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Conserved domains on  [gi|19113810|ref|NP_592898|]
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ARP2/3 actin-organizing complex actin-related protein subunit Arp3 [Schizosaccharomyces pombe]

Protein Classification

actin-related protein 3( domain architecture ID 19021160)

actin-related protein 3 (ACTR3) is an ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
7-419 0e+00

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: 780.98  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810   7 PIIMDNGTGYSKLGYAGNDAPSYVFPTVIATRSAgassgpavsskpsymASKGSGHLSSKRATEDLDFFIGNDALKKASa 86
Cdd:cd10221   1 AVVIDNGTGYTKMGYAGNTEPQFIIPTVIAIKES---------------AKVGDGQRRSKKGIEDLDFYIGDEALANSP- 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  87 GYSLDYPIRHGQIENWDHMERFWQQSLFKYLRCEPEDHYFLLTEPPLNPPENRENTAEIMFESFNCAGLYIAVQAVLALA 166
Cdd:cd10221  65 TYALKYPIRHGIVEDWDLMERFWEQCIFKYLRCEPEDHYFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQAVLALA 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 167 ASWTSSKVTDRSLTGTVVDSGDGVTHIIPVAEGYVIGSSIKTMPLAGRDVTYFVQSLLRDRNE---PDSSLKTAERIKEE 243
Cdd:cd10221 145 ASWTSRKVGERTLTGTVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREEgipPEDSLEVAKRIKER 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 244 CCYVCPDIVKEFSRFDREPDRYLK--YASESITGHSTTIDVGFERFLAPEIFFNPEIASSDFLTPLPELVDNVVQSSPID 321
Cdd:cd10221 225 YCYVCPDIVKEFAKYDSDPAKYIKqyTGINSVTGKPYTVDVGYERFLAPEIFFNPEIASSDFTTPLPEVVDQVIQSCPID 304
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 322 VRKGLYKNIVLSGGSTLFKNFGNRLQRDLKRIVDERIHRSEMLSG--AKSGGVDVNVISHKRQRNAVWFGGSLLAQTPEF 399
Cdd:cd10221 305 TRRGLYKNIVLSGGSTMFKDFGRRLQRDVKRIVDARLKASEELSGgkLKPKPIDVNVISHPMQRYAVWFGGSMLASTPEF 384
                       410       420
                ....*....|....*....|
gi 19113810 400 GSYCHTKADYEEYGASIARR 419
Cdd:cd10221 385 YTVCHTKAEYEEYGPSICRH 404
 
Name Accession Description Interval E-value
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
7-419 0e+00

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: 780.98  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810   7 PIIMDNGTGYSKLGYAGNDAPSYVFPTVIATRSAgassgpavsskpsymASKGSGHLSSKRATEDLDFFIGNDALKKASa 86
Cdd:cd10221   1 AVVIDNGTGYTKMGYAGNTEPQFIIPTVIAIKES---------------AKVGDGQRRSKKGIEDLDFYIGDEALANSP- 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  87 GYSLDYPIRHGQIENWDHMERFWQQSLFKYLRCEPEDHYFLLTEPPLNPPENRENTAEIMFESFNCAGLYIAVQAVLALA 166
Cdd:cd10221  65 TYALKYPIRHGIVEDWDLMERFWEQCIFKYLRCEPEDHYFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQAVLALA 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 167 ASWTSSKVTDRSLTGTVVDSGDGVTHIIPVAEGYVIGSSIKTMPLAGRDVTYFVQSLLRDRNE---PDSSLKTAERIKEE 243
Cdd:cd10221 145 ASWTSRKVGERTLTGTVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREEgipPEDSLEVAKRIKER 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 244 CCYVCPDIVKEFSRFDREPDRYLK--YASESITGHSTTIDVGFERFLAPEIFFNPEIASSDFLTPLPELVDNVVQSSPID 321
Cdd:cd10221 225 YCYVCPDIVKEFAKYDSDPAKYIKqyTGINSVTGKPYTVDVGYERFLAPEIFFNPEIASSDFTTPLPEVVDQVIQSCPID 304
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 322 VRKGLYKNIVLSGGSTLFKNFGNRLQRDLKRIVDERIHRSEMLSG--AKSGGVDVNVISHKRQRNAVWFGGSLLAQTPEF 399
Cdd:cd10221 305 TRRGLYKNIVLSGGSTMFKDFGRRLQRDVKRIVDARLKASEELSGgkLKPKPIDVNVISHPMQRYAVWFGGSMLASTPEF 384
                       410       420
                ....*....|....*....|
gi 19113810 400 GSYCHTKADYEEYGASIARR 419
Cdd:cd10221 385 YTVCHTKAEYEEYGPSICRH 404
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
8-425 0e+00

