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Conserved domains on  [gi|393693628|gb|AFN12060|]
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actin, partial [Alternaria passiflorae]

Protein Classification

acetate and sugar kinases/Hsc70/actin family protein( domain architecture ID 99298)

acetate and sugar kinases/Hsc70/actin (ASKHA) family protein catalyzes phosphoryl transfer from ATP to their respective substrates

CATH:  3.30.420.40
Gene Ontology:  GO:0000166
PubMed:  8800467|7781919
SCOP:  3000092

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ASKHA_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
1-269 0e+00

ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.


The actual alignment was detected with superfamily member cd10224:

Pssm-ID: 483947  Cd Length: 365  Bit Score: 655.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628   1 FPSIVGRPRHHGIMIGMGQKDSYVGDEAQSKRGILTLRYPIEHGVVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPI 80
Cdd:cd10224   26 FPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  81 NPKSNREKMTQIVFETFNAPAFYVSIQAVLSLYASGRTTGIVLDSGDGVTHVVPIYEGFALPHAISRVDMAGRDLTDYLM 160
Cdd:cd10224  106 NPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLM 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628 161 KILAERGYTFSTTAEREIVRDIKEKLCYVALDFEQEIQTASQSSSLEKSYELPDGQVITIGNERFRAPEALFQPSVLGLE 240
Cdd:cd10224  186 KILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGME 265
                        250       260
                 ....*....|....*....|....*....
gi 393693628 241 SGGIHVTTFNSIMKCDVDVRKDLYGNIVM 269
Cdd:cd10224  266 AAGIHETTYNSIMKCDVDIRKDLYANIVL 294
 
Name Accession Description Interval E-value
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
1-269 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: 655.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628   1 FPSIVGRPRHHGIMIGMGQKDSYVGDEAQSKRGILTLRYPIEHGVVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPI 80
Cdd:cd10224   26 FPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  81 NPKSNREKMTQIVFETFNAPAFYVSIQAVLSLYASGRTTGIVLDSGDGVTHVVPIYEGFALPHAISRVDMAGRDLTDYLM 160
Cdd:cd10224  106 NPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLM 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628 161 KILAERGYTFSTTAEREIVRDIKEKLCYVALDFEQEIQTASQSSSLEKSYELPDGQVITIGNERFRAPEALFQPSVLGLE 240
Cdd:cd10224  186 KILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGME 265
                        250       260
                 ....*....|....*....|....*....
gi 393693628 241 SGGIHVTTFNSIMKCDVDVRKDLYGNIVM 269
Cdd:cd10224  266 AAGIHETTYNSIMKCDVDIRKDLYANIVL 294
PTZ00281 PTZ00281
actin; Provisional
1-269 0e+00

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 520.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628   1 FPSIVGRPRHHGIMIGMGQKDSYVGDEAQSKRGILTLRYPIEHGVVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPI 80
Cdd:PTZ00281  32 FPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  81 NPKSNREKMTQIVFETFNAPAFYVSIQAVLSLYASGRTTGIVLDSGDGVTHVVPIYEGFALPHAISRVDMAGRDLTDYLM 160
Cdd:PTZ00281 112 NPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYMM 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628 161 KILAERGYTFSTTAEREIVRDIKEKLCYVALDFEQEIQTASQSSSLEKSYELPDGQVITIGNERFRAPEALFQPSVLGLE 240
Cdd:PTZ00281 192 KILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEMQTAASSSALEKSYELPDGQVITIGNERFRCPEALFQPSFLGME 271
                        250       260
                 ....*....|....*....|....*....
gi 393693628 241 SGGIHVTTFNSIMKCDVDVRKDLYGNIVM 269
Cdd:PTZ00281 272 SAGIHETTYNSIMKCDVDIRKDLYGNVVL 300
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
1-268 5.16e-160

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 449.02  E-value: 5.16e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628     1 FPSIVGRPRHHGIMIGmGQKDSYVGDEAQSKRGILTLRYPIEHGVVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPI 80
Cdd:smart00268  27 FPSIVGRPKDGKGMVG-DAKDIFVGDEAQEKRGGLELKYPIENGIVENWDDMEKIWDYTFFNELRVEPEEHPVLLTEPPM 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628    81 NPKSNREKMTQIVFETFNAPAFYVSIQAVLSLYASGRTTGIVLDSGDGVTHVVPIYEGFALPHAISRVDMAGRDLTDYLM 160
Cdd:smart00268 106 NPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVPVVDGYVLPHAIKRIDIAGRDITDYLK 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628   161 KILAERGYTFSTTAEREIVRDIKEKLCYVALDFEQEIQTA---SQSSSLEKSYELPDGQVITIGNERFRAPEALFQPSVL 237
Cdd:smart00268 186 ELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLAresSESSKLEKTYELPDGNTIKVGNERFRIPEILFSPELI 265
                          250       260       270
                   ....*....|....*....|....*....|.
gi 393693628   238 GLESGGIHVTTFNSIMKCDVDVRKDLYGNIV 268
Cdd:smart00268 266 GLEQKGIHELVYESIQKCDIDVRKDLYENIV 296
Actin pfam00022
Actin;
1-268 5.51e-126

