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Conserved domains on  [gi|1907068532|ref|XP_036020205|]
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beta-centractin isoform X2 [Mus musculus]

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_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
1-301 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: 665.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532   1 MEHGVVRDWNDMERIWQYVYSKDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTT 80
Cdd:cd10216    67 MEHGIVTDWNDMERIWQYVYSKLQLNTFSEEHPVLLTEAPLNPRKNREKAAEVFFETFNVPALFVSMQAVLSLYASGRTT 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  81 GVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAEFEVVRTIKERACYLSINPQKDEAL 160
Cdd:cd10216   147 GVVLDSGDGVTHAVPIYEGFALPHSIRRVDIAGRDVTEYLQLLLRKSGYNFHTSAEFEIVREIKEKACYVALNPQKEEKL 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 161 E---TEKVQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFG 237
Cdd:cd10216   227 EeekTEKAQYTLPDGSTIEIGPERFRAPEILFNPELIGLEYPGVHEVLVDSIQKSDLDLRKTLYSNIVLSGGSTLFKGFG 306
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907068532 238 DRLLSEVKKLAPKDVKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRKT 301
Cdd:cd10216   307 DRLLSEVKKLAPKDVKIRISAPPERLYSTWIGGSILASLSTFKKMWVSKKEYEEDGARILHRKT 370
 
Name Accession Description Interval E-value
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
1-301 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: 665.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532   1 MEHGVVRDWNDMERIWQYVYSKDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTT 80
Cdd:cd10216    67 MEHGIVTDWNDMERIWQYVYSKLQLNTFSEEHPVLLTEAPLNPRKNREKAAEVFFETFNVPALFVSMQAVLSLYASGRTT 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  81 GVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAEFEVVRTIKERACYLSINPQKDEAL 160
Cdd:cd10216   147 GVVLDSGDGVTHAVPIYEGFALPHSIRRVDIAGRDVTEYLQLLLRKSGYNFHTSAEFEIVREIKEKACYVALNPQKEEKL 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 161 E---TEKVQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFG 237
Cdd:cd10216   227 EeekTEKAQYTLPDGSTIEIGPERFRAPEILFNPELIGLEYPGVHEVLVDSIQKSDLDLRKTLYSNIVLSGGSTLFKGFG 306
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907068532 238 DRLLSEVKKLAPKDVKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRKT 301
Cdd:cd10216   307 DRLLSEVKKLAPKDVKIRISAPPERLYSTWIGGSILASLSTFKKMWVSKKEYEEDGARILHRKT 370
PTZ00466 PTZ00466
actin-like protein; Provisional
1-302 3.52e-168

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 471.35  E-value: 3.52e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532   1 MEHGVVRDWNDMERIWQYVYSkdQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTT 80
Cdd:PTZ00466   78 INHGIIENWNDMENIWIHVYN--SMKINSEEHPVLLTEAPLNPQKNKEKIAEVFFETFNVPALFISIQAILSLYSCGKTN 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  81 GVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAEFEVVRTIKERACYLSINPQKDEAl 160
Cdd:PTZ00466  156 GTVLDCGDGVCHCVSIYEGYSITNTITRTDVAGRDITTYLGYLLRKNGHLFNTSAEMEVVKNMKENCCYVSFNMNKEKN- 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 161 ETEK----VQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGF 236
Cdd:PTZ00466  235 SSEKalttLPYILPDGSQILIGSERYRAPEVLFNPSILGLEYLGLSELIVTSITRADMDLRRTLYSHIVLSGGTTMFHGF 314
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907068532 237 GDRLLSEVKKLAPKDVKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRKTF 302
Cdd:PTZ00466  315 GDRLLNEIRKFAPKDITIRISAPPERKFSTFIGGSILASLATFKKIWISKQEFDEYGSVILHRKTF 380
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
1-302 3.68e-162

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 455.95  E-value: 3.68e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532    1 MEHGVVRDWNDMERIWQYVYSKdQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTT 80
Cdd:smart00268  66 IENGIVENWDDMEKIWDYTFFN-ELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTT 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532   81 GVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAEFEVVRTIKERACYLSINPQKDEAL 160
Cdd:smart00268 145 GLVIDSGDGVTHVVPVVDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKL 224
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  161 E-------TEKVQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLF 233
Cdd:smart00268 225 AressessKLEKTYELPDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLI 304
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907068532  234 KGFGDRLLSEVKKLAPKDVKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRKTF 302
Cdd:smart00268 305 PGFGERLEKELKQLAPKKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERKCF 373
Actin pfam00022
Actin;
1-302 6.52e-158