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 631.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810    8 IIMDNGTGYSKLGYAGNDAPSYVFPTVIATRSAGASSgpavsskpsymaskgsghlSSKRATEDLDFFIGNDALKKASaG 87
Cdd:PTZ00280   7 VVIDNGTGYTKMGYAGNTEPTYIIPTLIADNSKQSRR-------------------RSKKGFEDLDFYIGDEALAASK-S 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810   88 YSLDYPIRHGQIENWDHMERFWQQSLFKYLRCEPEDHYFLLTEPPLNPPENRENTAEIMFESFNCAGLYIAVQAVLALAA 167
Cdd:PTZ00280  67 YTLTYPMKHGIVEDWDLMEKFWEQCIFKYLRCEPEEHYFILTEPPMNPPENREYTAEIMFETFNVKGLYIAVQAVLALRA 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  168 SWTSSKVTDR--SLTGTVVDSGDGVTHIIPVAEGYVIGSSIKTMPLAGRDVTYFVQSLLRDRNEP---DSSLKTAERIKE 242
Cdd:PTZ00280 147 SWTSKKAKELggTLTGTVIDSGDGVTHVIPVVDGYVIGSSIKHIPLAGRDITNFIQQMLRERGEPipaEDILLLAQRIKE 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  243 ECCYVCPDIVKEFSRFDREPDRYLK--YASESITGHSTTIDVGFERFLAPEIFFNPEIASSDFLTPLPELVDNVVQSSPI 320
Cdd:PTZ00280 227 KYCYVAPDIAKEFEKYDSDPKNHFKkyTAVNSVTKKPYTVDVGYERFLGPEMFFHPEIFSSEWTTPLPEVVDDAIQSCPI 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  321 DVRKGLYKNIVLSGGSTLFKNFGNRLQRDLKRIVDERIHRSEMLSGAKSGGV--DVNVISHKRQRNAVWFGGSLLAQTPE 398
Cdd:PTZ00280 307 DCRRPLYKNIVLSGGSTMFKGFDKRLQRDVRKRVDRRLKKAEELSGGKLKPIpiDVNVVSHPRQRYAVWYGGSMLASSPE 386
                        410       420
                 ....*....|....*....|....*..
gi 19113810  399 FGSYCHTKADYEEYGASIARRYQIFGN 425
Cdd:PTZ00280 387 FEKVCHTKAEYDEYGPSICRYNNVFHS 413
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
7-419 2.85e-140

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 405.49  E-value: 2.85e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810      7 PIIMDNGTGYSKLGYAGNDAPSYVFPTVIAtrsagassgpavssKPSYmaskgsghlSSKRATEDLDFFIGNDALKKASa 86
Cdd:smart00268   3 AIVIDNGSGTIKAGFAGEDFPQVVFPSIVG--------------RPKD---------GKGMVGDAKDIFVGDEAQEKRG- 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810     87 GYSLDYPIRHGQIENWDHMERFWQQSLFKYLRCEPEDHYFLLTEPPLNPPENRENTAEIMFESFNCAGLYIAVQAVLALA 166
Cdd:smart00268  59 GLELKYPIENGIVENWDDMEKIWDYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLY 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810    167 ASWtsskvtdrSLTGTVVDSGDGVTHIIPVAEGYVIGSSIKTMPLAGRDVTYFVQSLLRDRN---EPDSSLKTAERIKEE 243
Cdd:smart00268 139 ASG--------RTTGLVIDSGDGVTHVVPVVDGYVLPHAIKRIDIAGRDITDYLKELLSERGyqfNSSAEFEIVREIKEK 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810    244 CCYVCPDIVKEFSRfDREPDRYLKYASESITGHSTTIDVGFERFLAPEIFFNPEIASSDFlTPLPELVDNVVQSSPIDVR 323
Cdd:smart00268 211 LCYVAEDFEKEMKL-ARESSESSKLEKTYELPDGNTIKVGNERFRIPEILFSPELIGLEQ-KGIHELVYESIQKCDIDVR 288
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810    324 KGLYKNIVLSGGSTLFKNFGNRLQRDLKRIVDerihrsemlsgaksGGVDVNVISHKRQRNAVWFGGSLLAQTPEFGSYC 403
Cdd:smart00268 289 KDLYENIVLSGGSTLIPGFGERLEKELKQLAP--------------KKLKVKVIAPPERKYSVWLGGSILASLSTFEDMW 354
                          410
                   ....*....|....*.
gi 19113810    404 HTKADYEEYGASIARR 419
Cdd:smart00268 355 ITKKEYEESGSQIVER 370
Actin pfam00022
Actin;
7-420 1.54e-96

