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Conserved domains on  [gi|15227503|ref|NP_181740|]
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Actin-like ATPase superfamily protein [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 ...
9-373 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: 837.40  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503   9 VAIVCDNGTGMVKAGFAGDDAPRAVFPSVVGRPRHRGVMVGMDEKDTFVGDEAQARRGILSLKYPIEHGVVSNWDDMEKI 88
Cdd:cd10224   1 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  89 WHHTFYNELRLEPEEHPILLTEAPLNPKVNREKMTQIMFESFAFPSMYIGIQAVLSLYSSGRTTGIVLDSGDGVSHTVPI 168
Cdd:cd10224  81 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 169 YEGYALPHAILRLDLAGRDLTEYLTKIMMERGYTYTTSAEREIVRDIKEKLCYIAVDYEQEMEKATTSSAIDRTYELPDG 248
Cdd:cd10224 161 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 249 QVITIGAERFRCPEVLFQTSLIGMETSGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMNKEINALAPPSM 328
Cdd:cd10224 241 QVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTM 320
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 15227503 329 KIKVVAPPERKYSVWVGGSILASLSSFAPMWITKAEYDEQGGAIV 373
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 ...
9-373 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: 837.40  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503   9 VAIVCDNGTGMVKAGFAGDDAPRAVFPSVVGRPRHRGVMVGMDEKDTFVGDEAQARRGILSLKYPIEHGVVSNWDDMEKI 88
Cdd:cd10224   1 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  89 WHHTFYNELRLEPEEHPILLTEAPLNPKVNREKMTQIMFESFAFPSMYIGIQAVLSLYSSGRTTGIVLDSGDGVSHTVPI 168
Cdd:cd10224  81 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 169 YEGYALPHAILRLDLAGRDLTEYLTKIMMERGYTYTTSAEREIVRDIKEKLCYIAVDYEQEMEKATTSSAIDRTYELPDG 248
Cdd:cd10224 161 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 249 QVITIGAERFRCPEVLFQTSLIGMETSGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMNKEINALAPPSM 328
Cdd:cd10224 241 QVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTM 320
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 15227503 329 KIKVVAPPERKYSVWVGGSILASLSSFAPMWITKAEYDEQGGAIV 373
Cdd:cd10224 321 KIKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIV 365
PTZ00281 PTZ00281
actin; Provisional
6-378 0e+00

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 674.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503    6 DESVAIVCDNGTGMVKAGFAGDDAPRAVFPSVVGRPRHRGVMVGMDEKDTFVGDEAQARRGILSLKYPIEHGVVSNWDDM 85
Cdd:PTZ00281   4 EDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503   86 EKIWHHTFYNELRLEPEEHPILLTEAPLNPKVNREKMTQIMFESFAFPSMYIGIQAVLSLYSSGRTTGIVLDSGDGVSHT 165
Cdd:PTZ00281  84 EKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVSHT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  166 VPIYEGYALPHAILRLDLAGRDLTEYLTKIMMERGYTYTTSAEREIVRDIKEKLCYIAVDYEQEMEKATTSSAIDRTYEL 245
Cdd:PTZ00281 164 VPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEMQTAASSSALEKSYEL 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  246 PDGQVITIGAERFRCPEVLFQTSLIGMETSGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMNKEINALAP 325
Cdd:PTZ00281 244 PDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELTALAP 323
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15227503  326 PSMKIKVVAPPERKYSVWVGGSILASLSSFAPMWITKAEYDEQGGAIVHRKCF 378
Cdd:PTZ00281 324 STMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIVHRKCF 376
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
10-378 0e+00

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 618.12  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503     10 AIVCDNGTGMVKAGFAGDDAPRAVFPSVVGRPRHRGVMVGmDEKDTFVGDEAQARRGILSLKYPIEHGVVSNWDDMEKIW 89
Cdd:smart00268   3 AIVIDNGSGTIKAGFAGEDFPQVVFPSIVGRPKDGKGMVG-DAKDIFVGDEAQEKRGGLELKYPIENGIVENWDDMEKIW 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503     90 HHTFYNELRLEPEEHPILLTEAPLNPKVNREKMTQIMFESFAFPSMYIGIQAVLSLYSSGRTTGIVLDSGDGVSHTVPIY 169
Cdd:smart00268  82 DYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVPVV 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503    170 EGYALPHAILRLDLAGRDLTEYLTKIMMERGYTYTTSAEREIVRDIKEKLCYIAVDYEQEMEKATTSSAIDR---TYELP 246
Cdd:smart00268 162 DGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLARESSESSKlekTYELP 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503    247 DGQVITIGAERFRCPEVLFQTSLIGMETSGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMNKEINALAPP 326
Cdd:smart00268 242 DGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELKQLAPK 321
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 15227503    327 SMKIKVVAPPERKYSVWVGGSILASLSSFAPMWITKAEYDEQGGAIVHRKCF 378
Cdd:smart00268 322 KLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERKCF 373
Actin pfam00022
Actin;
10-378 0e+00

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 534.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503    10 AIVCDNGTGMVKAGFAGDDAPRAVFPSVVGRPRHRGVMvgmDEKDTFVGDEAQARRGILSLKYPIEHGVVSNWDDMEKIW 89
Cdd:pfam00022   3 ALVIDNGSHTTRAGFAGEDAPKAVIPSCVGKPRGTKVE---AANKYYVGDEALTYRPGMEVRSPVEDGIVVDWDAMEEIW 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503    90 HHTFYNELRLEPEEHPILLTEAPLNPKVNREKMTQIMFESFAFPSMYIGIQAVLSLYSSGRTTGIVLDSGDGVSHTVPIY 169
Cdd:pfam00022  80 EHVLKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVPVH 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503   170 EGYALPHAILRLDLAGRDLTEYLTKIMMER------------------------------GYTYTTSAEREIVRDIKEKL 219
Cdd:pfam00022 160 DGYVLQKAIRRSDLGGDFLTDYLRELLRSRnieitprylikskkpgdpapavtkrelpdtTYSYKTYQERRVLEEIKESV 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503   220 CYIAvDYEQEMEKaTTSSAIDRTYELPDGQVITIGAERFRCPEVLFQTSLIGMET--------SGIHETTYNSIMKCDVD 291
Cdd:pfam00022 240 CYVS-DDPFGDET-TSSSIPTRVYELPDGSTIILGAERFRVPEILFNPSLIGSESelpppqtaVGIPELIVDAINACDVD 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503   292 IRKDLYGNIVLSGGTTMFPGIADRMNKEINALAPPSMKIKVVAPP---ERKYSVWVGGSILASLSSFAPMWITKAEYDEQ 368
Cdd:pfam00022 318 LRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVKIIAPGntvERRYSAWIGGSILASLGTFQQMWVSKQEYEEH 397
                         410
                  ....*....|
gi 15227503   369 GGAIVHRKCF 378
Cdd:pfam00022 398 GASVVERKCK 407
COG5277 COG5277
Actin-related protein [Cytoskeleton];
1-367 1.35e-120

