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Conserved domains on  [gi|2217328134|ref|XP_047300376|]
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POTE ankyrin domain family member E isoform X3 [Homo sapiens]

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

 Zoom to residue level

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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 ...
288-652 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: 868.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 288 AVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEKI 367
Cdd:cd10224     1 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 368 WHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVPSLYTSGRTTGIVMDSGDGVTHTVPI 447
Cdd:cd10224    81 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 448 YEGNALPHATLRLDLAGRELPDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDG 527
Cdd:cd10224   161 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 528 QVITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMM 607
Cdd:cd10224   241 QVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTM 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 2217328134 608 KIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIV 652
Cdd:cd10224   321 KIKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIV 365
CCDC144C super family cl25942
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ...
230-283 7.86e-18

CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.


The actual alignment was detected with superfamily member pfam14915:

Pssm-ID: 464371 [Multi-domain]  Cd Length: 304  Bit Score: 84.65  E-value: 7.86e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217328134 230 NSTLREEIAMLRLELDTMKHQSQLREKKYLEDIESVKKKNDNLLKALQLNELTM 283
Cdd:pfam14915   1 NCMLQDEIAMLRLEIDTIKNQNQEKEKKYLEDIEILKEKNDDLQKTLKLNEETL 54
 
Name Accession Description Interval E-value
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
288-652 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: 868.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 288 AVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEKI 367
Cdd:cd10224     1 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 368 WHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVPSLYTSGRTTGIVMDSGDGVTHTVPI 447
Cdd:cd10224    81 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 448 YEGNALPHATLRLDLAGRELPDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDG 527
Cdd:cd10224   161 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 528 QVITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMM 607
Cdd:cd10224   241 QVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTM 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 2217328134 608 KIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIV 652
Cdd:cd10224   321 KIKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIV 365
PTZ00281 PTZ00281
actin; Provisional
283-657 0e+00

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 718.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 283 MDDDTAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWD 362
Cdd:PTZ00281    2 DGEDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 363 DMEKIWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVPSLYTSGRTTGIVMDSGDGVT 442
Cdd:PTZ00281   82 DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 443 HTVPIYEGNALPHATLRLDLAGRELPDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSY 522
Cdd:PTZ00281  162 HTVPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEMQTAASSSALEKSY 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 523 ELPDGQVITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAAL 602
Cdd:PTZ00281  242 ELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELTAL 321
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217328134 603 APSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF 657
Cdd:PTZ00281  322 APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIVHRKCF 376
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
287-657 0e+00

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 615.42  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134  287 TAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMhQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEK 366
Cdd:smart00268   1 VPAIVIDNGSGTIKAGFAGEDFPQVVFPSIVGRPKDGKGMVGD-AKDIFVGDEAQEKRGGLELKYPIENGIVENWDDMEK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134  367 IWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVPSLYTSGRTTGIVMDSGDGVTHTVP 446
Cdd:smart00268  80 IWDYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134  447 IYEGNALPHATLRLDLAGRELPDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMATAAS---SSSLEKSYE 523
Cdd:smart00268 160 VVDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLAREsseSSKLEKTYE 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134  524 LPDGQVITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALA 603
Cdd:smart00268 240 LPDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELKQLA 319
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2217328134  604 PSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF 657
Cdd:smart00268 320 PKKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERKCF 373
Actin pfam00022
Actin;
287-657 0e+00

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 537.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 287 TAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGmmgGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEK 366
Cdd:pfam00022   1 VSALVIDNGSHTTRAGFAGEDAPKAVIPSCVGKPRGTK---VEAANKYYVGDEALTYRPGMEVRSPVEDGIVVDWDAMEE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 367 IWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVPSLYTSGRTTGIVMDSGDGVTHTVP 446
Cdd:pfam00022  78 IWEHVLKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 447 IYEGNALPHATLRLDLAGRELPDYLMKILTER------------------------------GYRFTTMAEREIVRDIKE 496
Cdd:pfam00022 158 VHDGYVLQKAIRRSDLGGDFLTDYLRELLRSRnieitprylikskkpgdpapavtkrelpdtTYSYKTYQERRVLEEIKE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 497 KLCYVALDFeqEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPCFLGMES--------CGIHETTFNSIMKSD 568
Cdd:pfam00022 238 SVCYVSDDP--FGDETTSSSIPTRVYELPDGSTIILGAERFRVPEILFNPSLIGSESelpppqtaVGIPELIVDAINACD 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 569 VDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMMKIRIIAPPK---RKYSVWVGGSILASLSTFQQMWISKQEYD 645
Cdd:pfam00022 316 VDLRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVKIIAPGNtveRRYSAWIGGSILASLGTFQQMWVSKQEYE 395
                         410
                  ....*....|..
gi 2217328134 646 ESGPSIVHRKCF 657
Cdd:pfam00022 396 EHGASVVERKCK 407
COG5277 COG5277
Actin-related protein [Cytoskeleton];
289-647 1.33e-126

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 381.06  E-value: 1.33e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 289 VLVIDNGSGMCKAG-FAGDDAP-----RAVFPSIVGRPRQQGMMGGMhQKESYVGKEAQS-----KRGILTLKYPMEHGI 357
Cdd:COG5277    10 VIGIDFGTSYVKYGpIALEEKPrviqtRGLFLRIVGESKLLGPMEGL-SRGLVVGDEVSKylssvRDAIRNLKYPLRDGI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 358 IT-----NWDDMEKIWHHTFYNELRVAPEEHP--ILLTEAPLNPKANREKMTQIMFETF---NTPAMYVAIQAVPSLYTS 427
Cdd:COG5277    89 VRrddedAWRVLKELLRYTFAQFLVVDPEFHGflVVVALSALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPLAVAIAE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 428 GRTTGIVMDSGDGVTHTVPIYEGnALPHATLRLDLAGRELPDYLMKILTERGYRFTTMAEReIVRDIKEKLCYVALDFEQ 507
Cdd:COG5277   169 KAVTCVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSDTAREEY-VVRVVKEALGLVPRDLAK 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 508 EM-ATAASSSSLEKSYELPDGQV-ITIGN---ERFRCPEALFQPCFLGMESC----------------------GIHETT 560
Cdd:COG5277   247 AIqKAASNPDSFEAKVRLPNPTVeIELGNyawERFLIGEILFNPNHEGFESYiqqgrlriedavigdvvlygemGLAEAI 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 561 FNSIMKSDVDIRKDLYTNTVLSGGTTMY---PGMA-------HRMQKEIAALAPSmMKIRIIAPPKRKYSVWVGGSILAS 630
Cdd:COG5277   327 INSIMKCDVEIQDELYSNIILSGGAFNWsvpPGLEdvavdsvTRVQIELSELAPE-LKVNVRLVSDPQYSVWKGAIIYGY 405
                         410
                  ....*....|....*....
gi 2217328134 631 LSTFQQMW--ISKQEYDES 647
Cdd:COG5277   406 ALPFSVKWswITKEGWYFL 424
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
585-656 1.76e-34