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 295.37  E-value: 1.54e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810     7 PIIMDNGTGYSKLGYAGNDAPSYVFPTVIatrsagassgpavsskpsymaskgsGHLSSKRATEDLDFFIGNDALKKaSA 86
Cdd:pfam00022   3 ALVIDNGSHTTRAGFAGEDAPKAVIPSCV-------------------------GKPRGTKVEAANKYYVGDEALTY-RP 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810    87 GYSLDYPIRHGQIENWDHMERFWQQSLFKYLRCEPEDHYFLLTEPPLNPPENRENTAEIMFESFNCAGLYIavqAVLALA 166
Cdd:pfam00022  57 GMEVRSPVEDGIVVDWDAMEEIWEHVLKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYL---AKNPVL 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810   167 ASWTSSKVtdrslTGTVVDSGDGVTHIIPVAEGYVIGSSIKTMPLAGRDVTYFVQSLLRDRN------------------ 228
Cdd:pfam00022 134 SAFASGRT-----TGLVVDSGAGVTSVVPVHDGYVLQKAIRRSDLGGDFLTDYLRELLRSRNieitprylikskkpgdpa 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810   229 ---------EPDSSLKTAER------IKEECCYVCPDIVKefsrfDREPdrylkyASESITGH-----STTIDVGFERFL 288
Cdd:pfam00022 209 pavtkrelpDTTYSYKTYQErrvleeIKESVCYVSDDPFG-----DETT------SSSIPTRVyelpdGSTIILGAERFR 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810   289 APEIFFNPEIASSDFLTP-------LPELVDNVVQSSPIDVRKGLYKNIVLSGGSTLFKNFGNRLQRDLKRIVderihrs 361
Cdd:pfam00022 278 VPEILFNPSLIGSESELPppqtavgIPELIVDAINACDVDLRPSLLANIVVTGGNSLFPGFTERLEKELAQLA------- 350
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113810   362 emlsgakSGGVDVNVISHKRQ---RNAVWFGGSLLAQTPEFGSYCHTKADYEEYGASIARRY 420
Cdd:pfam00022 351 -------PPGVKVKIIAPGNTverRYSAWIGGSILASLGTFQQMWVSKQEYEEHGASVVERK 405
COG5277 COG5277
Actin-related protein [Cytoskeleton];
4-394 1.54e-38

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 143.78  E-value: 1.54e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810   4 FNVPIIMDNGTGYSKLG-YAGNDAPSYVFPTVIATRSAGAS--SGPA-VSSKPSYMASKGSGHLSSKRatedldffignd 79
Cdd:COG5277   7 LKYVIGIDFGTSYVKYGpIALEEKPRVIQTRGLFLRIVGESklLGPMeGLSRGLVVGDEVSKYLSSVR------------ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  80 alkkaSAGYSLDYPIRHGQIE-----NWDHMERFWQQSLFKYLRCEPEDHYFL--LTEPPLNPPENRENTAEIMFESFNC 152
Cdd:COG5277  75 -----DAIRNLKYPLRDGIVRrddedAWRVLKELLRYTFAQFLVVDPEFHGFLvvVALSALAPDYMRERLFDIHFEVFSE 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 153 AGLYIAVQAVLALAASWTSSKVTdrsltGTVVDSGDGVTHIIPVAEGyVIGSSIKTMPLAGRDVTYFVQSLLRDRNEPDS 232
Cdd:COG5277 150 EGAPAVTIIPQPLAVAIAEKAVT-----CVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSDT 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 233 SL--KTAERIKEECCYVCPDIVKEFSRFDREPDRYLkyASESITGHSTTIDVG---FERFLAPEIFFNPE------IASS 301
Cdd:COG5277 224 AReeYVVRVVKEALGLVPRDLAKAIQKAASNPDSFE--AKVRLPNPTVEIELGnyaWERFLIGEILFNPNhegfesYIQQ 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 302 DFLTP---------------LPELVDNVVQSSPIDVRKGLYKNIVLSGGSTLFknfgnRLQRDLKRIVDERIHRSEMLSG 366
Cdd:COG5277 302 GRLRIedavigdvvlygemgLAEAIINSIMKCDVEIQDELYSNIILSGGAFNW-----SVPPGLEDVAVDSVTRVQIELS 376
                       410       420
                ....*....|....*....|....*...
gi 19113810 367 AKSGGVDVNVISHKRQRNAVWFGGSLLA 394
Cdd:COG5277 377 ELAPELKVNVRLVSDPQYSVWKGAIIYG 404
 