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 355.64  E-value: 1.35e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503   1 MSDLGDESVAIVCDNGTGMVKAG-FAGDDAP-----RAVFPSVVGRPRHRGVMVGMDeKDTFVGDEAQ-----ARRGILS 69
Cdd:COG5277   1 MSDAYKLKYVIGIDFGTSYVKYGpIALEEKPrviqtRGLFLRIVGESKLLGPMEGLS-RGLVVGDEVSkylssVRDAIRN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  70 LKYPIEHGVV-----SNWDDMEKIWHHTFYNELRLEPEEHP--ILLTEAPLNPKVNREKMTQIMFESFA---FPSMYIGI 139
Cdd:COG5277  80 LKYPLRDGIVrrddeDAWRVLKELLRYTFAQFLVVDPEFHGflVVVALSALAPDYMRERLFDIHFEVFSeegAPAVTIIP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 140 QAVLSLYSSGRTTGIVLDSGDGVSHTVPIYEGyALPHAILRLDLAGRDLTEYLTKIMMERGYTYTTSAEReIVRDIKEKL 219
Cdd:COG5277 160 QPLAVAIAEKAVTCVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSDTAREEY-VVRVVKEAL 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 220 CYIAVDYEQEMEKA-TTSSAIDRTYELPDGQV-ITIG---AERFRCPEVLFQTSLIGME--------------------- 273
Cdd:COG5277 238 GLVPRDLAKAIQKAaSNPDSFEAKVRLPNPTVeIELGnyaWERFLIGEILFNPNHEGFEsyiqqgrlriedavigdvvly 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 274 -TSGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMF---PGIAD-------RMNKEINALApPSMKIKVVAPPERKYSV 342
Cdd:COG5277 318 gEMGLAEAIINSIMKCDVEIQDELYSNIILSGGAFNWsvpPGLEDvavdsvtRVQIELSELA-PELKVNVRLVSDPQYSV 396
                       410       420
                ....*....|....*....|....*..
gi 15227503 343 WVGGSILASLSSFAPMW--ITKAEYDE 367
Cdd:COG5277 397 WKGAIIYGYALPFSVKWswITKEGWYF 423
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
306-377 4.37e-26

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: 101.59  E-value: 4.37e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15227503  306 TTMFPGIADRMNKEINALAPPSMKIKVVAPPERKYSVWVGGSILASLSSFAPMWITKAEYDEQGGAIVHRKC 377
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 ...
9-373 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: 837.40  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503   9 VAIVCDNGTGMVKAGFAGDDAPRAVFPSVVGRPRHRGVMVGMDEKDTFVGDEAQARRGILSLKYPIEHGVVSNWDDMEKI 88
Cdd:cd10224   1 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  89 WHHTFYNELRLEPEEHPILLTEAPLNPKVNREKMTQIMFESFAFPSMYIGIQAVLSLYSSGRTTGIVLDSGDGVSHTVPI 168
Cdd:cd10224  81 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 169 YEGYALPHAILRLDLAGRDLTEYLTKIMMERGYTYTTSAEREIVRDIKEKLCYIAVDYEQEMEKATTSSAIDRTYELPDG 248
Cdd:cd10224 161 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 249 QVITIGAERFRCPEVLFQTSLIGMETSGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMNKEINALAPPSM 328
Cdd:cd10224 241 QVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTM 320
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 15227503 329 KIKVVAPPERKYSVWVGGSILASLSSFAPMWITKAEYDEQGGAIV 373
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 ...
10-369 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: 727.06  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  10 AIVCDNGTGMVKAGFAGDDAPRAVFPSVVGRPRHRGVMVGMDEKDTFVGDEAQARRGILSLKYPIEHGVVSNWDDMEKIW 89
Cdd:cd13397   2 AVVIDNGSGLIKAGFAGEDLPRAVFPSVVGRPKYKAVMLGAGQKEVYVGDEAQEKRGVLTLSYPIEHGIVTNWDDMEKIW 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  90 HHTFYNELRLEPEEHPILLTEAPLNPKVNREKMTQIMFESFAFPSMYIGIQAVLSLYSSGRTTGIVLDSGDGVSHTVPIY 169
Cdd:cd13397  82 HHTFENELRVKPEEHPVLLTEAPLNPKQNREKMAEIMFETFGVPAFYVAIQAVLSLYSSGRTTGLVLDSGDGVTHTVPIY 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 170 EGYALPHAILRLDLAGRDLTEYLTKIMMERGYTYTTSAEREIVRDIKEKLCYIAVDYEQEMEKatTSSAIDRTYELPDGQ 249
Cdd:cd13397 162 EGYALPHAVQRLDLAGRDLTEYLMKLLKERGHSFTTTAEREIVRDIKEKLCYVALDYEEELKK--KSEELEKEYTLPDGQ 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 250 VITIGAERFRCPEVLFQTSLIGMETSGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMNKEINALAPPSMK 329
Cdd:cd13397 240 VIKIGSERFRCPEALFRPSLIGREAPGIHKLVYNSIMKCDIDIRKDLYSNIVLSGGSTMFPGLPERLQKELEALAPSSTK 319
                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 15227503 330 IKVVAPPERKYSVWVGGSILASLSSFAPMWITKAEYDEQG 369
Cdd:cd13397 320 VKVIAPPERKYSVWIGGSILASLSTFKSMWITRAEYDEFG 359
PTZ00281 PTZ00281
actin; Provisional
6-378 0e+00

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 674.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503    6 DESVAIVCDNGTGMVKAGFAGDDAPRAVFPSVVGRPRHRGVMVGMDEKDTFVGDEAQARRGILSLKYPIEHGVVSNWDDM 85
Cdd:PTZ00281   4 EDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503   86 EKIWHHTFYNELRLEPEEHPILLTEAPLNPKVNREKMTQIMFESFAFPSMYIGIQAVLSLYSSGRTTGIVLDSGDGVSHT 165
Cdd:PTZ00281  84 EKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVSHT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  166 VPIYEGYALPHAILRLDLAGRDLTEYLTKIMMERGYTYTTSAEREIVRDIKEKLCYIAVDYEQEMEKATTSSAIDRTYEL 245
Cdd:PTZ00281 164 VPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEMQTAASSSALEKSYEL 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  246 PDGQVITIGAERFRCPEVLFQTSLIGMETSGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMNKEINALAP 325
Cdd:PTZ00281 244 PDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELTALAP 323
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15227503  326 PSMKIKVVAPPERKYSVWVGGSILASLSSFAPMWITKAEYDEQGGAIVHRKCF 378
Cdd:PTZ00281 324 STMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIVHRKCF 376
PTZ00004 PTZ00004
actin-2; Provisional
1-378 0e+00

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 666.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503    1 MSDLgdESVAIVCDNGTGMVKAGFAGDDAPRAVFPSVVGRPRHRGVMVGMDEKDTFVGDEAQARRGILSLKYPIEHGVVS 80
Cdd:PTZ00004   1 MSVE--ETNAAVVDNGSGMVKAGFAGDDAPRCVFPSIVGRPKNPGIMVGMEEKDCYVGDEAQDKRGILTLKYPIEHGIVT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503   81 NWDDMEKIWHHTFYNELRLEPEEHPILLTEAPLNPKVNREKMTQIMFESFAFPSMYIGIQAVLSLYSSGRTTGIVLDSGD 160
Cdd:PTZ00004  79 NWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETHNVPAMYVAIQAVLSLYASGRTTGIVLDSGD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  161 GVSHTVPIYEGYALPHAILRLDLAGRDLTEYLTKIMMERGYTYTTSAEREIVRDIKEKLCYIAVDYEQEM-EKATTSSAI 239
Cdd:PTZ00004 159 GVSHTVPIYEGYSLPHAIHRLDVAGRDLTEYMMKILHERGTTFTTTAEKEIVRDIKEKLCYIALDFDEEMgNSAGSSDKY 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  240 DRTYELPDGQVITIGAERFRCPEVLFQTSLIGMETS-GIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMNK 318
Cdd:PTZ00004 239 EESYELPDGTIITVGSERFRCPEALFQPSLIGKEEPpGIHELTFQSINKCDIDIRKDLYGNIVLSGGTTMYRGLPERLTK 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  319 EINALAPPSMKIKVVAPPERKYSVWVGGSILASLSSFAPMWITKAEYDEQGGAIVHRKCF 378
Cdd:PTZ00004 319 ELTTLAPSTMKIKVVAPPERKYSVWIGGSILSSLPTFQQMWVTKEEYDESGPSIVHRKCF 378
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
10-378 0e+00

