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Conserved domains on  [gi|161077869|ref|NP_001097001|]
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Actin-related protein 2, isoform B [Drosophila melanogaster]

Protein Classification

actin family protein( domain architecture ID 12199243)

actin family protein has well-characterized cytoskeletal functions and has also been implicated in nuclear activities

CATH:  3.30.420.40
Gene Ontology:  GO:0031491|GO:0006338
SCOP:  3000092

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ASKHA_NBD_Arp2 cd10220
nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, ...
7-388 0e+00

nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, also called actin-like protein 2, is the ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex is comprised of 7 proteins (Arp2, Arp3, and five conserved proteins, ARPC1-5). It generates cytoplasmic branched filaments networks, by promoting nucleation of actin filaments as 70 degrees branches on the side of older filaments. It is activated, by simultaneously binding to a pre-existing filament and a nucleation promoting factor plus an actin monomer. Daughter branches subsequently detach/debranch from the mother filament. Its Arp2 and Arp3 subunits must be loaded with ATP for it to initiate the assembly of branched actin filaments. ATP hydrolysis may be required for branch initiation or debranching. The Arp2/3 complex is also found in the nucleus where it plays a role in promoting de novo actin polymerization and in RNA polymerase II-dependent transcription. This may in part be through regulating nuclear actin polymerization in a way like its function in the cytoplasm. Human Arp2 is encoded by the ACTR2 gene.


:

Pssm-ID: 466821  Cd Length: 381  Bit Score: 856.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869   7 NVIVCDNGTGFVKCGYAGSNFPTHIFPSMVGRPMIRAVNKIGDIEVKDLMVGDEASQLRSLLEVSYPMENGVVRNWDDMC 86
Cdd:cd10220    1 KVVVCDNGTGFVKCGFAGSNFPEHVFPSLVGRPILRAEEKVGDIEIKDIMVGDEASELRSMLEVTYPMENGIVRNWDDME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  87 HVWDYTFGPKkMDIDPTNTKILLTEPPMNPTKNREKMIEVMFEKYGFDSAYIAIQAVLTLYAQGLISGVVIDSGDGVTHI 166
Cdd:cd10220   81 HLWDYTFGEK-LKIDPRECKILLTEPPMNPTKNREKMVEVMFEKYGFAGVYVAIQAVLTLYAQGLLTGVVVDSGDGVTHI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 167 CPVYEEFALPHLTRRLDIAGRDITRYLIKLLLLRGYAFNHSADFETVRIMKEKLCYIGYDIEMEQRLALETTVLVESYTL 246
Cdd:cd10220  160 VPVYEGFSLPHLTRRLDVAGRDITRYLIKLLLLRGYAFNRTADFETVREIKEKLCYVAYDIELEQKLALETTVLVESYTL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 247 PDGRVIKVGGERFEAPEALFQPHLINVEGPGIAELAFNTIQAADIDIRPELYKHIVLSGGSTMYPGLPSRLEREIKQLYL 326
Cdd:cd10220  240 PDGRVIKVGGERFEAPEALFQPHLIDVEGPGIAELLFNTIQAADIDTRPELYKHIVLSGGSTMYPGLPSRLEKEIKQLYL 319
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161077869 327 ERVLKNDTEKLAKFKIRIEDPPRRKDMVFIGGAVLAEVTKDRDGFWMSKQEYQEQGLKVLQK 388
Cdd:cd10220  320 ERVLKGDTERLSKFKIRIEDPPRRKHMVFLGGAVLADIMKDKDEFWITRQEYEEQGVRVLDK 381
 
Name Accession Description Interval E-value
ASKHA_NBD_Arp2 cd10220
nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, ...
7-388 0e+00

nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, also called actin-like protein 2, is the ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex is comprised of 7 proteins (Arp2, Arp3, and five conserved proteins, ARPC1-5). It generates cytoplasmic branched filaments networks, by promoting nucleation of actin filaments as 70 degrees branches on the side of older filaments. It is activated, by simultaneously binding to a pre-existing filament and a nucleation promoting factor plus an actin monomer. Daughter branches subsequently detach/debranch from the mother filament. Its Arp2 and Arp3 subunits must be loaded with ATP for it to initiate the assembly of branched actin filaments. ATP hydrolysis may be required for branch initiation or debranching. The Arp2/3 complex is also found in the nucleus where it plays a role in promoting de novo actin polymerization and in RNA polymerase II-dependent transcription. This may in part be through regulating nuclear actin polymerization in a way like its function in the cytoplasm. Human Arp2 is encoded by the ACTR2 gene.


Pssm-ID: 466821  Cd Length: 381  Bit Score: 856.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869   7 NVIVCDNGTGFVKCGYAGSNFPTHIFPSMVGRPMIRAVNKIGDIEVKDLMVGDEASQLRSLLEVSYPMENGVVRNWDDMC 86
Cdd:cd10220    1 KVVVCDNGTGFVKCGFAGSNFPEHVFPSLVGRPILRAEEKVGDIEIKDIMVGDEASELRSMLEVTYPMENGIVRNWDDME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  87 HVWDYTFGPKkMDIDPTNTKILLTEPPMNPTKNREKMIEVMFEKYGFDSAYIAIQAVLTLYAQGLISGVVIDSGDGVTHI 166
Cdd:cd10220   81 HLWDYTFGEK-LKIDPRECKILLTEPPMNPTKNREKMVEVMFEKYGFAGVYVAIQAVLTLYAQGLLTGVVVDSGDGVTHI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 167 CPVYEEFALPHLTRRLDIAGRDITRYLIKLLLLRGYAFNHSADFETVRIMKEKLCYIGYDIEMEQRLALETTVLVESYTL 246
Cdd:cd10220  160 VPVYEGFSLPHLTRRLDVAGRDITRYLIKLLLLRGYAFNRTADFETVREIKEKLCYVAYDIELEQKLALETTVLVESYTL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 247 PDGRVIKVGGERFEAPEALFQPHLINVEGPGIAELAFNTIQAADIDIRPELYKHIVLSGGSTMYPGLPSRLEREIKQLYL 326
Cdd:cd10220  240 PDGRVIKVGGERFEAPEALFQPHLIDVEGPGIAELLFNTIQAADIDTRPELYKHIVLSGGSTMYPGLPSRLEKEIKQLYL 319
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161077869 327 ERVLKNDTEKLAKFKIRIEDPPRRKDMVFIGGAVLAEVTKDRDGFWMSKQEYQEQGLKVLQK 388
Cdd:cd10220  320 ERVLKGDTERLSKFKIRIEDPPRRKHMVFLGGAVLADIMKDKDEFWITRQEYEEQGVRVLDK 381
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
6-388 3.26e-177

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 497.94  E-value: 3.26e-177
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869     6 RNVIVCDNGTGFVKCGYAGSNFPTHIFPSMVGRPMIRavnKIGDIEVKDLMVGDEASQLRSLLEVSYPMENGVVRNWDDM 85
Cdd:smart00268   1 VPAIVIDNGSGTIKAGFAGEDFPQVVFPSIVGRPKDG---KGMVGDAKDIFVGDEAQEKRGGLELKYPIENGIVENWDDM 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869    86 CHVWDYTFGpKKMDIDPTNTKILLTEPPMNPTKNREKMIEVMFEKYGFDSAYIAIQAVLTLYAQGLISGVVIDSGDGVTH 165
Cdd:smart00268  78 EKIWDYTFF-NELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTH 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869   166 ICPVYEEFALPHLTRRLDIAGRDITRYLIKLLLLRGYAFNHSADFETVRIMKEKLCYIGYDIEMEQRLALE---TTVLVE 242
Cdd:smart00268 157 VVPVVDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLAREsseSSKLEK 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869   243 SYTLPDGRVIKVGGERFEAPEALFQPHLINVEGPGIAELAFNTIQAADIDIRPELYKHIVLSGGSTMYPGLPSRLEREIK 322
Cdd:smart00268 237 TYELPDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELK 316
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161077869   323 QLYlervlkndtekLAKFKIRIEDPPRRKDMVFIGGAVLAEVTKDRDgFWMSKQEYQEQGLKVLQK 388
Cdd:smart00268 317 QLA-----------PKKLKVKVIAPPERKYSVWLGGSILASLSTFED-MWITKKEYEESGSQIVER 370
PTZ00004 PTZ00004
actin-2; Provisional
6-382 1.68e-136

