYEQEMETANT---SSSVEKSYEL 244
Cdd:smart00268 161 VDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLAREsseSSKLEKTYEL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955    245 PDGQVITIGGERFRCPEVLFQPSLVGMEAAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMSKEITALAP 324
Cdd:smart00268 241 PDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELKQLAP 320
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 15229955    325 SSMKIKVVAPPERKYSVWIGGSILASLSTFQQMWIAKAEYDESGPSIVHRKCF 377
Cdd:smart00268 321 KKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERKCF 373
Actin pfam00022
Actin;
7-377 0e+00

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 555.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955     7 IQPLVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGmgqKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDMEK 86
Cdd:pfam00022   1 VSALVIDNGSHTTRAGFAGEDAPKAVIPSCVGKPRGTKVEAA---NKYYVGDEALTYRPGMEVRSPVEDGIVVDWDAMEE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955    87 IWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVP 166
Cdd:pfam00022  78 IWEHVLKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955   167 IYEGYALPHAILRLDLAGRDLTDYLMKILTER------------------------------GYSFTTSAEREIVRDVKE 216
Cdd:pfam00022 158 VHDGYVLQKAIRRSDLGGDFLTDYLRELLRSRnieitprylikskkpgdpapavtkrelpdtTYSYKTYQERRVLEEIKE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955   217 KLAYIALDYEQEMETAntSSSVEKSYELPDGQVITIGGERFRCPEVLFQPSLVGME--------AAGIHETTYNSIMKCD 288
Cdd:pfam00022 238 SVCYVSDDPFGDETTS--SSIPTRVYELPDGSTIILGAERFRVPEILFNPSLIGSEselpppqtAVGIPELIVDAINACD 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955   289 VDIRKDLYGNIVLSGGTTMFPGIADRMSKEITALAPSSMKIKVVAPP---ERKYSVWIGGSILASLSTFQQMWIAKAEYD 365
Cdd:pfam00022 316 VDLRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVKIIAPGntvERRYSAWIGGSILASLGTFQQMWVSKQEYE 395
                         410
                  ....*....|..
gi 15229955   366 ESGPSIVHRKCF 377
Cdd:pfam00022 396 EHGASVVERKCK 407
COG5277 COG5277
Actin-related protein [Cytoskeleton];
9-367 2.65e-133

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 387.61  E-value: 2.65e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955   9 PLVCDNGTGMVKAG-FAGDDAP-----RAVFPSIVGRPRHTGVMVGMGqKDAYVGDEAQS-----KRGILTLKYPIEHGI 77
Cdd:COG5277  10 VIGIDFGTSYVKYGpIALEEKPrviqtRGLFLRIVGESKLLGPMEGLS-RGLVVGDEVSKylssvRDAIRNLKYPLRDGI 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  78 V-----SNWDDMEKIWHHTFYNELRVAPEEHP--VLLTEAPLNPKANREKMTQIMFETF---NTPAMYVAIQAVLSLYAS 147
Cdd:COG5277  89 VrrddeDAWRVLKELLRYTFAQFLVVDPEFHGflVVVALSALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPLAVAIAE 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 148 GRTTGIVLDSGDGVSHTVPIYEGyALPHAILRLDLAGRDLTDYLMKILTERGYSFTTSAEReIVRDVKEKLAYIALDYEQ 227
Cdd:COG5277 169 KAVTCVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSDTAREEY-VVRVVKEALGLVPRDLAK 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 228 EME-TANTSSSVEKSYELPDGQV-ITIG---GERFRCPEVLFQPSLVGMEA----------------------AGIHETT 280
Cdd:COG5277 247 AIQkAASNPDSFEAKVRLPNPTVeIELGnyaWERFLIGEILFNPNHEGFESyiqqgrlriedavigdvvlygeMGLAEAI 326
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 281 YNSIMKCDVDIRKDLYGNIVLSGGTTMF---PGIAD-------RMSKEITALAPsSMKIKVVAPPERKYSVWIGGSILAS 350
Cdd:COG5277 327 INSIMKCDVEIQDELYSNIILSGGAFNWsvpPGLEDvavdsvtRVQIELSELAP-ELKVNVRLVSDPQYSVWKGAIIYGY 405
                       410
                ....*....|....*....
gi 15229955 351 LSTFQQMW--IAKAEYDES 367
Cdd:COG5277 406 ALPFSVKWswITKEGWYFL 424
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
305-376 1.86e-31

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: 115.85  E-value: 1.86e-31
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229955  305 TTMFPGIADRMSKEITALAPSSMKIKVVAPPERKYSVWIGGSILASLSTFQQMWIAKAEYDESGPSIVHRKC 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: 912.90  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955   8 QPLVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDMEKI 87
Cdd:cd10224   1 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  88 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 167
Cdd:cd10224  81 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 168 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTSAEREIVRDVKEKLAYIALDYEQEMETANTSSSVEKSYELPDG 247
Cdd:cd10224 161 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 248 QVITIGGERFRCPEVLFQPSLVGMEAAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMSKEITALAPSSM 327
Cdd:cd10224 241 QVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTM 320
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 15229955 328 KIKVVAPPERKYSVWIGGSILASLSTFQQMWIAKAEYDESGPSIV 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 ...
9-368 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: 755.18  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955   9 PLVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDMEKIW 88
Cdd:cd13397   2 AVVIDNGSGLIKAGFAGEDLPRAVFPSVVGRPKYKAVMLGAGQKEVYVGDEAQEKRGVLTLSYPIEHGIVTNWDDMEKIW 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  89 HHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIY 168
Cdd:cd13397  82 HHTFENELRVKPEEHPVLLTEAPLNPKQNREKMAEIMFETFGVPAFYVAIQAVLSLYSSGRTTGLVLDSGDGVTHTVPIY 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 169 EGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTSAEREIVRDVKEKLAYIALDYEQEMETanTSSSVEKSYELPDGQ 248
Cdd:cd13397 162 EGYALPHAVQRLDLAGRDLTEYLMKLLKERGHSFTTTAEREIVRDIKEKLCYVALDYEEELKK--KSEELEKEYTLPDGQ 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 249 VITIGGERFRCPEVLFQPSLVGMEAAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMSKEITALAPSSMK 328
Cdd:cd13397 240 VIKIGSERFRCPEALFRPSLIGREAPGIHKLVYNSIMKCDIDIRKDLYSNIVLSGGSTMFPGLPERLQKELEALAPSSTK 319
                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 15229955 329 IKVVAPPERKYSVWIGGSILASLSTFQQMWIAKAEYDESG 368
Cdd:cd13397 320 VKVIAPPERKYSVWIGGSILASLSTFKSMWITRAEYDEFG 359
PTZ00281 PTZ00281
actin; Provisional
5-377 0e+00