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 618.12  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503     10 AIVCDNGTGMVKAGFAGDDAPRAVFPSVVGRPRHRGVMVGmDEKDTFVGDEAQARRGILSLKYPIEHGVVSNWDDMEKIW 89
Cdd:smart00268   3 AIVIDNGSGTIKAGFAGEDFPQVVFPSIVGRPKDGKGMVG-DAKDIFVGDEAQEKRGGLELKYPIENGIVENWDDMEKIW 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503     90 HHTFYNELRLEPEEHPILLTEAPLNPKVNREKMTQIMFESFAFPSMYIGIQAVLSLYSSGRTTGIVLDSGDGVSHTVPIY 169
Cdd:smart00268  82 DYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVPVV 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503    170 EGYALPHAILRLDLAGRDLTEYLTKIMMERGYTYTTSAEREIVRDIKEKLCYIAVDYEQEMEKATTSSAIDR---TYELP 246
Cdd:smart00268 162 DGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLARESSESSKlekTYELP 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503    247 DGQVITIGAERFRCPEVLFQTSLIGMETSGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMNKEINALAPP 326
Cdd:smart00268 242 DGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELKQLAPK 321
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 15227503    327 SMKIKVVAPPERKYSVWVGGSILASLSSFAPMWITKAEYDEQGGAIVHRKCF 378
Cdd:smart00268 322 KLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERKCF 373
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
11-377 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: 604.92  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  11 IVCDNGTGMVKAGFAGDDAPRAVFPSVVGRPRHRGVMVGMDEKDTFVGDEAQARRGILSLKYPIEHGVVSNWDDMEKIWH 90
Cdd:cd10216   4 VVIDNGSGVIKAGFAGDDIPKVVFPSYVGRPKHVRVMAGALEGDVFVGPKAEEHRGLLKIRYPMEHGIVTDWNDMERIWQ 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  91 HTfYNELRLE--PEEHPILLTEAPLNPKVNREKMTQIMFESFAFPSMYIGIQAVLSLYSSGRTTGIVLDSGDGVSHTVPI 168
Cdd:cd10216  84 YV-YSKLQLNtfSEEHPVLLTEAPLNPRKNREKAAEVFFETFNVPALFVSMQAVLSLYASGRTTGVVLDSGDGVTHAVPI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 169 YEGYALPHAILRLDLAGRDLTEYLTKIMMERGYTYTTSAEREIVRDIKEKLCYIAVDyEQEMEKATTSSAIDRTYELPDG 248
Cdd:cd10216 163 YEGFALPHSIRRVDIAGRDVTEYLQLLLRKSGYNFHTSAEFEIVREIKEKACYVALN-PQKEEKLEEEKTEKAQYTLPDG 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 249 QVITIGAERFRCPEVLFQTSLIGMETSGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMNKEINALAPPSM 328
Cdd:cd10216 242 STIEIGPERFRAPEILFNPELIGLEYPGVHEVLVDSIQKSDLDLRKTLYSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDV 321
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 15227503 329 KIKVVAPPERKYSVWVGGSILASLSSFAPMWITKAEYDEQGGAIVHRKC 377
Cdd:cd10216 322 KIRISAPPERLYSTWIGGSILASLSTFKKMWVSKKEYEEDGARILHRKT 370
Actin pfam00022
Actin;
10-378 0e+00

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 534.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503    10 AIVCDNGTGMVKAGFAGDDAPRAVFPSVVGRPRHRGVMvgmDEKDTFVGDEAQARRGILSLKYPIEHGVVSNWDDMEKIW 89
Cdd:pfam00022   3 ALVIDNGSHTTRAGFAGEDAPKAVIPSCVGKPRGTKVE---AANKYYVGDEALTYRPGMEVRSPVEDGIVVDWDAMEEIW 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503    90 HHTFYNELRLEPEEHPILLTEAPLNPKVNREKMTQIMFESFAFPSMYIGIQAVLSLYSSGRTTGIVLDSGDGVSHTVPIY 169
Cdd:pfam00022  80 EHVLKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVPVH 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503   170 EGYALPHAILRLDLAGRDLTEYLTKIMMER------------------------------GYTYTTSAEREIVRDIKEKL 219
Cdd:pfam00022 160 DGYVLQKAIRRSDLGGDFLTDYLRELLRSRnieitprylikskkpgdpapavtkrelpdtTYSYKTYQERRVLEEIKESV 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503   220 CYIAvDYEQEMEKaTTSSAIDRTYELPDGQVITIGAERFRCPEVLFQTSLIGMET--------SGIHETTYNSIMKCDVD 291
Cdd:pfam00022 240 CYVS-DDPFGDET-TSSSIPTRVYELPDGSTIILGAERFRVPEILFNPSLIGSESelpppqtaVGIPELIVDAINACDVD 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503   292 IRKDLYGNIVLSGGTTMFPGIADRMNKEINALAPPSMKIKVVAPP---ERKYSVWVGGSILASLSSFAPMWITKAEYDEQ 368
Cdd:pfam00022 318 LRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVKIIAPGntvERRYSAWIGGSILASLGTFQQMWVSKQEYEEH 397
                         410
                  ....*....|
gi 15227503   369 GGAIVHRKCF 378
Cdd:pfam00022 398 GASVVERKCK 407
ASKHA_NBD_Arp2 cd10220
nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, ...
11-369 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: 518.66  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  11 IVCDNGTGMVKAGFAGDDAPRAVFPSVVGRP--RHRGVMVGMDEKDTFVGDEAQARRGILSLKYPIEHGVVSNWDDMEKI 88
Cdd:cd10220   3 VVCDNGTGFVKCGFAGSNFPEHVFPSLVGRPilRAEEKVGDIEIKDIMVGDEASELRSMLEVTYPMENGIVRNWDDMEHL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  89 WHHTFYNELRLEPEEHPILLTEAPLNPKVNREKMTQIMFESFAFPSMYIGIQAVLSLYSSGRTTGIVLDSGDGVSHTVPI 168
Cdd:cd10220  83 WDYTFGEKLKIDPRECKILLTEPPMNPTKNREKMVEVMFEKYGFAGVYVAIQAVLTLYAQGLLTGVVVDSGDGVTHIVPV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 169 YEGYALPHAILRLDLAGRDLTEYLTKIMMERGYTYTTSAEREIVRDIKEKLCYIAVDYEQEMEKATTSSAIDRTYELPDG 248
Cdd:cd10220 163 YEGFSLPHLTRRLDVAGRDITRYLIKLLLLRGYAFNRTADFETVREIKEKLCYVAYDIELEQKLALETTVLVESYTLPDG 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 249 QVITIGAERFRCPEVLFQTSLIGMETSGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMNKEINAL----- 323
Cdd:cd10220 243 RVIKVGGERFEAPEALFQPHLIDVEGPGIAELLFNTIQAADIDTRPELYKHIVLSGGSTMYPGLPSRLEKEIKQLylerv 322
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 15227503 324 ------APPSMKIKVVAPPERKYSVWVGGSILASLSSFAP-MWITKAEYDEQG 369
Cdd:cd10220 323 lkgdteRLSKFKIRIEDPPRRKHMVFLGGAVLADIMKDKDeFWITRQEYEEQG 375
PTZ00466 PTZ00466
actin-like protein; Provisional
11-378 9.36e-174