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 363.93  E-value: 5.51e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628    1 FPSIVGRPRHHGIMigMGQKDsYVGDEAQSKRGILTLRYPIEHGVVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPI 80
Cdd:pfam00022  27 IPSCVGKPRGTKVE--AANKY-YVGDEALTYRPGMEVRSPVEDGIVVDWDAMEEIWEHVLKEELQVDPEEHPLLLTEPPW 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628   81 NPKSNREKMTQIVFETFNAPAFYVSIQAVLSLYASGRTTGIVLDSGDGVTHVVPIYEGFALPHAISRVDMAGRDLTDYLM 160
Cdd:pfam00022 104 NPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVPVHDGYVLQKAIRRSDLGGDFLTDYLR 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  161 KILAER------------------------------GYTFSTTAEREIVRDIKEKLCYVALDFEQEIQTAsqSSSLEKSY 210
Cdd:pfam00022 184 ELLRSRnieitprylikskkpgdpapavtkrelpdtTYSYKTYQERRVLEEIKESVCYVSDDPFGDETTS--SSIPTRVY 261
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 393693628  211 ELPDGQVITIGNERFRAPEALFQPSVLGLESG--------GIHVTTFNSIMKCDVDVRKDLYGNIV 268
Cdd:pfam00022 262 ELPDGSTIILGAERFRVPEILFNPSLIGSESElpppqtavGIPELIVDAINACDVDLRPSLLANIV 327
COG5277 COG5277
Actin-related protein [Cytoskeleton];
1-269 3.40e-97

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 291.31  E-value: 3.40e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628   1 FPSIVGRPRHHGIMIGMGqKDSYVGDEAQS-----KRGILTLRYPIEHGVVT-----NWDDMEKIWHHTFYNELRVAPEE 70
Cdd:COG5277   40 FLRIVGESKLLGPMEGLS-RGLVVGDEVSKylssvRDAIRNLKYPLRDGIVRrddedAWRVLKELLRYTFAQFLVVDPEF 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  71 HP--VLLTEAPINPKSNREKMTQIVFETF---NAPAFYVSIQAVLSLYASGRTTGIVLDSGDGVTHVVPIYEGfALPHAI 145
Cdd:COG5277  119 HGflVVVALSALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPLAVAIAEKAVTCVVVEAGHGNSQVAPISRG-PIREGL 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628 146 SRVDMAGRDLTDYLMKILAERGYTFSTTAEReIVRDIKEKLCYVALDFEQEIQ-TASQSSSLEKSYELPDGQV-ITIGN- 222
Cdd:COG5277  198 VALNRGGAEANAITREILKDRGYSDTAREEY-VVRVVKEALGLVPRDLAKAIQkAASNPDSFEAKVRLPNPTVeIELGNy 276
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 393693628 223 --ERFRAPEALFQPSVLGLESG----------------------GIHVTTFNSIMKCDVDVRKDLYGNIVM 269
Cdd:COG5277  277 awERFLIGEILFNPNHEGFESYiqqgrlriedavigdvvlygemGLAEAIINSIMKCDVEIQDELYSNIIL 347
 
Name Accession Description Interval E-value
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
1-269 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: 655.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628   1 FPSIVGRPRHHGIMIGMGQKDSYVGDEAQSKRGILTLRYPIEHGVVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPI 80
Cdd:cd10224   26 FPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  81 NPKSNREKMTQIVFETFNAPAFYVSIQAVLSLYASGRTTGIVLDSGDGVTHVVPIYEGFALPHAISRVDMAGRDLTDYLM 160
Cdd:cd10224  106 NPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLM 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628 161 KILAERGYTFSTTAEREIVRDIKEKLCYVALDFEQEIQTASQSSSLEKSYELPDGQVITIGNERFRAPEALFQPSVLGLE 240
Cdd:cd10224  186 KILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGME 265
                        250       260
                 ....*....|....*....|....*....
gi 393693628 241 SGGIHVTTFNSIMKCDVDVRKDLYGNIVM 269
Cdd:cd10224  266 AAGIHETTYNSIMKCDVDIRKDLYANIVL 294
ASKHA_NBD_actin_Arp-T1-3 cd13397
nucleotide-binding domain (NBD) of actin, actin-related proteins T1-T3 (Arp-T1-3), and similar ...
1-269 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: 556.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628   1 FPSIVGRPRHHGIMIGMGQKDSYVGDEAQSKRGILTLRYPIEHGVVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPI 80
Cdd:cd13397   26 FPSVVGRPKYKAVMLGAGQKEVYVGDEAQEKRGVLTLSYPIEHGIVTNWDDMEKIWHHTFENELRVKPEEHPVLLTEAPL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  81 NPKSNREKMTQIVFETFNAPAFYVSIQAVLSLYASGRTTGIVLDSGDGVTHVVPIYEGFALPHAISRVDMAGRDLTDYLM 160
Cdd:cd13397  106 NPKQNREKMAEIMFETFGVPAFYVAIQAVLSLYSSGRTTGLVLDSGDGVTHTVPIYEGYALPHAVQRLDLAGRDLTEYLM 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628 161 KILAERGYTFSTTAEREIVRDIKEKLCYVALDFEQEIQTASQssSLEKSYELPDGQVITIGNERFRAPEALFQPSVLGLE 240
Cdd:cd13397  186 KLLKERGHSFTTTAEREIVRDIKEKLCYVALDYEEELKKKSE--ELEKEYTLPDGQVIKIGSERFRCPEALFRPSLIGRE 263
                        250       260
                 ....*....|....*....|....*....
gi 393693628 241 SGGIHVTTFNSIMKCDVDVRKDLYGNIVM 269
Cdd:cd13397  264 APGIHKLVYNSIMKCDIDIRKDLYSNIVL 292
PTZ00281 PTZ00281
actin; Provisional
1-269 0e+00