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 739.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955    5 EDIQPLVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDM 84
Cdd:PTZ00281   4 EDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955   85 EKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHT 164
Cdd:PTZ00281  84 EKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVSHT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  165 VPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTSAEREIVRDVKEKLAYIALDYEQEMETANTSSSVEKSYEL 244
Cdd:PTZ00281 164 VPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEMQTAASSSALEKSYEL 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  245 PDGQVITIGGERFRCPEVLFQPSLVGMEAAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMSKEITALAP 324
Cdd:PTZ00281 244 PDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELTALAP 323
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15229955  325 SSMKIKVVAPPERKYSVWIGGSILASLSTFQQMWIAKAEYDESGPSIVHRKCF 377
Cdd:PTZ00281 324 STMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIVHRKCF 376
PTZ00004 PTZ00004
actin-2; Provisional
1-377 0e+00

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 705.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955    1 MADgEDIQPLVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVSN 80
Cdd:PTZ00004   1 MSV-EETNAAVVDNGSGMVKAGFAGDDAPRCVFPSIVGRPKNPGIMVGMEEKDCYVGDEAQDKRGILTLKYPIEHGIVTN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955   81 WDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDG 160
Cdd:PTZ00004  80 WDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETHNVPAMYVAIQAVLSLYASGRTTGIVLDSGDG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  161 VSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTSAEREIVRDVKEKLAYIALDYEQEM-ETANTSSSVE 239
Cdd:PTZ00004 160 VSHTVPIYEGYSLPHAIHRLDVAGRDLTEYMMKILHERGTTFTTTAEKEIVRDIKEKLCYIALDFDEEMgNSAGSSDKYE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  240 KSYELPDGQVITIGGERFRCPEVLFQPSLVGM-EAAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMSKE 318
Cdd:PTZ00004 240 ESYELPDGTIITVGSERFRCPEALFQPSLIGKeEPPGIHELTFQSINKCDIDIRKDLYGNIVLSGGTTMYRGLPERLTKE 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15229955  319 ITALAPSSMKIKVVAPPERKYSVWIGGSILASLSTFQQMWIAKAEYDESGPSIVHRKCF 377
Cdd:PTZ00004 320 LTTLAPSTMKIKVVAPPERKYSVWIGGSILSSLPTFQQMWVTKEEYDESGPSIVHRKCF 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: 638.53  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955      8 QPLVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGmGQKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDMEKI 87
Cdd:smart00268   2 PAIVIDNGSGTIKAGFAGEDFPQVVFPSIVGRPKDGKGMVG-DAKDIFVGDEAQEKRGGLELKYPIENGIVENWDDMEKI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955     88 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 167
Cdd:smart00268  81 WDYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVPV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955    168 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTSAEREIVRDVKEKLAYIALDYEQEMETANT---SSSVEKSYEL 244
Cdd:smart00268 161 VDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLAREsseSSKLEKTYEL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955    245 PDGQVITIGGERFRCPEVLFQPSLVGMEAAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMSKEITALAP 324
Cdd:smart00268 241 PDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELKQLAP 320
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 15229955    325 SSMKIKVVAPPERKYSVWIGGSILASLSTFQQMWIAKAEYDESGPSIVHRKCF 377
Cdd:smart00268 321 KKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERKCF 373
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
8-376 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 15229955   8 QPLVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDMEKI 87
Cdd:cd10216   2 QPVVIDNGSGVIKAGFAGDDIPKVVFPSYVGRPKHVRVMAGALEGDVFVGPKAEEHRGLLKIRYPMEHGIVTDWNDMERI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  88 WHHTFYNE-LRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVP 166
Cdd:cd10216  82 WQYVYSKLqLNTFSEEHPVLLTEAPLNPRKNREKAAEVFFETFNVPALFVSMQAVLSLYASGRTTGVVLDSGDGVTHAVP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 167 IYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTSAEREIVRDVKEKLAYIALDyEQEMETANTSSSVEKSYELPD 246
Cdd:cd10216 162 IYEGFALPHSIRRVDIAGRDVTEYLQLLLRKSGYNFHTSAEFEIVREIKEKACYVALN-PQKEEKLEEEKTEKAQYTLPD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 247 GQVITIGGERFRCPEVLFQPSLVGMEAAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMSKEITALAPSS 326
Cdd:cd10216 241 GSTIEIGPERFRAPEILFNPELIGLEYPGVHEVLVDSIQKSDLDLRKTLYSNIVLSGGSTLFKGFGDRLLSEVKKLAPKD 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 15229955 327 MKIKVVAPPERKYSVWIGGSILASLSTFQQMWIAKAEYDESGPSIVHRKC 376
Cdd:cd10216 321 VKIRISAPPERLYSTWIGGSILASLSTFKKMWVSKKEYEEDGARILHRKT 370
Actin pfam00022
Actin;
7-377 0e+00