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 394.91  E-value: 1.68e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869   6 RNVIVCDNGTGFVKCGYAGSNFPTHIFPSMVGRPmiRAVNKIGDIEVKDLMVGDEASQLRSLLEVSYPMENGVVRNWDDM 85
Cdd:PTZ00004   6 TNAAVVDNGSGMVKAGFAGDDAPRCVFPSIVGRP--KNPGIMVGMEEKDCYVGDEAQDKRGILTLKYPIEHGIVTNWDDM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  86 CHVWDYTFgPKKMDIDPTNTKILLTEPPMNPTKNREKMIEVMFEKYGFDSAYIAIQAVLTLYAQGLISGVVIDSGDGVTH 165
Cdd:PTZ00004  84 EKIWHHTF-YNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETHNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSH 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 166 ICPVYEEFALPHLTRRLDIAGRDITRYLIKLLLLRGYAFNHSADFETVRIMKEKLCYIGYDIEMEQRLALETT-VLVESY 244
Cdd:PTZ00004 163 TVPIYEGYSLPHAIHRLDVAGRDLTEYMMKILHERGTTFTTTAEKEIVRDIKEKLCYIALDFDEEMGNSAGSSdKYEESY 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 245 TLPDGRVIKVGGERFEAPEALFQPHLINVEGP-GIAELAFNTIQAADIDIRPELYKHIVLSGGSTMYPGLPSRLEREIKQ 323
Cdd:PTZ00004 243 ELPDGTIITVGSERFRCPEALFQPSLIGKEEPpGIHELTFQSINKCDIDIRKDLYGNIVLSGGTTMYRGLPERLTKELTT 322
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 161077869 324 LylervlkndteKLAKFKIRIEDPPRRKDMVFIGGAVLAEVTKDRDgFWMSKQEYQEQG 382
Cdd:PTZ00004 323 L-----------APSTMKIKVVAPPERKYSVWIGGSILSSLPTFQQ-MWVTKEEYDESG 369
Actin pfam00022
Actin;
7-388 8.68e-117

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 345.83  E-value: 8.68e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869    7 NVIVCDNGTGFVKCGYAGSNFPTHIFPSMVGRPMIRAVNKIGDIEVkdlmvGDEASQLRSLLEVSYPMENGVVRNWDDMC 86
Cdd:pfam00022   2 SALVIDNGSHTTRAGFAGEDAPKAVIPSCVGKPRGTKVEAANKYYV-----GDEALTYRPGMEVRSPVEDGIVVDWDAME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869   87 HVWDYTFGpKKMDIDPTNTKILLTEPPMNPTKNREKMIEVMFEKYGFDSAYIAIQAVLTLYAQGLISGVVIDSGDGVTHI 166
Cdd:pfam00022  77 EIWEHVLK-EELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  167 CPVYEEFALPHLTRRLDIAGRDITRYLIKLLLLR------------------------------GYAFNHSADFETVRIM 216
Cdd:pfam00022 156 VPVHDGYVLQKAIRRSDLGGDFLTDYLRELLRSRnieitprylikskkpgdpapavtkrelpdtTYSYKTYQERRVLEEI 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  217 KEKLCYIGYDIEMeqRLALETTVLVESYTLPDGRVIKVGGERFEAPEALFQPHLINVEGP--------GIAELAFNTIQA 288
Cdd:pfam00022 236 KESVCYVSDDPFG--DETTSSSIPTRVYELPDGSTIILGAERFRVPEILFNPSLIGSESElpppqtavGIPELIVDAINA 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  289 ADIDIRPELYKHIVLSGGSTMYPGLPSRLEREIKQLYlervlkndtekLAKFKIRI---EDPPRRKDMVFIGGAVLAEvt 365
Cdd:pfam00022 314 CDVDLRPSLLANIVVTGGNSLFPGFTERLEKELAQLA-----------PPGVKVKIiapGNTVERRYSAWIGGSILAS-- 380
                         410       420
                  ....*....|....*....|....*.
gi 161077869  366 kdRDGF---WMSKQEYQEQGLKVLQK 388
Cdd:pfam00022 381 --LGTFqqmWVSKQEYEEHGASVVER 404
COG5277 COG5277
Actin-related protein [Cytoskeleton];
8-380 3.50e-61

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 203.10  E-value: 3.50e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869   8 VIVCDNGTGFVKCG-YAGSNFPTHI-----FPSMVGRPMIRAVNKIGDievKDLMVGDEASQ-LRSLLEVS----YPMEN 76
Cdd:COG5277   10 VIGIDFGTSYVKYGpIALEEKPRVIqtrglFLRIVGESKLLGPMEGLS---RGLVVGDEVSKyLSSVRDAIrnlkYPLRD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  77 GVVR-----NWDDMCHVWDYTFGPKK-MDIDPTNTKILLTEPPMNPTKNREKMIEVMFEK---YGFDSAYIAIQAVLTLY 147
Cdd:COG5277   87 GIVRrddedAWRVLKELLRYTFAQFLvVDPEFHGFLVVVALSALAPDYMRERLFDIHFEVfseEGAPAVTIIPQPLAVAI 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 148 AQGLISGVVIDSGDGVTHICPVYEEfALPHLTRRLDIAGRDITRYLIKLLLLRGYAFNHSADfETVRIMKEKLCYIGYDI 227
Cdd:COG5277  167 AEKAVTCVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSDTAREE-YVVRVVKEALGLVPRDL 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 228 EMEQRLAL-ETTVLVESYTLPDGRVIKVGGE----RFEAPEALFQPHLINVEG----------------------PGIAE 280
Cdd:COG5277  245 AKAIQKAAsNPDSFEAKVRLPNPTVEIELGNyaweRFLIGEILFNPNHEGFESyiqqgrlriedavigdvvlygeMGLAE 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 281 LAFNTIQAADIDIRPELYKHIVLSGGSTMY---PGL-------PSRLEREIKQLYLErvlkndteklAKFKIRIedPPRR 350
Cdd:COG5277  325 AIINSIMKCDVEIQDELYSNIILSGGAFNWsvpPGLedvavdsVTRVQIELSELAPE----------LKVNVRL--VSDP 392
                        410       420       430
                 ....*....|....*....|....*....|.
gi 161077869 351 KDMVFIGGAVLA-EVTKDRDGFWMSKQEYQE 380
Cdd:COG5277  393 QYSVWKGAIIYGyALPFSVKWSWITKEGWYF 423
 
Name Accession Description Interval E-value
ASKHA_NBD_Arp2 cd10220
nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, ...
7-388 0e+00

nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, also called actin-like protein 2, is the ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex is comprised of 7 proteins (Arp2, Arp3, and five conserved proteins, ARPC1-5). It generates cytoplasmic branched filaments networks, by promoting nucleation of actin filaments as 70 degrees branches on the side of older filaments. It is activated, by simultaneously binding to a pre-existing filament and a nucleation promoting factor plus an actin monomer. Daughter branches subsequently detach/debranch from the mother filament. Its Arp2 and Arp3 subunits must be loaded with ATP for it to initiate the assembly of branched actin filaments. ATP hydrolysis may be required for branch initiation or debranching. The Arp2/3 complex is also found in the nucleus where it plays a role in promoting de novo actin polymerization and in RNA polymerase II-dependent transcription. This may in part be through regulating nuclear actin polymerization in a way like its function in the cytoplasm. Human Arp2 is encoded by the ACTR2 gene.