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 520.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628   1 FPSIVGRPRHHGIMIGMGQKDSYVGDEAQSKRGILTLRYPIEHGVVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPI 80
Cdd:PTZ00281  32 FPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  81 NPKSNREKMTQIVFETFNAPAFYVSIQAVLSLYASGRTTGIVLDSGDGVTHVVPIYEGFALPHAISRVDMAGRDLTDYLM 160
Cdd:PTZ00281 112 NPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYMM 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628 161 KILAERGYTFSTTAEREIVRDIKEKLCYVALDFEQEIQTASQSSSLEKSYELPDGQVITIGNERFRAPEALFQPSVLGLE 240
Cdd:PTZ00281 192 KILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEMQTAASSSALEKSYELPDGQVITIGNERFRCPEALFQPSFLGME 271
                        250       260
                 ....*....|....*....|....*....
gi 393693628 241 SGGIHVTTFNSIMKCDVDVRKDLYGNIVM 269
Cdd:PTZ00281 272 SAGIHETTYNSIMKCDVDIRKDLYGNVVL 300
PTZ00004 PTZ00004
actin-2; Provisional
1-269 4.80e-173

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 482.35  E-value: 4.80e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628   1 FPSIVGRPRHHGIMIGMGQKDSYVGDEAQSKRGILTLRYPIEHGVVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPI 80
Cdd:PTZ00004  32 FPSIVGRPKNPGIMVGMEEKDCYVGDEAQDKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  81 NPKSNREKMTQIVFETFNAPAFYVSIQAVLSLYASGRTTGIVLDSGDGVTHVVPIYEGFALPHAISRVDMAGRDLTDYLM 160
Cdd:PTZ00004 112 NPKANREKMTQIMFETHNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYSLPHAIHRLDVAGRDLTEYMM 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628 161 KILAERGYTFSTTAEREIVRDIKEKLCYVALDFEQEIQTASQSSSL-EKSYELPDGQVITIGNERFRAPEALFQPSVLGL 239
Cdd:PTZ00004 192 KILHERGTTFTTTAEKEIVRDIKEKLCYIALDFDEEMGNSAGSSDKyEESYELPDGTIITVGSERFRCPEALFQPSLIGK 271
                        250       260       270
                 ....*....|....*....|....*....|.
gi 393693628 240 ESG-GIHVTTFNSIMKCDVDVRKDLYGNIVM 269
Cdd:PTZ00004 272 EEPpGIHELTFQSINKCDIDIRKDLYGNIVL 302
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
1-269 1.47e-161

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: 452.77  E-value: 1.47e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628   1 FPSIVGRPRHHGIMIGMGQKDSYVGDEAQSKRGILTLRYPIEHGVVTNWDDMEKIWHHTFYNE-LRVAPEEHPVLLTEAP 79
Cdd:cd10216   27 FPSYVGRPKHVRVMAGALEGDVFVGPKAEEHRGLLKIRYPMEHGIVTDWNDMERIWQYVYSKLqLNTFSEEHPVLLTEAP 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  80 INPKSNREKMTQIVFETFNAPAFYVSIQAVLSLYASGRTTGIVLDSGDGVTHVVPIYEGFALPHAISRVDMAGRDLTDYL 159
Cdd:cd10216  107 LNPRKNREKAAEVFFETFNVPALFVSMQAVLSLYASGRTTGVVLDSGDGVTHAVPIYEGFALPHSIRRVDIAGRDVTEYL 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628 160 MKILAERGYTFSTTAEREIVRDIKEKLCYVALDFEQEIQTaSQSSSLEKSYELPDGQVITIGNERFRAPEALFQPSVLGL 239
Cdd:cd10216  187 QLLLRKSGYNFHTSAEFEIVREIKEKACYVALNPQKEEKL-EEEKTEKAQYTLPDGSTIEIGPERFRAPEILFNPELIGL 265
                        250       260       270
                 ....*....|....*....|....*....|
gi 393693628 240 ESGGIHVTTFNSIMKCDVDVRKDLYGNIVM 269
Cdd:cd10216  266 EYPGVHEVLVDSIQKSDLDLRKTLYSNIVL 295
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
1-268 5.16e-160

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 449.02  E-value: 5.16e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628     1 FPSIVGRPRHHGIMIGmGQKDSYVGDEAQSKRGILTLRYPIEHGVVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPI 80
Cdd:smart00268  27 FPSIVGRPKDGKGMVG-DAKDIFVGDEAQEKRGGLELKYPIENGIVENWDDMEKIWDYTFFNELRVEPEEHPVLLTEPPM 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628    81 NPKSNREKMTQIVFETFNAPAFYVSIQAVLSLYASGRTTGIVLDSGDGVTHVVPIYEGFALPHAISRVDMAGRDLTDYLM 160
Cdd:smart00268 106 NPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVPVVDGYVLPHAIKRIDIAGRDITDYLK 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628   161 KILAERGYTFSTTAEREIVRDIKEKLCYVALDFEQEIQTA---SQSSSLEKSYELPDGQVITIGNERFRAPEALFQPSVL 237
Cdd:smart00268 186 ELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLAresSESSKLEKTYELPDGNTIKVGNERFRIPEILFSPELI 265
                          250       260       270
                   ....*....|....*....|....*....|.
gi 393693628   238 GLESGGIHVTTFNSIMKCDVDVRKDLYGNIV 268
Cdd:smart00268 266 GLEQKGIHELVYESIQKCDIDVRKDLYENIV 296
ASKHA_NBD_Arp2 cd10220
nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, ...
1-269 8.99e-141