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 446.37  E-value: 6.52e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532   1 MEHGVVRDWNDMERIWQYVYsKDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTT 80
Cdd:pfam00022  64 VEDGIVVDWDAMEEIWEHVL-KEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTT 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  81 GVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGAD------------------------------ 130
Cdd:pfam00022 143 GLVVDSGAGVTSVVPVHDGYVLQKAIRRSDLGGDFLTDYLRELLRSRNIEitprylikskkpgdpapavtkrelpdttys 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 131 FHTSAEFEVVRTIKERACYLSINPQKDEALETE--KVQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESE--------G 200
Cdd:pfam00022 223 YKTYQERRVLEEIKESVCYVSDDPFGDETTSSSipTRVYELPDGSTIILGAERFRVPEILFNPSLIGSESElpppqtavG 302
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 201 LHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDVKIKISAPQ---ERLYSTWIGGSILASLD 277
Cdd:pfam00022 303 IPELIVDAINACDVDLRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVKIIAPGntvERRYSAWIGGSILASLG 382
                         330       340
                  ....*....|....*....|....*
gi 1907068532 278 TFKKMWVSKKEYEEDGSRAIHRKTF 302
Cdd:pfam00022 383 TFQQMWVSKQEYEEHGASVVERKCK 407
COG5277 COG5277
Actin-related protein [Cytoskeleton];
1-291 7.33e-62

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 201.94  E-value: 7.33e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532   1 MEHGVVR-----DWNDMERIWQYVYSKdQLQTFSEEHP--VLLTEAPLNPSKNREKAAEVFFETF---NVPALFISMQAV 70
Cdd:COG5277    84 LRDGIVRrddedAWRVLKELLRYTFAQ-FLVVDPEFHGflVVVALSALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPL 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  71 LSLYATGRTTGVVLDSGDGVTHAVPIYEGfAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFhTSAEFEVVRTIKERACYL 150
Cdd:COG5277   163 AVAIAEKAVTCVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSD-TAREEYVVRVVKEALGLV 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 151 ------SINPQKDEALETEKVqYTLPDGSTL----DVGPARFRAPELLFQPDLVGDESE--------------------- 199
Cdd:COG5277   241 prdlakAIQKAASNPDSFEAK-VRLPNPTVEielgNYAWERFLIGEILFNPNHEGFESYiqqgrlriedavigdvvlyge 319
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 200 -GLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLF---KGFGD-------RLLSEVKKLAPkDVKIKISAPQERLYSTWI 268
Cdd:COG5277   320 mGLAEAIINSIMKCDVEIQDELYSNIILSGGAFNWsvpPGLEDvavdsvtRVQIELSELAP-ELKVNVRLVSDPQYSVWK 398
                         330       340
                  ....*....|....*....|....*
gi 1907068532 269 GGSILASLDTFKKMW--VSKKEYEE 291
Cdd:COG5277   399 GAIIYGYALPFSVKWswITKEGWYF 423
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
235-300 2.19e-16

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: 74.25  E-value: 2.19e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907068532 235 GFGDRLLSEVKKLAPKDVKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRK 300
Cdd:NF040575   66 GFYEKLKKSITEKAPKGALIGMTLDPKPESAAWRGAAMYAASEGFVEMAITKQEYDESGPSIVHRK 131
 
Name Accession Description Interval E-value
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
1-301 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: 665.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532   1 MEHGVVRDWNDMERIWQYVYSKDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTT 80
Cdd:cd10216    67 MEHGIVTDWNDMERIWQYVYSKLQLNTFSEEHPVLLTEAPLNPRKNREKAAEVFFETFNVPALFVSMQAVLSLYASGRTT 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  81 GVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAEFEVVRTIKERACYLSINPQKDEAL 160
Cdd:cd10216   147 GVVLDSGDGVTHAVPIYEGFALPHSIRRVDIAGRDVTEYLQLLLRKSGYNFHTSAEFEIVREIKEKACYVALNPQKEEKL 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 161 E---TEKVQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFG 237
Cdd:cd10216   227 EeekTEKAQYTLPDGSTIEIGPERFRAPEILFNPELIGLEYPGVHEVLVDSIQKSDLDLRKTLYSNIVLSGGSTLFKGFG 306
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907068532 238 DRLLSEVKKLAPKDVKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRKT 301
Cdd:cd10216   307 DRLLSEVKKLAPKDVKIRISAPPERLYSTWIGGSILASLSTFKKMWVSKKEYEEDGARILHRKT 370
ASKHA_NBD_actin_Arp-T1-3 cd13397
nucleotide-binding domain (NBD) of actin, actin-related proteins T1-T3 (Arp-T1-3), and similar ...
1-293 1.08e-172

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: 482.07  E-value: 1.08e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532   1 MEHGVVRDWNDMERIWQYVYsKDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTT 80
Cdd:cd13397    66 IEHGIVTNWDDMEKIWHHTF-ENELRVKPEEHPVLLTEAPLNPKQNREKMAEIMFETFGVPAFYVAIQAVLSLYSSGRTT 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  81 GVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAEFEVVRTIKERACYLSINPQKDEAL 160
Cdd:cd13397   145 GLVLDSGDGVTHTVPIYEGYALPHAVQRLDLAGRDLTEYLMKLLKERGHSFTTTAEREIVRDIKEKLCYVALDYEEELKK 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 161 ETEKVQ--YTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFGD 238
Cdd:cd13397   225 KSEELEkeYTLPDGQVIKIGSERFRCPEALFRPSLIGREAPGIHKLVYNSIMKCDIDIRKDLYSNIVLSGGSTMFPGLPE 304
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907068532 239 RLLSEVKKLAPKDVKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDG 293
Cdd:cd13397   305 RLQKELEALAPSSTKVKVIAPPERKYSVWIGGSILASLSTFKSMWITRAEYDEFG 359
PTZ00466 PTZ00466
actin-like protein; Provisional
1-302 3.52e-168