Pssm-ID: 466821  Cd Length: 381  Bit Score: 856.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869   7 NVIVCDNGTGFVKCGYAGSNFPTHIFPSMVGRPMIRAVNKIGDIEVKDLMVGDEASQLRSLLEVSYPMENGVVRNWDDMC 86
Cdd:cd10220    1 KVVVCDNGTGFVKCGFAGSNFPEHVFPSLVGRPILRAEEKVGDIEIKDIMVGDEASELRSMLEVTYPMENGIVRNWDDME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  87 HVWDYTFGPKkMDIDPTNTKILLTEPPMNPTKNREKMIEVMFEKYGFDSAYIAIQAVLTLYAQGLISGVVIDSGDGVTHI 166
Cdd:cd10220   81 HLWDYTFGEK-LKIDPRECKILLTEPPMNPTKNREKMVEVMFEKYGFAGVYVAIQAVLTLYAQGLLTGVVVDSGDGVTHI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 167 CPVYEEFALPHLTRRLDIAGRDITRYLIKLLLLRGYAFNHSADFETVRIMKEKLCYIGYDIEMEQRLALETTVLVESYTL 246
Cdd:cd10220  160 VPVYEGFSLPHLTRRLDVAGRDITRYLIKLLLLRGYAFNRTADFETVREIKEKLCYVAYDIELEQKLALETTVLVESYTL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 247 PDGRVIKVGGERFEAPEALFQPHLINVEGPGIAELAFNTIQAADIDIRPELYKHIVLSGGSTMYPGLPSRLEREIKQLYL 326
Cdd:cd10220  240 PDGRVIKVGGERFEAPEALFQPHLIDVEGPGIAELLFNTIQAADIDTRPELYKHIVLSGGSTMYPGLPSRLEKEIKQLYL 319
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161077869 327 ERVLKNDTEKLAKFKIRIEDPPRRKDMVFIGGAVLAEVTKDRDGFWMSKQEYQEQGLKVLQK 388
Cdd:cd10220  320 ERVLKGDTERLSKFKIRIEDPPRRKHMVFLGGAVLADIMKDKDEFWITRQEYEEQGVRVLDK 381
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
6-388 3.26e-177

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 497.94  E-value: 3.26e-177
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869     6 RNVIVCDNGTGFVKCGYAGSNFPTHIFPSMVGRPMIRavnKIGDIEVKDLMVGDEASQLRSLLEVSYPMENGVVRNWDDM 85
Cdd:smart00268   1 VPAIVIDNGSGTIKAGFAGEDFPQVVFPSIVGRPKDG---KGMVGDAKDIFVGDEAQEKRGGLELKYPIENGIVENWDDM 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869    86 CHVWDYTFGpKKMDIDPTNTKILLTEPPMNPTKNREKMIEVMFEKYGFDSAYIAIQAVLTLYAQGLISGVVIDSGDGVTH 165
Cdd:smart00268  78 EKIWDYTFF-NELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTH 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869   166 ICPVYEEFALPHLTRRLDIAGRDITRYLIKLLLLRGYAFNHSADFETVRIMKEKLCYIGYDIEMEQRLALE---TTVLVE 242
Cdd:smart00268 157 VVPVVDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLAREsseSSKLEK 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869   243 SYTLPDGRVIKVGGERFEAPEALFQPHLINVEGPGIAELAFNTIQAADIDIRPELYKHIVLSGGSTMYPGLPSRLEREIK 322
Cdd:smart00268 237 TYELPDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELK 316
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161077869   323 QLYlervlkndtekLAKFKIRIEDPPRRKDMVFIGGAVLAEVTKDRDgFWMSKQEYQEQGLKVLQK 388
Cdd:smart00268 317 QLA-----------PKKLKVKVIAPPERKYSVWLGGSILASLSTFED-MWITKKEYEESGSQIVER 370
ASKHA_NBD_actin_Arp-T1-3 cd13397
nucleotide-binding domain (NBD) of actin, actin-related proteins T1-T3 (Arp-T1-3), and similar ...
8-382 1.15e-166

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: 470.52  E-value: 1.15e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869   8 VIVCDNGTGFVKCGYAGSNFPTHIFPSMVGRPMIRAVnkIGDIEVKDLMVGDEASQLRSLLEVSYPMENGVVRNWDDMCH 87
Cdd:cd13397    2 AVVIDNGSGLIKAGFAGEDLPRAVFPSVVGRPKYKAV--MLGAGQKEVYVGDEAQEKRGVLTLSYPIEHGIVTNWDDMEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  88 VWDYTFgPKKMDIDPTNTKILLTEPPMNPTKNREKMIEVMFEKYGFDSAYIAIQAVLTLYAQGLISGVVIDSGDGVTHIC 167
Cdd:cd13397   80 IWHHTF-ENELRVKPEEHPVLLTEAPLNPKQNREKMAEIMFETFGVPAFYVAIQAVLSLYSSGRTTGLVLDSGDGVTHTV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 168 PVYEEFALPHLTRRLDIAGRDITRYLIKLLLLRGYAFNHSADFETVRIMKEKLCYIGYDIEMEqrLALETTVLVESYTLP 247
Cdd:cd13397  159 PIYEGYALPHAVQRLDLAGRDLTEYLMKLLKERGHSFTTTAEREIVRDIKEKLCYVALDYEEE--LKKKSEELEKEYTLP 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 248 DGRVIKVGGERFEAPEALFQPHLINVEGPGIAELAFNTIQAADIDIRPELYKHIVLSGGSTMYPGLPSRLEREIKQLYLE 327
Cdd:cd13397  237 DGQVIKIGSERFRCPEALFRPSLIGREAPGIHKLVYNSIMKCDIDIRKDLYSNIVLSGGSTMFPGLPERLQKELEALAPS 316
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 161077869 328 RVlkndteklakfKIRIEDPPRRKDMVFIGGAVLAEVTKdRDGFWMSKQEYQEQG 382
Cdd:cd13397  317 ST-----------KVKVIAPPERKYSVWIGGSILASLST-FKSMWITRAEYDEFG 359
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
9-382 1.05e-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: 442.96  E-value: 1.05e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869   9 IVCDNGTGFVKCGYAGSNFPTHIFPSMVGRPMIRAVNkIGdIEVKDLMVGDEASQLRSLLEVSYPMENGVVRNWDDMCHV 88
Cdd:cd10224    3 LVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVM-VG-MGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  89 WDYTFgPKKMDIDPTNTKILLTEPPMNPTKNREKMIEVMFEKYGFDSAYIAIQAVLTLYAQGLISGVVIDSGDGVTHICP 168
Cdd:cd10224   81 WHHTF-YNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 169 VYEEFALPHLTRRLDIAGRDITRYLIKLLLLRGYAFNHSADFETVRIMKEKLCYIGYDIEMEQRLALETTVLVESYTLPD 248
Cdd:cd10224  160 IYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 249 GRVIKVGGERFEAPEALFQPHLINVEGPGIAELAFNTIQAADIDIRPELYKHIVLSGGSTMYPGLPSRLEREIKQLyler 328
Cdd:cd10224  240 GQVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITAL---- 315
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 161077869 329 vlkndteKLAKFKIRIEDPPRRKDMVFIGGAVLAEVTKDRDgFWMSKQEYQEQG 382
Cdd:cd10224  316 -------APSTMKIKIVAPPERKYSVWIGGSILASLSTFQQ-MWISKQEYDESG 361
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
9-388 2.77e-149

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: 426.96  E-value: 2.77e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869   9 IVCDNGTGFVKCGYAGSNFPTHIFPSMVGRPMIRAVnKIGDIEvKDLMVGDEASQLRSLLEVSYPMENGVVRNWDDMCHV 88
Cdd:cd10216    4 VVIDNGSGVIKAGFAGDDIPKVVFPSYVGRPKHVRV-MAGALE-GDVFVGPKAEEHRGLLKIRYPMEHGIVTDWNDMERI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  89 WDYTFGPKKMDIDPTNTKILLTEPPMNPTKNREKMIEVMFEKYGFDSAYIAIQAVLTLYAQGLISGVVIDSGDGVTHICP 168
Cdd:cd10216   82 WQYVYSKLQLNTFSEEHPVLLTEAPLNPRKNREKAAEVFFETFNVPALFVSMQAVLSLYASGRTTGVVLDSGDGVTHAVP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 169 VYEEFALPHLTRRLDIAGRDITRYLIKLLLLRGYAFNHSADFETVRIMKEKLCYIGYDIEMEQRLALETTVLVeSYTLPD 248
Cdd:cd10216  162 IYEGFALPHSIRRVDIAGRDVTEYLQLLLRKSGYNFHTSAEFEIVREIKEKACYVALNPQKEEKLEEEKTEKA-QYTLPD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 249 GRVIKVGGERFEAPEALFQPHLINVEGPGIAELAFNTIQAADIDIRPELYKHIVLSGGSTMYPGLPSRLEREIKqlyleR 328
Cdd:cd10216  241 GSTIEIGPERFRAPEILFNPELIGLEYPGVHEVLVDSIQKSDLDLRKTLYSNIVLSGGSTLFKGFGDRLLSEVK-----K 315
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 329 VLKNDTeklakfKIRIEDPPRRKDMVFIGGAVLAEVTKDRDgFWMSKQEYQEQGLKVLQK 388
Cdd:cd10216  316 LAPKDV------KIRISAPPERLYSTWIGGSILASLSTFKK-MWVSKKEYEEDGARILHR 368
PTZ00004 PTZ00004
actin-2; Provisional
6-382 1.68e-136