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: 400.40  E-value: 8.99e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628   1 FPSIVGRP--RHHGIMIGMGQKDSYVGDEAQSKRGILTLRYPIEHGVVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEA 78
Cdd:cd10220   26 FPSLVGRPilRAEEKVGDIEIKDIMVGDEASELRSMLEVTYPMENGIVRNWDDMEHLWDYTFGEKLKIDPRECKILLTEP 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  79 PINPKSNREKMTQIVFETFNAPAFYVSIQAVLSLYASGRTTGIVLDSGDGVTHVVPIYEGFALPHAISRVDMAGRDLTDY 158
Cdd:cd10220  106 PMNPTKNREKMVEVMFEKYGFAGVYVAIQAVLTLYAQGLLTGVVVDSGDGVTHIVPVYEGFSLPHLTRRLDVAGRDITRY 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628 159 LMKILAERGYTFSTTAEREIVRDIKEKLCYVALDFEQEIQTASQSSSLEKSYELPDGQVITIGNERFRAPEALFQPSVLG 238
Cdd:cd10220  186 LIKLLLLRGYAFNRTADFETVREIKEKLCYVAYDIELEQKLALETTVLVESYTLPDGRVIKVGGERFEAPEALFQPHLID 265
                        250       260       270
                 ....*....|....*....|....*....|.
gi 393693628 239 LESGGIHVTTFNSIMKCDVDVRKDLYGNIVM 269
Cdd:cd10220  266 VEGPGIAELLFNTIQAADIDTRPELYKHIVL 296
Actin pfam00022
Actin;
1-268 5.51e-126

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 363.93  E-value: 5.51e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628    1 FPSIVGRPRHHGIMigMGQKDsYVGDEAQSKRGILTLRYPIEHGVVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPI 80
Cdd:pfam00022  27 IPSCVGKPRGTKVE--AANKY-YVGDEALTYRPGMEVRSPVEDGIVVDWDAMEEIWEHVLKEELQVDPEEHPLLLTEPPW 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628   81 NPKSNREKMTQIVFETFNAPAFYVSIQAVLSLYASGRTTGIVLDSGDGVTHVVPIYEGFALPHAISRVDMAGRDLTDYLM 160
Cdd:pfam00022 104 NPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVPVHDGYVLQKAIRRSDLGGDFLTDYLR 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  161 KILAER------------------------------GYTFSTTAEREIVRDIKEKLCYVALDFEQEIQTAsqSSSLEKSY 210
Cdd:pfam00022 184 ELLRSRnieitprylikskkpgdpapavtkrelpdtTYSYKTYQERRVLEEIKESVCYVSDDPFGDETTS--SSIPTRVY 261
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 393693628  211 ELPDGQVITIGNERFRAPEALFQPSVLGLESG--------GIHVTTFNSIMKCDVDVRKDLYGNIV 268
Cdd:pfam00022 262 ELPDGSTIILGAERFRVPEILFNPSLIGSESElpppqtavGIPELIVDAINACDVDLRPSLLANIV 327
PTZ00466 PTZ00466
actin-like protein; Provisional
1-269 5.78e-118

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 342.69  E-value: 5.78e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628   1 FPSIVGRPRHHGIMIGMGQKDSYVGDEAQSKRGILTLRYPIEHGVVTNWDDMEKIWHHTfYNELRVAPEEHPVLLTEAPI 80
Cdd:PTZ00466  38 FPSYVGRPKYKRVMAGAVEGNIFVGNKAEEYRGLLKVTYPINHGIIENWNDMENIWIHV-YNSMKINSEEHPVLLTEAPL 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  81 NPKSNREKMTQIVFETFNAPAFYVSIQAVLSLYASGRTTGIVLDSGDGVTHVVPIYEGFALPHAISRVDMAGRDLTDYLM 160
Cdd:PTZ00466 117 NPQKNKEKIAEVFFETFNVPALFISIQAILSLYSCGKTNGTVLDCGDGVCHCVSIYEGYSITNTITRTDVAGRDITTYLG 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628 161 KILAERGYTFSTTAEREIVRDIKEKLCYVALDFEQEiQTASQSSSLEKSYELPDGQVITIGNERFRAPEALFQPSVLGLE 240
Cdd:PTZ00466 197 YLLRKNGHLFNTSAEMEVVKNMKENCCYVSFNMNKE-KNSSEKALTTLPYILPDGSQILIGSERYRAPEVLFNPSILGLE 275
                        250       260
                 ....*....|....*....|....*....
gi 393693628 241 SGGIHVTTFNSIMKCDVDVRKDLYGNIVM 269
Cdd:PTZ00466 276 YLGLSELIVTSITRADMDLRRTLYSHIVL 304
PTZ00452 PTZ00452
actin; Provisional
1-269 1.41e-113