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 555.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955     7 IQPLVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGmgqKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDMEK 86
Cdd:pfam00022   1 VSALVIDNGSHTTRAGFAGEDAPKAVIPSCVGKPRGTKVEAA---NKYYVGDEALTYRPGMEVRSPVEDGIVVDWDAMEE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955    87 IWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVP 166
Cdd:pfam00022  78 IWEHVLKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955   167 IYEGYALPHAILRLDLAGRDLTDYLMKILTER------------------------------GYSFTTSAEREIVRDVKE 216
Cdd:pfam00022 158 VHDGYVLQKAIRRSDLGGDFLTDYLRELLRSRnieitprylikskkpgdpapavtkrelpdtTYSYKTYQERRVLEEIKE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955   217 KLAYIALDYEQEMETAntSSSVEKSYELPDGQVITIGGERFRCPEVLFQPSLVGME--------AAGIHETTYNSIMKCD 288
Cdd:pfam00022 238 SVCYVSDDPFGDETTS--SSIPTRVYELPDGSTIILGAERFRVPEILFNPSLIGSEselpppqtAVGIPELIVDAINACD 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955   289 VDIRKDLYGNIVLSGGTTMFPGIADRMSKEITALAPSSMKIKVVAPP---ERKYSVWIGGSILASLSTFQQMWIAKAEYD 365
Cdd:pfam00022 316 VDLRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVKIIAPGntvERRYSAWIGGSILASLGTFQQMWVSKQEYE 395
                         410
                  ....*....|..
gi 15229955   366 ESGPSIVHRKCF 377
Cdd:pfam00022 396 EHGASVVERKCK 407
ASKHA_NBD_Arp2 cd10220
nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, ...
8-372 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: 533.30  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955   8 QPLVCDNGTGMVKAGFAGDDAPRAVFPSIVGRP--RHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDME 85
Cdd:cd10220   1 KVVVCDNGTGFVKCGFAGSNFPEHVFPSLVGRPilRAEEKVGDIEIKDIMVGDEASELRSMLEVTYPMENGIVRNWDDME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  86 KIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTV 165
Cdd:cd10220  81 HLWDYTFGEKLKIDPRECKILLTEPPMNPTKNREKMVEVMFEKYGFAGVYVAIQAVLTLYAQGLLTGVVVDSGDGVTHIV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 166 PIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTSAEREIVRDVKEKLAYIALDYEQEMETANTSSSVEKSYELP 245
Cdd:cd10220 161 PVYEGFSLPHLTRRLDVAGRDITRYLIKLLLLRGYAFNRTADFETVREIKEKLCYVAYDIELEQKLALETTVLVESYTLP 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 246 DGQVITIGGERFRCPEVLFQPSLVGMEAAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMSKEITAL--- 322
Cdd:cd10220 241 DGRVIKVGGERFEAPEALFQPHLIDVEGPGIAELLFNTIQAADIDTRPELYKHIVLSGGSTMYPGLPSRLEKEIKQLyle 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15229955 323 --------APSSMKIKVVAPPERKYSVWIGGSILASLSTFQ-QMWIAKAEYDESGPSIV 372
Cdd:cd10220 321 rvlkgdteRLSKFKIRIEDPPRRKHMVFLGGAVLADIMKDKdEFWITRQEYEEQGVRVL 379
PTZ00466 PTZ00466
actin-like protein; Provisional
8-377 6.25e-179

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 501.78  E-value: 6.25e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955    8 QPLVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDMEKI 87
Cdd:PTZ00466  13 QPIIIDNGTGYIKAGFAGEDVPNLVFPSYVGRPKYKRVMAGAVEGNIFVGNKAEEYRGLLKVTYPINHGIIENWNDMENI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955   88 WHHTfYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 167
Cdd:PTZ00466  93 WIHV-YNSMKINSEEHPVLLTEAPLNPQKNKEKIAEVFFETFNVPALFISIQAILSLYSCGKTNGTVLDCGDGVCHCVSI 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  168 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTSAEREIVRDVKEKLAYIALDYEQEMETANTSSSVeKSYELPDG 247
Cdd:PTZ00466 172 YEGYSITNTITRTDVAGRDITTYLGYLLRKNGHLFNTSAEMEVVKNMKENCCYVSFNMNKEKNSSEKALTT-LPYILPDG 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  248 QVITIGGERFRCPEVLFQPSLVGMEAAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMSKEITALAPSSM 327
Cdd:PTZ00466 251 SQILIGSERYRAPEVLFNPSILGLEYLGLSELIVTSITRADMDLRRTLYSHIVLSGGTTMFHGFGDRLLNEIRKFAPKDI 330
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 15229955  328 KIKVVAPPERKYSVWIGGSILASLSTFQQMWIAKAEYDESGPSIVHRKCF 377
Cdd:PTZ00466 331 TIRISAPPERKFSTFIGGSILASLATFKKIWISKQEFDEYGSVILHRKTF 380
PTZ00452 PTZ00452
actin; Provisional
10-377 3.87e-175

actin; Provisional


Pssm-ID: 185631  Cd Length: 375  Bit Score: 492.35  E-value: 3.87e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955   10 LVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDMEKIWH 89
Cdd:PTZ00452   8 VVIDNGSGYCKIGIAGDDAPTSCFPAIVGRSKQNDGIFSTFNKEYYVGEEAQAKRGVLAIKEPIQNGIINSWDDIEIIWH 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955   90 HTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYE 169
Cdd:PTZ00452  88 HAFYNELCMSPEDQPVFMTDAPMNSKFNRERMTQIMFETFNTPCLYISNEAVLSLYTSGKTIGLVVDSGEGVTHCVPVFE 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  170 GYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTSAEREIVRDVKEKLAYIALDYEQEMETANTSSSVEKSYELPDGQV 249
Cdd:PTZ00452 168 GHQIPQAITKINLAGRLCTDYLTQILQELGYSLTEPHQRIIVKNIKERLCYTALDPQDEKRIYKESNSQDSPYKLPDGNI 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  250 ITIGGERFRCPEVLFQPSLVGMEAAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMSKEITALAPSSMKI 329
Cdd:PTZ00452 248 LTIKSQKFRCSEILFQPKLIGLEVAGIHHLAYSSIKKCDLDLRQELCRNIVLSGGTTLFPGIANRLSNELTNLVPSQLKI 327
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 15229955  330 KVVAPPERKYSVWIGGSILASLSTFQQMWIAKAEYDESGPSIVHRKCF 377
Cdd:PTZ00452 328 QVAAPPDRRFSAWIGGSIQCTLSTQQPQWIKRQEYDEQGPSIVHRKCF 375
ASKHA_NBD_ACTL7 cd10214
nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ...
5-376 1.45e-167