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 394.91  E-value: 1.68e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869   6 RNVIVCDNGTGFVKCGYAGSNFPTHIFPSMVGRPmiRAVNKIGDIEVKDLMVGDEASQLRSLLEVSYPMENGVVRNWDDM 85
Cdd:PTZ00004   6 TNAAVVDNGSGMVKAGFAGDDAPRCVFPSIVGRP--KNPGIMVGMEEKDCYVGDEAQDKRGILTLKYPIEHGIVTNWDDM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  86 CHVWDYTFgPKKMDIDPTNTKILLTEPPMNPTKNREKMIEVMFEKYGFDSAYIAIQAVLTLYAQGLISGVVIDSGDGVTH 165
Cdd:PTZ00004  84 EKIWHHTF-YNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETHNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSH 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 166 ICPVYEEFALPHLTRRLDIAGRDITRYLIKLLLLRGYAFNHSADFETVRIMKEKLCYIGYDIEMEQRLALETT-VLVESY 244
Cdd:PTZ00004 163 TVPIYEGYSLPHAIHRLDVAGRDLTEYMMKILHERGTTFTTTAEKEIVRDIKEKLCYIALDFDEEMGNSAGSSdKYEESY 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 245 TLPDGRVIKVGGERFEAPEALFQPHLINVEGP-GIAELAFNTIQAADIDIRPELYKHIVLSGGSTMYPGLPSRLEREIKQ 323
Cdd:PTZ00004 243 ELPDGTIITVGSERFRCPEALFQPSLIGKEEPpGIHELTFQSINKCDIDIRKDLYGNIVLSGGTTMYRGLPERLTKELTT 322
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 161077869 324 LylervlkndteKLAKFKIRIEDPPRRKDMVFIGGAVLAEVTKDRDgFWMSKQEYQEQG 382
Cdd:PTZ00004 323 L-----------APSTMKIKVVAPPERKYSVWIGGSILSSLPTFQQ-MWVTKEEYDESG 369
PTZ00281 PTZ00281
actin; Provisional
1-388 1.09e-127

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 372.50  E-value: 1.09e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869   1 MDSKGRNVIVCDNGTGFVKCGYAGSNFPTHIFPSMVGRPmiRAVNKIGDIEVKDLMVGDEASQLRSLLEVSYPMENGVVR 80
Cdd:PTZ00281   1 MDGEDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRP--RHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  81 NWDDMCHVWDYTFgPKKMDIDPTNTKILLTEPPMNPTKNREKMIEVMFEKYGFDSAYIAIQAVLTLYAQGLISGVVIDSG 160
Cdd:PTZ00281  79 NWDDMEKIWHHTF-YNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 161 DGVTHICPVYEEFALPHLTRRLDIAGRDITRYLIKLLLLRGYAFNHSADFETVRIMKEKLCYIGYDIEMEQRLALETTVL 240
Cdd:PTZ00281 158 DGVSHTVPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEMQTAASSSAL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 241 VESYTLPDGRVIKVGGERFEAPEALFQPHLINVEGPGIAELAFNTIQAADIDIRPELYKHIVLSGGSTMYPGLPSRLERE 320
Cdd:PTZ00281 238 EKSYELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKE 317
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161077869 321 IKQLylervlkndteKLAKFKIRIEDPPRRKDMVFIGGAVLAEVTKDRDgFWMSKQEYQEQGLKVLQK 388
Cdd:PTZ00281 318 LTAL-----------APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQ-MWISKEEYDESGPSIVHR 373
PTZ00466 PTZ00466
actin-like protein; Provisional
9-388 9.80e-120

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 352.32  E-value: 9.80e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869   9 IVCDNGTGFVKCGYAGSNFPTHIFPSMVGRPMIRAVnKIGDIEvKDLMVGDEASQLRSLLEVSYPMENGVVRNWDDMCHV 88
Cdd:PTZ00466  15 IIIDNGTGYIKAGFAGEDVPNLVFPSYVGRPKYKRV-MAGAVE-GNIFVGNKAEEYRGLLKVTYPINHGIIENWNDMENI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  89 WDYTFgpKKMDIDPTNTKILLTEPPMNPTKNREKMIEVMFEKYGFDSAYIAIQAVLTLYAQGLISGVVIDSGDGVTHICP 168
Cdd:PTZ00466  93 WIHVY--NSMKINSEEHPVLLTEAPLNPQKNKEKIAEVFFETFNVPALFISIQAILSLYSCGKTNGTVLDCGDGVCHCVS 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 169 VYEEFALPHLTRRLDIAGRDITRYLIKLLLLRGYAFNHSADFETVRIMKEKLCYIGYDIEMEQRLAlETTVLVESYTLPD 248
Cdd:PTZ00466 171 IYEGYSITNTITRTDVAGRDITTYLGYLLRKNGHLFNTSAEMEVVKNMKENCCYVSFNMNKEKNSS-EKALTTLPYILPD 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 249 GRVIKVGGERFEAPEALFQPHLINVEGPGIAELAFNTIQAADIDIRPELYKHIVLSGGSTMYPGLPSRLEREIKQLYLER 328
Cdd:PTZ00466 250 GSQILIGSERYRAPEVLFNPSILGLEYLGLSELIVTSITRADMDLRRTLYSHIVLSGGTTMFHGFGDRLLNEIRKFAPKD 329
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 329 VlkndteklakfKIRIEDPPRRKDMVFIGGAVLAEVTKDRDgFWMSKQEYQEQGLKVLQK 388
Cdd:PTZ00466 330 I-----------TIRISAPPERKFSTFIGGSILASLATFKK-IWISKQEFDEYGSVILHR 377
Actin pfam00022
Actin;
7-388 8.68e-117

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 345.83  E-value: 8.68e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869    7 NVIVCDNGTGFVKCGYAGSNFPTHIFPSMVGRPMIRAVNKIGDIEVkdlmvGDEASQLRSLLEVSYPMENGVVRNWDDMC 86
Cdd:pfam00022   2 SALVIDNGSHTTRAGFAGEDAPKAVIPSCVGKPRGTKVEAANKYYV-----GDEALTYRPGMEVRSPVEDGIVVDWDAME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869   87 HVWDYTFGpKKMDIDPTNTKILLTEPPMNPTKNREKMIEVMFEKYGFDSAYIAIQAVLTLYAQGLISGVVIDSGDGVTHI 166
Cdd:pfam00022  77 EIWEHVLK-EELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  167 CPVYEEFALPHLTRRLDIAGRDITRYLIKLLLLR------------------------------GYAFNHSADFETVRIM 216
Cdd:pfam00022 156 VPVHDGYVLQKAIRRSDLGGDFLTDYLRELLRSRnieitprylikskkpgdpapavtkrelpdtTYSYKTYQERRVLEEI 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  217 KEKLCYIGYDIEMeqRLALETTVLVESYTLPDGRVIKVGGERFEAPEALFQPHLINVEGP--------GIAELAFNTIQA 288
Cdd:pfam00022 236 KESVCYVSDDPFG--DETTSSSIPTRVYELPDGSTIILGAERFRVPEILFNPSLIGSESElpppqtavGIPELIVDAINA 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  289 ADIDIRPELYKHIVLSGGSTMYPGLPSRLEREIKQLYlervlkndtekLAKFKIRI---EDPPRRKDMVFIGGAVLAEvt 365
Cdd:pfam00022 314 CDVDLRPSLLANIVVTGGNSLFPGFTERLEKELAQLA-----------PPGVKVKIiapGNTVERRYSAWIGGSILAS-- 380
                         410       420
                  ....*....|....*....|....*.
gi 161077869  366 kdRDGF---WMSKQEYQEQGLKVLQK 388
Cdd:pfam00022 381 --LGTFqqmWVSKQEYEEHGASVVER 404
ASKHA_NBD_actin-like cd10169
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ...
9-382 8.89e-107