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: 127.40  E-value: 1.76e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217328134 585 TTMYPGMAHRMQKEIAALAPSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKC 656
Cdd:NF040575   61 RVNESGFYEKLKKSITEKAPKGALIGMTLDPKPESAAWRGAAMYAASEGFVEMAITKQEYDESGPSIVHRKC 132
CCDC144C pfam14915
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ...
230-283 7.86e-18

CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.


Pssm-ID: 464371 [Multi-domain]  Cd Length: 304  Bit Score: 84.65  E-value: 7.86e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217328134 230 NSTLREEIAMLRLELDTMKHQSQLREKKYLEDIESVKKKNDNLLKALQLNELTM 283
Cdd:pfam14915   1 NCMLQDEIAMLRLEIDTIKNQNQEKEKKYLEDIEILKEKNDDLQKTLKLNEETL 54
 
Name Accession Description Interval E-value
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
288-652 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: 868.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 288 AVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEKI 367
Cdd:cd10224     1 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 368 WHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVPSLYTSGRTTGIVMDSGDGVTHTVPI 447
Cdd:cd10224    81 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 448 YEGNALPHATLRLDLAGRELPDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDG 527
Cdd:cd10224   161 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 528 QVITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMM 607
Cdd:cd10224   241 QVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTM 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 2217328134 608 KIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIV 652
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 ...
288-648 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: 729.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 288 AVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEKI 367
Cdd:cd13397     1 PAVVIDNGSGLIKAGFAGEDLPRAVFPSVVGRPKYKAVMLGAGQKEVYVGDEAQEKRGVLTLSYPIEHGIVTNWDDMEKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 368 WHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVPSLYTSGRTTGIVMDSGDGVTHTVPI 447
Cdd:cd13397    81 WHHTFENELRVKPEEHPVLLTEAPLNPKQNREKMAEIMFETFGVPAFYVAIQAVLSLYSSGRTTGLVLDSGDGVTHTVPI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 448 YEGNALPHATLRLDLAGRELPDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMatAASSSSLEKSYELPDG 527
Cdd:cd13397   161 YEGYALPHAVQRLDLAGRDLTEYLMKLLKERGHSFTTTAEREIVRDIKEKLCYVALDYEEEL--KKKSEELEKEYTLPDG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 528 QVITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMM 607
Cdd:cd13397   239 QVIKIGSERFRCPEALFRPSLIGREAPGIHKLVYNSIMKCDIDIRKDLYSNIVLSGGSTMFPGLPERLQKELEALAPSST 318
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 2217328134 608 KIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESG 648
Cdd:cd13397   319 KVKVIAPPERKYSVWIGGSILASLSTFKSMWITRAEYDEFG 359
PTZ00281 PTZ00281
actin; Provisional
283-657 0e+00

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 718.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 283 MDDDTAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWD 362
Cdd:PTZ00281    2 DGEDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 363 DMEKIWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVPSLYTSGRTTGIVMDSGDGVT 442
Cdd:PTZ00281   82 DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 443 HTVPIYEGNALPHATLRLDLAGRELPDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSY 522
Cdd:PTZ00281  162 HTVPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEMQTAASSSALEKSY 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 523 ELPDGQVITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAAL 602
Cdd:PTZ00281  242 ELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELTAL 321
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217328134 603 APSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF 657
Cdd:PTZ00281  322 APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIVHRKCF 376
PTZ00004 PTZ00004
actin-2; Provisional
283-657 0e+00

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 664.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 283 MDDDTAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWD 362
Cdd:PTZ00004    2 SVEETNAAVVDNGSGMVKAGFAGDDAPRCVFPSIVGRPKNPGIMVGMEEKDCYVGDEAQDKRGILTLKYPIEHGIVTNWD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 363 DMEKIWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVPSLYTSGRTTGIVMDSGDGVT 442
Cdd:PTZ00004   82 DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETHNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 443 HTVPIYEGNALPHATLRLDLAGRELPDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMATAASSSSL-EKS 521
Cdd:PTZ00004  162 HTVPIYEGYSLPHAIHRLDVAGRDLTEYMMKILHERGTTFTTTAEKEIVRDIKEKLCYIALDFDEEMGNSAGSSDKyEES 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 522 YELPDGQVITIGNERFRCPEALFQPCFLGMESC-GIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIA 600
Cdd:PTZ00004  242 YELPDGTIITVGSERFRCPEALFQPSLIGKEEPpGIHELTFQSINKCDIDIRKDLYGNIVLSGGTTMYRGLPERLTKELT 321
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217328134 601 ALAPSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF 657
Cdd:PTZ00004  322 TLAPSTMKIKVVAPPERKYSVWIGGSILSSLPTFQQMWVTKEEYDESGPSIVHRKCF 378
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
287-657 0e+00