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: 472.68  E-value: 1.45e-167
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955   5 EDIQPLVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDM 84
Cdd:cd10214   1 KETKAVIIDLGTGYCKAGFAGQPRPSYVISSTVGKPPQESAKTGDNRKETFVGKELANVEPPLKLVNPLRHGIVVDWDCV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  85 EKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHT 164
Cdd:cd10214  81 QDIWEYIFEKEMKILPEEHAVLVSDPPLSPTTNREKYAELMFETFSIPAMHIAYQSRLSLYSYGRTSGLVVESGHGVSYV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 165 VPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTSaEREIVRDVKEKLAYIALDYEQEMetANTSSSVEKSYEL 244
Cdd:cd10214 161 VPIHEGYNLPHITGRADYAGSDLTAYLMKLLNEAGNKFTDD-QLHIVEDIKKKCCYVALDFEEEM--GLPPQEYTVDYEL 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 245 PDGQVITIGGERFRCPEVLFQPSLVGMEAAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMSKEITALAP 324
Cdd:cd10214 238 PDGHLITIGKERFRCPEMLFNPSLIGSKQPGLHTLTMNSLNKCDANLKKDLAKNILLCGGSTMFDGFPDRFQKELSKLCP 317
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 15229955 325 SSMKIkVVAPPERKYSVWIGGSILASLSTFQQMWIAKAEYDESGPSIVHRKC 376
Cdd:cd10214 318 NDNPI-VAASPERKYSVWTGGSILASLKSFQQLWVRRREYEERGPFVIYRKC 368
ASKHA_NBD_actin-like cd10169
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ...
10-368 1.15e-159

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: 448.09  E-value: 1.15e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  10 LVCDNGTGMVKAGFAGDDAPRAVFPsivgrprhtgvmvgmgqkdayvgdeaqskrgiltlkypiehgivsnWDDMEKIWH 89
Cdd:cd10169   1 IVIDNGSGTIKAGFAGEDAPRLIFP----------------------------------------------WDDMEKIWE 34
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  90 HTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYE 169
Cdd:cd10169  35 HVFYNLLRVDPEEHPVLLTEPPLNPKANREKLAEILFETFNVPSLYIANQAVLSLYASGRTTGLVVDSGEGVTHIVPVYE 114
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 170 GYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTSAEREIVRDVKEKLayialdyeqemetantsssveksyelpdgqv 249
Cdd:cd10169 115 GYVLPHAVRRLDIGGRDLTDYLAKLLREKGYSFSTSAEREIVRDIKEKL------------------------------- 163
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 250 itiggerfrcpevlfqpslvgmeaAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMSKEITALAPSSMKI 329
Cdd:cd10169 164 ------------------------CGLHELIYDSIMKCDIDLRKELYSNIVLSGGTTLFPGFAERLQKELSKLAPSSVKV 219
                       330       340       350
                ....*....|....*....|....*....|....*....
gi 15229955 330 KVVAPPERKYSVWIGGSILASLSTFQQMWIAKAEYDESG 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 ...
4-368 5.88e-156

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: 444.70  E-value: 5.88e-156
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955   4 GEDIQPLVCDNGTGMVKAGFAGDDAPRAVFPSIVG-RPRHTGVMVGMGQKDA-----YVGDEA-QSKRGILTLKYPIEHG 76
Cdd:cd13395   1 GDEVGALVLDIGSYSTRAGYAGEDTPKAVFPSVVGvVTDDDDAEDYVGGSGEkkrkyYIGTNSiGVPRPNMEVISPLKDG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  77 IVSNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLD 156
Cdd:cd13395  81 LIEDWDAFEKLWDHALKNRLRVDPSEHPLLLTEPSWNTRANREKLTELMFEKYNVPAFFLAKNAVLSAFANGRSTALVVD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 157 SGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERG------YSF----------------------TTS--- 205
Cdd:cd13395 161 SGATSTSVVPVHDGYVLQKAIVRSPLGGDFLTDQLLKLLESKNieiiprYMIkskepveggapakytkkdlpntTSSyhr 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 206 -AEREIVRDVKEKLAYIALDYEQEMETANTSSsveKSYELPDGQVITIGGERFRCPEVLFQPSLV---------GMEAAG 275
Cdd:cd13395 241 yMVRRVLQDFKESVCQVSDSPFDESEAASIPT---VSYELPDGYNIEFGAERFKIPELLFDPSLVkgipappseGNELLG 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 276 IHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMSKEITALAPSSMKIKVVAPP---ERKYSVWIGGSILASLS 352
Cdd:cd13395 318 LPQLVYTSIGSCDVDIRPELYGNVVLTGGNSLLPGFTDRLNRELSEKAPGSLKLKILASGntvERRFSSWIGGSILASLG 397
                       410
                ....*....|....*.
gi 15229955 353 TFQQMWIAKAEYDESG 368
Cdd:cd13395 398 SFQQMWISKQEYEEHG 413
COG5277 COG5277
Actin-related protein [Cytoskeleton];
9-367 2.65e-133