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: 314.81  E-value: 8.89e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869   9 IVCDNGTGFVKCGYAGSNFPTHIFPsmvgrpmiravnkigdievkdlmvgdeasqlrsllevsypmengvvrnWDDMCHV 88
Cdd:cd10169    1 IVIDNGSGTIKAGFAGEDAPRLIFP------------------------------------------------WDDMEKI 32
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  89 WDYTFGpKKMDIDPTNTKILLTEPPMNPTKNREKMIEVMFEKYGFDSAYIAIQAVLTLYAQGLISGVVIDSGDGVTHICP 168
Cdd:cd10169   33 WEHVFY-NLLRVDPEEHPVLLTEPPLNPKANREKLAEILFETFNVPSLYIANQAVLSLYASGRTTGLVVDSGEGVTHIVP 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 169 VYEEFALPHLTRRLDIAGRDITRYLIKLLLLRGYAFNHSADFETVRIMKEKLCyigydiemeqrlalettvlvesytlpd 248
Cdd:cd10169  112 VYEGYVLPHAVRRLDIGGRDLTDYLAKLLREKGYSFSTSAEREIVRDIKEKLC--------------------------- 164
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 249 grvikvggerfeapealfqphlinvegpGIAELAFNTIQAADIDIRPELYKHIVLSGGSTMYPGLPSRLEREIKQLYLER 328
Cdd:cd10169  165 ----------------------------GLHELIYDSIMKCDIDLRKELYSNIVLSGGTTLFPGFAERLQKELSKLAPSS 216
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 161077869 329 VlkndteklakfKIRIEDPPRRKDMVFIGGAVLAEVTKDRDgFWMSKQEYQEQG 382
Cdd:cd10169  217 V-----------KVKVIAPPERKYSAWIGGSILASLSTFQQ-MWITKEEYEEHG 258
ASKHA_NBD_ACTL7 cd10214
nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ...
4-382 1.64e-105

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: 315.52  E-value: 1.64e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869   4 KGRNVIVcDNGTGFVKCGYAGSNFPTHIFPSMVGRPMIRAVnKIGDiEVKDLMVGDEASQLRSLLEVSYPMENGVVRNWD 83
Cdd:cd10214    2 ETKAVII-DLGTGYCKAGFAGQPRPSYVISSTVGKPPQESA-KTGD-NRKETFVGKELANVEPPLKLVNPLRHGIVVDWD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  84 DMCHVWDYTFgPKKMDIDPTNTKILLTEPPMNPTKNREKMIEVMFEKYGFDSAYIAIQAVLTLYAQGLISGVVIDSGDGV 163
Cdd:cd10214   79 CVQDIWEYIF-EKEMKILPEEHAVLVSDPPLSPTTNREKYAELMFETFSIPAMHIAYQSRLSLYSYGRTSGLVVESGHGV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 164 THICPVYEEFALPHLTRRLDIAGRDITRYLIKLLLLRGYAFNHSaDFETVRIMKEKLCYIGYDIEMEQRLAL-ETTVlve 242
Cdd:cd10214  158 SYVVPIHEGYNLPHITGRADYAGSDLTAYLMKLLNEAGNKFTDD-QLHIVEDIKKKCCYVALDFEEEMGLPPqEYTV--- 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 243 SYTLPDGRVIKVGGERFEAPEALFQPHLINVEGPGIAELAFNTIQAADIDIRPELYKHIVLSGGSTMYPGLPSRLEREik 322
Cdd:cd10214  234 DYELPDGHLITIGKERFRCPEMLFNPSLIGSKQPGLHTLTMNSLNKCDANLKKDLAKNILLCGGSTMFDGFPDRFQKE-- 311
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 323 qlyLERVLKNDTEKLAKfkiriedPPRRKDMVFIGGAVLAEVtKDRDGFWMSKQEYQEQG 382
Cdd:cd10214  312 ---LSKLCPNDNPIVAA-------SPERKYSVWTGGSILASL-KSFQQLWVRRREYEERG 360
PTZ00452 PTZ00452
actin; Provisional
9-388 3.60e-92

actin; Provisional


Pssm-ID: 185631  Cd Length: 375  Bit Score: 281.64  E-value: 3.60e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869   9 IVCDNGTGFVKCGYAGSNFPTHIFPSMVGRPmiRAVNKIGDIEVKDLMVGDEASQLRSLLEVSYPMENGVVRNWDDMCHV 88
Cdd:PTZ00452   8 VVIDNGSGYCKIGIAGDDAPTSCFPAIVGRS--KQNDGIFSTFNKEYYVGEEAQAKRGVLAIKEPIQNGIINSWDDIEII 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  89 WDYTFgPKKMDIDPTNTKILLTEPPMNPTKNREKMIEVMFEKYGFDSAYIAIQAVLTLYAQGLISGVVIDSGDGVTHICP 168
Cdd:PTZ00452  86 WHHAF-YNELCMSPEDQPVFMTDAPMNSKFNRERMTQIMFETFNTPCLYISNEAVLSLYTSGKTIGLVVDSGEGVTHCVP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 169 VYEEFALPHLTRRLDIAGRDITRYLIKLLLLRGYAFNHSADFETVRIMKEKLCYIGYDIEMEQRLALETTVLVESYTLPD 248
Cdd:PTZ00452 165 VFEGHQIPQAITKINLAGRLCTDYLTQILQELGYSLTEPHQRIIVKNIKERLCYTALDPQDEKRIYKESNSQDSPYKLPD 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 249 GRVIKVGGERFEAPEALFQPHLINVEGPGIAELAFNTIQAADIDIRPELYKHIVLSGGSTMYPGLPSRLEREIKQLYler 328
Cdd:PTZ00452 245 GNILTIKSQKFRCSEILFQPKLIGLEVAGIHHLAYSSIKKCDLDLRQELCRNIVLSGGTTLFPGIANRLSNELTNLV--- 321
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 329 vlkndtekLAKFKIRIEDPPRRKDMVFIGGAVLAEVTKDRDGfWMSKQEYQEQGLKVLQK 388
Cdd:PTZ00452 322 --------PSQLKIQVAAPPDRRFSAWIGGSIQCTLSTQQPQ-WIKRQEYDEQGPSIVHR 372
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
8-382 3.69e-88

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: 272.52  E-value: 3.69e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869   8 VIVCDNGTGFVKCGYAGSNFPTHIFPS--------MVGRPMIRAVNKIGDIevkDLMVGDEASQLRSLLEVSYPMENGVV 79
Cdd:cd10221    1 AVVIDNGTGYTKMGYAGNTEPQFIIPTviaikesaKVGDGQRRSKKGIEDL---DFYIGDEALANSPTYALKYPIRHGIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  80 RNWDDMCHVWDYTFGpKKMDIDPTNTKILLTEPPMNPTKNREKMIEVMFEKYGFDSAYIAIQAVLTLYA--------QGL 151
Cdd:cd10221   78 EDWDLMERFWEQCIF-KYLRCEPEDHYFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQAVLALAAswtsrkvgERT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 152 ISGVVIDSGDGVTHICPVYEEFALPHLTRRLDIAGRDITRYLIKLLLLRGYAFNHSADFETVRIMKEKLCYIGYDIEME- 230
Cdd:cd10221  157 LTGTVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREEGIPPEDSLEVAKRIKERYCYVCPDIVKEf 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 231 QRLALETTVLVESYTLPDGR-----VIKVGGERFEAPEALFQPHLINVEG-PGIAELAFNTIQAADIDIRPELYKHIVLS 304
Cdd:cd10221  237 AKYDSDPAKYIKQYTGINSVtgkpyTVDVGYERFLAPEIFFNPEIASSDFtTPLPEVVDQVIQSCPIDTRRGLYKNIVLS 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 305 GGSTMYPGLPSRLEREIKQLYLERVLKNdtEKLAKFKIR---IE----DPPRRKDMVFIGGAVLAEvTKDRDGFWMSKQE 377
Cdd:cd10221  317 GGSTMFKDFGRRLQRDVKRIVDARLKAS--EELSGGKLKpkpIDvnviSHPMQRYAVWFGGSMLAS-TPEFYTVCHTKAE 393