Name Accession Description Interval E-value
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
7-419 0e+00

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: 780.98  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810   7 PIIMDNGTGYSKLGYAGNDAPSYVFPTVIATRSAgassgpavsskpsymASKGSGHLSSKRATEDLDFFIGNDALKKASa 86
Cdd:cd10221   1 AVVIDNGTGYTKMGYAGNTEPQFIIPTVIAIKES---------------AKVGDGQRRSKKGIEDLDFYIGDEALANSP- 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  87 GYSLDYPIRHGQIENWDHMERFWQQSLFKYLRCEPEDHYFLLTEPPLNPPENRENTAEIMFESFNCAGLYIAVQAVLALA 166
Cdd:cd10221  65 TYALKYPIRHGIVEDWDLMERFWEQCIFKYLRCEPEDHYFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQAVLALA 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 167 ASWTSSKVTDRSLTGTVVDSGDGVTHIIPVAEGYVIGSSIKTMPLAGRDVTYFVQSLLRDRNE---PDSSLKTAERIKEE 243
Cdd:cd10221 145 ASWTSRKVGERTLTGTVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREEgipPEDSLEVAKRIKER 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 244 CCYVCPDIVKEFSRFDREPDRYLK--YASESITGHSTTIDVGFERFLAPEIFFNPEIASSDFLTPLPELVDNVVQSSPID 321
Cdd:cd10221 225 YCYVCPDIVKEFAKYDSDPAKYIKqyTGINSVTGKPYTVDVGYERFLAPEIFFNPEIASSDFTTPLPEVVDQVIQSCPID 304
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 322 VRKGLYKNIVLSGGSTLFKNFGNRLQRDLKRIVDERIHRSEMLSG--AKSGGVDVNVISHKRQRNAVWFGGSLLAQTPEF 399
Cdd:cd10221 305 TRRGLYKNIVLSGGSTMFKDFGRRLQRDVKRIVDARLKASEELSGgkLKPKPIDVNVISHPMQRYAVWFGGSMLASTPEF 384
                       410       420
                ....*....|....*....|
gi 19113810 400 GSYCHTKADYEEYGASIARR 419
Cdd:cd10221 385 YTVCHTKAEYEEYGPSICRH 404
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
8-425 0e+00

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 631.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810    8 IIMDNGTGYSKLGYAGNDAPSYVFPTVIATRSAGASSgpavsskpsymaskgsghlSSKRATEDLDFFIGNDALKKASaG 87
Cdd:PTZ00280   7 VVIDNGTGYTKMGYAGNTEPTYIIPTLIADNSKQSRR-------------------RSKKGFEDLDFYIGDEALAASK-S 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810   88 YSLDYPIRHGQIENWDHMERFWQQSLFKYLRCEPEDHYFLLTEPPLNPPENRENTAEIMFESFNCAGLYIAVQAVLALAA 167
Cdd:PTZ00280  67 YTLTYPMKHGIVEDWDLMEKFWEQCIFKYLRCEPEEHYFILTEPPMNPPENREYTAEIMFETFNVKGLYIAVQAVLALRA 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  168 SWTSSKVTDR--SLTGTVVDSGDGVTHIIPVAEGYVIGSSIKTMPLAGRDVTYFVQSLLRDRNEP---DSSLKTAERIKE 242
Cdd:PTZ00280 147 SWTSKKAKELggTLTGTVIDSGDGVTHVIPVVDGYVIGSSIKHIPLAGRDITNFIQQMLRERGEPipaEDILLLAQRIKE 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  243 ECCYVCPDIVKEFSRFDREPDRYLK--YASESITGHSTTIDVGFERFLAPEIFFNPEIASSDFLTPLPELVDNVVQSSPI 320
Cdd:PTZ00280 227 KYCYVAPDIAKEFEKYDSDPKNHFKkyTAVNSVTKKPYTVDVGYERFLGPEMFFHPEIFSSEWTTPLPEVVDDAIQSCPI 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  321 DVRKGLYKNIVLSGGSTLFKNFGNRLQRDLKRIVDERIHRSEMLSGAKSGGV--DVNVISHKRQRNAVWFGGSLLAQTPE 398
Cdd:PTZ00280 307 DCRRPLYKNIVLSGGSTMFKGFDKRLQRDVRKRVDRRLKKAEELSGGKLKPIpiDVNVVSHPRQRYAVWYGGSMLASSPE 386
                        410       420
                 ....*....|....*....|....*..
gi 19113810  399 FGSYCHTKADYEEYGASIARRYQIFGN 425
Cdd:PTZ00280 387 FEKVCHTKAEYDEYGPSICRYNNVFHS 413
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
7-419 2.85e-140