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 387.61  E-value: 2.65e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955   9 PLVCDNGTGMVKAG-FAGDDAP-----RAVFPSIVGRPRHTGVMVGMGqKDAYVGDEAQS-----KRGILTLKYPIEHGI 77
Cdd:COG5277  10 VIGIDFGTSYVKYGpIALEEKPrviqtRGLFLRIVGESKLLGPMEGLS-RGLVVGDEVSKylssvRDAIRNLKYPLRDGI 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  78 V-----SNWDDMEKIWHHTFYNELRVAPEEHP--VLLTEAPLNPKANREKMTQIMFETF---NTPAMYVAIQAVLSLYAS 147
Cdd:COG5277  89 VrrddeDAWRVLKELLRYTFAQFLVVDPEFHGflVVVALSALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPLAVAIAE 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 148 GRTTGIVLDSGDGVSHTVPIYEGyALPHAILRLDLAGRDLTDYLMKILTERGYSFTTSAEReIVRDVKEKLAYIALDYEQ 227
Cdd:COG5277 169 KAVTCVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSDTAREEY-VVRVVKEALGLVPRDLAK 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 228 EME-TANTSSSVEKSYELPDGQV-ITIG---GERFRCPEVLFQPSLVGMEA----------------------AGIHETT 280
Cdd:COG5277 247 AIQkAASNPDSFEAKVRLPNPTVeIELGnyaWERFLIGEILFNPNHEGFESyiqqgrlriedavigdvvlygeMGLAEAI 326
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 281 YNSIMKCDVDIRKDLYGNIVLSGGTTMF---PGIAD-------RMSKEITALAPsSMKIKVVAPPERKYSVWIGGSILAS 350
Cdd:COG5277 327 INSIMKCDVEIQDELYSNIILSGGAFNWsvpPGLEDvavdsvtRVQIELSELAP-ELKVNVRLVSDPQYSVWKGAIIYGY 405
                       410
                ....*....|....*....
gi 15229955 351 LSTFQQMW--IAKAEYDES 367
Cdd:COG5277 406 ALPFSVKWswITKEGWYFL 424
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
9-372 6.11e-123

nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, also called actin-like protein 3, is the ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex is comprised of 7 proteins (Arp2, Arp3, and five conserved proteins, ARPC1-5). It generates cytoplasmic branched filaments networks, by promoting nucleation of actin filaments as 70 degrees branches on the side of older filaments. It is activated, by simultaneously binding to a pre-existing filament and a nucleation promoting factor plus an actin monomer. Daughter branches subsequently detach/debranch from the mother filament. Its Arp2 and Arp3 subunits must be loaded with ATP for it to initiate the assembly of branched actin filaments. ATP hydrolysis may be required for branch initiation or debranching. The Arp2/3 complex is also found in the nucleus where it plays a role in promoting de novo actin polymerization and in RNA polymerase II-dependent transcription. This may in part be through regulating nuclear actin polymerization in a way like its function in the cytoplasm. Human Arp3 and Arp3B are encoded by the ACTR3 and ACTR3B genes respectively. Arp3B is also known as actin-related protein Arp4.


Pssm-ID: 466822  Cd Length: 404  Bit Score: 360.73  E-value: 6.11e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955   9 PLVCDNGTGMVKAGFAGDDAPRAVFPSIVG-------RPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVSNW 81
Cdd:cd10221   1 AVVIDNGTGYTKMGYAGNTEPQFIIPTVIAikesakvGDGQRRSKKGIEDLDFYIGDEALANSPTYALKYPIRHGIVEDW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  82 DDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRT--------TGI 153
Cdd:cd10221  81 DLMERFWEQCIFKYLRCEPEDHYFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQAVLALAASWTSrkvgertlTGT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 154 VLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTSAEREIVRDVKEKLAYIALD-------YE 226
Cdd:cd10221 161 VIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREEGIPPEDSLEVAKRIKERYCYVCPDivkefakYD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 227 QE----METANTSSSVEK-SYElpdgqvITIGGERFRCPEVLFQPSLVGMEA-AGIHETTYNSIMKCDVDIRKDLYGNIV 300
Cdd:cd10221 241 SDpakyIKQYTGINSVTGkPYT------VDVGYERFLAPEIFFNPEIASSDFtTPLPEVVDQVIQSCPIDTRRGLYKNIV 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 301 LSGGTTMFPGIADRMSKEITA----------------LAPSSMKIKVVAPPERKYSVWIGGSILASLSTFQQMWIAKAEY 364
Cdd:cd10221 315 LSGGSTMFKDFGRRLQRDVKRivdarlkaseelsggkLKPKPIDVNVISHPMQRYAVWFGGSMLASTPEFYTVCHTKAEY 394

                ....*...
gi 15229955 365 DESGPSIV 372
Cdd:cd10221 395 EEYGPSIC 402
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
10-374 1.88e-119

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 352.11  E-value: 1.88e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955   10 LVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMV---GMGQKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDMEK 86
Cdd:PTZ00280   7 VVIDNGTGYTKMGYAGNTEPTYIIPTLIADNSKQSRRRskkGFEDLDFYIGDEALAASKSYTLTYPMKHGIVEDWDLMEK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955   87 IWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYAS----------GRTTGIVLD 156
Cdd:PTZ00280  87 FWEQCIFKYLRCEPEEHYFILTEPPMNPPENREYTAEIMFETFNVKGLYIAVQAVLALRASwtskkakelgGTLTGTVID 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  157 SGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTSAEREIVRDVKEKLAYIALDYEQEMETAN--- 233
Cdd:PTZ00280 167 SGDGVTHVIPVVDGYVIGSSIKHIPLAGRDITNFIQQMLRERGEPIPAEDILLLAQRIKEKYCYVAPDIAKEFEKYDsdp 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  234 ---------TSSSVEKSYElpdgqvITIGGERFRCPEVLFQPSLVGME-AAGIHETTYNSIMKCDVDIRKDLYGNIVLSG 303
Cdd:PTZ00280 247 knhfkkytaVNSVTKKPYT------VDVGYERFLGPEMFFHPEIFSSEwTTPLPEVVDDAIQSCPIDCRRPLYKNIVLSG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  304 GTTMFPGIADRMSKEITA----------------LAPSSMKIKVVAPPERKYSVWIGGSILASLSTFQQMWIAKAEYDES 367
Cdd:PTZ00280 321 GSTMFKGFDKRLQRDVRKrvdrrlkkaeelsggkLKPIPIDVNVVSHPRQRYAVWYGGSMLASSPEFEKVCHTKAEYDEY 400