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 471.35  E-value: 3.52e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532   1 MEHGVVRDWNDMERIWQYVYSkdQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTT 80
Cdd:PTZ00466   78 INHGIIENWNDMENIWIHVYN--SMKINSEEHPVLLTEAPLNPQKNKEKIAEVFFETFNVPALFISIQAILSLYSCGKTN 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  81 GVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAEFEVVRTIKERACYLSINPQKDEAl 160
Cdd:PTZ00466  156 GTVLDCGDGVCHCVSIYEGYSITNTITRTDVAGRDITTYLGYLLRKNGHLFNTSAEMEVVKNMKENCCYVSFNMNKEKN- 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 161 ETEK----VQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGF 236
Cdd:PTZ00466  235 SSEKalttLPYILPDGSQILIGSERYRAPEVLFNPSILGLEYLGLSELIVTSITRADMDLRRTLYSHIVLSGGTTMFHGF 314
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907068532 237 GDRLLSEVKKLAPKDVKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRKTF 302
Cdd:PTZ00466  315 GDRLLNEIRKFAPKDITIRISAPPERKFSTFIGGSILASLATFKKIWISKQEFDEYGSVILHRKTF 380
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
1-302 3.68e-162

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 455.95  E-value: 3.68e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532    1 MEHGVVRDWNDMERIWQYVYSKdQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTT 80
Cdd:smart00268  66 IENGIVENWDDMEKIWDYTFFN-ELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTT 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532   81 GVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAEFEVVRTIKERACYLSINPQKDEAL 160
Cdd:smart00268 145 GLVIDSGDGVTHVVPVVDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKL 224
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  161 E-------TEKVQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLF 233
Cdd:smart00268 225 AressessKLEKTYELPDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLI 304
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907068532  234 KGFGDRLLSEVKKLAPKDVKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRKTF 302
Cdd:smart00268 305 PGFGERLEKELKQLAPKKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERKCF 373
Actin pfam00022
Actin;
1-302 6.52e-158

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 446.37  E-value: 6.52e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532   1 MEHGVVRDWNDMERIWQYVYsKDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTT 80
Cdd:pfam00022  64 VEDGIVVDWDAMEEIWEHVL-KEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTT 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  81 GVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGAD------------------------------ 130
Cdd:pfam00022 143 GLVVDSGAGVTSVVPVHDGYVLQKAIRRSDLGGDFLTDYLRELLRSRNIEitprylikskkpgdpapavtkrelpdttys 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 131 FHTSAEFEVVRTIKERACYLSINPQKDEALETE--KVQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESE--------G 200
Cdd:pfam00022 223 YKTYQERRVLEEIKESVCYVSDDPFGDETTSSSipTRVYELPDGSTIILGAERFRVPEILFNPSLIGSESElpppqtavG 302
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 201 LHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDVKIKISAPQ---ERLYSTWIGGSILASLD 277
Cdd:pfam00022 303 IPELIVDAINACDVDLRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVKIIAPGntvERRYSAWIGGSILASLG 382
                         330       340
                  ....*....|....*....|....*
gi 1907068532 278 TFKKMWVSKKEYEEDGSRAIHRKTF 302
Cdd:pfam00022 383 TFQQMWVSKQEYEEHGASVVERKCK 407
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
1-293 1.78e-155

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: 438.72  E-value: 1.78e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532   1 MEHGVVRDWNDMERIWQYVYSkDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTT 80
Cdd:cd10224    66 IEHGIVTNWDDMEKIWHHTFY-NELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTT 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  81 GVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAEFEVVRTIKERACYLSINpqKDEAL 160
Cdd:cd10224   145 GIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALD--FEQEM 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 161 ET-------EKvQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLF 233
Cdd:cd10224   223 QTaasssslEK-SYELPDGQVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMF 301
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 234 KGFGDRLLSEVKKLAPKDVKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDG 293
Cdd:cd10224   302 PGIADRMQKEITALAPSTMKIKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESG 361
PTZ00004 PTZ00004
actin-2; Provisional
1-302 2.41e-140

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 400.68  E-value: 2.41e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532   1 MEHGVVRDWNDMERIWQYVYSkDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTT 80
Cdd:PTZ00004   72 IEHGIVTNWDDMEKIWHHTFY-NELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETHNVPAMYVAIQAVLSLYASGRTT 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  81 GVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAEFEVVRTIKERACYLSINPQK---- 156
Cdd:PTZ00004  151 GIVLDSGDGVSHTVPIYEGYSLPHAIHRLDVAGRDLTEYMMKILHERGTTFTTTAEKEIVRDIKEKLCYIALDFDEemgn 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 157 -DEALETEKVQYTLPDGSTLDVGPARFRAPELLFQPDLVG-DESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFK 234
Cdd:PTZ00004  231 sAGSSDKYEESYELPDGTIITVGSERFRCPEALFQPSLIGkEEPPGIHELTFQSINKCDIDIRKDLYGNIVLSGGTTMYR 310
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907068532 235 GFGDRLLSEVKKLAPKDVKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRKTF 302
Cdd:PTZ00004  311 GLPERLTKELTTLAPSTMKIKVVAPPERKYSVWIGGSILSSLPTFQQMWVTKEEYDESGPSIVHRKCF 378
PTZ00281 PTZ00281
actin; Provisional
1-302 7.37e-129