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 405.49  E-value: 2.85e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810      7 PIIMDNGTGYSKLGYAGNDAPSYVFPTVIAtrsagassgpavssKPSYmaskgsghlSSKRATEDLDFFIGNDALKKASa 86
Cdd:smart00268   3 AIVIDNGSGTIKAGFAGEDFPQVVFPSIVG--------------RPKD---------GKGMVGDAKDIFVGDEAQEKRG- 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810     87 GYSLDYPIRHGQIENWDHMERFWQQSLFKYLRCEPEDHYFLLTEPPLNPPENRENTAEIMFESFNCAGLYIAVQAVLALA 166
Cdd:smart00268  59 GLELKYPIENGIVENWDDMEKIWDYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLY 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810    167 ASWtsskvtdrSLTGTVVDSGDGVTHIIPVAEGYVIGSSIKTMPLAGRDVTYFVQSLLRDRN---EPDSSLKTAERIKEE 243
Cdd:smart00268 139 ASG--------RTTGLVIDSGDGVTHVVPVVDGYVLPHAIKRIDIAGRDITDYLKELLSERGyqfNSSAEFEIVREIKEK 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810    244 CCYVCPDIVKEFSRfDREPDRYLKYASESITGHSTTIDVGFERFLAPEIFFNPEIASSDFlTPLPELVDNVVQSSPIDVR 323
Cdd:smart00268 211 LCYVAEDFEKEMKL-ARESSESSKLEKTYELPDGNTIKVGNERFRIPEILFSPELIGLEQ-KGIHELVYESIQKCDIDVR 288
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810    324 KGLYKNIVLSGGSTLFKNFGNRLQRDLKRIVDerihrsemlsgaksGGVDVNVISHKRQRNAVWFGGSLLAQTPEFGSYC 403
Cdd:smart00268 289 KDLYENIVLSGGSTLIPGFGERLEKELKQLAP--------------KKLKVKVIAPPERKYSVWLGGSILASLSTFEDMW 354
                          410
                   ....*....|....*.
gi 19113810    404 HTKADYEEYGASIARR 419
Cdd:smart00268 355 ITKKEYEESGSQIVER 370
ASKHA_NBD_actin_Arp-T1-3 cd13397
nucleotide-binding domain (NBD) of actin, actin-related proteins T1-T3 (Arp-T1-3), and similar ...
7-413 3.43e-111

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: 331.07  E-value: 3.43e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810   7 PIIMDNGTGYSKLGYAGNDAPSYVFPTVIAtrsagassgpavssKPSYMASKGSghlsskrATEDlDFFIGNDALKKASA 86
Cdd:cd13397   2 AVVIDNGSGLIKAGFAGEDLPRAVFPSVVG--------------RPKYKAVMLG-------AGQK-EVYVGDEAQEKRGV 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  87 gYSLDYPIRHGQIENWDHMERFWQQSLFKYLRCEPEDHYFLLTEPPLNPPENRENTAEIMFESFNCAGLYIavqaVLALA 166
Cdd:cd13397  60 -LTLSYPIEHGIVTNWDDMEKIWHHTFENELRVKPEEHPVLLTEAPLNPKQNREKMAEIMFETFGVPAFYV----AIQAV 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 167 ASWTSSKVTdrslTGTVVDSGDGVTHIIPVAEGYVIGSSIKTMPLAGRDVTYFVQSLLRDR---NEPDSSLKTAERIKEE 243
Cdd:cd13397 135 LSLYSSGRT----TGLVLDSGDGVTHTVPIYEGYALPHAVQRLDLAGRDLTEYLMKLLKERghsFTTTAEREIVRDIKEK 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 244 CCYVCPDivkefsrFDREpdryLKYASESITGHST-----TIDVGFERFLAPEIFFNPEIASSDflTP-LPELVDNVVQS 317
Cdd:cd13397 211 LCYVALD-------YEEE----LKKKSEELEKEYTlpdgqVIKIGSERFRCPEALFRPSLIGRE--APgIHKLVYNSIMK 277
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 318 SPIDVRKGLYKNIVLSGGSTLFKNFGNRLQRDLKRIVDErihrsemlsgaksgGVDVNVISHKRQRNAVWFGGSLLAQTP 397
Cdd:cd13397 278 CDIDIRKDLYSNIVLSGGSTMFPGLPERLQKELEALAPS--------------STKVKVIAPPERKYSVWIGGSILASLS 343
                       410
                ....*....|....*.
gi 19113810 398 EFGSYCHTKADYEEYG 413
Cdd:cd13397 344 TFKSMWITRAEYDEFG 359
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
5-419 3.84e-98