                 ....*..
gi 15229955  368 GPSIVHR 374
Cdd:PTZ00280 401 GPSICRY 407
ASKHA_NBD_Arp6 cd10210
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ...
10-368 3.12e-94

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: 286.75  E-value: 3.12e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  10 LVCDNGTGMVKAGFAGDDAPRaVFPSIVGRPRHtgvmvgmgQKDAYVGDEAQSK---RGILTLKYPIEHGIVSNWDDMEK 86
Cdd:cd10210   2 LVLDNGAYTIKAGFASDDPPR-VIPNCIAKPKS--------ERRRLFGDDQLDEckdLSGLFYRRPFERGYLVNWDLQRQ 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  87 IWHHTFYNE-LRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYA----------SGRTTGIVL 155
Cdd:cd10210  73 IWDHLFGKLlLNVDPSDTALVLTEPPFNPPSIQEAMDEIVFEEYGFQSLYRTTAAALSAFAyladseqsssSSSQCCLVV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 156 DSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFttsaERE--IVRDVKEKLAYIALDYEQEMETA- 232
Cdd:cd10210 153 DSGFSFTHIVPFFDGKPVKRAVRRIDVGGKLLTNYLKEIISYRQLNV----MDEtyLVNQIKEDLCFVSTDFYEDLEIAk 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 233 --NTSSSVEKSYELPDG-----------------------QVITIGGERFRCPEVLFQPSLVGMEAAGIHETTYNSIMKC 287
Cdd:cd10210 229 kkGKENTIRRDYVLPDYttskrgyvrdpeepnrgklkedeQVLRLNNERFTVPELLFHPSDIGIQQAGIAEAIVQSINAC 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 288 DVDIRKDLYGNIVLSGGTTMFPGIADRMSKEITALAPSSMKIKVVAPPERKYSVWIGGSILASLSTFQQMWIAKAEYDES 367
Cdd:cd10210 309 PEELQPLLYANIVLTGGNALFPGFRERLEAELRSLAPDDYDVNVTLPEDPITYAWEGGSLLAQSPEFEELAVTRAEYEEH 388

                .
gi 15229955 368 G 368
Cdd:cd10210 389 G 389
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
10-373 1.28e-89

nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar proteins; Arabidopsis thaliana ARP7 is an essential nuclear protein, ubiquitously expressed in all cell types. It is needed for normal embryogenesis, plant architecture, and floral organ abscission. It may play a role in regulating various phases of plant development through chromatin-mediated gene regulation.


Pssm-ID: 466815 [Multi-domain]  Cd Length: 354  Bit Score: 273.88  E-value: 1.28e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  10 LVCDNGTGMVKAGFAGDDApravFPSIVGRPRHTGVMVGMGQKDAYVGDEAQSkrgiltlkyPIEHGIVSNWDDMEKIWH 89
Cdd:cd10209   1 VVIDAGSRLLKAGYAYPDR----EPSVVEPTRVTPAVEDGEESDTVVEGNTVS---------PIRRGRIEDWDALEALLR 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  90 HTFYNELR-VAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIY 168
Cdd:cd10209  68 YVFYTGLGwEEGNEGQVLIAEPLLTSKAERERLTQLMFETFNVSGLYASEQAVLSLYAVGRISGCVVDVGHGKIDIAPVW 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 169 EGYALPHAILRLDLAGRDLTDYLMKILTERGYSftTSAEREIVRDVKEKLAYIALDYEQEMETANTSSSVekSYELPDGQ 248
Cdd:cd10209 148 EGAIQHNAVRRFEIGGRDLTELLAAELGKSNPK--VKLDRSIVERLKEAVAWSADDEEAYEKKVLTCSPE--TYTLPDGR 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 249 VITIGGERFRCPEVLFQPSLVGMEAAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMSKEITALAPSSMK 328
Cdd:cd10209 224 VISVGKERYCVGEALFRPSILGIEEYGIVEQLVRAVSTSPSENRRQLLENIVLCGGTSSVPGLEARLQKEIRLLSSPSSR 303
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 15229955 329 IKVVAPPE------RKYSVWIGGSILASLSTFQQMWIAKAEYDESGPSIVH 373
Cdd:cd10209 304 PALVKPPEympentLRYSAWIGGAILAKVVFPQNQHVTKADYDETGPSVVH 354
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
9-369 2.94e-70