actin; Provisional


Pssm-ID: 185631  Cd Length: 375  Bit Score: 331.33  E-value: 1.41e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628   1 FPSIVGRPRHHGIMIGMGQKDSYVGDEAQSKRGILTLRYPIEHGVVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPI 80
Cdd:PTZ00452  31 FPAIVGRSKQNDGIFSTFNKEYYVGEEAQAKRGVLAIKEPIQNGIINSWDDIEIIWHHAFYNELCMSPEDQPVFMTDAPM 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  81 NPKSNREKMTQIVFETFNAPAFYVSIQAVLSLYASGRTTGIVLDSGDGVTHVVPIYEGFALPHAISRVDMAGRDLTDYLM 160
Cdd:PTZ00452 111 NSKFNRERMTQIMFETFNTPCLYISNEAVLSLYTSGKTIGLVVDSGEGVTHCVPVFEGHQIPQAITKINLAGRLCTDYLT 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628 161 KILAERGYTFSTTAEREIVRDIKEKLCYVALDFEQEIQTASQSSSLEKSYELPDGQVITIGNERFRAPEALFQPSVLGLE 240
Cdd:PTZ00452 191 QILQELGYSLTEPHQRIIVKNIKERLCYTALDPQDEKRIYKESNSQDSPYKLPDGNILTIKSQKFRCSEILFQPKLIGLE 270
                        250       260
                 ....*....|....*....|....*....
gi 393693628 241 SGGIHVTTFNSIMKCDVDVRKDLYGNIVM 269
Cdd:PTZ00452 271 VAGIHHLAYSSIKKCDLDLRQELCRNIVL 299
ASKHA_NBD_ACTL7 cd10214
nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ...
3-269 2.69e-111

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: 325.15  E-value: 2.69e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628   3 SIVGRPRHHGIMIGMGQKDSYVGDEAQSKRGILTLRYPIEHGVVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPINP 82
Cdd:cd10214   31 STVGKPPQESAKTGDNRKETFVGKELANVEPPLKLVNPLRHGIVVDWDCVQDIWEYIFEKEMKILPEEHAVLVSDPPLSP 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  83 KSNREKMTQIVFETFNAPAFYVSIQAVLSLYASGRTTGIVLDSGDGVTHVVPIYEGFALPHAISRVDMAGRDLTDYLMKI 162
Cdd:cd10214  111 TTNREKYAELMFETFSIPAMHIAYQSRLSLYSYGRTSGLVVESGHGVSYVVPIHEGYNLPHITGRADYAGSDLTAYLMKL 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628 163 LAERGYTFsTTAEREIVRDIKEKLCYVALDFEQEIQTASQSSSLEksYELPDGQVITIGNERFRAPEALFQPSVLGLESG 242
Cdd:cd10214  191 LNEAGNKF-TDDQLHIVEDIKKKCCYVALDFEEEMGLPPQEYTVD--YELPDGHLITIGKERFRCPEMLFNPSLIGSKQP 267
                        250       260
                 ....*....|....*....|....*..
gi 393693628 243 GIHVTTFNSIMKCDVDVRKDLYGNIVM 269
Cdd:cd10214  268 GLHTLTMNSLNKCDANLKKDLAKNILL 294
ASKHA_NBD_actin-like cd10169
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ...
49-268 4.94e-99

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: 290.16  E-value: 4.94e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  49 WDDMEKIWHHTFYNELRVAPEEHPVLLTEAPINPKSNREKMTQIVFETFNAPAFYVSIQAVLSLYASGRTTGIVLDSGDG 128
Cdd:cd10169   26 WDDMEKIWEHVFYNLLRVDPEEHPVLLTEPPLNPKANREKLAEILFETFNVPSLYIANQAVLSLYASGRTTGLVVDSGEG 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628 129 VTHVVPIYEGFALPHAISRVDMAGRDLTDYLMKILAERGYTFSTTAEREIVRDIKEKLCyvaldfeqeiqtasqssslek 208
Cdd:cd10169  106 VTHIVPVYEGYVLPHAVRRLDIGGRDLTDYLAKLLREKGYSFSTSAEREIVRDIKEKLC--------------------- 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628 209 syelpdgqvitignerfrapealfqpsvlglesgGIHVTTFNSIMKCDVDVRKDLYGNIV 268
Cdd:cd10169  165 ----------------------------------GLHELIYDSIMKCDIDLRKELYSNIV 190
COG5277 COG5277
Actin-related protein [Cytoskeleton];
1-269 3.40e-97

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 291.31  E-value: 3.40e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628   1 FPSIVGRPRHHGIMIGMGqKDSYVGDEAQS-----KRGILTLRYPIEHGVVT-----NWDDMEKIWHHTFYNELRVAPEE 70
Cdd:COG5277   40 FLRIVGESKLLGPMEGLS-RGLVVGDEVSKylssvRDAIRNLKYPLRDGIVRrddedAWRVLKELLRYTFAQFLVVDPEF 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  71 HP--VLLTEAPINPKSNREKMTQIVFETF---NAPAFYVSIQAVLSLYASGRTTGIVLDSGDGVTHVVPIYEGfALPHAI 145
Cdd:COG5277  119 HGflVVVALSALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPLAVAIAEKAVTCVVVEAGHGNSQVAPISRG-PIREGL 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628 146 SRVDMAGRDLTDYLMKILAERGYTFSTTAEReIVRDIKEKLCYVALDFEQEIQ-TASQSSSLEKSYELPDGQV-ITIGN- 222
Cdd:COG5277  198 VALNRGGAEANAITREILKDRGYSDTAREEY-VVRVVKEALGLVPRDLAKAIQkAASNPDSFEAKVRLPNPTVeIELGNy 276
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 393693628 223 --ERFRAPEALFQPSVLGLESG----------------------GIHVTTFNSIMKCDVDVRKDLYGNIVM 269
Cdd:COG5277  277 awERFLIGEILFNPNHEGFESYiqqgrlriedavigdvvlygemGLAEAIINSIMKCDVEIQDELYSNIIL 347
ASKHA_NBD_Arp4_ACTL6-like cd13395
nucleotide-binding domain (NBD) of the actin-related protein 4 (Arp4)-like subfamily; The ...
1-268 9.05e-93