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 489.07  E-value: 9.36e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503   11 IVCDNGTGMVKAGFAGDDAPRAVFPSVVGRPRHRGVMVGMDEKDTFVGDEAQARRGILSLKYPIEHGVVSNWDDMEKIWH 90
Cdd:PTZ00466  15 IIIDNGTGYIKAGFAGEDVPNLVFPSYVGRPKYKRVMAGAVEGNIFVGNKAEEYRGLLKVTYPINHGIIENWNDMENIWI 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503   91 HTfYNELRLEPEEHPILLTEAPLNPKVNREKMTQIMFESFAFPSMYIGIQAVLSLYSSGRTTGIVLDSGDGVSHTVPIYE 170
Cdd:PTZ00466  95 HV-YNSMKINSEEHPVLLTEAPLNPQKNKEKIAEVFFETFNVPALFISIQAILSLYSCGKTNGTVLDCGDGVCHCVSIYE 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  171 GYALPHAILRLDLAGRDLTEYLTKIMMERGYTYTTSAEREIVRDIKEKLCYIAVDYEQE---MEKATTSSAidrtYELPD 247
Cdd:PTZ00466 174 GYSITNTITRTDVAGRDITTYLGYLLRKNGHLFNTSAEMEVVKNMKENCCYVSFNMNKEknsSEKALTTLP----YILPD 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  248 GQVITIGAERFRCPEVLFQTSLIGMETSGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMNKEINALAPPS 327
Cdd:PTZ00466 250 GSQILIGSERYRAPEVLFNPSILGLEYLGLSELIVTSITRADMDLRRTLYSHIVLSGGTTMFHGFGDRLLNEIRKFAPKD 329
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15227503  328 MKIKVVAPPERKYSVWVGGSILASLSSFAPMWITKAEYDEQGGAIVHRKCF 378
Cdd:PTZ00466 330 ITIRISAPPERKFSTFIGGSILASLATFKKIWISKQEFDEYGSVILHRKTF 380
PTZ00452 PTZ00452
actin; Provisional
10-378 1.33e-167

actin; Provisional


Pssm-ID: 185631  Cd Length: 375  Bit Score: 473.09  E-value: 1.33e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503   10 AIVCDNGTGMVKAGFAGDDAPRAVFPSVVGRPRHRGVMVGMDEKDTFVGDEAQARRGILSLKYPIEHGVVSNWDDMEKIW 89
Cdd:PTZ00452   7 AVVIDNGSGYCKIGIAGDDAPTSCFPAIVGRSKQNDGIFSTFNKEYYVGEEAQAKRGVLAIKEPIQNGIINSWDDIEIIW 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503   90 HHTFYNELRLEPEEHPILLTEAPLNPKVNREKMTQIMFESFAFPSMYIGIQAVLSLYSSGRTTGIVLDSGDGVSHTVPIY 169
Cdd:PTZ00452  87 HHAFYNELCMSPEDQPVFMTDAPMNSKFNRERMTQIMFETFNTPCLYISNEAVLSLYTSGKTIGLVVDSGEGVTHCVPVF 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  170 EGYALPHAILRLDLAGRDLTEYLTKIMMERGYTYTTSAEREIVRDIKEKLCYIAVDYEQEMEKATTSSAIDRTYELPDGQ 249
Cdd:PTZ00452 167 EGHQIPQAITKINLAGRLCTDYLTQILQELGYSLTEPHQRIIVKNIKERLCYTALDPQDEKRIYKESNSQDSPYKLPDGN 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  250 VITIGAERFRCPEVLFQTSLIGMETSGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMNKEINALAPPSMK 329
Cdd:PTZ00452 247 ILTIKSQKFRCSEILFQPKLIGLEVAGIHHLAYSSIKKCDLDLRQELCRNIVLSGGTTLFPGIANRLSNELTNLVPSQLK 326
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 15227503  330 IKVVAPPERKYSVWVGGSILASLSSFAPMWITKAEYDEQGGAIVHRKCF 378
Cdd:PTZ00452 327 IQVAAPPDRRFSAWIGGSIQCTLSTQQPQWIKRQEYDEQGPSIVHRKCF 375
ASKHA_NBD_ACTL7 cd10214
nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ...
7-377 1.99e-160

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: 454.57  E-value: 1.99e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503   7 ESVAIVCDNGTGMVKAGFAGDDAPRAVFPSVVGRPRHRGVMVGMDEKDTFVGDEAQARRGILSLKYPIEHGVVSNWDDME 86
Cdd:cd10214   2 ETKAVIIDLGTGYCKAGFAGQPRPSYVISSTVGKPPQESAKTGDNRKETFVGKELANVEPPLKLVNPLRHGIVVDWDCVQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  87 KIWHHTFYNELRLEPEEHPILLTEAPLNPKVNREKMTQIMFESFAFPSMYIGIQAVLSLYSSGRTTGIVLDSGDGVSHTV 166
Cdd:cd10214  82 DIWEYIFEKEMKILPEEHAVLVSDPPLSPTTNREKYAELMFETFSIPAMHIAYQSRLSLYSYGRTSGLVVESGHGVSYVV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 167 PIYEGYALPHAILRLDLAGRDLTEYLTKIMMERGYTYTTSaEREIVRDIKEKLCYIAVDYEQEMekATTSSAIDRTYELP 246
Cdd:cd10214 162 PIHEGYNLPHITGRADYAGSDLTAYLMKLLNEAGNKFTDD-QLHIVEDIKKKCCYVALDFEEEM--GLPPQEYTVDYELP 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 247 DGQVITIGAERFRCPEVLFQTSLIGMETSGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMNKEINALAPP 326
Cdd:cd10214 239 DGHLITIGKERFRCPEMLFNPSLIGSKQPGLHTLTMNSLNKCDANLKKDLAKNILLCGGSTMFDGFPDRFQKELSKLCPN 318
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 15227503 327 SMKIkVVAPPERKYSVWVGGSILASLSSFAPMWITKAEYDEQGGAIVHRKC 377
Cdd:cd10214 319 DNPI-VAASPERKYSVWTGGSILASLKSFQQLWVRRREYEERGPFVIYRKC 368
ASKHA_NBD_actin-like cd10169
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ...
11-369 6.10e-157