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: 297.92  E-value: 3.84e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810   5 NVPIIMDNGTGYSKLGYAGNDAPSYVFPTVIAtrsagassgpavssKPSY---MASkgsghlsskrATEDlDFFIGNDAl 81
Cdd:cd10216   1 NQPVVIDNGSGVIKAGFAGDDIPKVVFPSYVG--------------RPKHvrvMAG----------ALEG-DVFVGPKA- 54
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  82 KKASAGYSLDYPIRHGQIENWDHMERFWQQSLFK-YLRCEPEDHYFLLTEPPLNPPENRENTAEIMFESFNCAGLYIavq 160
Cdd:cd10216  55 EEHRGLLKIRYPMEHGIVTDWNDMERIWQYVYSKlQLNTFSEEHPVLLTEAPLNPRKNREKAAEVFFETFNVPALFV--- 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 161 aVLALAASWTSSKVTdrslTGTVVDSGDGVTHIIPVAEGYVIGSSIKTMPLAGRDVTYFVQSLLrdRNEPDSSLKTAER- 239
Cdd:cd10216 132 -SMQAVLSLYASGRT----TGVVLDSGDGVTHAVPIYEGFALPHSIRRVDIAGRDVTEYLQLLL--RKSGYNFHTSAEFe 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 240 ----IKEECCYVCPDIVKEFSRFDREPDrylkyASESITGHSTTIDVGFERFLAPEIFFNPEIASSDFLTpLPELVDNVV 315
Cdd:cd10216 205 ivreIKEKACYVALNPQKEEKLEEEKTE-----KAQYTLPDGSTIEIGPERFRAPEILFNPELIGLEYPG-VHEVLVDSI 278
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 316 QSSPIDVRKGLYKNIVLSGGSTLFKNFGNRLQRDLKRIV--DERIHrsemlsgaksggvdvnvISHKRQRN-AVWFGGSL 392
Cdd:cd10216 279 QKSDLDLRKTLYSNIVLSGGSTLFKGFGDRLLSEVKKLApkDVKIR-----------------ISAPPERLySTWIGGSI 341
                       410       420
                ....*....|....*....|....*..
gi 19113810 393 LAQTPEFGSYCHTKADYEEYGASIARR 419
Cdd:cd10216 342 LASLSTFKKMWVSKKEYEEDGARILHR 368
Actin pfam00022
Actin;
7-420 1.54e-96