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: 223.60  E-value: 2.94e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955   9 PLVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGvmvgMGQKDAYVGDEA---QSKRGilTLKYPIEHGIVSNWDDME 85
Cdd:cd10211   1 PIVIDNGSYQCRAGWAGDKEPRLVFRNLVAKPRDRK----KGITVTLVGNDIlndEAVRS--HLRSPFDRNVVTNFDLQE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  86 KIWHHTFyNELRVAPE---EHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRT----TGIVLDSG 158
Cdd:cd10211  75 QILDYIF-SHLGINSEgsvDHPIVLTEALCNPNYSRQLMSELLFECYGVPSVAYGIDSLFSYYHNQPQgdpsDGLVISSG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 159 DGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTSAEREIVRDVKEKLAYIALDYEQEMetantsssv 238
Cdd:cd10211 154 YSTTHVIPVLNGRLDLSQCKRINLGGFHATDYLQRLLQLKYPTHPSAITLSRAEELVHEHCYVAEDYDEEL--------- 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 239 eksyelpdgqvitiggERFRCPEVLFQPSLVgMEAA-GIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMSK 317
Cdd:cd10211 225 ----------------KKWEDPEYYEENVRK-IQLPfGLVETIEFVLKRYPAEQQDRLVQNVFLTGGNALFPGLKERLEK 287
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 15229955 318 EITALAPSSMKIKVVAPPERKYSVWIGGSILASLSTFQQMWIAKAEYDESGP 369
Cdd:cd10211 288 ELRAIRPFGSPFNVVRAKDPVLDAWRGAAKWALDSTFEKVWITKQEYEEKGG 339
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
40-375 1.65e-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: 193.68  E-value: 1.65e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  40 PRHTGVMVGMGQKDAYVGD--EAQSKRGILtlkYPIEHGIVSNWDDMEKIWHHTFYNEL--RVAPEEHPVLLTEAPLNPK 115
Cdd:cd10208   7 PGSQTTRAGLGLGELLTPPtiEIPTRVEII---WPIQDGRVVDWDALEALWRHILFSLLsiPRPTNNSPVLLSVPPSWSK 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 116 ANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKIL 195
Cdd:cd10208  84 SDLELLTQLFFERLNVPAFAILEAPLAALYAAGATSGIVVDIGHEKTDITPIVDSQVVPHALVSIPIGGQDCTAHLAQLL 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 196 TER--GYSFTTSAEREIVRDVKEKLayialdyeqemETANTSSSVEKSYELPDGQVITIGGERFRCPEVLFQPSLVGM-- 271
Cdd:cd10208 164 KSDepELKSQAESGEEATLDLAEAL-----------KKSPICEVLSDGADLASGTEITVGKERFRACEPLFKPSSLRVdl 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 272 --EAAGIHETTYNSimkCDVDIRKDLYGNIVLSGGTTMFPGIADRMSKEITA-LAPSSMKIKVVAP------------PE 336
Cdd:cd10208 233 liAAIAGALVLNAS---DEPDKRPALWENIIIVGGGSRIRGLKEALLSELQQfHLISETSASPQQPriirlakipdyfPE 309
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 15229955 337 RK-----YSVWIGGSILASLsTF----QQMWIAKAEYDESGPSIVHRK 375
Cdd:cd10208 310 WKksgyeEAAFLGASIVAKL-VFndpsSKHYISKVDYNEKGPAAIHTK 356
ASKHA_NBD_AtArp8-like cd13396
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and ...
91-363 9.66e-47

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: 162.33  E-value: 9.66e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  91 TFYNELRVAPEEHPVLLTEaPL-------NPKANREKMTQIMFETF---NTPAMYVAIQAVLSLYASGRTTGIVLDSGDG 160
Cdd:cd13396  47 TIMTRMQVKPSRQPVVVSL-PLchsddteSAAASRRQLRGTIFNVLfdmNVPAVCAVDQAVLALYAANRTSGIVVNIGFR 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 161 VSHTVPIYEGYALPH-AILRLDLAGRDLTDYLMKILTERGYSFTTSAereIVRDVKEKLAYIALDYEQEMeTANTSSSVE 239
Cdd:cd13396 126 VTTIVPVYRGRVMHDiGVEVVGQGALRLTGFLKELMQQNGIRFPSLY---TVRTIKEKLCYVAEDYEAEL-AKDTQASCE 201
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 240 KSyelpDGQVITIGGERFRCPEVLFQPSLVGMEAAGIHETTYNSIMKCDVDIR---KDLYGNIVLSGGTTMFPGIADRMS 316
Cdd:cd13396 202 VA----GEGWFTLSNERFKTGEILFQPGLGGMRAMGLHQAVALCMDHCALVHSqgdDGWFKTIVLSGGSACLPGLSERLE 277
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 15229955 317 KEITALAPSSMK--IKVVAPPERKYSVWIGGSILASLSTFQQMWIAKAE 363
Cdd:cd13396 278 RELRKLLPKSLSegIRIIPPPLGPDSAWQGAKLISNLSNFPDGWCITKK 326
ASKHA_NBD_Arp10 cd10207
nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins; ...
11-368 6.60e-45

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: 158.57  E-value: 6.60e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  11 VCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRhtgvmvgmGQKDAYVGDeaqskrgiltlkypIEHGIVSNWDDM-EKIWH 89
Cdd:cd10207   2 VLDIGSAYTKCGFAGESAPRCIIPSEVKLPG--------GKKVIRVVD--------------QRSGNEEELYEAlKEFLH 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  90 HTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYE 169
Cdd:cd10207  60 ELYFKHLLVNPKDRRVVVVESVLCPTPFRETLAKVLFKHFEVPSVLFAPSHLLSLLTLGIRTALVVDCGYRETRVLPVYE 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 170 GYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTSAER------------EIVRDVKEKLAYIA-LDYEQEMETANTSS 236
Cdd:cd10207 140 GVPLLSAWQSTPLGGKALHKRLKKLLLEHATVVTGDNKGqllssvdsllseEVLEDIKVRACFVTsLERGKTLQSATEEG 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 237 SVEKS-------YELPDGQVITIGGERFRCPEVLFQPslVGMEAAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFP 309
Cdd:cd10207 220 STEEPsppppvdYPLDGEKILIVPGSIRESAEELLFE--GDNEEKSLPTLILDSLLKCPIDVRKQLAENIVVIGGTSMLP 297
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 310 GIADRMSKEITAL--------APSSMKIKVVAPPER---KYSVWIGGSILASLSTFQQMWIAKAEYDESG 368
Cdd:cd10207 298 GFKHRLLEELRALlrkpkyfeELAPKTFRFHTPPSVfkpNYLAWLGGSIFGALESILGRSLSREAYLQTG 367
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
305-376 1.86e-31