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 615.42  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134  287 TAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMhQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEK 366
Cdd:smart00268   1 VPAIVIDNGSGTIKAGFAGEDFPQVVFPSIVGRPKDGKGMVGD-AKDIFVGDEAQEKRGGLELKYPIENGIVENWDDMEK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134  367 IWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVPSLYTSGRTTGIVMDSGDGVTHTVP 446
Cdd:smart00268  80 IWDYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134  447 IYEGNALPHATLRLDLAGRELPDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMATAAS---SSSLEKSYE 523
Cdd:smart00268 160 VVDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLAREsseSSKLEKTYE 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134  524 LPDGQVITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALA 603
Cdd:smart00268 240 LPDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELKQLA 319
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2217328134  604 PSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF 657
Cdd:smart00268 320 PKKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERKCF 373
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
290-656 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: 588.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 290 LVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEKIWH 369
Cdd:cd10216     4 VVIDNGSGVIKAGFAGDDIPKVVFPSYVGRPKHVRVMAGALEGDVFVGPKAEEHRGLLKIRYPMEHGIVTDWNDMERIWQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 370 HTFYNE-LRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVPSLYTSGRTTGIVMDSGDGVTHTVPIY 448
Cdd:cd10216    84 YVYSKLqLNTFSEEHPVLLTEAPLNPRKNREKAAEVFFETFNVPALFVSMQAVLSLYASGRTTGVVLDSGDGVTHAVPIY 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 449 EGNALPHATLRLDLAGRELPDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFeQEMATAASSSSLEKSYELPDGQ 528
Cdd:cd10216   164 EGFALPHSIRRVDIAGRDVTEYLQLLLRKSGYNFHTSAEFEIVREIKEKACYVALNP-QKEEKLEEEKTEKAQYTLPDGS 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 529 VITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMMK 608
Cdd:cd10216   243 TIEIGPERFRAPEILFNPELIGLEYPGVHEVLVDSIQKSDLDLRKTLYSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDVK 322
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 2217328134 609 IRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKC 656
Cdd:cd10216   323 IRISAPPERLYSTWIGGSILASLSTFKKMWVSKKEYEEDGARILHRKT 370
Actin pfam00022
Actin;
287-657 0e+00

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 537.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 287 TAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGmmgGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEK 366
Cdd:pfam00022   1 VSALVIDNGSHTTRAGFAGEDAPKAVIPSCVGKPRGTK---VEAANKYYVGDEALTYRPGMEVRSPVEDGIVVDWDAMEE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 367 IWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVPSLYTSGRTTGIVMDSGDGVTHTVP 446
Cdd:pfam00022  78 IWEHVLKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 447 IYEGNALPHATLRLDLAGRELPDYLMKILTER------------------------------GYRFTTMAEREIVRDIKE 496
Cdd:pfam00022 158 VHDGYVLQKAIRRSDLGGDFLTDYLRELLRSRnieitprylikskkpgdpapavtkrelpdtTYSYKTYQERRVLEEIKE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 497 KLCYVALDFeqEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPCFLGMES--------CGIHETTFNSIMKSD 568
Cdd:pfam00022 238 SVCYVSDDP--FGDETTSSSIPTRVYELPDGSTIILGAERFRVPEILFNPSLIGSESelpppqtaVGIPELIVDAINACD 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 569 VDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMMKIRIIAPPK---RKYSVWVGGSILASLSTFQQMWISKQEYD 645
Cdd:pfam00022 316 VDLRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVKIIAPGNtveRRYSAWIGGSILASLGTFQQMWVSKQEYE 395
                         410
                  ....*....|..
gi 2217328134 646 ESGPSIVHRKCF 657
Cdd:pfam00022 396 EHGASVVERKCK 407
ASKHA_NBD_Arp2 cd10220
nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, ...
289-652 2.95e-177

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: 508.64  E-value: 2.95e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 289 VLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRP--RQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEK 366
Cdd:cd10220     2 VVVCDNGTGFVKCGFAGSNFPEHVFPSLVGRPilRAEEKVGDIEIKDIMVGDEASELRSMLEVTYPMENGIVRNWDDMEH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 367 IWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVPSLYTSGRTTGIVMDSGDGVTHTVP 446
Cdd:cd10220    82 LWDYTFGEKLKIDPRECKILLTEPPMNPTKNREKMVEVMFEKYGFAGVYVAIQAVLTLYAQGLLTGVVVDSGDGVTHIVP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 447 IYEGNALPHATLRLDLAGRELPDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPD 526
Cdd:cd10220   162 VYEGFSLPHLTRRLDVAGRDITRYLIKLLLLRGYAFNRTADFETVREIKEKLCYVAYDIELEQKLALETTVLVESYTLPD 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 527 GQVITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAAL---- 602
Cdd:cd10220   242 GRVIKVGGERFEAPEALFQPHLIDVEGPGIAELLFNTIQAADIDTRPELYKHIVLSGGSTMYPGLPSRLEKEIKQLyler 321
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217328134 603 -------APSMMKIRIIAPPKRKYSVWVGGSILASLSTFQ-QMWISKQEYDESGPSIV 652
Cdd:cd10220   322 vlkgdteRLSKFKIRIEDPPRRKHMVFLGGAVLADIMKDKdEFWITRQEYEEQGVRVL 379
PTZ00466 PTZ00466
actin-like protein; Provisional
290-657 4.19e-162

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 470.19  E-value: 4.19e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 290 LVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEKIWH 369
Cdd:PTZ00466   15 IIIDNGTGYIKAGFAGEDVPNLVFPSYVGRPKYKRVMAGAVEGNIFVGNKAEEYRGLLKVTYPINHGIIENWNDMENIWI 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 370 HTfYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVPSLYTSGRTTGIVMDSGDGVTHTVPIYE 449
Cdd:PTZ00466   95 HV-YNSMKINSEEHPVLLTEAPLNPQKNKEKIAEVFFETFNVPALFISIQAILSLYSCGKTNGTVLDCGDGVCHCVSIYE 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 450 GNALPHATLRLDLAGRELPDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMATAASSSSlEKSYELPDGQV 529
Cdd:PTZ00466  174 GYSITNTITRTDVAGRDITTYLGYLLRKNGHLFNTSAEMEVVKNMKENCCYVSFNMNKEKNSSEKALT-TLPYILPDGSQ 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 530 ITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMMKI 609
Cdd:PTZ00466  253 ILIGSERYRAPEVLFNPSILGLEYLGLSELIVTSITRADMDLRRTLYSHIVLSGGTTMFHGFGDRLLNEIRKFAPKDITI 332
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 2217328134 610 RIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF 657
Cdd:PTZ00466  333 RISAPPERKFSTFIGGSILASLATFKKIWISKQEFDEYGSVILHRKTF 380
PTZ00452 PTZ00452
actin; Provisional
283-657 4.94e-162