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: 441.55  E-value: 6.10e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  11 IVCDNGTGMVKAGFAGDDAPRAVFPsvvgrprhrgvmvgmdekdtfvgdeaqarrgilslkypiehgvvsnWDDMEKIWH 90
Cdd:cd10169   1 IVIDNGSGTIKAGFAGEDAPRLIFP----------------------------------------------WDDMEKIWE 34
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  91 HTFYNELRLEPEEHPILLTEAPLNPKVNREKMTQIMFESFAFPSMYIGIQAVLSLYSSGRTTGIVLDSGDGVSHTVPIYE 170
Cdd:cd10169  35 HVFYNLLRVDPEEHPVLLTEPPLNPKANREKLAEILFETFNVPSLYIANQAVLSLYASGRTTGLVVDSGEGVTHIVPVYE 114
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 171 GYALPHAILRLDLAGRDLTEYLTKIMMERGYTYTTSAEREIVRDIKEKLCyiavdyeqemekattssaidrtyelpdgqv 250
Cdd:cd10169 115 GYVLPHAVRRLDIGGRDLTDYLAKLLREKGYSFSTSAEREIVRDIKEKLC------------------------------ 164
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 251 itigaerfrcpevlfqtsligmetsGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMNKEINALAPPSMKI 330
Cdd:cd10169 165 -------------------------GLHELIYDSIMKCDIDLRKELYSNIVLSGGTTLFPGFAERLQKELSKLAPSSVKV 219
                       330       340       350
                ....*....|....*....|....*....|....*....
gi 15227503 331 KVVAPPERKYSVWVGGSILASLSSFAPMWITKAEYDEQG 369
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 ...
5-369 9.17e-148

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: 424.29  E-value: 9.17e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503   5 GDESVAIVCDNGTGMVKAGFAGDDAPRAVFPSVVG-RPRHRGVMVGMDEKDT-----FVGDEA-QARRGILSLKYPIEHG 77
Cdd:cd13395   1 GDEVGALVLDIGSYSTRAGYAGEDTPKAVFPSVVGvVTDDDDAEDYVGGSGEkkrkyYIGTNSiGVPRPNMEVISPLKDG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  78 VVSNWDDMEKIWHHTFYNELRLEPEEHPILLTEAPLNPKVNREKMTQIMFESFAFPSMYIGIQAVLSLYSSGRTTGIVLD 157
Cdd:cd13395  81 LIEDWDAFEKLWDHALKNRLRVDPSEHPLLLTEPSWNTRANREKLTELMFEKYNVPAFFLAKNAVLSAFANGRSTALVVD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 158 SGDGVSHTVPIYEGYALPHAILRLDLAGRDLTEYLTKIMMERGYT----Y------------------------TTS--- 206
Cdd:cd13395 161 SGATSTSVVPVHDGYVLQKAIVRSPLGGDFLTDQLLKLLESKNIEiiprYmikskepveggapakytkkdlpntTSSyhr 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 207 -AEREIVRDIKEKLCYIAVDYEQEMEKATTSSaidRTYELPDGQVITIGAERFRCPEVLFQTSLI---------GMETSG 276
Cdd:cd13395 241 yMVRRVLQDFKESVCQVSDSPFDESEAASIPT---VSYELPDGYNIEFGAERFKIPELLFDPSLVkgipappseGNELLG 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 277 IHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMNKEINALAPPSMKIKVVAPP---ERKYSVWVGGSILASLS 353
Cdd:cd13395 318 LPQLVYTSIGSCDVDIRPELYGNVVLTGGNSLLPGFTDRLNRELSEKAPGSLKLKILASGntvERRFSSWIGGSILASLG 397
                       410
                ....*....|....*.
gi 15227503 354 SFAPMWITKAEYDEQG 369
Cdd:cd13395 398 SFQQMWISKQEYEEHG 413
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
10-373 2.17e-122

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


Pssm-ID: 466822  Cd Length: 404  Bit Score: 359.19  E-value: 2.17e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  10 AIVCDNGTGMVKAGFAGDDAPRAVFPSVVG-------RPRHRGVMVGMDEKDTFVGDEAQARRGILSLKYPIEHGVVSNW 82
Cdd:cd10221   1 AVVIDNGTGYTKMGYAGNTEPQFIIPTVIAikesakvGDGQRRSKKGIEDLDFYIGDEALANSPTYALKYPIRHGIVEDW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  83 DDMEKIWHHTFYNELRLEPEEHPILLTEAPLNPKVNREKMTQIMFESFAFPSMYIGIQAVLSLYSSGRT--------TGI 154
Cdd:cd10221  81 DLMERFWEQCIFKYLRCEPEDHYFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQAVLALAASWTSrkvgertlTGT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 155 VLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTEYLTKIMMERGYTYTTSAEREIVRDIKEKLCYIAVDYEQEMEKAT 234
Cdd:cd10221 161 VIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREEGIPPEDSLEVAKRIKERYCYVCPDIVKEFAKYD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 235 TSSA--IdRTYELPD---GQ--VITIGAERFRCPEVLFQTSLIGME-TSGIHETTYNSIMKCDVDIRKDLYGNIVLSGGT 306
Cdd:cd10221 241 SDPAkyI-KQYTGINsvtGKpyTVDVGYERFLAPEIFFNPEIASSDfTTPLPEVVDQVIQSCPIDTRRGLYKNIVLSGGS 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 307 TMFPGIADRMNKEINA----------------LAPPSMKIKVVAPPERKYSVWVGGSILASLSSFAPMWITKAEYDEQGG 370
Cdd:cd10221 320 TMFKDFGRRLQRDVKRivdarlkaseelsggkLKPKPIDVNVISHPMQRYAVWFGGSMLASTPEFYTVCHTKAEYEEYGP 399

                ...
gi 15227503 371 AIV 373
Cdd:cd10221 400 SIC 402
COG5277 COG5277
Actin-related protein [Cytoskeleton];
1-367 1.35e-120

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 355.64  E-value: 1.35e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503   1 MSDLGDESVAIVCDNGTGMVKAG-FAGDDAP-----RAVFPSVVGRPRHRGVMVGMDeKDTFVGDEAQ-----ARRGILS 69
Cdd:COG5277   1 MSDAYKLKYVIGIDFGTSYVKYGpIALEEKPrviqtRGLFLRIVGESKLLGPMEGLS-RGLVVGDEVSkylssVRDAIRN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  70 LKYPIEHGVV-----SNWDDMEKIWHHTFYNELRLEPEEHP--ILLTEAPLNPKVNREKMTQIMFESFA---FPSMYIGI 139
Cdd:COG5277  80 LKYPLRDGIVrrddeDAWRVLKELLRYTFAQFLVVDPEFHGflVVVALSALAPDYMRERLFDIHFEVFSeegAPAVTIIP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 140 QAVLSLYSSGRTTGIVLDSGDGVSHTVPIYEGyALPHAILRLDLAGRDLTEYLTKIMMERGYTYTTSAEReIVRDIKEKL 219
Cdd:COG5277 160 QPLAVAIAEKAVTCVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSDTAREEY-VVRVVKEAL 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 220 CYIAVDYEQEMEKA-TTSSAIDRTYELPDGQV-ITIG---AERFRCPEVLFQTSLIGME--------------------- 273
Cdd:COG5277 238 GLVPRDLAKAIQKAaSNPDSFEAKVRLPNPTVeIELGnyaWERFLIGEILFNPNHEGFEsyiqqgrlriedavigdvvly 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 274 -TSGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMF---PGIAD-------RMNKEINALApPSMKIKVVAPPERKYSV 342
Cdd:COG5277 318 gEMGLAEAIINSIMKCDVEIQDELYSNIILSGGAFNWsvpPGLEDvavdsvtRVQIELSELA-PELKVNVRLVSDPQYSV 396
                       410       420
                ....*....|....*....|....*..
gi 15227503 343 WVGGSILASLSSFAPMW--ITKAEYDE 367
Cdd:COG5277 397 WKGAIIYGYALPFSVKWswITKEGWYF 423
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
10-375 5.75e-117