                 ....*
gi 161077869 378 YQEQG 382
Cdd:cd10221  394 YEEYG 398
ASKHA_NBD_Arp4_ACTL6-like cd13395
nucleotide-binding domain (NBD) of the actin-related protein 4 (Arp4)-like subfamily; The ...
9-382 5.95e-87

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: 269.44  E-value: 5.95e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869   9 IVCDNGTGFVKCGYAGSNFPTHIFPSMVG-RPMIRAVNKIGDIEVKD---LMVGDEASQL-RSLLEVSYPMENGVVRNWD 83
Cdd:cd13395    7 LVLDIGSYSTRAGYAGEDTPKAVFPSVVGvVTDDDDAEDYVGGSGEKkrkYYIGTNSIGVpRPNMEVISPLKDGLIEDWD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  84 DMCHVWDYTFGpKKMDIDPTNTKILLTEPPMNPTKNREKMIEVMFEKYGFDSAYIAIQAVLTLYAQGLISGVVIDSGDGV 163
Cdd:cd13395   87 AFEKLWDHALK-NRLRVDPSEHPLLLTEPSWNTRANREKLTELMFEKYNVPAFFLAKNAVLSAFANGRSTALVVDSGATS 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 164 THICPVYEEFALPHLTRRLDIAGRDITRYLIKLLLLRGYAFNHSADF--ETVRIMKEKLCYIGYDIE---------MEQR 232
Cdd:cd13395  166 TSVVPVHDGYVLQKAIVRSPLGGDFLTDQLLKLLESKNIEIIPRYMIksKEPVEGGAPAKYTKKDLPnttssyhryMVRR 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 233 LA------------------LETTVLVESYTLPDGRVIKVGGERFEAPEALFQPHLINVEGP---------GIAELAFNT 285
Cdd:cd13395  246 VLqdfkesvcqvsdspfdesEAASIPTVSYELPDGYNIEFGAERFKIPELLFDPSLVKGIPAppsegnellGLPQLVYTS 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 286 IQAADIDIRPELYKHIVLSGGSTMYPGLPSRLEREIKQLYlervlkndtekLAKFKIRIEDPP---RRKDMVFIGGAVLA 362
Cdd:cd13395  326 IGSCDVDIRPELYGNVVLTGGNSLLPGFTDRLNRELSEKA-----------PGSLKLKILASGntvERRFSSWIGGSILA 394
                        410       420
                 ....*....|....*....|....
gi 161077869 363 EVtkdrdG-F---WMSKQEYQEQG 382
Cdd:cd13395  395 SL-----GsFqqmWISKQEYEEHG 413
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
8-382 2.66e-86

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 268.14  E-value: 2.66e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869   8 VIVCDNGTGFVKCGYAGSNFPTHIFPSMVG--RPMIRAVNKIGdIEVKDLMVGDEASQLRSLLEVSYPMENGVVRNWDDM 85
Cdd:PTZ00280   6 VVVIDNGTGYTKMGYAGNTEPTYIIPTLIAdnSKQSRRRSKKG-FEDLDFYIGDEALAASKSYTLTYPMKHGIVEDWDLM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  86 CHVWDYTFGpKKMDIDPTNTKILLTEPPMNPTKNREKMIEVMFEKYGFDSAYIAIQAVLTLYAQ----------GLISGV 155
Cdd:PTZ00280  85 EKFWEQCIF-KYLRCEPEEHYFILTEPPMNPPENREYTAEIMFETFNVKGLYIAVQAVLALRASwtskkakelgGTLTGT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 156 VIDSGDGVTHICPVYEEFALPHLTRRLDIAGRDITRYLIKLLLLRGYAFNHSADFETVRIMKEKLCYIGYDIEME----- 230
Cdd:PTZ00280 164 VIDSGDGVTHVIPVVDGYVIGSSIKHIPLAGRDITNFIQQMLRERGEPIPAEDILLLAQRIKEKYCYVAPDIAKEfekyd 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 231 -------QRLALETTVLVESYTlpdgrvIKVGGERFEAPEALFQPHLINVE-GPGIAELAFNTIQAADIDIRPELYKHIV 302
Cdd:PTZ00280 244 sdpknhfKKYTAVNSVTKKPYT------VDVGYERFLGPEMFFHPEIFSSEwTTPLPEVVDDAIQSCPIDCRRPLYKNIV 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 303 LSGGSTMYPGLPSRLEREIKQLYLERVLKNDTEKLAKFK-----IRIEDPPRRKDMVFIGGAVLAEvTKDRDGFWMSKQE 377
Cdd:PTZ00280 318 LSGGSTMFKGFDKRLQRDVRKRVDRRLKKAEELSGGKLKpipidVNVVSHPRQRYAVWYGGSMLAS-SPEFEKVCHTKAE 396

                 ....*
gi 161077869 378 YQEQG 382
Cdd:PTZ00280 397 YDEYG 401
ASKHA_NBD_Arp6 cd10210
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ...
8-382 1.63e-79

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: 249.78  E-value: 1.63e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869   8 VIVCDNGTGFVKCGYAGSNfPTHIFPSMVGRPmiRAVNK--IGDI---EVKDLmvgdeaSQLRSLLevsyPMENGVVRNW 82
Cdd:cd10210    1 TLVLDNGAYTIKAGFASDD-PPRVIPNCIAKP--KSERRrlFGDDqldECKDL------SGLFYRR----PFERGYLVNW 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  83 DDMCHVWDYTFGPKKMDIDPTNTKILLTEPPMNPTKNREKMIEVMFEKYGFDSAYIAIQAVLTLYAQGLISG-------- 154
Cdd:cd10210   68 DLQRQIWDHLFGKLLLNVDPSDTALVLTEPPFNPPSIQEAMDEIVFEEYGFQSLYRTTAAALSAFAYLADSEqssssssq 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 155 --VVIDSGDGVTHICPVYEEFALPHLTRRLDIAGRDITRYLIKLLLLRgyAFNHSADFETVRIMKEKLCYIG--YDIEME 230
Cdd:cd10210  148 ccLVVDSGFSFTHIVPFFDGKPVKRAVRRIDVGGKLLTNYLKEIISYR--QLNVMDETYLVNQIKEDLCFVStdFYEDLE 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 231 --QRLALETTVLVEsYTLPDG-----------------------RVIKVGGERFEAPEALFQPHLINVEGPGIAELAFNT 285
Cdd:cd10210  226 iaKKKGKENTIRRD-YVLPDYttskrgyvrdpeepnrgklkedeQVLRLNNERFTVPELLFHPSDIGIQQAGIAEAIVQS 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 286 IQAADIDIRPELYKHIVLSGGSTMYPGLPSRLEREIKQLylervlkndteKLAKFKIRIEDPPRRKDMVFIGGAVLAEvT 365
Cdd:cd10210  305 INACPEELQPLLYANIVLTGGNALFPGFRERLEAELRSL-----------APDDYDVNVTLPEDPITYAWEGGSLLAQ-S 372
                        410
                 ....*....|....*..
gi 161077869 366 KDRDGFWMSKQEYQEQG 382
Cdd:cd10210  373 PEFEELAVTRAEYEEHG 389
COG5277 COG5277
Actin-related protein [Cytoskeleton];
8-380 3.50e-61

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 203.10  E-value: 3.50e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869   8 VIVCDNGTGFVKCG-YAGSNFPTHI-----FPSMVGRPMIRAVNKIGDievKDLMVGDEASQ-LRSLLEVS----YPMEN 76
Cdd:COG5277   10 VIGIDFGTSYVKYGpIALEEKPRVIqtrglFLRIVGESKLLGPMEGLS---RGLVVGDEVSKyLSSVRDAIrnlkYPLRD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  77 GVVR-----NWDDMCHVWDYTFGPKK-MDIDPTNTKILLTEPPMNPTKNREKMIEVMFEK---YGFDSAYIAIQAVLTLY 147
Cdd:COG5277   87 GIVRrddedAWRVLKELLRYTFAQFLvVDPEFHGFLVVVALSALAPDYMRERLFDIHFEVfseEGAPAVTIIPQPLAVAI 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 148 AQGLISGVVIDSGDGVTHICPVYEEfALPHLTRRLDIAGRDITRYLIKLLLLRGYAFNHSADfETVRIMKEKLCYIGYDI 227
Cdd:COG5277  167 AEKAVTCVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSDTAREE-YVVRVVKEALGLVPRDL 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 228 EMEQRLAL-ETTVLVESYTLPDGRVIKVGGE----RFEAPEALFQPHLINVEG----------------------PGIAE 280
Cdd:COG5277  245 AKAIQKAAsNPDSFEAKVRLPNPTVEIELGNyaweRFLIGEILFNPNHEGFESyiqqgrlriedavigdvvlygeMGLAE 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 281 LAFNTIQAADIDIRPELYKHIVLSGGSTMY---PGL-------PSRLEREIKQLYLErvlkndteklAKFKIRIedPPRR 350
Cdd:COG5277  325 AIINSIMKCDVEIQDELYSNIILSGGAFNWsvpPGLedvavdsVTRVQIELSELAPE----------LKVNVRL--VSDP 392
                        410       420       430
                 ....*....|....*....|....*....|.
gi 161077869 351 KDMVFIGGAVLA-EVTKDRDGFWMSKQEYQE 380
Cdd:COG5277  393 QYSVWKGAIIYGyALPFSVKWSWITKEGWYF 423
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
9-382 5.77e-59