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: 279.45  E-value: 9.05e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628   1 FPSIVG-RPRHHGIMIGMGQKDS-----YVGDEA-QSKRGILTLRYPIEHGVVTNWDDMEKIWHHTFYNELRVAPEEHPV 73
Cdd:cd13395   30 FPSVVGvVTDDDDAEDYVGGSGEkkrkyYIGTNSiGVPRPNMEVISPLKDGLIEDWDAFEKLWDHALKNRLRVDPSEHPL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  74 LLTEAPINPKSNREKMTQIVFETFNAPAFYVSIQAVLSLYASGRTTGIVLDSGDGVTHVVPIYEGFALPHAISRVDMAGR 153
Cdd:cd13395  110 LLTEPSWNTRANREKLTELMFEKYNVPAFFLAKNAVLSAFANGRSTALVVDSGATSTSVVPVHDGYVLQKAIVRSPLGGD 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628 154 DLTDYLMKILAERGYTF--------------------------STT------AEREIVRDIKEKLCYVALDFEQEIQTAS 201
Cdd:cd13395  190 FLTDQLLKLLESKNIEIiprymikskepveggapakytkkdlpNTTssyhryMVRRVLQDFKESVCQVSDSPFDESEAAS 269
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 393693628 202 QSSsleKSYELPDGQVITIGNERFRAPEALFQPSVLGLESG---------GIHVTTFNSIMKCDVDVRKDLYGNIV 268
Cdd:cd13395  270 IPT---VSYELPDGYNIEFGAERFKIPELLFDPSLVKGIPAppsegnellGLPQLVYTSIGSCDVDIRPELYGNVV 342
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
16-268 1.32e-84

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: 258.27  E-value: 1.32e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  16 GMGQKDSYVGDEAQSKRGILTLRYPIEHGVVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPINPKSNREKMTQIVFE 95
Cdd:cd10221   47 GIEDLDFYIGDEALANSPTYALKYPIRHGIVEDWDLMERFWEQCIFKYLRCEPEDHYFLLTEPPLNPPENREYTAEIMFE 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  96 TFNAPAFYVSIQAVLSLYASGRT--------TGIVLDSGDGVTHVVPIYEGFALPHAISRVDMAGRDLTDYLMKILAERG 167
Cdd:cd10221  127 TFNVPGLYIAVQAVLALAASWTSrkvgertlTGTVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLRERE 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628 168 YTFSTTAEREIVRDIKEKLCYVALD-------FEQE-----IQTASQSSSLEKSYElpdgqvITIGNERFRAPEALFQPS 235
Cdd:cd10221  207 EGIPPEDSLEVAKRIKERYCYVCPDivkefakYDSDpakyiKQYTGINSVTGKPYT------VDVGYERFLAPEIFFNPE 280
                        250       260       270
                 ....*....|....*....|....*....|....
gi 393693628 236 VLGLE-SGGIHVTTFNSIMKCDVDVRKDLYGNIV 268
Cdd:cd10221  281 IASSDfTTPLPEVVDQVIQSCPIDTRRGLYKNIV 314
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
21-269 1.14e-81

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 251.19  E-value: 1.14e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  21 DSYVGDEAQSKRGILTLRYPIEHGVVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPINPKSNREKMTQIVFETFNAP 100
Cdd:PTZ00280  53 DFYIGDEALAASKSYTLTYPMKHGIVEDWDLMEKFWEQCIFKYLRCEPEEHYFILTEPPMNPPENREYTAEIMFETFNVK 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628 101 AFYVSIQAVLSLYAS----------GRTTGIVLDSGDGVTHVVPIYEGFALPHAISRVDMAGRDLTDYLMKILAERGYTF 170
Cdd:PTZ00280 133 GLYIAVQAVLALRASwtskkakelgGTLTGTVIDSGDGVTHVIPVVDGYVIGSSIKHIPLAGRDITNFIQQMLRERGEPI 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628 171 STTAEREIVRDIKEKLCYVALDFEQEIQT------------ASQSSSLEKSYElpdgqvITIGNERFRAPEALFQPSVLG 238
Cdd:PTZ00280 213 PAEDILLLAQRIKEKYCYVAPDIAKEFEKydsdpknhfkkyTAVNSVTKKPYT------VDVGYERFLGPEMFFHPEIFS 286
                        250       260       270
                 ....*....|....*....|....*....|..
gi 393693628 239 LE-SGGIHVTTFNSIMKCDVDVRKDLYGNIVM 269
Cdd:PTZ00280 287 SEwTTPLPEVVDDAIQSCPIDCRRPLYKNIVL 318
ASKHA_NBD_Arp6 cd10210
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ...
1-268 3.92e-65

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: 208.17  E-value: 3.92e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628   1 FPSIVGRPRHhgimigmgQKDSYVGDEAQSK---RGILTLRYPIEHGVVTNWDDMEKIWHHTFYNE-LRVAPEEHPVLLT 76
Cdd:cd10210   24 IPNCIAKPKS--------ERRRLFGDDQLDEckdLSGLFYRRPFERGYLVNWDLQRQIWDHLFGKLlLNVDPSDTALVLT 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  77 EAPINPKSNREKMTQIVFETFNAPAFYVSIQAVLSLYA----------SGRTTGIVLDSGDGVTHVVPIYEGFALPHAIS 146
Cdd:cd10210   96 EPPFNPPSIQEAMDEIVFEEYGFQSLYRTTAAALSAFAyladseqsssSSSQCCLVVDSGFSFTHIVPFFDGKPVKRAVR 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628 147 RVDMAGRDLTDYLMKILAERGY-----TFsttaereIVRDIKEKLCYVALDFEQEIQTASQ---SSSLEKSYELPDG--- 215
Cdd:cd10210  176 RIDVGGKLLTNYLKEIISYRQLnvmdeTY-------LVNQIKEDLCFVSTDFYEDLEIAKKkgkENTIRRDYVLPDYtts 248
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 393693628 216 --------------------QVITIGNERFRAPEALFQPSVLGLESGGIHVTTFNSIMKCDVDVRKDLYGNIV 268
Cdd:cd10210  249 krgyvrdpeepnrgklkedeQVLRLNNERFTVPELLFHPSDIGIQQAGIAEAIVQSINACPEELQPLLYANIV 321
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
40-268 1.64e-57