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 295.37  E-value: 1.54e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810     7 PIIMDNGTGYSKLGYAGNDAPSYVFPTVIatrsagassgpavsskpsymaskgsGHLSSKRATEDLDFFIGNDALKKaSA 86
Cdd:pfam00022   3 ALVIDNGSHTTRAGFAGEDAPKAVIPSCV-------------------------GKPRGTKVEAANKYYVGDEALTY-RP 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810    87 GYSLDYPIRHGQIENWDHMERFWQQSLFKYLRCEPEDHYFLLTEPPLNPPENRENTAEIMFESFNCAGLYIavqAVLALA 166
Cdd:pfam00022  57 GMEVRSPVEDGIVVDWDAMEEIWEHVLKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYL---AKNPVL 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810   167 ASWTSSKVtdrslTGTVVDSGDGVTHIIPVAEGYVIGSSIKTMPLAGRDVTYFVQSLLRDRN------------------ 228
Cdd:pfam00022 134 SAFASGRT-----TGLVVDSGAGVTSVVPVHDGYVLQKAIRRSDLGGDFLTDYLRELLRSRNieitprylikskkpgdpa 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810   229 ---------EPDSSLKTAER------IKEECCYVCPDIVKefsrfDREPdrylkyASESITGH-----STTIDVGFERFL 288
Cdd:pfam00022 209 pavtkrelpDTTYSYKTYQErrvleeIKESVCYVSDDPFG-----DETT------SSSIPTRVyelpdGSTIILGAERFR 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810   289 APEIFFNPEIASSDFLTP-------LPELVDNVVQSSPIDVRKGLYKNIVLSGGSTLFKNFGNRLQRDLKRIVderihrs 361
Cdd:pfam00022 278 VPEILFNPSLIGSESELPppqtavgIPELIVDAINACDVDLRPSLLANIVVTGGNSLFPGFTERLEKELAQLA------- 350
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113810   362 emlsgakSGGVDVNVISHKRQ---RNAVWFGGSLLAQTPEFGSYCHTKADYEEYGASIARRY 420
Cdd:pfam00022 351 -------PPGVKVKIIAPGNTverRYSAWIGGSILASLGTFQQMWVSKQEYEEHGASVVERK 405
ASKHA_NBD_Arp2 cd10220
nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, ...
7-419 8.51e-89

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: 274.44  E-value: 8.51e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810   7 PIIMDNGTGYSKLGYAGNDAPSYVFPTVIAtrsagassgpavssKPSYMASKGSGHLSSKratedlDFFIGNDALKKASA 86
Cdd:cd10220   2 VVVCDNGTGFVKCGFAGSNFPEHVFPSLVG--------------RPILRAEEKVGDIEIK------DIMVGDEASELRSM 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  87 gysLD--YPIRHGQIENWDHMERFWQQSLFKYLRCEPEDHYFLLTEPPLNPPENRENTAEIMFESFNCAGLYIavqavla 164
Cdd:cd10220  62 ---LEvtYPMENGIVRNWDDMEHLWDYTFGEKLKIDPRECKILLTEPPMNPTKNREKMVEVMFEKYGFAGVYV------- 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 165 laasWTSSKVTDRS---LTGTVVDSGDGVTHIIPVAEGYVIGSSIKTMPLAGRDVT-YFVQSLLRdRNEP---DSSLKTA 237
Cdd:cd10220 132 ----AIQAVLTLYAqglLTGVVVDSGDGVTHIVPVYEGFSLPHLTRRLDVAGRDITrYLIKLLLL-RGYAfnrTADFETV 206
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 238 ERIKEECCYVCPDIVKEfSRFDRE----------PDrylkyasesitghSTTIDVGFERFLAPEIFFNPEIASSDflTP- 306
Cdd:cd10220 207 REIKEKLCYVAYDIELE-QKLALEttvlvesytlPD-------------GRVIKVGGERFEAPEALFQPHLIDVE--GPg 270
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 307 LPELVDNVVQSSPIDVRKGLYKNIVLSGGSTLFKNFGNRLQRDLKRIVDERIhrsemLSGAKSG--GVDVNVISHKRQRN 384
Cdd:cd10220 271 IAELLFNTIQAADIDTRPELYKHIVLSGGSTMYPGLPSRLEKEIKQLYLERV-----LKGDTERlsKFKIRIEDPPRRKH 345
                       410       420       430
                ....*....|....*....|....*....|....*....
gi 19113810 385 AVWFGGSLLA----QTPEFGSychTKADYEEYGASIARR 419
Cdd:cd10220 346 MVFLGGAVLAdimkDKDEFWI---TRQEYEEQGVRVLDK 381
PTZ00004 PTZ00004
actin-2; Provisional
8-419 1.27e-86