actin; Provisional


Pssm-ID: 185631  Cd Length: 375  Bit Score: 470.01  E-value: 4.94e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 283 MDDDTAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWD 362
Cdd:PTZ00452    1 MQAQYPAVVIDNGSGYCKIGIAGDDAPTSCFPAIVGRSKQNDGIFSTFNKEYYVGEEAQAKRGVLAIKEPIQNGIINSWD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 363 DMEKIWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVPSLYTSGRTTGIVMDSGDGVT 442
Cdd:PTZ00452   81 DIEIIWHHAFYNELCMSPEDQPVFMTDAPMNSKFNRERMTQIMFETFNTPCLYISNEAVLSLYTSGKTIGLVVDSGEGVT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 443 HTVPIYEGNALPHATLRLDLAGRELPDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSY 522
Cdd:PTZ00452  161 HCVPVFEGHQIPQAITKINLAGRLCTDYLTQILQELGYSLTEPHQRIIVKNIKERLCYTALDPQDEKRIYKESNSQDSPY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 523 ELPDGQVITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAAL 602
Cdd:PTZ00452  241 KLPDGNILTIKSQKFRCSEILFQPKLIGLEVAGIHHLAYSSIKKCDLDLRQELCRNIVLSGGTTLFPGIANRLSNELTNL 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217328134 603 APSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF 657
Cdd:PTZ00452  321 VPSQLKIQVAAPPDRRFSAWIGGSIQCTLSTQQPQWIKRQEYDEQGPSIVHRKCF 375
ASKHA_NBD_ACTL7 cd10214
nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ...
287-656 1.03e-159

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: 463.43  E-value: 1.03e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 287 TAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEK 366
Cdd:cd10214     3 TKAVIIDLGTGYCKAGFAGQPRPSYVISSTVGKPPQESAKTGDNRKETFVGKELANVEPPLKLVNPLRHGIVVDWDCVQD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 367 IWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVPSLYTSGRTTGIVMDSGDGVTHTVP 446
Cdd:cd10214    83 IWEYIFEKEMKILPEEHAVLVSDPPLSPTTNREKYAELMFETFSIPAMHIAYQSRLSLYSYGRTSGLVVESGHGVSYVVP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 447 IYEGNALPHATLRLDLAGRELPDYLMKILTERGYRFTTmAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEksYELPD 526
Cdd:cd10214   163 IHEGYNLPHITGRADYAGSDLTAYLMKLLNEAGNKFTD-DQLHIVEDIKKKCCYVALDFEEEMGLPPQEYTVD--YELPD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 527 GQVITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSM 606
Cdd:cd10214   240 GHLITIGKERFRCPEMLFNPSLIGSKQPGLHTLTMNSLNKCDANLKKDLAKNILLCGGSTMFDGFPDRFQKELSKLCPND 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217328134 607 MKIrIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKC 656
Cdd:cd10214   320 NPI-VAASPERKYSVWTGGSILASLKSFQQLWVRRREYEERGPFVIYRKC 368
ASKHA_NBD_actin-like cd10169
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ...
290-648 3.28e-146

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: 424.60  E-value: 3.28e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 290 LVIDNGSGMCKAGFAGDDAPRAVFPsivgrprqqgmmggmhqkesyvgkeaqskrgiltlkypmehgiitnWDDMEKIWH 369
Cdd:cd10169     1 IVIDNGSGTIKAGFAGEDAPRLIFP----------------------------------------------WDDMEKIWE 34
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 370 HTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVPSLYTSGRTTGIVMDSGDGVTHTVPIYE 449
Cdd:cd10169    35 HVFYNLLRVDPEEHPVLLTEPPLNPKANREKLAEILFETFNVPSLYIANQAVLSLYASGRTTGLVVDSGEGVTHIVPVYE 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 450 GNALPHATLRLDLAGRELPDYLMKILTERGYRFTTMAEREIVRDIKEKLcyvaldfeqemataassssleksyelpdgqv 529
Cdd:cd10169   115 GYVLPHAVRRLDIGGRDLTDYLAKLLREKGYSFSTSAEREIVRDIKEKL------------------------------- 163
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 530 itignerfrcpealfqpcflgmesCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMMKI 609
Cdd:cd10169   164 ------------------------CGLHELIYDSIMKCDIDLRKELYSNIVLSGGTTLFPGFAERLQKELSKLAPSSVKV 219
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 2217328134 610 RIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESG 648
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 ...
285-648 1.32e-138

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: 411.19  E-value: 1.32e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 285 DDTAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRP--RQQGMMGGMHQKES----YVGKEA-QSKRGILTLKYPMEHGI 357
Cdd:cd13395     2 DEVGALVLDIGSYSTRAGYAGEDTPKAVFPSVVGVVtdDDDAEDYVGGSGEKkrkyYIGTNSiGVPRPNMEVISPLKDGL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 358 ITNWDDMEKIWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVPSLYTSGRTTGIVMDS 437
Cdd:cd13395    82 IEDWDAFEKLWDHALKNRLRVDPSEHPLLLTEPSWNTRANREKLTELMFEKYNVPAFFLAKNAVLSAFANGRSTALVVDS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 438 GDGVTHTVPIYEGNALPHATLRLDLAGRELPDYLMKILTERG------YRF---------------------TT-----M 485
Cdd:cd13395   162 GATSTSVVPVHDGYVLQKAIVRSPLGGDFLTDQLLKLLESKNieiiprYMIkskepveggapakytkkdlpnTTssyhrY 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 486 AEREIVRDIKEKLCYVALDFEQEmatAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPCFL---------GMESCGI 556
Cdd:cd13395   242 MVRRVLQDFKESVCQVSDSPFDE---SEAASIPTVSYELPDGYNIEFGAERFKIPELLFDPSLVkgipappseGNELLGL 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 557 HETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMMKIRIIAPPK---RKYSVWVGGSILASLST 633
Cdd:cd13395   319 PQLVYTSIGSCDVDIRPELYGNVVLTGGNSLLPGFTDRLNRELSEKAPGSLKLKILASGNtveRRFSSWIGGSILASLGS 398
                         410
                  ....*....|....*
gi 2217328134 634 FQQMWISKQEYDESG 648
Cdd:cd13395   399 FQQMWISKQEYEEHG 413
COG5277 COG5277
Actin-related protein [Cytoskeleton];
289-647 1.33e-126