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 371.73  E-value: 7.37e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532   1 MEHGVVRDWNDMERIWQYVYSkDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTT 80
Cdd:PTZ00281   72 IEHGIVTNWDDMEKIWHHTFY-NELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTT 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  81 GVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAEFEVVRTIKERACYLSINPQKD--- 157
Cdd:PTZ00281  151 GIVMDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEmqt 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 158 ----EALETekvQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLF 233
Cdd:PTZ00281  231 aassSALEK---SYELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMF 307
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907068532 234 KGFGDRLLSEVKKLAPKDVKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRKTF 302
Cdd:PTZ00281  308 PGIADRMNKELTALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIVHRKCF 376
ASKHA_NBD_Arp2 cd10220
nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, ...
1-297 2.99e-128

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: 370.36  E-value: 2.99e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532   1 MEHGVVRDWNDMERIWQYVYsKDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTT 80
Cdd:cd10220    68 MENGIVRNWDDMEHLWDYTF-GEKLKIDPRECKILLTEPPMNPTKNREKMVEVMFEKYGFAGVYVAIQAVLTLYAQGLLT 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  81 GVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYL-RLLLRKeGADFHTSAEFEVVRTIKERACYLSINPQKDE- 158
Cdd:cd10220   147 GVVVDSGDGVTHIVPVYEGFSLPHLTRRLDVAGRDITRYLiKLLLLR-GYAFNRTADFETVREIKEKLCYVAYDIELEQk 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 159 -ALETEKV--QYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKG 235
Cdd:cd10220   226 lALETTVLveSYTLPDGRVIKVGGERFEAPEALFQPHLIDVEGPGIAELLFNTIQAADIDTRPELYKHIVLSGGSTMYPG 305
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907068532 236 FGDRLLSEVKKLAPKDV-----------KIKISAPQERLYSTWIGGSILASL----DTFkkmWVSKKEYEEDGSRAI 297
Cdd:cd10220   306 LPSRLEKEIKQLYLERVlkgdterlskfKIRIEDPPRRKHMVFLGGAVLADImkdkDEF---WITRQEYEEQGVRVL 379
ASKHA_NBD_actin-like cd10169
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ...
9-293 4.16e-126

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: 360.27  E-value: 4.16e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532   9 WNDMERIWQYVYSKdQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGD 88
Cdd:cd10169    26 WDDMEKIWEHVFYN-LLRVDPEEHPVLLTEPPLNPKANREKLAEILFETFNVPSLYIANQAVLSLYASGRTTGLVVDSGE 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  89 GVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAEFEVVRTIKERACylsinpqkdealetekvqyt 168
Cdd:cd10169   105 GVTHIVPVYEGYVLPHAVRRLDIGGRDLTDYLAKLLREKGYSFSTSAEREIVRDIKEKLC-------------------- 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 169 lpdgstldvgparfrapellfqpdlvgdeseGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKKLA 248
Cdd:cd10169   165 -------------------------------GLHELIYDSIMKCDIDLRKELYSNIVLSGGTTLFPGFAERLQKELSKLA 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1907068532 249 PKDVKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDG 293
Cdd:cd10169   214 PSSVKVKVIAPPERKYSAWIGGSILASLSTFQQMWITKEEYEEHG 258
ASKHA_NBD_ACTL7 cd10214
nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ...
1-300 7.20e-119

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: 345.95  E-value: 7.20e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532   1 MEHGVVRDWNDMERIWQYVYSKDqLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTT 80
Cdd:cd10214    69 LRHGIVVDWDCVQDIWEYIFEKE-MKILPEEHAVLVSDPPLSPTTNREKYAELMFETFSIPAMHIAYQSRLSLYSYGRTS 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  81 GVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFhTSAEFEVVRTIKERACYLSINPQKDEAL 160
Cdd:cd10214   148 GLVVESGHGVSYVVPIHEGYNLPHITGRADYAGSDLTAYLMKLLNEAGNKF-TDDQLHIVEDIKKKCCYVALDFEEEMGL 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 161 ETE--KVQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFGD 238
Cdd:cd10214   227 PPQeyTVDYELPDGHLITIGKERFRCPEMLFNPSLIGSKQPGLHTLTMNSLNKCDANLKKDLAKNILLCGGSTMFDGFPD 306
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907068532 239 RLLSEVKKLAPKDVKIKISAPqERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRK 300
Cdd:cd10214   307 RFQKELSKLCPNDNPIVAASP-ERKYSVWTGGSILASLKSFQQLWVRRREYEERGPFVIYRK 367
ASKHA_NBD_Arp4_ACTL6-like cd13395
nucleotide-binding domain (NBD) of the actin-related protein 4 (Arp4)-like subfamily; The ...
1-293 5.33e-115