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: 195.30  E-value: 5.77e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869   9 IVCDNGTGFVKCGYAGS-NFPTHIFPSMvgrpMIRAVNkigDIEVKDLMVGDEASQlrsllevsyPMENGVVRNWDDMCH 87
Cdd:cd10209    1 VVIDAGSRLLKAGYAYPdREPSVVEPTR----VTPAVE---DGEESDTVVEGNTVS---------PIRRGRIEDWDALEA 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  88 VWDYTFGPKKMDIDPTNTKILLTEPPMNPTKNREKMIEVMFEKYGFDSAYIAIQAVLTLYAQGLISGVVIDSGDGVTHIC 167
Cdd:cd10209   65 LLRYVFYTGLGWEEGNEGQVLIAEPLLTSKAERERLTQLMFETFNVSGLYASEQAVLSLYAVGRISGCVVDVGHGKIDIA 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 168 PVYEEFALPHLTRRLDIAGRDITRYLIKLLLLRGYAFNHSADfeTVRIMKEKlcyigYDIEMEQRLALETTVL---VESY 244
Cdd:cd10209  145 PVWEGAIQHNAVRRFEIGGRDLTELLAAELGKSNPKVKLDRS--IVERLKEA-----VAWSADDEEAYEKKVLtcsPETY 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 245 TLPDGRVIKVGGERFEAPEALFQPHLINVEGPGIAELAFNTIQAADIDIRPELYKHIVLSGGSTMYPGLPSRLEREIKQL 324
Cdd:cd10209  218 TLPDGRVISVGKERYCVGEALFRPSILGIEEYGIVEQLVRAVSTSPSENRRQLLENIVLCGGTSSVPGLEARLQKEIRLL 297
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161077869 325 ylervlknDTEKLAKFKIRIED--PPRRKDMV-FIGGAVLAEVTKDRDGFwMSKQEYQEQG 382
Cdd:cd10209  298 --------SSPSSRPALVKPPEymPENTLRYSaWIGGAILAKVVFPQNQH-VTKADYDETG 349
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
8-382 2.64e-51

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: 175.07  E-value: 2.64e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869   8 VIVCDNGTGFVKCGYAGSNFPTHIFPSMVGRP--------MIRAVNKIGDIEVKDlmvgdeaSQLRSllevsyPMENGVV 79
Cdd:cd10211    1 PIVIDNGSYQCRAGWAGDKEPRLVFRNLVAKPrdrkkgitVTLVGNDILNDEAVR-------SHLRS------PFDRNVV 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  80 RNWDDMCHVWDYTFGpkKMDIDPTNTK---ILLTEPPMNPTKNREKMIEVMFEKYGFDSAYIAIQAVLTLYAQ----GLI 152
Cdd:cd10211   68 TNFDLQEQILDYIFS--HLGINSEGSVdhpIVLTEALCNPNYSRQLMSELLFECYGVPSVAYGIDSLFSYYHNqpqgDPS 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 153 SGVVIDSGDGVTHICPVYEEFALPHLTRRLDIAGRDITRYLIKLLLLRGYAFNHSADFETVRIMKEKLCYIGYDIEMEqr 232
Cdd:cd10211  146 DGLVISSGYSTTHVIPVLNGRLDLSQCKRINLGGFHATDYLQRLLQLKYPTHPSAITLSRAEELVHEHCYVAEDYDEE-- 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 233 laLETTVLVESYTLPDgRVIKVggerfeaPealfqphlinvegPGIAELAFNTIQAADIDIRPELYKHIVLSGGSTMYPG 312
Cdd:cd10211  224 --LKKWEDPEYYEENV-RKIQL-------P-------------FGLVETIEFVLKRYPAEQQDRLVQNVFLTGGNALFPG 280
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161077869 313 LPSRLEREIKQLYLERvlkndteklAKFKIRiedppRRKDMVF---IGGAVLAeVTKDRDGFWMSKQEYQEQG 382
Cdd:cd10211  281 LKERLEKELRAIRPFG---------SPFNVV-----RAKDPVLdawRGAAKWA-LDSTFEKVWITKQEYEEKG 338
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
64-382 2.32e-41

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: 148.99  E-value: 2.32e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  64 LRSLLEVSYPMENGVVRNWDDMCHVWDYT-FGPKKMDIDPTNTKILLTEPPMNPTKNREKMIEVMFEKYGFDSAYIAIQA 142
Cdd:cd10208   29 IPTRVEIIWPIQDGRVVDWDALEALWRHIlFSLLSIPRPTNNSPVLLSVPPSWSKSDLELLTQLFFERLNVPAFAILEAP 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 143 VLTLYAQGLISGVVIDSGDGVTHICPVYEEFALPHLTRRLDIAGRDITRYLIKLL------LLRGYAFNHSADFETVRIM 216
Cdd:cd10208  109 LAALYAAGATSGIVVDIGHEKTDITPIVDSQVVPHALVSIPIGGQDCTAHLAQLLksdepeLKSQAESGEEATLDLAEAL 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 217 KE-KLCyigydiemeqrlaletTVLVESYTLPDGRVIKVGGERFEAPEALFQPHLINVEGPGIAE-LAFNTIQAADIDIR 294
Cdd:cd10208  189 KKsPIC----------------EVLSDGADLASGTEITVGKERFRACEPLFKPSSLRVDLLIAAIaGALVLNASDEPDKR 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 295 PELYKHIVLSGGSTMYPGLPSRLEREIKQLYL---ERVLKNDTE--KLAK-------FKIRIEDpprrkDMVFIGGAVLA 362
Cdd:cd10208  253 PALWENIIIVGGGSRIRGLKEALLSELQQFHLiseTSASPQQPRiiRLAKipdyfpeWKKSGYE-----EAAFLGASIVA 327
                        330       340
                 ....*....|....*....|..
gi 161077869 363 EV--TKDRDGFWMSKQEYQEQG 382
Cdd:cd10208  328 KLvfNDPSSKHYISKVDYNEKG 349
ASKHA_NBD_Arp10 cd10207
nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins; ...
9-382 1.63e-33

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: 128.52  E-value: 1.63e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869   9 IVCDNGTGFVKCGYAGSNFPTHIFPSMVGRPMIRAVNKIGDIEVKDLMvgdeasQLRSLLEvsypmengvvrnwddMCHV 88
Cdd:cd10207    1 VVLDIGSAYTKCGFAGESAPRCIIPSEVKLPGGKKVIRVVDQRSGNEE------ELYEALK---------------EFLH 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  89 WDYTfgpKKMDIDPTNTKILLTEPPMNPTKNREKMIEVMFEKYGFDSAYIAIQAVLTLYAQGLISGVVIDSGDGVTHICP 168
Cdd:cd10207   60 ELYF---KHLLVNPKDRRVVVVESVLCPTPFRETLAKVLFKHFEVPSVLFAPSHLLSLLTLGIRTALVVDCGYRETRVLP 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 169 VYEEFALPHLTRRLDIAGRDITRYLIKLLLLRGYAFNHSA------------DFETVRIMKEKLCYIG--------YDIE 228
Cdd:cd10207  137 VYEGVPLLSAWQSTPLGGKALHKRLKKLLLEHATVVTGDNkgqllssvdsllSEEVLEDIKVRACFVTslergktlQSAT 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 229 MEQRLALETTVLVESYTLPDGRV-IKVGGERFEAPEALFQPhliNVEGPGIAELAFNTIQAADIDIRPELYKHIVLSGGS 307
Cdd:cd10207  217 EEGSTEEPSPPPPVDYPLDGEKIlIVPGSIRESAEELLFEG---DNEEKSLPTLILDSLLKCPIDVRKQLAENIVVIGGT 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 308 TMYPGLPSRLEREIKQLylervLKND--TEKLAKFKIRIEDPPRR--KDMV-FIGGAVLAeVTKDRDGFWMSKQEYQEQG 382
Cdd:cd10207  294 SMLPGFKHRLLEELRAL-----LRKPkyFEELAPKTFRFHTPPSVfkPNYLaWLGGSIFG-ALESILGRSLSREAYLQTG 367
ASKHA_NBD_AtArp8-like cd13396
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and ...
120-382 4.66e-26