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 381.06  E-value: 1.33e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 289 VLVIDNGSGMCKAG-FAGDDAP-----RAVFPSIVGRPRQQGMMGGMhQKESYVGKEAQS-----KRGILTLKYPMEHGI 357
Cdd:COG5277    10 VIGIDFGTSYVKYGpIALEEKPrviqtRGLFLRIVGESKLLGPMEGL-SRGLVVGDEVSKylssvRDAIRNLKYPLRDGI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 358 IT-----NWDDMEKIWHHTFYNELRVAPEEHP--ILLTEAPLNPKANREKMTQIMFETF---NTPAMYVAIQAVPSLYTS 427
Cdd:COG5277    89 VRrddedAWRVLKELLRYTFAQFLVVDPEFHGflVVVALSALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPLAVAIAE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 428 GRTTGIVMDSGDGVTHTVPIYEGnALPHATLRLDLAGRELPDYLMKILTERGYRFTTMAEReIVRDIKEKLCYVALDFEQ 507
Cdd:COG5277   169 KAVTCVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSDTAREEY-VVRVVKEALGLVPRDLAK 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 508 EM-ATAASSSSLEKSYELPDGQV-ITIGN---ERFRCPEALFQPCFLGMESC----------------------GIHETT 560
Cdd:COG5277   247 AIqKAASNPDSFEAKVRLPNPTVeIELGNyawERFLIGEILFNPNHEGFESYiqqgrlriedavigdvvlygemGLAEAI 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 561 FNSIMKSDVDIRKDLYTNTVLSGGTTMY---PGMA-------HRMQKEIAALAPSmMKIRIIAPPKRKYSVWVGGSILAS 630
Cdd:COG5277   327 INSIMKCDVEIQDELYSNIILSGGAFNWsvpPGLEdvavdsvTRVQIELSELAPE-LKVNVRLVSDPQYSVWKGAIIYGY 405
                         410
                  ....*....|....*....
gi 2217328134 631 LSTFQQMW--ISKQEYDES 647
Cdd:COG5277   406 ALPFSVKWswITKEGWYFL 424
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
289-652 6.06e-108

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: 332.23  E-value: 6.06e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 289 VLVIDNGSGMCKAGFAGDDAPRAVFPSIVGrPRQQGMMGGMHQKES--------YVGKEAQSKRGILTLKYPMEHGIITN 360
Cdd:cd10221     1 AVVIDNGTGYTKMGYAGNTEPQFIIPTVIA-IKESAKVGDGQRRSKkgiedldfYIGDEALANSPTYALKYPIRHGIVED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 361 WDDMEKIWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVPSLYTSGRT--------TG 432
Cdd:cd10221    80 WDLMERFWEQCIFKYLRCEPEDHYFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQAVLALAASWTSrkvgertlTG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 433 IVMDSGDGVTHTVPIYEGNALPHATLRLDLAGRELPDYLMKILTERGyrFTTMAE--REIVRDIKEKLCYVALDFEQEMA 510
Cdd:cd10221   160 TVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLRERE--EGIPPEdsLEVAKRIKERYCYVCPDIVKEFA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 511 TAASS-SSLEKSYELPD---GQ--VITIGNERFRCPEALFQPCFLGMESC-GIHETTFNSIMKSDVDIRKDLYTNTVLSG 583
Cdd:cd10221   238 KYDSDpAKYIKQYTGINsvtGKpyTVDVGYERFLAPEIFFNPEIASSDFTtPLPEVVDQVIQSCPIDTRRGLYKNIVLSG 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 584 GTTMYPGMAHRMQKEI----------------AALAPSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDES 647
Cdd:cd10221   318 GSTMFKDFGRRLQRDVkrivdarlkaseelsgGKLKPKPIDVNVISHPMQRYAVWFGGSMLASTPEFYTVCHTKAEYEEY 397

                  ....*
gi 2217328134 648 GPSIV 652
Cdd:cd10221   398 GPSIC 402
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
289-654 1.30e-107

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 331.70  E-value: 1.30e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 289 VLVIDNGSGMCKAGFAGDDAPRAVFPSIVG-RPRQQGMMG--GMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDME 365
Cdd:PTZ00280    6 VVVIDNGTGYTKMGYAGNTEPTYIIPTLIAdNSKQSRRRSkkGFEDLDFYIGDEALAASKSYTLTYPMKHGIVEDWDLME 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 366 KIWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVPSLYTS----------GRTTGIVM 435
Cdd:PTZ00280   86 KFWEQCIFKYLRCEPEEHYFILTEPPMNPPENREYTAEIMFETFNVKGLYIAVQAVLALRASwtskkakelgGTLTGTVI 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 436 DSGDGVTHTVPIYEGNALPHATLRLDLAGRELPDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMAT---- 511
Cdd:PTZ00280  166 DSGDGVTHVIPVVDGYVIGSSIKHIPLAGRDITNFIQQMLRERGEPIPAEDILLLAQRIKEKYCYVAPDIAKEFEKydsd 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 512 --------AASSSSLEKSYElpdgqvITIGNERFRCPEALFQPCFLGME-SCGIHETTFNSIMKSDVDIRKDLYTNTVLS 582
Cdd:PTZ00280  246 pknhfkkyTAVNSVTKKPYT------VDVGYERFLGPEMFFHPEIFSSEwTTPLPEVVDDAIQSCPIDCRRPLYKNIVLS 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 583 GGTTMYPGMAHRMQKEI----------------AALAPSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDE 646
Cdd:PTZ00280  320 GGSTMFKGFDKRLQRDVrkrvdrrlkkaeelsgGKLKPIPIDVNVVSHPRQRYAVWYGGSMLASSPEFEKVCHTKAEYDE 399