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: 187.21  E-value: 1.64e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  40 PIEHGVVTNWDDMEKIWHHTFYNELR-VAPEEHPVLLTEAPINPKSNREKMTQIVFETFNAPAFYVSIQAVLSLYASGRT 118
Cdd:cd10209   50 PIRRGRIEDWDALEALLRYVFYTGLGwEEGNEGQVLIAEPLLTSKAERERLTQLMFETFNVSGLYASEQAVLSLYAVGRI 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628 119 TGIVLDSGDGVTHVVPIYEGFALPHAISRVDMAGRDLTDYLMKILAERGYtfSTTAEREIVRDIKEKLCYVALDFEQEIQ 198
Cdd:cd10209  130 SGCVVDVGHGKIDIAPVWEGAIQHNAVRRFEIGGRDLTELLAAELGKSNP--KVKLDRSIVERLKEAVAWSADDEEAYEK 207
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628 199 TASQSSslEKSYELPDGQVITIGNERFRAPEALFQPSVLGLESGGIHVTTFNSIMKCDVDVRKDLYGNIV 268
Cdd:cd10209  208 KVLTCS--PETYTLPDGRVISVGKERYCVGEALFRPSILGIEEYGIVEQLVRAVSTSPSENRRQLLENIV 275
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
8-268 2.95e-47

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: 160.94  E-value: 2.95e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628   8 PRHHGIMIGMGQKDSYVGD--EAQSKRGIltlRYPIEHGVVTNWDDMEKIWHHTFYNEL--RVAPEEHPVLLTEAPINPK 83
Cdd:cd10208    7 PGSQTTRAGLGLGELLTPPtiEIPTRVEI---IWPIQDGRVVDWDALEALWRHILFSLLsiPRPTNNSPVLLSVPPSWSK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  84 SNREKMTQIVFETFNAPAFYVSIQAVLSLYASGRTTGIVLDSGDGVTHVVPIYEGFALPHAISRVDMAGRDLTDYLMKIL 163
Cdd:cd10208   84 SDLELLTQLFFERLNVPAFAILEAPLAALYAAGATSGIVVDIGHEKTDITPIVDSQVVPHALVSIPIGGQDCTAHLAQLL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628 164 AERGYTFSTTAE--REIVRDIKEKLcyvaldFEQEIqtasqSSSLEKSYELPDGQVITIGNERFRAPEALFQPSVLGLES 241
Cdd:cd10208  164 KSDEPELKSQAEsgEEATLDLAEAL------KKSPI-----CEVLSDGADLASGTEITVGKERFRACEPLFKPSSLRVDL 232
                        250       260
                 ....*....|....*....|....*...
gi 393693628 242 GGIHVTTFNSIMKC-DVDVRKDLYGNIV 268
Cdd:cd10208  233 LIAAIAGALVLNASdEPDKRPALWENII 260
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
1-222 2.88e-42

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: 147.33  E-value: 2.88e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628   1 FPSIVGRPRHHGimigMGQKDSYVGDEA---QSKRGilTLRYPIEHGVVTNWDDMEKIWHHTFyNELRVAPE---EHPVL 74
Cdd:cd10211   25 FRNLVAKPRDRK----KGITVTLVGNDIlndEAVRS--HLRSPFDRNVVTNFDLQEQILDYIF-SHLGINSEgsvDHPIV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  75 LTEAPINPKSNREKMTQIVFETFNAPAFYVSIQAVLSLYASGRT----TGIVLDSGDGVTHVVPIYEGFALPHAISRVDM 150
Cdd:cd10211   98 LTEALCNPNYSRQLMSELLFECYGVPSVAYGIDSLFSYYHNQPQgdpsDGLVISSGYSTTHVIPVLNGRLDLSQCKRINL 177
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 393693628 151 AGRDLTDYLMKILAERGYTFST--TAEReiVRDIKEKLCYVALDFEQEIQTASQSSSLEKS---YELPDGQVITIGN 222
Cdd:cd10211  178 GGFHATDYLQRLLQLKYPTHPSaiTLSR--AEELVHEHCYVAEDYDEELKKWEDPEYYEENvrkIQLPFGLVETIEF 252
ASKHA_NBD_AtArp8-like cd13396
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and ...
59-258 4.88e-29