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: 337.62  E-value: 5.33e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532   1 MEHGVVRDWNDMERIWQYVYsKDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTT 80
Cdd:cd13395    77 LKDGLIEDWDAFEKLWDHAL-KNRLRVDPSEHPLLLTEPSWNTRANREKLTELMFEKYNVPAFFLAKNAVLSAFANGRST 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  81 GVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGAD------------------------------ 130
Cdd:cd13395   156 ALVVDSGATSTSVVPVHDGYVLQKAIVRSPLGGDFLTDQLLKLLESKNIEiiprymikskepveggapakytkkdlpntt 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 131 --FHTSAEFEVVRTIKERACYLSINP-QKDEALETEKVQYTLPDGSTLDVGPARFRAPELLFQPDLV---------GDES 198
Cdd:cd13395   236 ssYHRYMVRRVLQDFKESVCQVSDSPfDESEAASIPTVSYELPDGYNIEFGAERFKIPELLFDPSLVkgipappseGNEL 315
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 199 EGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDVKIKISAPQ---ERLYSTWIGGSILAS 275
Cdd:cd13395   316 LGLPQLVYTSIGSCDVDIRPELYGNVVLTGGNSLLPGFTDRLNRELSEKAPGSLKLKILASGntvERRFSSWIGGSILAS 395
                         330
                  ....*....|....*...
gi 1907068532 276 LDTFKKMWVSKKEYEEDG 293
Cdd:cd13395   396 LGSFQQMWISKQEYEEHG 413
PTZ00452 PTZ00452
actin; Provisional
1-302 1.16e-98

actin; Provisional


Pssm-ID: 185631  Cd Length: 375  Bit Score: 294.74  E-value: 1.16e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532   1 MEHGVVRDWNDMERIWQYVYSkDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTT 80
Cdd:PTZ00452   71 IQNGIINSWDDIEIIWHHAFY-NELCMSPEDQPVFMTDAPMNSKFNRERMTQIMFETFNTPCLYISNEAVLSLYTSGKTI 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  81 GVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAEFEVVRTIKERACYLSINPQKDEAL 160
Cdd:PTZ00452  150 GLVVDSGEGVTHCVPVFEGHQIPQAITKINLAGRLCTDYLTQILQELGYSLTEPHQRIIVKNIKERLCYTALDPQDEKRI 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 161 ----ETEKVQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGF 236
Cdd:PTZ00452  230 ykesNSQDSPYKLPDGNILTIKSQKFRCSEILFQPKLIGLEVAGIHHLAYSSIKKCDLDLRQELCRNIVLSGGTTLFPGI 309
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907068532 237 GDRLLSEVKKLAPKDVKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRKTF 302
Cdd:PTZ00452  310 ANRLSNELTNLVPSQLKIQVAAPPDRRFSAWIGGSIQCTLSTQQPQWIKRQEYDEQGPSIVHRKCF 375
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
1-293 1.64e-95

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: 287.54  E-value: 1.64e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532   1 MEHGVVRDWNDMERIWQYVYSKdQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYA----- 75
Cdd:cd10221    72 IRHGIVEDWDLMERFWEQCIFK-YLRCEPEDHYFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQAVLALAAswtsr 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  76 --TGRT-TGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAEFEVVRTIKERACYLSi 152
Cdd:cd10221   151 kvGERTlTGTVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREEGIPPEDSLEVAKRIKERYCYVC- 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 153 npqKDEALETEK---------VQYTLPDGST-----LDVGPARFRAPELLFQPDLV-GDESEGLHEVLAFAIHKSDMDLR 217
Cdd:cd10221   230 ---PDIVKEFAKydsdpakyiKQYTGINSVTgkpytVDVGYERFLAPEIFFNPEIAsSDFTTPLPEVVDQVIQSCPIDTR 306
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 218 RTLFSNIVLSGGSTLFKGFGDRLLSEVKKL------------------APKDVKIkISAPQERlYSTWIGGSILASLDTF 279
Cdd:cd10221   307 RGLYKNIVLSGGSTMFKDFGRRLQRDVKRIvdarlkaseelsggklkpKPIDVNV-ISHPMQR-YAVWFGGSMLASTPEF 384
                         330
                  ....*....|....
gi 1907068532 280 KKMWVSKKEYEEDG 293
Cdd:cd10221   385 YTVCHTKAEYEEYG 398
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
1-293 2.04e-89