                  ....*...
gi 2217328134 647 SGPSIVHR 654
Cdd:PTZ00280  400 YGPSICRY 407
ASKHA_NBD_Arp6 cd10210
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ...
289-648 4.02e-92

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: 290.61  E-value: 4.02e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 289 VLVIDNGSGMCKAGFAGDDAPRaVFPSIVGRPRqqgmmggmHQKESYVGKEAQSK---RGILTLKYPMEHGIITNWDDME 365
Cdd:cd10210     1 TLVLDNGAYTIKAGFASDDPPR-VIPNCIAKPK--------SERRRLFGDDQLDEckdLSGLFYRRPFERGYLVNWDLQR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 366 KIWHHTFYNE-LRVAPEEHPILLTEAPLNPKANREKMTQIMFETF--------NTPAM---YVAIQAVPSLYTSGRTTgI 433
Cdd:cd10210    72 QIWDHLFGKLlLNVDPSDTALVLTEPPFNPPSIQEAMDEIVFEEYgfqslyrtTAAALsafAYLADSEQSSSSSSQCC-L 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 434 VMDSGDGVTHTVPIYEGNALPHATLRLDLAGRELPDYLMKILTergYR-FTTMAEREIVRDIKEKLCYVALDFEQEMATA 512
Cdd:cd10210   151 VVDSGFSFTHIVPFFDGKPVKRAVRRIDVGGKLLTNYLKEIIS---YRqLNVMDETYLVNQIKEDLCFVSTDFYEDLEIA 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 513 AS---SSSLEKSYELPDG-----------------------QVITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMK 566
Cdd:cd10210   228 KKkgkENTIRRDYVLPDYttskrgyvrdpeepnrgklkedeQVLRLNNERFTVPELLFHPSDIGIQQAGIAEAIVQSINA 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 567 SDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDE 646
Cdd:cd10210   308 CPEELQPLLYANIVLTGGNALFPGFRERLEAELRSLAPDDYDVNVTLPEDPITYAWEGGSLLAQSPEFEELAVTRAEYEE 387

                  ..
gi 2217328134 647 SG 648
Cdd:cd10210   388 HG 389
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
290-653 1.60e-77

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: 251.15  E-value: 1.60e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 290 LVIDNGSGMCKAGFAGDDApravFPSIVGRPRQQGMM-GGMHQKESYVGKEAQskrgiltlkyPMEHGIITNWDDMEKIW 368
Cdd:cd10209     1 VVIDAGSRLLKAGYAYPDR----EPSVVEPTRVTPAVeDGEESDTVVEGNTVS----------PIRRGRIEDWDALEALL 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 369 HHTFYNELR-VAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVPSLYTSGRTTGIVMDSGDGVTHTVPI 447
Cdd:cd10209    67 RYVFYTGLGwEEGNEGQVLIAEPLLTSKAERERLTQLMFETFNVSGLYASEQAVLSLYAVGRISGCVVDVGHGKIDIAPV 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 448 YEGNALPHATLRLDLAGRELPDYLMKILTERGyRFTTmAEREIVRDIKEKLCYVALDFEQEMATAASSSslEKSYELPDG 527
Cdd:cd10209   147 WEGAIQHNAVRRFEIGGRDLTELLAAELGKSN-PKVK-LDRSIVERLKEAVAWSADDEEAYEKKVLTCS--PETYTLPDG 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 528 QVITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMM 607
Cdd:cd10209   223 RVISVGKERYCVGEALFRPSILGIEEYGIVEQLVRAVSTSPSENRRQLLENIVLCGGTSSVPGLEARLQKEIRLLSSPSS 302
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217328134 608 KIRIIAPPK------RKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVH 653
Cdd:cd10209   303 RPALVKPPEympentLRYSAWIGGAILAKVVFPQNQHVTKADYDETGPSVVH 354
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
289-649 5.40e-66

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: 220.52  E-value: 5.40e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 289 VLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMHQKESYVGKEAQSKrgiLTLKYPMEHGIITNWDDMEKIW 368
Cdd:cd10211     1 PIVIDNGSYQCRAGWAGDKEPRLVFRNLVAKPRDRKKGITVTLVGNDILNDEAVR---SHLRSPFDRNVVTNFDLQEQIL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 369 HHTFyNELRVAPE---EHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVPSLY----TSGRTTGIVMDSGDGV 441
Cdd:cd10211    78 DYIF-SHLGINSEgsvDHPIVLTEALCNPNYSRQLMSELLFECYGVPSVAYGIDSLFSYYhnqpQGDPSDGLVISSGYST 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 442 THTVPIYEGNALPHATLRLDLAGRELPDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKS 521
Cdd:cd10211   157 THVIPVLNGRLDLSQCKRINLGGFHATDYLQRLLQLKYPTHPSAITLSRAEELVHEHCYVAEDYDEELKKWEDPEYYEEN 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 522 yelpdgqvitigNERFRCPealFqpcflgmescGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAA 601
Cdd:cd10211   237 ------------VRKIQLP---F----------GLVETIEFVLKRYPAEQQDRLVQNVFLTGGNALFPGLKERLEKELRA 291
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217328134 602 LAPSMMKIRII--APPkrKYSVWVGGSILASLSTFQQMWISKQEYDESGP 649
Cdd:cd10211   292 IRPFGSPFNVVraKDP--VLDAWRGAAKWALDSTFEKVWITKQEYEEKGG 339
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
289-655 8.74e-49