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: 112.25  E-value: 4.88e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  59 TFYNELRVAPEEHPVLLTEaPI-------NPKSNREKMTQIVFETF---NAPAFYVSIQAVLSLYASGRTTGIVLDSGDG 128
Cdd:cd13396   47 TIMTRMQVKPSRQPVVVSL-PLchsddteSAAASRRQLRGTIFNVLfdmNVPAVCAVDQAVLALYAANRTSGIVVNIGFR 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628 129 VTHVVPIYEGFALpHAISrVDMAGR---DLTDYLMKILAERGYTFSTTAereIVRDIKEKLCYVALDFEQEIqtasqSSS 205
Cdd:cd13396  126 VTTIVPVYRGRVM-HDIG-VEVVGQgalRLTGFLKELMQQNGIRFPSLY---TVRTIKEKLCYVAEDYEAEL-----AKD 195
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 393693628 206 LEKSYELPDGQVITIGNERFRAPEALFQPSVLGLESGGIHVTTFNSIMKCDVD 258
Cdd:cd13396  196 TQASCEVAGEGWFTLSNERFKTGEILFQPGLGGMRAMGLHQAVALCMDHCALV 248
ASKHA_NBD_Arp10 cd10207
nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins; ...
57-269 5.12e-27

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: 107.72  E-value: 5.12e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  57 HHTFYNELRVAPEEHPVLLTEAPINPKSNREKMTQIVFETFNAPA--FYVSiqAVLSLYASGRTTGIVLDSGDGVTHVVP 134
Cdd:cd10207   59 HELYFKHLLVNPKDRRVVVVESVLCPTPFRETLAKVLFKHFEVPSvlFAPS--HLLSLLTLGIRTALVVDCGYRETRVLP 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628 135 IYEGFALPHAISRVDMAGRDLTDYLMKILAERGYTFSTTAER------------EIVRDIKEKLCYVA-LDFEQEIQTAS 201
Cdd:cd10207  137 VYEGVPLLSAWQSTPLGGKALHKRLKKLLLEHATVVTGDNKGqllssvdsllseEVLEDIKVRACFVTsLERGKTLQSAT 216
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 393693628 202 QSSSLEKS-------YELPDGQVITIGNERFRAPEALFQPSVLGLESggIHVTTFNSIMKCDVDVRKDLYGNIVM 269
Cdd:cd10207  217 EEGSTEEPsppppvdYPLDGEKILIVPGSIRESAEELLFEGDNEEKS--LPTLILDSLLKCPIDVRKQLAENIVV 289
ASKHA_NBD_Arp8-like cd10206
nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The ...
18-268 2.63e-15

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: 74.97  E-value: 2.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  18 GQKDSYVGDEAQ--SKRGILTLRYPIEHGVVtNW-----------DDMEKIWHHTFYNELRVAPEEHP----VLLteapI 80
Cdd:cd10206  118 DYPDFLVGEEALrlPPSEEYNLHWPIRRGRL-NVhsdggsltavlDDLEDIWSHALEEKLEIPRKDLKnyraVLV----I 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  81 NPKSNR---EKMTQIVFETFNAPAFYVSIQAVLSLYASGRTTGIVLDSGDGVTHVVPIYEGFALPHAISRVDMAGRDLTD 157
Cdd:cd10206  193 PDLFDRrhvKELVDLLLRRLGFSSVFVHQESVCATFGAGLSSACVVDIGAQKTSVACVEDGLSIPNSRIRLPYGGDDITR 272
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628 158 YLMKILAERG--YTF---STTAEREIVRDIKEKLCYvaldFEQEIQTASQSSSLEKSyelPDGqvitignerfraPEALF 232
Cdd:cd10206  273 CFLWLLRRSGfpYREcnlNSPLDFLLLERLKETYCT----LDQDDIGVQLHEFYVRE---PGQ------------PTLKY 333
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 393693628 233 QPSVLGLESGGIHvttfnSIMKC-DVDVRKDLYGNIV 268
Cdd:cd10206  334 QFKLLPLDEAIVQ-----SILSCaSDELKRKMYSSIL 365
ASKHA_NBD_ScArp7-like cd10212
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and ...
43-158 1.03e-13

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: 70.52  E-value: 1.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  43 HGVVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPINPKSNR---EKMTQIVFETFNAPAFYVSIQAVLSLYASGRTT 119
Cdd:cd10212   72 QGLPYNWDALEMQWRYLYDTQLKVSPEELPLVITMPATNGKPDMailERYYELAFDKLNVPVFQIVIEPLAIALSMGKSS 151
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 393693628 120 GIVLDSGDGVTHVVPIYEGFALPHAISRVDMAGrDLTDY 158
Cdd:cd10212  152 AFVIDIGASGCNVTPIIDGIVVKNAVVRSKFGG-DFLDF 189
ASKHA_NBD_MamK cd24009
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ...
1-189 2.84e-06

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: 47.59  E-value: 2.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628   1 FPSIVGRPRHHGIMIGMGqKDSYVGDEAQSKRGILTLRYPIEHGVVTNWDDmekiwhhtfyNELRVAPE--EHPVLLTEA 78
Cdd:cd24009   25 FRSVVGYPKDIIARKLLG-KEVLFGDEALENRLALDLRRPLEDGVIKEGDD----------RDLEAAREllQHLIELALP 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393693628  79 PINPK-------------SNREKMTQIVFETFNApAFYVS-IQAVlsLYASGRTTG-IVLDSGDGVTHVVPIYEGFALPH 143
Cdd:cd24009   94 GPDDEiyavigvparasaENKQALLEIARELVDG-VMVVSePFAV--AYGLDRLDNsLIVDIGAGTTDLCRMKGTIPTEE 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 393693628 144 AISRVDMAGRDLTDYLMKILAER--GYTFSttaeREIVRDIKEKLCYV 189
Cdd:cd24009  171 DQITLPKAGDYIDEELVDLIKERypEVQLT----LNMARRWKEKYGFV 214
 
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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