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 272.38  E-value: 2.04e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532   1 MEHGVVRDWNDMERIWQYVYSKdQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYAT---- 76
Cdd:PTZ00280   73 MKHGIVEDWDLMEKFWEQCIFK-YLRCEPEEHYFILTEPPMNPPENREYTAEIMFETFNVKGLYIAVQAVLALRASwtsk 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  77 ------GRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAEFEVVRTIKERACYL 150
Cdd:PTZ00280  152 kakelgGTLTGTVIDSGDGVTHVIPVVDGYVIGSSIKHIPLAGRDITNFIQQMLRERGEPIPAEDILLLAQRIKEKYCYV 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 151 SINPQK-----DEALETEKVQYTLPDGST-----LDVGPARFRAPELLFQPDLV-GDESEGLHEVLAFAIHKSDMDLRRT 219
Cdd:PTZ00280  232 APDIAKefekyDSDPKNHFKKYTAVNSVTkkpytVDVGYERFLGPEMFFHPEIFsSEWTTPLPEVVDDAIQSCPIDCRRP 311
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 220 LFSNIVLSGGSTLFKGFGDRLLSEVKKL------------------APKDVKIkISAPQERlYSTWIGGSILASLDTFKK 281
Cdd:PTZ00280  312 LYKNIVLSGGSTMFKGFDKRLQRDVRKRvdrrlkkaeelsggklkpIPIDVNV-VSHPRQR-YAVWYGGSMLASSPEFEK 389
                         330
                  ....*....|..
gi 1907068532 282 MWVSKKEYEEDG 293
Cdd:PTZ00280  390 VCHTKAEYDEYG 401
ASKHA_NBD_Arp6 cd10210
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ...
1-293 2.77e-73

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: 230.13  E-value: 2.77e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532   1 MEHGVVRDWnDMER-IWQYVYSKDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYA---- 75
Cdd:cd10210    59 FERGYLVNW-DLQRqIWDHLFGKLLLNVDPSDTALVLTEPPFNPPSIQEAMDEIVFEEYGFQSLYRTTAAALSAFAylad 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  76 ------TGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLrlllrKEGADFHT---SAEFEVVRTIKER 146
Cdd:cd10210   138 seqsssSSSQCCLVVDSGFSFTHIVPFFDGKPVKRAVRRIDVGGKLLTNYL-----KEIISYRQlnvMDETYLVNQIKED 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 147 ACYLSIN-------PQKDEALETEKVQYTLPDGST------LDVGPA-----------------RFRAPELLFQPDLVGD 196
Cdd:cd10210   213 LCFVSTDfyedleiAKKKGKENTIRRDYVLPDYTTskrgyvRDPEEPnrgklkedeqvlrlnneRFTVPELLFHPSDIGI 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 197 ESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDVKIKISAPQERLYSTWIGGSILASL 276
Cdd:cd10210   293 QQAGIAEAIVQSINACPEELQPLLYANIVLTGGNALFPGFRERLEAELRSLAPDDYDVNVTLPEDPITYAWEGGSLLAQS 372
                         330
                  ....*....|....*..
gi 1907068532 277 DTFKKMWVSKKEYEEDG 293
Cdd:cd10210   373 PEFEELAVTRAEYEEHG 389
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
2-298 7.17e-62

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: 199.92  E-value: 7.17e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532   2 EHGVVRDWNDMERIWQYVYSKDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTTG 81
Cdd:cd10209    52 RRGRIEDWDALEALLRYVFYTGLGWEEGNEGQVLIAEPLLTSKAERERLTQLMFETFNVSGLYASEQAVLSLYAVGRISG 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  82 VVLDSGDGVTHAVPIYEGfAMPHS-IMRVDIAGRDVSRYLRLLLRKEGAdfHTSAEFEVVRTIKERACYLSINPQKDEA- 159
Cdd:cd10209   132 CVVDVGHGKIDIAPVWEG-AIQHNaVRRFEIGGRDLTELLAAELGKSNP--KVKLDRSIVERLKEAVAWSADDEEAYEKk 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 160 -LETEKVQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFGD 238
Cdd:cd10209   209 vLTCSPETYTLPDGRVISVGKERYCVGEALFRPSILGIEEYGIVEQLVRAVSTSPSENRRQLLENIVLCGGTSSVPGLEA 288
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907068532 239 RLLSEVKKLAPKDVKIKISAPQERL------YSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIH 298
Cdd:cd10209   289 RLQKEIRLLSSPSSRPALVKPPEYMpentlrYSAWIGGAILAKVVFPQNQHVTKADYDETGPSVVH 354
COG5277 COG5277
Actin-related protein [Cytoskeleton];
1-291 7.33e-62