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: 174.42  E-value: 8.74e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 289 VLVIDNGSGMCKAGFAGDDA---PRAVFPSIVGRPrqqgmmggmhqkesyvgkeaqskrgiltlkYPMEHGIITNWDDME 365
Cdd:cd10208     2 ILVIDPGSQTTRAGLGLGELltpPTIEIPTRVEII------------------------------WPIQDGRVVDWDALE 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 366 KIWHHTFYNEL--RVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVPSLYTSGRTTGIVMDSGDGVTH 443
Cdd:cd10208    52 ALWRHILFSLLsiPRPTNNSPVLLSVPPSWSKSDLELLTQLFFERLNVPAFAILEAPLAALYAAGATSGIVVDIGHEKTD 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 444 TVPIYEGNALPHATLRLDLAGRELPDYLMKILTER--GYRFTTMAEREIVRDIKEKLcyvaldFEQEMATAASSSSleks 521
Cdd:cd10208   132 ITPIVDSQVVPHALVSIPIGGQDCTAHLAQLLKSDepELKSQAESGEEATLDLAEAL------KKSPICEVLSDGA---- 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 522 yELPDGQVITIGNERFRCPEALFQP----CFLGMESCGIHETTFNSimkSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQK 597
Cdd:cd10208   202 -DLASGTEITVGKERFRACEPLFKPsslrVDLLIAAIAGALVLNAS---DEPDKRPALWENIIIVGGGSRIRGLKEALLS 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 598 EIAA--LAPSM----MKIRIIAPPK--------RK----YSVWVGGSILASLsTF----QQMWISKQEYDESGPSIVHRK 655
Cdd:cd10208   278 ELQQfhLISETsaspQQPRIIRLAKipdyfpewKKsgyeEAAFLGASIVAKL-VFndpsSKHYISKVDYNEKGPAAIHTK 356
ASKHA_NBD_Arp10 cd10207
nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins; ...
291-648 1.88e-43

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: 160.50  E-value: 1.88e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 291 VIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQgmmggmhqKESYVGKeaqsKRGILTLKypmehgiitnWDDM-EKIWH 369
Cdd:cd10207     2 VLDIGSAYTKCGFAGESAPRCIIPSEVKLPGGK--------KVIRVVD----QRSGNEEE----------LYEAlKEFLH 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 370 HTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVPSLYTSGRTTGIVMDSGDGVTHTVPIYE 449
Cdd:cd10207    60 ELYFKHLLVNPKDRRVVVVESVLCPTPFRETLAKVLFKHFEVPSVLFAPSHLLSLLTLGIRTALVVDCGYRETRVLPVYE 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 450 GNALPHATLRLDLAGRELPDYLMKILTERGYRFTTMAER------------EIVRDIKEKLCYVA-LDFEQEMATAASSS 516
Cdd:cd10207   140 GVPLLSAWQSTPLGGKALHKRLKKLLLEHATVVTGDNKGqllssvdsllseEVLEDIKVRACFVTsLERGKTLQSATEEG 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 517 SLEKS-------YELPDGQVITIGNERFRCPEALFqpcFLGMESC-GIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMY 588
Cdd:cd10207   220 STEEPsppppvdYPLDGEKILIVPGSIRESAEELL---FEGDNEEkSLPTLILDSLLKCPIDVRKQLAENIVVIGGTSML 296
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217328134 589 PGMAHRMQKEIAAL--------APSMMKIRIIAPP---KRKYSVWVGGSILASLSTFQQMWISKQEYDESG 648
Cdd:cd10207   297 PGFKHRLLEELRALlrkpkyfeELAPKTFRFHTPPsvfKPNYLAWLGGSIFGALESILGRSLSREAYLQTG 367
ASKHA_NBD_AtArp8-like cd13396
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and ...
371-648 9.78e-42

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: 154.24  E-value: 9.78e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 371 TFYNELRVAPEEHPILLTEaPL-------NPKANREKMTQIMFETF---NTPAMYVAIQAVPSLYTSGRTTGIVMDSGDG 440
Cdd:cd13396    47 TIMTRMQVKPSRQPVVVSL-PLchsddteSAAASRRQLRGTIFNVLfdmNVPAVCAVDQAVLALYAANRTSGIVVNIGFR 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 441 VTHTVPIYEGNALPH-ATLRLDLAGRELPDYLMKILTERGYRFTTMAereIVRDIKEKLCYVALDFEQEMAtaassSSLE 519
Cdd:cd13396   126 VTTIVPVYRGRVMHDiGVEVVGQGALRLTGFLKELMQQNGIRFPSLY---TVRTIKEKLCYVAEDYEAELA-----KDTQ 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 520 KSYELPDGQVITIGNERFRCPEALFQPCFLGMESCGIH-------ETTFNSIMKSDvdirKDLYTNTVLSGGTTMYPGMA 592
Cdd:cd13396   198 ASCEVAGEGWFTLSNERFKTGEILFQPGLGGMRAMGLHqavalcmDHCALVHSQGD----DGWFKTIVLSGGSACLPGLS 273
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217328134 593 HRMQKEIAALAPSMMK--IRIIAPPKRKYSVWVGGSILASLSTFQQMW-ISKQEYDESG 648
Cdd:cd13396   274 ERLERELRKLLPKSLSegIRIIPPPLGPDSAWQGAKLISNLSNFPDGWcITKKQFRNKP 332
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
585-656 1.76e-34

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: 127.40  E-value: 1.76e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217328134 585 TTMYPGMAHRMQKEIAALAPSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKC 656
Cdd:NF040575   61 RVNESGFYEKLKKSITEKAPKGALIGMTLDPKPESAAWRGAAMYAASEGFVEMAITKQEYDESGPSIVHRKC 132
ASKHA_NBD_Arp8-like cd10206
nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The ...
330-651 3.20e-22