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: 115.85  E-value: 1.86e-31
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229955  305 TTMFPGIADRMSKEITALAPSSMKIKVVAPPERKYSVWIGGSILASLSTFQQMWIAKAEYDESGPSIVHRKC 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 7.56e-28

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: 113.49  E-value: 7.56e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  50 GQKDAYVGDEAQ--SKRGILTLKYPIEHGIVsNW-----------DDMEKIWHHTFYNELRVAPEEHP----VLLTEAPL 112
Cdd:cd10206 118 DYPDFLVGEEALrlPPSEEYNLHWPIRRGRL-NVhsdggsltavlDDLEDIWSHALEEKLEIPRKDLKnyraVLVIPDLF 196
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 113 NpKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLM 192
Cdd:cd10206 197 D-RRHVKELVDLLLRRLGFSSVFVHQESVCATFGAGLSSACVVDIGAQKTSVACVEDGLSIPNSRIRLPYGGDDITRCFL 275
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 193 KILTERGY-----SFTTSAEREIVRDVKEKLAYIaldyEQEMETANTSSSVEKSyelPDGqvitiggerfrcPEVLFQps 267
Cdd:cd10206 276 WLLRRSGFpyrecNLNSPLDFLLLERLKETYCTL----DQDDIGVQLHEFYVRE---PGQ------------PTLKYQ-- 334
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 268 lvgMEAAGIHETTYNSIMKC-DVDIRKDLYGNIVLSGGTTMFPGIA----DRMSKEITALAPSSMKIKVVAPPERK---Y 339
Cdd:cd10206 335 ---FKLLPLDEAIVQSILSCaSDELKRKMYSSILLVGGGAKIPGLAealeDRLLIKIPSLFEAVETVEVLPPPKDMdpsL 411
                       330       340       350
                ....*....|....*....|....*....|..
gi 15229955 340 SVWIGGSILASLSTFQQMWIAKAEYDESGPSI 371
Cdd:cd10206 412 LAWKGGAVLACLDSAQELWITRKEWQRLGVRA 443
ASKHA_NBD_ScArp7-like cd10212
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and ...
10-365 3.51e-20

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


Pssm-ID: 466818 [Multi-domain]  Cd Length: 424  Bit Score: 91.32  E-value: 3.51e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  10 LVCDNGTGMVKAGFAGDDAPRAVFPS-IVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDMEKIW 88
Cdd:cd10212   6 VVIHNGSHRTVAGFSNVELPQCIIPSsYIKRTDEGGEAEFIFGTYNMIDAAAEKRNGDEVYTLVDSQGLPYNWDALEMQW 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  89 HHTFYNELRVAPEEHPVLLTEAPLNPKANR---EKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTV 165
Cdd:cd10212  86 RYLYDTQLKVSPEELPLVITMPATNGKPDMailERYYELAFDKLNVPVFQIVIEPLAIALSMGKSSAFVIDIGASGCNVT 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 166 PIYEGYALPHAILRLDLAGrDLTDYLM---------------------KILTERGYSFTTSAER--------------EI 210
Cdd:cd10212 166 PIIDGIVVKNAVVRSKFGG-DFLDFQVherlaplikeendmenmadeqKRSTDVWYEASTWIQQfkstmlqvsekdlfEL 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 211 VRDVKEKLAYIALDYEQ--EME-----TANTSSS----VEKSYEL--PDGQVITIG-GERFRCPEVLFQPSLVGMEAA-- 274
Cdd:cd10212 245 ERYYKEQADIYAKQQEQlkQMDqqlqyTALTGSPnnplVQKKNFLfkPLNKTLTLDlKECYQFAEYLFKPQLISDKFSpe 324
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 275 -GIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMSKEITALAPsSMKIKVVAPP---ERKYSVWIGGSILAS 350
Cdd:cd10212 325 dGLGPLMAKSVKKAPEQVYSLLLTNVIITGSTSLIEGMEQRIIKELSIRFP-QYKLTTFANQvmmDRKIQGWLGALTMAN 403
                       410
                ....*....|....*.
gi 15229955 351 LSTFQ-QMWIAKAEYD 365
Cdd:cd10212 404 LPSWSlGKWYSKEDYE 419
ASKHA_NBD_MamK cd24009
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ...
17-318 1.67e-09

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


Pssm-ID: 466859 [Multi-domain]  Cd Length: 328  Bit Score: 58.38  E-value: 1.67e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  17 GMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGqKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDmekiwhhtfyNEL 96
Cdd:cd24009   9 GTSRSAVVTSRGKRFSFRSVVGYPKDIIARKLLG-KEVLFGDEALENRLALDLRRPLEDGVIKEGDD----------RDL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955  97 RVAPE--EHPVLLTEAPLNPK-------------ANREKMTQIMFETFNTPAMYVAIQAVlsLYASGRTTG-IVLDSGDG 160
Cdd:cd24009  78 EAAREllQHLIELALPGPDDEiyavigvparasaENKQALLEIARELVDGVMVVSEPFAV--AYGLDRLDNsLIVDIGAG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 161 VSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTER--GYSFTtsaeREIVRDVKEKLAYIaldyeqemetanTSSSV 238
Cdd:cd24009 156 TTDLCRMKGTIPTEEDQITLPKAGDYIDEELVDLIKERypEVQLT----LNMARRWKEKYGFV------------GDASE 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229955 239 EKSYELP-DGQVIT--IGGE-RFRCPEVLfqpslvgmeaAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADR 314
Cdd:cd24009 220 PVKVELPvDGKPVTydITEElRIACESLV----------PDIVEGIKKLIASFDPEFQEELRNNIVLAGGGSRIRGLDTY 289

                ....
gi 15229955 315 MSKE 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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