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: 107.25  E-value: 4.66e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 120 REKMIEVMFEKyGFDSAYIAIQAVLTLYAQGLISGVVIDSGDGVTHICPVYEEFALPHLTrrLDIAGR---DITRYLIKL 196
Cdd:cd13396   84 RGTIFNVLFDM-NVPAVCAVDQAVLALYAANRTSGIVVNIGFRVTTIVPVYRGRVMHDIG--VEVVGQgalRLTGFLKEL 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 197 LLLRGYAFNhsaDFETVRIMKEKLCYIGYDIEMEQRLALETTVLVESytlpDGRVIkVGGERFEAPEALFQPHLINVEGP 276
Cdd:cd13396  161 MQQNGIRFP---SLYTVRTIKEKLCYVAEDYEAELAKDTQASCEVAG----EGWFT-LSNERFKTGEILFQPGLGGMRAM 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 277 GIAELAFNTIQAADIDIRPE---LYKHIVLSGGSTMYPGLPSRLEREIKQLYLERVLKNdteklakfkIRIEDPPRRKDM 353
Cdd:cd13396  233 GLHQAVALCMDHCALVHSQGddgWFKTIVLSGGSACLPGLSERLERELRKLLPKSLSEG---------IRIIPPPLGPDS 303
                        250       260
                 ....*....|....*....|....*....
gi 161077869 354 VFIGGAVLAEVTKDRDGFWMSKQEYQEQG 382
Cdd:cd13396  304 AWQGAKLISNLSNFPDGWCITKKQFRNKP 332
ASKHA_NBD_Arp8-like cd10206
nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The ...
121-387 6.78e-22

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


Pssm-ID: 466812 [Multi-domain]  Cd Length: 447  Bit Score: 96.93  E-value: 6.78e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 121 EKMIEVMFEKYGFDSAYIAIQAVLTLYAQGLISGVVIDSGDGVTHICPVYEEFALPHlTR-RLDIAGRDITRYLIKLLLL 199
Cdd:cd10206  202 KELVDLLLRRLGFSSVFVHQESVCATFGAGLSSACVVDIGAQKTSVACVEDGLSIPN-SRiRLPYGGDDITRCFLWLLRR 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 200 RG--YAF---NHSADFETVRIMKEKLCYIgydiemeqRLALETTVLVESYTLPDGRVIKVggerfeapealfqpHLINVe 274
Cdd:cd10206  281 SGfpYREcnlNSPLDFLLLERLKETYCTL--------DQDDIGVQLHEFYVREPGQPTLK--------------YQFKL- 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 275 gPGIAELAFNTI-QAADIDIRPELYKHIVLSGGSTMYPGLPSRLEreikqlylERVLKN-DTEKLAKFKIRIEDPPRRKD 352
Cdd:cd10206  338 -LPLDEAIVQSIlSCASDELKRKMYSSILLVGGGAKIPGLAEALE--------DRLLIKiPSLFEAVETVEVLPPPKDMD 408
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 161077869 353 ---MVFIGGAVLA--EVTKDrdgFWMSKQEYQEQGLKVLQ 387
Cdd:cd10206  409 pslLAWKGGAVLAclDSAQE---LWITRKEWQRLGVRALR 445
ASKHA_NBD_MamK cd24009
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ...
6-324 3.60e-10

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: 60.69  E-value: 3.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869   6 RNVIVCDNGTGFVkcgyagsnfpthiFPSMVGRP--MIrAVNKIGdievKDLMVGDEASQLRSLLEVSYPMENGVVRNWD 83
Cdd:cd24009   12 RSAVVTSRGKRFS-------------FRSVVGYPkdII-ARKLLG----KEVLFGDEALENRLALDLRRPLEDGVIKEGD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  84 D---------MCHVWDYTFGPKKmdidpTNTKILLTEPPMNPTKNREKMIEVMFEKygFDSAYIAIQAVLTLYAQG-LIS 153
Cdd:cd24009   74 DrdleaarelLQHLIELALPGPD-----DEIYAVIGVPARASAENKQALLEIAREL--VDGVMVVSEPFAVAYGLDrLDN 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 154 GVVIDSGDGVTHICPVYEEFALPHLTRRLDIAGRDITRYLIKLLLLRgYAfNHSADFETVRIMKEKLCYIGydiEMEQRL 233
Cdd:cd24009  147 SLIVDIGAGTTDLCRMKGTIPTEEDQITLPKAGDYIDEELVDLIKER-YP-EVQLTLNMARRWKEKYGFVG---DASEPV 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 234 ALETTVlvesytlpDGRVIK--VGGERFEAPEALFqPHLINvegpGIAELafntIQAADIDIRPELYKHIVLSGGSTMYP 311
Cdd:cd24009  222 KVELPV--------DGKPVTydITEELRIACESLV-PDIVE----GIKKL----IASFDPEFQEELRNNIVLAGGGSRIR 284
                        330
                 ....*....|...
gi 161077869 312 GLPSRLEREIKQL 324
Cdd:cd24009  285 GLDTYIEKALKEY 297
ASKHA_NBD_ScArp7-like cd10212
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and ...
6-379 5.76e-06

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: 48.18  E-value: 5.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869   6 RNVIVCDNGTGFVKCGYAGSNFPTHIFPSmvgrPMIRAVNKIGDIEvkdLMVG-----DEASQLRSLLEVSYPMEN-GVV 79
Cdd:cd10212    3 RKCVVIHNGSHRTVAGFSNVELPQCIIPS----SYIKRTDEGGEAE---FIFGtynmiDAAAEKRNGDEVYTLVDSqGLP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869  80 RNWDDMCHVWDYTFGpKKMDIDPTNTKILLTEPPMNPTKNR---EKMIEVMFEKYGFDSAYIAIQAVLTLYAQGLISGVV 156
Cdd:cd10212   76 YNWDALEMQWRYLYD-TQLKVSPEELPLVITMPATNGKPDMailERYYELAFDKLNVPVFQIVIEPLAIALSMGKSSAFV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 157 IDSGDGVTHICPVYEEFALPHLTRR-------LDIAGRDITRYLIK---------------------------------- 195
Cdd:cd10212  155 IDIGASGCNVTPIIDGIVVKNAVVRskfggdfLDFQVHERLAPLIKeendmenmadeqkrstdvwyeastwiqqfkstml 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 196 ------LLLLRGYaFNHSADF-----ETVRIMKEKLCYIGYDIEMEQRLALETTVLVEsytlPDGRVIKVG-GERFEAPE 263
Cdd:cd10212  235 qvsekdLFELERY-YKEQADIyakqqEQLKQMDQQLQYTALTGSPNNPLVQKKNFLFK----PLNKTLTLDlKECYQFAE 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077869 264 ALFQPHLINVE-GP--GIAELAFNTIQAADIDIRPELYKHIVLSGGSTMYPGLPSRLEREIKqlylervLKNDTEKLAKF 340
Cdd:cd10212  310 YLFKPQLISDKfSPedGLGPLMAKSVKKAPEQVYSLLLTNVIITGSTSLIEGMEQRIIKELS-------IRFPQYKLTTF 382
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 161077869 341 KIRIEdpPRRKDMVFIGGAVLAEVTKDRDGFWMSKQEYQ 379
Cdd:cd10212  383 ANQVM--MDRKIQGWLGALTMANLPSWSLGKWYSKEDYE 419
 
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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