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 201.94  E-value: 7.33e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532   1 MEHGVVR-----DWNDMERIWQYVYSKdQLQTFSEEHP--VLLTEAPLNPSKNREKAAEVFFETF---NVPALFISMQAV 70
Cdd:COG5277    84 LRDGIVRrddedAWRVLKELLRYTFAQ-FLVVDPEFHGflVVVALSALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPL 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  71 LSLYATGRTTGVVLDSGDGVTHAVPIYEGfAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFhTSAEFEVVRTIKERACYL 150
Cdd:COG5277   163 AVAIAEKAVTCVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSD-TAREEYVVRVVKEALGLV 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 151 ------SINPQKDEALETEKVqYTLPDGSTL----DVGPARFRAPELLFQPDLVGDESE--------------------- 199
Cdd:COG5277   241 prdlakAIQKAASNPDSFEAK-VRLPNPTVEielgNYAWERFLIGEILFNPNHEGFESYiqqgrlriedavigdvvlyge 319
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 200 -GLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLF---KGFGD-------RLLSEVKKLAPkDVKIKISAPQERLYSTWI 268
Cdd:COG5277   320 mGLAEAIINSIMKCDVEIQDELYSNIILSGGAFNWsvpPGLEDvavdsvtRVQIELSELAP-ELKVNVRLVSDPQYSVWK 398
                         330       340
                  ....*....|....*....|....*
gi 1907068532 269 GGSILASLDTFKKMW--VSKKEYEE 291
Cdd:COG5277   399 GAIIYGYALPFSVKWswITKEGWYF 423
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
4-300 5.41e-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: 166.33  E-value: 5.41e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532   4 GVVRDWNDMERIWQYVYSK---DQLQTFseEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTT 80
Cdd:cd10208    42 GRVVDWDALEALWRHILFSllsIPRPTN--NSPVLLSVPPSWSKSDLELLTQLFFERLNVPAFAILEAPLAALYAAGATS 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  81 GVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAE------FEVVRTIKEracylsinp 154
Cdd:cd10208   120 GIVVDIGHEKTDITPIVDSQVVPHALVSIPIGGQDCTAHLAQLLKSDEPELKSQAEsgeeatLDLAEALKK--------- 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 155 qkDEALETEKVQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKS-DMDLRRTLFSNIVLSGGSTLF 233
Cdd:cd10208   191 --SPICEVLSDGADLASGTEITVGKERFRACEPLFKPSSLRVDLLIAAIAGALVLNASdEPDKRPALWENIIIVGGGSRI 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 234 KGFGDRLLSEVKKL-----------APKDVKI-KI----SAPQERLY--STWIGGSILASL---DTFKKMWVSKKEYEED 292
Cdd:cd10208   269 RGLKEALLSELQQFhlisetsaspqQPRIIRLaKIpdyfPEWKKSGYeeAAFLGASIVAKLvfnDPSSKHYISKVDYNEK 348

                  ....*...
gi 1907068532 293 GSRAIHRK 300
Cdd:cd10208   349 GPAAIHTK 356
ASKHA_NBD_Arp10 cd10207
nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins; ...
34-294 4.16e-44

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: 154.33  E-value: 4.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  34 VLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAG 113
Cdd:cd10207    75 VVVVESVLCPTPFRETLAKVLFKHFEVPSVLFAPSHLLSLLTLGIRTALVVDCGYRETRVLPVYEGVPLLSAWQSTPLGG 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 114 RDVSRYLRLLLRKEG------------ADFHTSAEFEVVRTIKERACYL-SINPQKDEALETEKVQYTLP---------- 170
Cdd:cd10207   155 KALHKRLKKLLLEHAtvvtgdnkgqllSSVDSLLSEEVLEDIKVRACFVtSLERGKTLQSATEEGSTEEPsppppvdypl 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 171 DGSTLDVGPARFRAP--ELLFQPDlvgDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKKLA 248
Cdd:cd10207   235 DGEKILIVPGSIRESaeELLFEGD---NEEKSLPTLILDSLLKCPIDVRKQLAENIVVIGGTSMLPGFKHRLLEELRALL 311
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907068532 249 PKDV-KIKISAPQERLYST----------WIGGSILASLDTFKKMWVSKKEYEEDGS 294
Cdd:cd10207   312 RKPKyFEELAPKTFRFHTPpsvfkpnylaWLGGSIFGALESILGRSLSREAYLQTGR 368
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
2-293 2.12e-43

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: 151.57  E-value: 2.12e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532   2 EHGVVRDWNDMERIWQYVYSKdqL---QTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGR 78
Cdd:cd10211    63 DRNVVTNFDLQEQILDYIFSH--LginSEGSVDHPIVLTEALCNPNYSRQLMSELLFECYGVPSVAYGIDSLFSYYHNQP 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  79 T----TGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYL-RLLLRKEgaDFHTSA-EFEVVRTIKERACYLSi 152
Cdd:cd10211   141 QgdpsDGLVISSGYSTTHVIPVLNGRLDLSQCKRINLGGFHATDYLqRLLQLKY--PTHPSAiTLSRAEELVHEHCYVA- 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 153 nPQKDEALEtekvqytlpdgstldvgpaRFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTL 232
Cdd:cd10211   218 -EDYDEELK-------------------KWEDPEYYEENVRKIQLPFGLVETIEFVLKRYPAEQQDRLVQNVFLTGGNAL 277
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907068532 233 FKGFGDRLLSEVKKLAPKDVKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDG 293
Cdd:cd10211   278 FPGLKERLEKELRAIRPFGSPFNVVRAKDPVLDAWRGAAKWALDSTFEKVWITKQEYEEKG 338
ASKHA_NBD_AtArp8-like cd13396
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and ...
25-293 1.47e-38