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 345.95  E-value: 5.75e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503   10 AIVCDNGTGMVKAGFAGDDAPRAVFPSVVGRPRHRGVMV---GMDEKDTFVGDEAQARRGILSLKYPIEHGVVSNWDDME 86
Cdd:PTZ00280   6 VVVIDNGTGYTKMGYAGNTEPTYIIPTLIADNSKQSRRRskkGFEDLDFYIGDEALAASKSYTLTYPMKHGIVEDWDLME 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503   87 KIWHHTFYNELRLEPEEHPILLTEAPLNPKVNREKMTQIMFESFAFPSMYIGIQAVLSLYSS----------GRTTGIVL 156
Cdd:PTZ00280  86 KFWEQCIFKYLRCEPEEHYFILTEPPMNPPENREYTAEIMFETFNVKGLYIAVQAVLALRASwtskkakelgGTLTGTVI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  157 DSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTEYLTKIMMERGYTYTTSAEREIVRDIKEKLCYIAVDYEQEMEKA--- 233
Cdd:PTZ00280 166 DSGDGVTHVIPVVDGYVIGSSIKHIPLAGRDITNFIQQMLRERGEPIPAEDILLLAQRIKEKYCYVAPDIAKEFEKYdsd 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  234 -----TTSSAIDRTyelpDGQVITI--GAERFRCPEVLFQTSLIGME-TSGIHETTYNSIMKCDVDIRKDLYGNIVLSGG 305
Cdd:PTZ00280 246 pknhfKKYTAVNSV----TKKPYTVdvGYERFLGPEMFFHPEIFSSEwTTPLPEVVDDAIQSCPIDCRRPLYKNIVLSGG 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  306 TTMFPGIADRMNKEINA----------------LAPPSMKIKVVAPPERKYSVWVGGSILASLSSFAPMWITKAEYDEQG 369
Cdd:PTZ00280 322 STMFKGFDKRLQRDVRKrvdrrlkkaeelsggkLKPIPIDVNVVSHPRQRYAVWYGGSMLASSPEFEKVCHTKAEYDEYG 401

                 ....*.
gi 15227503  370 GAIVHR 375
Cdd:PTZ00280 402 PSICRY 407
ASKHA_NBD_Arp6 cd10210
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ...
11-369 3.26e-97

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: 294.46  E-value: 3.26e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  11 IVCDNGTGMVKAGFAGDDAPRaVFPSVVGRPRHRGVMVGMDEkdtfVGDEAQARRGiLSLKYPIEHGVVSNWDDMEKIWH 90
Cdd:cd10210   2 LVLDNGAYTIKAGFASDDPPR-VIPNCIAKPKSERRRLFGDD----QLDECKDLSG-LFYRRPFERGYLVNWDLQRQIWD 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  91 HTFYNE-LRLEPEEHPILLTEAPLNPKVNREKMTQIMFESFAFPSMYIGIQAVLSLY----------SSGRTTGIVLDSG 159
Cdd:cd10210  76 HLFGKLlLNVDPSDTALVLTEPPFNPPSIQEAMDEIVFEEYGFQSLYRTTAAALSAFayladseqssSSSSQCCLVVDSG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 160 DGVSHTVPIYEGYALPHAILRLDLAGRDLTEYLTKI-------MMErgYTYttsaereIVRDIKEKLCYIAVDYEQEMEK 232
Cdd:cd10210 156 FSFTHIVPFFDGKPVKRAVRRIDVGGKLLTNYLKEIisyrqlnVMD--ETY-------LVNQIKEDLCFVSTDFYEDLEI 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 233 A---TTSSAIDRTYELPDG-----------------------QVITIGAERFRCPEVLFQTSLIGMETSGIHETTYNSIM 286
Cdd:cd10210 227 AkkkGKENTIRRDYVLPDYttskrgyvrdpeepnrgklkedeQVLRLNNERFTVPELLFHPSDIGIQQAGIAEAIVQSIN 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 287 KCDVDIRKDLYGNIVLSGGTTMFPGIADRMNKEINALAPPSMKIKVVAPPERKYSVWVGGSILASLSSFAPMWITKAEYD 366
Cdd:cd10210 307 ACPEELQPLLYANIVLTGGNALFPGFRERLEAELRSLAPDDYDVNVTLPEDPITYAWEGGSLLAQSPEFEELAVTRAEYE 386

                ...
gi 15227503 367 EQG 369
Cdd:cd10210 387 EHG 389
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
11-374 4.14e-84

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: 259.63  E-value: 4.14e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  11 IVCDNGTGMVKAGFAGDDApravFPSVVgRPRhrgVMVGMDEkdtFVGDEAQARRGILSlkYPIEHGVVSNWDDMEKIWH 90
Cdd:cd10209   1 VVIDAGSRLLKAGYAYPDR----EPSVV-EPT---RVTPAVE---DGEESDTVVEGNTV--SPIRRGRIEDWDALEALLR 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  91 HTFYNELRLEP-EEHPILLTEAPLNPKVNREKMTQIMFESFAFPSMYIGIQAVLSLYSSGRTTGIVLDSGDGVSHTVPIY 169
Cdd:cd10209  68 YVFYTGLGWEEgNEGQVLIAEPLLTSKAERERLTQLMFETFNVSGLYASEQAVLSLYAVGRISGCVVDVGHGKIDIAPVW 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 170 EGYALPHAILRLDLAGRDLTEYLTKIMMERGYTytTSAEREIVRDIKEKLCYIAVDYEQEMEKATTSSAIdrTYELPDGQ 249
Cdd:cd10209 148 EGAIQHNAVRRFEIGGRDLTELLAAELGKSNPK--VKLDRSIVERLKEAVAWSADDEEAYEKKVLTCSPE--TYTLPDGR 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 250 VITIGAERFRCPEVLFQTSLIGMETSGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMNKEINALAPPSMK 329
Cdd:cd10209 224 VISVGKERYCVGEALFRPSILGIEEYGIVEQLVRAVSTSPSENRRQLLENIVLCGGTSSVPGLEARLQKEIRLLSSPSSR 303
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 15227503 330 IKVVAPPE------RKYSVWVGGSILASLSSFAPMWITKAEYDEQGGAIVH 374
Cdd:cd10209 304 PALVKPPEympentLRYSAWIGGAILAKVVFPQNQHVTKADYDETGPSVVH 354
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
10-370 1.59e-71