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: 100.01  E-value: 3.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 330 HQKESYVGKEAQ--SKRGILTLKYPMEHGIItNW-----------DDMEKIWHHTFYNELRVAPEEHP----ILLTEAPL 392
Cdd:cd10206   118 DYPDFLVGEEALrlPPSEEYNLHWPIRRGRL-NVhsdggsltavlDDLEDIWSHALEEKLEIPRKDLKnyraVLVIPDLF 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 393 NpKANREKMTQIMFETFNTPAMYVAIQAVPSLYTSGRTTGIVMDSGDGVTHTVPIYEGNALPHATLRLDLAGRELPDYLM 472
Cdd:cd10206   197 D-RRHVKELVDLLLRRLGFSSVFVHQESVCATFGAGLSSACVVDIGAQKTSVACVEDGLSIPNSRIRLPYGGDDITRCFL 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 473 KILTERG--YRFTTMAER---EIVRDIKEKLCYVALDFeqemataassssleksyelpDGQVITIGNERFRC-PEALFQp 546
Cdd:cd10206   276 WLLRRSGfpYRECNLNSPldfLLLERLKETYCTLDQDD--------------------IGVQLHEFYVREPGqPTLKYQ- 334
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 547 cflgMESCGIHETTFNSI-MKSDVDIRKDLYTNTVLSGGTTMYPGMA----HRMQKEIAALAPSMMKIRIIAPPKRK--- 618
Cdd:cd10206   335 ----FKLLPLDEAIVQSIlSCASDELKRKMYSSILLVGGGAKIPGLAealeDRLLIKIPSLFEAVETVEVLPPPKDMdps 410
                         330       340       350
                  ....*....|....*....|....*....|...
gi 2217328134 619 YSVWVGGSILASLSTFQQMWISKQEYDESGPSI 651
Cdd:cd10206   411 LLAWKGGAVLACLDSAQELWITRKEWQRLGVRA 443
ASKHA_NBD_ScArp7-like cd10212
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and ...
290-645 1.04e-19

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


Pssm-ID: 466818 [Multi-domain]  Cd Length: 424  Bit Score: 92.09  E-value: 1.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 290 LVIDNGSGMCKAGFAGDDAPRAVFPS-IVGRPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEKIW 368
Cdd:cd10212     6 VVIHNGSHRTVAGFSNVELPQCIIPSsYIKRTDEGGEAEFIFGTYNMIDAAAEKRNGDEVYTLVDSQGLPYNWDALEMQW 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 369 HHTFYNELRVAPEEHPILLTEAPLNPKANR---EKMTQIMFETFNTPAMYVAIQAVPSLYTSGRTTGIVMDSGDGVTHTV 445
Cdd:cd10212    86 RYLYDTQLKVSPEELPLVITMPATNGKPDMailERYYELAFDKLNVPVFQIVIEPLAIALSMGKSSAFVIDIGASGCNVT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 446 PIYEGNALPHATLRLDLAGR----ELPDYLMKILTERG----------------YRFTTMAER--------------EIV 491
Cdd:cd10212   166 PIIDGIVVKNAVVRSKFGGDfldfQVHERLAPLIKEENdmenmadeqkrstdvwYEASTWIQQfkstmlqvsekdlfELE 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 492 RDIKEKLCYVALDFEQ--EMATAASSSSLEKSyelPDGQVITIGN---------------ERFRCPEALFQPCFLGMESC 554
Cdd:cd10212   246 RYYKEQADIYAKQQEQlkQMDQQLQYTALTGS---PNNPLVQKKNflfkplnktltldlkECYQFAEYLFKPQLISDKFS 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 555 ---GIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSmMKIRIIAPP---KRKYSVWVGGSIL 628
Cdd:cd10212   323 pedGLGPLMAKSVKKAPEQVYSLLLTNVIITGSTSLIEGMEQRIIKELSIRFPQ-YKLTTFANQvmmDRKIQGWLGALTM 401
                         410
                  ....*....|....*...
gi 2217328134 629 ASLSTFQ-QMWISKQEYD 645
Cdd:cd10212   402 ANLPSWSlGKWYSKEDYE 419
CCDC144C pfam14915
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ...
230-283 7.86e-18

CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.


Pssm-ID: 464371 [Multi-domain]  Cd Length: 304  Bit Score: 84.65  E-value: 7.86e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217328134 230 NSTLREEIAMLRLELDTMKHQSQLREKKYLEDIESVKKKNDNLLKALQLNELTM 283
Cdd:pfam14915   1 NCMLQDEIAMLRLEIDTIKNQNQEKEKKYLEDIEILKEKNDDLQKTLKLNEETL 54
ASKHA_NBD_MamK cd24009
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ...
297-604 3.07e-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: 3.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 297 GMCKAGFAGDDAPRAVFPSIVGRPRqqGMMGGMHQKESYV-GKEAQSKRGILTLKYPMEHGIITNWDDmekiwhhtfyNE 375
Cdd:cd24009     9 GTSRSAVVTSRGKRFSFRSVVGYPK--DIIARKLLGKEVLfGDEALENRLALDLRRPLEDGVIKEGDD----------RD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 376 LRVAPE--EHPILLTEAPLNPK-------------ANREKMTQIMFETFNTPAMYVAIQAVPslYTSGRTTG-IVMDSGD 439
Cdd:cd24009    77 LEAAREllQHLIELALPGPDDEiyavigvparasaENKQALLEIARELVDGVMVVSEPFAVA--YGLDRLDNsLIVDIGA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 440 GVThTVPIYEGnALPHAT--LRLDLAGRELPDYLMKILTER--GYRFTtmaeREIVRDIKEKLCYValdfeqemataaSS 515
Cdd:cd24009   155 GTT-DLCRMKG-TIPTEEdqITLPKAGDYIDEELVDLIKERypEVQLT----LNMARRWKEKYGFV------------GD 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328134 516 SSLEKSYELP-DGQVIT--IGNE-RFRCpEALFQPcflgmescgIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGM 591
Cdd:cd24009   217 ASEPVKVELPvDGKPVTydITEElRIAC-ESLVPD---------IVEGIKKLIASFDPEFQEELRNNIVLAGGGSRIRGL 286
                         330
                  ....*....|...
gi 2217328134 592 AHRMQKEIAALAP 604
Cdd:cd24009   287 DTYIEKALKEYGG 299
 
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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