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: 138.45  E-value: 1.47e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  25 LQTFSEEHPVLLTEaPLNPSKNREKAA-----------EVFFEtFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHA 93
Cdd:cd13396    52 MQVKPSRQPVVVSL-PLCHSDDTESAAasrrqlrgtifNVLFD-MNVPAVCAVDQAVLALYAANRTSGIVVNIGFRVTTI 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  94 VPIYEGFAMpHSI--MRVDIAGRDVSRYLRLLLRKEGADFHTsaeFEVVRTIKERACYLSINPQKDEALETEKVQYTLPD 171
Cdd:cd13396   130 VPVYRGRVM-HDIgvEVVGQGALRLTGFLKELMQQNGIRFPS---LYTVRTIKEKLCYVAEDYEAELAKDTQASCEVAGE 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 172 GSTLdVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLR---RTLFSNIVLSGGSTLFKGFGDRLLSEVKKLA 248
Cdd:cd13396   206 GWFT-LSNERFKTGEILFQPGLGGMRAMGLHQAVALCMDHCALVHSqgdDGWFKTIVLSGGSACLPGLSERLERELRKLL 284
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1907068532 249 PKDVK--IKISAPQERLYSTWIGGSILASLDTFKKMW-VSKKEYEEDG 293
Cdd:cd13396   285 PKSLSegIRIIPPPLGPDSAWQGAKLISNLSNFPDGWcITKKQFRNKP 332
ASKHA_NBD_Arp8-like cd10206
nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The ...
10-297 6.19e-29

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


Pssm-ID: 466812 [Multi-domain]  Cd Length: 447  Bit Score: 114.65  E-value: 6.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  10 NDMERIWQYVYSKD---QLQTFSEEHPVLLTeaplnPSK-NREKAAE---VFFETFNVPALFISMQAVLSLYATGRTTGV 82
Cdd:cd10206   162 DDLEDIWSHALEEKleiPRKDLKNYRAVLVI-----PDLfDRRHVKElvdLLLRRLGFSSVFVHQESVCATFGAGLSSAC 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  83 VLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKegADFH-------TSAEFEVVRTIKERACYLS---I 152
Cdd:cd10206   237 VVDIGAQKTSVACVEDGLSIPNSRIRLPYGGDDITRCFLWLLRR--SGFPyrecnlnSPLDFLLLERLKETYCTLDqddI 314
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 153 NPQKDEALETEKVQytlpdgstldvgparfraPELLFQPDLVgdeseGLHEvlafAIHKS-----DMDLRRTLFSNIVLS 227
Cdd:cd10206   315 GVQLHEFYVREPGQ------------------PTLKYQFKLL-----PLDE----AIVQSilscaSDELKRKMYSSILLV 367
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907068532 228 GGSTLFKGFG----DRLLSEVKKL--APKDVKIkISAPQER--LYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAI 297
Cdd:cd10206   368 GGGAKIPGLAealeDRLLIKIPSLfeAVETVEV-LPPPKDMdpSLLAWKGGAVLACLDSAQELWITRKEWQRLGVRAL 444
ASKHA_NBD_ScArp7-like cd10212
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and ...
3-290 1.17e-20

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


Pssm-ID: 466818 [Multi-domain]  Cd Length: 424  Bit Score: 91.32  E-value: 1.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532   3 HGVVRDWNDMERIWQYVYSKdQLQTFSEEHPVLLTEAPLNPSKNR---EKAAEVFFETFNVPALFISMQAVLSLYATGRT 79
Cdd:cd10212    72 QGLPYNWDALEMQWRYLYDT-QLKVSPEELPLVITMPATNGKPDMailERYYELAFDKLNVPVFQIVIEPLAIALSMGKS 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532  80 TGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGR--DVSRYLRLL-LRKEGADFHTSAE-------------------- 136
Cdd:cd10212   151 SAFVIDIGASGCNVTPIIDGIVVKNAVVRSKFGGDflDFQVHERLApLIKEENDMENMADeqkrstdvwyeastwiqqfk 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 137 -----------FEVVRTIKERAcylSINPQKDEALET--EKVQYTLPDGS--------------------TLDVGPArFR 183
Cdd:cd10212   231 stmlqvsekdlFELERYYKEQA---DIYAKQQEQLKQmdQQLQYTALTGSpnnplvqkknflfkplnktlTLDLKEC-YQ 306
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068532 184 APELLFQPDLVGDE---SEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKKLAPKdVKIKISAPQ 260
Cdd:cd10212   307 FAEYLFKPQLISDKfspEDGLGPLMAKSVKKAPEQVYSLLLTNVIITGSTSLIEGMEQRIIKELSIRFPQ-YKLTTFANQ 385
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1907068532 261 ---ERLYSTWIGGSILASLDTFK-KMWVSKKEYE 290
Cdd:cd10212   386 vmmDRKIQGWLGALTMANLPSWSlGKWYSKEDYE 419
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
235-300 2.19e-16

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: 74.25  E-value: 2.19e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907068532 235 GFGDRLLSEVKKLAPKDVKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRK 300
Cdd:NF040575   66 GFYEKLKKSITEKAPKGALIGMTLDPKPESAAWRGAAMYAASEGFVEMAITKQEYDESGPSIVHRK 131
 
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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