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: 227.07  E-value: 1.59e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  10 AIVCDNGTGMVKAGFAGDDAPRAVFPSVVGRPRHRgvmvGMDEKDTFVGDEA---QARRGilSLKYPIEHGVVSNWDDME 86
Cdd:cd10211   1 PIVIDNGSYQCRAGWAGDKEPRLVFRNLVAKPRDR----KKGITVTLVGNDIlndEAVRS--HLRSPFDRNVVTNFDLQE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  87 KIWHHTFyNELRLEPE---EHPILLTEAPLNPKVNREKMTQIMFESFAFPSMYIGIQAVLSLY----SSGRTTGIVLDSG 159
Cdd:cd10211  75 QILDYIF-SHLGINSEgsvDHPIVLTEALCNPNYSRQLMSELLFECYGVPSVAYGIDSLFSYYhnqpQGDPSDGLVISSG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 160 DGVSHTVPIYEGYALPHAILRLDLAGRDLTEYLTKIMMERGYTYTTSAEREIVRDIKEKLCYIAVDYEQEMEK---ATTS 236
Cdd:cd10211 154 YSTTHVIPVLNGRLDLSQCKRINLGGFHATDYLQRLLQLKYPTHPSAITLSRAEELVHEHCYVAEDYDEELKKwedPEYY 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 237 SAIDRTYELPdgqvitigaerFrcpevlfqtsligmetsGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRM 316
Cdd:cd10211 234 EENVRKIQLP-----------F-----------------GLVETIEFVLKRYPAEQQDRLVQNVFLTGGNALFPGLKERL 285
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 15227503 317 NKEINALAPPSMKIKVVAPPERKYSVWVGGSILASLSSFAPMWITKAEYDEQGG 370
Cdd:cd10211 286 EKELRAIRPFGSPFNVVRAKDPVLDAWRGAAKWALDSTFEKVWITKQEYEEKGG 339
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
41-376 6.41e-53

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: 179.04  E-value: 6.41e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  41 PRHRGVMVGMDEKDTFVGD--EAQARRGILslkYPIEHGVVSNWDDMEKIWHHTFYNELRLEPE--EHPILLTEAPLNPK 116
Cdd:cd10208   7 PGSQTTRAGLGLGELLTPPtiEIPTRVEII---WPIQDGRVVDWDALEALWRHILFSLLSIPRPtnNSPVLLSVPPSWSK 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 117 VNREKMTQIMFESFAFPSMYIGIQAVLSLYSSGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTEYLTKIM 196
Cdd:cd10208  84 SDLELLTQLFFERLNVPAFAILEAPLAALYAAGATSGIVVDIGHEKTDITPIVDSQVVPHALVSIPIGGQDCTAHLAQLL 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 197 MERGYTYTTSAE--REIVRDIKEKLcyiavdYEQEMEKATTSSAidrtyELPDGQVITIGAERFRCPEVLFQTSLIGMET 274
Cdd:cd10208 164 KSDEPELKSQAEsgEEATLDLAEAL------KKSPICEVLSDGA-----DLASGTEITVGKERFRACEPLFKPSSLRVDL 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 275 SGIHETTYNSIMK-CDVDIRKDLYGNIVLSGGTTMFPGIADRMNKEINA-LAPPSMKIKVVAP------------PERK- 339
Cdd:cd10208 233 LIAAIAGALVLNAsDEPDKRPALWENIIIVGGGSRIRGLKEALLSELQQfHLISETSASPQQPriirlakipdyfPEWKk 312
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 15227503 340 ----YSVWVGGSILASL---SSFAPMWITKAEYDEQGGAIVHRK 376
Cdd:cd10208 313 sgyeEAAFLGASIVAKLvfnDPSSKHYISKVDYNEKGPAAIHTK 356
ASKHA_NBD_Arp10 cd10207
nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins; ...
11-370 8.00e-50

nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins; Arp10, also known as actin-related protein 11 (Arp11), is a subunit of the cargo-binding portion of the dynein activator, dynactin. It, together with dynactin4 (p62), -5(p25), and -6(p27), forms a heterotetrameric complex located at the pointed end of Arp1. Arp1 forms a mini-filament of uniform size, with proteins bound along its length and at both ends. Human Arp10 is encoded by the ACTR10 gene.


Pssm-ID: 466813 [Multi-domain]  Cd Length: 375  Bit Score: 171.67  E-value: 8.00e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  11 IVCDNGTGMVKAGFAGDDAPRAVFPSVVGRPRhrgvmvgmdekdtfvgdeaqarRGILSLKYPIEHGVVSNWDDM-EKIW 89
Cdd:cd10207   1 VVLDIGSAYTKCGFAGESAPRCIIPSEVKLPG----------------------GKKVIRVVDQRSGNEEELYEAlKEFL 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  90 HHTFYNELRLEPEEHPILLTEAPLNPKVNREKMTQIMFESFA------FPSMyigiqaVLSLYSSGRTTGIVLDSGDGVS 163
Cdd:cd10207  59 HELYFKHLLVNPKDRRVVVVESVLCPTPFRETLAKVLFKHFEvpsvlfAPSH------LLSLLTLGIRTALVVDCGYRET 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 164 HTVPIYEGYALPHAILRLDLAGRDLTEYLTKIMMERGYTYTTSAER------------EIVRDIKEKLCYIA-------- 223
Cdd:cd10207 133 RVLPVYEGVPLLSAWQSTPLGGKALHKRLKKLLLEHATVVTGDNKGqllssvdsllseEVLEDIKVRACFVTslergktl 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 224 VDYEQEMEKATTSSAIDRTYELPDGQVITIGAERFRCPEVLFQTSLIGMETsgIHETTYNSIMKCDVDIRKDLYGNIVLS 303
Cdd:cd10207 213 QSATEEGSTEEPSPPPPVDYPLDGEKILIVPGSIRESAEELLFEGDNEEKS--LPTLILDSLLKCPIDVRKQLAENIVVI 290
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15227503 304 GGTTMFPGIADRMNKEINALA-PPSMK-------IKVVAPPER---KYSVWVGGSILASLSSFAPMWITKAEYDEQGG 370
Cdd:cd10207 291 GGTSMLPGFKHRLLEELRALLrKPKYFeelapktFRFHTPPSVfkpNYLAWLGGSIFGALESILGRSLSREAYLQTGR 368
ASKHA_NBD_AtArp8-like cd13396
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and ...
92-369 6.44e-43

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: 152.31  E-value: 6.44e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  92 TFYNELRLEPEEHPILLTEaPL-------NPKVNREKMTQIMFE---SFAFPSMYIGIQAVLSLYSSGRTTGIVLDSGDG 161
Cdd:cd13396  47 TIMTRMQVKPSRQPVVVSL-PLchsddteSAAASRRQLRGTIFNvlfDMNVPAVCAVDQAVLALYAANRTSGIVVNIGFR 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 162 VSHTVPIYEGYALPH-AILRLDLAGRDLTEYLTKIMMERGYTYTTSAereIVRDIKEKLCYIAVDYEQEMEKATTSSAid 240
Cdd:cd13396 126 VTTIVPVYRGRVMHDiGVEVVGQGALRLTGFLKELMQQNGIRFPSLY---TVRTIKEKLCYVAEDYEAELAKDTQASC-- 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 241 rtyELPDGQVITIGAERFRCPEVLFQTSLIGMETSGIHETTYNSIMKCDVDIR---KDLYGNIVLSGGTTMFPGIADRMN 317
Cdd:cd13396 201 ---EVAGEGWFTLSNERFKTGEILFQPGLGGMRAMGLHQAVALCMDHCALVHSqgdDGWFKTIVLSGGSACLPGLSERLE 277
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15227503 318 KEINALAPPSMK--IKVVAPPERKYSVWVGGSILASLSSFAPMW-ITKAEYDEQG 369
Cdd:cd13396 278 RELRKLLPKSLSegIRIIPPPLGPDSAWQGAKLISNLSNFPDGWcITKKQFRNKP 332
ASKHA_NBD_Arp8-like cd10206
nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The ...
51-369 5.56e-29

nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The Arp8-like family includes Arp8, also called actin-like protein 8, from vertebrates and fungi. Human Arp8 is encoded by the ACTR8 gene and is also known as INO80 complex subunit N. It plays an important role in the functional organization of mitotic chromosomes. Arp8 exhibits low basal ATPase activity, and is unable to polymerize. It is probably a core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication, and probably DNA repair. it is required for the recruitment of INO80 (and probably the INO80 complex) to sites of DNA damage. Arp8 strongly prefers nucleosomes and H3-H4 tetramers over H2A-H2B dimers, suggesting it may act as a nucleosome recognition module within the complex. This subfamily also contains Arabidopsis thaliana Arp9.


Pssm-ID: 466812 [Multi-domain]  Cd Length: 447  Bit Score: 116.96  E-value: 5.56e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  51 DEKDTFVGDEAQ--ARRGILSLKYPIEHGVVsNW-----------DDMEKIWHHTFYNELRLEPEEHP----ILLTEAPL 113
Cdd:cd10206 118 DYPDFLVGEEALrlPPSEEYNLHWPIRRGRL-NVhsdggsltavlDDLEDIWSHALEEKLEIPRKDLKnyraVLVIPDLF 196
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 114 NpKVNREKMTQIMFESFAFPSMYIGIQAVLSLYSSGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTEYLT 193
Cdd:cd10206 197 D-RRHVKELVDLLLRRLGFSSVFVHQESVCATFGAGLSSACVVDIGAQKTSVACVEDGLSIPNSRIRLPYGGDDITRCFL 275
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 194 KIMMERGYTYT-----TSAEREIVRDIKEKLCYIAVDyeqemekattssaidrtyelPDGQVITIGAERFRC-PEVLFQT 267
Cdd:cd10206 276 WLLRRSGFPYRecnlnSPLDFLLLERLKETYCTLDQD--------------------DIGVQLHEFYVREPGqPTLKYQF 335
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 268 SLIGmetsgIHETTYNSIMKC-DVDIRKDLYGNIVLSGGTTMFPGIA----DRMNKEINALAPPSMKIKVVAPPERK--- 339
Cdd:cd10206 336 KLLP-----LDEAIVQSILSCaSDELKRKMYSSILLVGGGAKIPGLAealeDRLLIKIPSLFEAVETVEVLPPPKDMdps 410
                       330       340       350
                ....*....|....*....|....*....|
gi 15227503 340 YSVWVGGSILASLSSFAPMWITKAEYDEQG 369
Cdd:cd10206 411 LLAWKGGAVLACLDSAQELWITRKEWQRLG 440
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
306-377 4.37e-26

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: 101.59  E-value: 4.37e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15227503  306 TTMFPGIADRMNKEINALAPPSMKIKVVAPPERKYSVWVGGSILASLSSFAPMWITKAEYDEQGGAIVHRKC 377
Cdd:NF040575  61 RVNESGFYEKLKKSITEKAPKGALIGMTLDPKPESAAWRGAAMYAASEGFVEMAITKQEYDESGPSIVHRKC 132
ASKHA_NBD_ScArp7-like cd10212
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and ...
11-366 6.82e-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: 84.77  E-value: 6.82e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  11 IVCDNGTGMVKAGFAGDDAPRAVFPS-VVGRPRHRGVMVGMDEKDTFVGDEAQARRGILSLKYPIEHGVVSNWDDMEKIW 89
Cdd:cd10212   6 VVIHNGSHRTVAGFSNVELPQCIIPSsYIKRTDEGGEAEFIFGTYNMIDAAAEKRNGDEVYTLVDSQGLPYNWDALEMQW 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  90 HHTFYNELRLEPEEHPILLTEAPLNPKVNR---EKMTQIMFESFAFPSMYIGIQAVLSLYSSGRTTGIVLDSGDGVSHTV 166
Cdd:cd10212  86 RYLYDTQLKVSPEELPLVITMPATNGKPDMailERYYELAFDKLNVPVFQIVIEPLAIALSMGKSSAFVIDIGASGCNVT 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 167 PIYEGYALPHAILRLDLAGRDLT----EYLTKIMMERGYTYTTSAER------------------------------EIV 212
Cdd:cd10212 166 PIIDGIVVKNAVVRSKFGGDFLDfqvhERLAPLIKEENDMENMADEQkrstdvwyeastwiqqfkstmlqvsekdlfELE 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 213 RDIKEKLCYIAVDYEQ--EMEKATTSSAIDRTYELPDGQ-----------VITIG-AERFRCPEVLFQTSLIGMETS--- 275
Cdd:cd10212 246 RYYKEQADIYAKQQEQlkQMDQQLQYTALTGSPNNPLVQkknflfkplnkTLTLDlKECYQFAEYLFKPQLISDKFSped 325
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 276 GIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMNKEInALAPPSMKIKVVAPP---ERKYSVWVGGSILASL 352
Cdd:cd10212 326 GLGPLMAKSVKKAPEQVYSLLLTNVIITGSTSLIEGMEQRIIKEL-SIRFPQYKLTTFANQvmmDRKIQGWLGALTMANL 404
                       410
                ....*....|....*
gi 15227503 353 SSFA-PMWITKAEYD 366
Cdd:cd10212 405 PSWSlGKWYSKEDYE 419
ASKHA_NBD_MamK cd24009
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ...
3-319 1.07e-08

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: 56.07  E-value: 1.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503   3 DLGDESVAIVCDNGTgmvkagfagddapRAVFPSVVGRPRHRGVMVGMdEKDTFVGDEAQARRGILSLKYPIEHGVVSNW 82
Cdd:cd24009   7 DLGTSRSAVVTSRGK-------------RFSFRSVVGYPKDIIARKLL-GKEVLFGDEALENRLALDLRRPLEDGVIKEG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503  83 DDMEkiwhhtfYNELRlEPEEHPILLTEAPLNPKV-------------NREKMTQIMFESfaFPSMYIGIQAVLSLYSSG 149
Cdd:cd24009  73 DDRD-------LEAAR-ELLQHLIELALPGPDDEIyavigvparasaeNKQALLEIAREL--VDGVMVVSEPFAVAYGLD 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 150 RTTG-IVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTEYLTKIMMERgytYT-TSAEREIVRDIKEKLCYIavdye 227
Cdd:cd24009 143 RLDNsLIVDIGAGTTDLCRMKGTIPTEEDQITLPKAGDYIDEELVDLIKER---YPeVQLTLNMARRWKEKYGFV----- 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227503 228 qemekATTSSAIdrTYELP-DGQVIT--IGAE-RFRCPEVLfqtsligmetSGIHETTYNSIMKCDVDIRKDLYGNIVLS 303
Cdd:cd24009 215 -----GDASEPV--KVELPvDGKPVTydITEElRIACESLV----------PDIVEGIKKLIASFDPEFQEELRNNIVLA 277
                       330
                ....*....|....*.
gi 15227503 304 GGTTMFPGIADRMNKE 319
Cdd:cd24009 278 GGGSRIRGLDTYIEKA 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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