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 268.95  E-value: 1.27e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810    8 IIMDNGTGYSKLGYAGNDAPSYVFPTVIatrsaGASSGPAVSSKpsyMASKgsghlsskratedlDFFIGNDALKKASAG 87
Cdd:PTZ00004   9 AVVDNGSGMVKAGFAGDDAPRCVFPSIV-----GRPKNPGIMVG---MEEK--------------DCYVGDEAQDKRGIL 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810   88 ySLDYPIRHGQIENWDHMERFWQQSLFKYLRCEPEDHYFLLTEPPLNPPENRENTAEIMFESFNCAGLYIavqaVLALAA 167
Cdd:PTZ00004  67 -TLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETHNVPAMYV----AIQAVL 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  168 SWTSSKVTdrslTGTVVDSGDGVTHIIPVAEGYVIGSSIKTMPLAGRDVTYFVQSLLRDRnePDSSLKTAER-----IKE 242
Cdd:PTZ00004 142 SLYASGRT----TGIVLDSGDGVSHTVPIYEGYSLPHAIHRLDVAGRDLTEYMMKILHER--GTTFTTTAEKeivrdIKE 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  243 ECCYVCPDIVKEFSRFDREPDRYLKyASESITGhsTTIDVGFERFLAPEIFFNPEIASSDFLTPLPELVDNVVQSSPIDV 322
Cdd:PTZ00004 216 KLCYIALDFDEEMGNSAGSSDKYEE-SYELPDG--TIITVGSERFRCPEALFQPSLIGKEEPPGIHELTFQSINKCDIDI 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  323 RKGLYKNIVLSGGSTLFKNFGNRLQRDLKRIVDERIhrsemlsgaksggvDVNVISHKRQRNAVWFGGSLLAQTPEFGSY 402
Cdd:PTZ00004 293 RKDLYGNIVLSGGTTMYRGLPERLTKELTTLAPSTM--------------KIKVVAPPERKYSVWIGGSILSSLPTFQQM 358
                        410
                 ....*....|....*..
gi 19113810  403 CHTKADYEEYGASIARR 419
Cdd:PTZ00004 359 WVTKEEYDESGPSIVHR 375
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
6-416 2.48e-86

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: 267.69  E-value: 2.48e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810   6 VPIIMDNGTGYSKLGYAGNDAPSYVFPTVIA-TRSAGASSGpavsskpsyMASKgsghlsskratedlDFFIGNDALKKA 84
Cdd:cd10224   1 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGrPRHQGVMVG---------MGQK--------------DSYVGDEAQSKR 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  85 SAgYSLDYPIRHGQIENWDHMERFWQQSLFKYLRCEPEDHYFLLTEPPLNPPENRENTAEIMFESFNCAGLYIavqaVLA 164
Cdd:cd10224  58 GI-LTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYV----AIQ 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 165 LAASWTSSKVTdrslTGTVVDSGDGVTHIIPVAEGYVIGSSIKTMPLAGRDVTYFVQSLLRDRNEPDSSlkTAER----- 239
Cdd:cd10224 133 AVLSLYASGRT----TGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTT--TAEReivrd 206
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 240 IKEECCYVCPDivkefsrFDREpdryLKYASESITGHST-------TIDVGFERFLAPEIFFNPEIASSDFlTPLPELVD 312
Cdd:cd10224 207 IKEKLCYVALD-------FEQE----MQTAASSSSLEKSyelpdgqVITIGNERFRCPEALFQPSFLGMEA-AGIHETTY 274
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 313 NVVQSSPIDVRKGLYKNIVLSGGSTLFKNFGNRLQRDLKRIVDerihrSEMlsgaksggvDVNVISHKRQRNAVWFGGSL 392
Cdd:cd10224 275 NSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAP-----STM---------KIKIVAPPERKYSVWIGGSI 340
                       410       420
                ....*....|....*....|....
gi 19113810 393 LAQTPEFGSYCHTKADYEEYGASI 416
Cdd:cd10224 341 LASLSTFQQMWISKQEYDESGPSI 364
ASKHA_NBD_actin-like cd10169
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ...
8-413 9.63e-84

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: 257.03  E-value: 9.63e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810   8 IIMDNGTGYSKLGYAGNDAPSYVFPtviatrsagassgpavsskpsymaskgsghlsskratedldffigndalkkasag 87
Cdd:cd10169   1 IVIDNGSGTIKAGFAGEDAPRLIFP------------------------------------------------------- 25
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  88 ysldypirhgqienWDHMERFWQQSLFKYLRCEPEDHYFLLTEPPLNPPENRENTAEIMFESFNCAGLYIavqaVLALAA 167
Cdd:cd10169  26 --------------WDDMEKIWEHVFYNLLRVDPEEHPVLLTEPPLNPKANREKLAEILFETFNVPSLYI----ANQAVL 87
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 168 SWTSSKVTdrslTGTVVDSGDGVTHIIPVAEGYVIGSSIKTMPLAGRDVTYFVQSLLRDRNEPDSS---LKTAERIKEEC 244
Cdd:cd10169  88 SLYASGRT----TGLVVDSGEGVTHIVPVYEGYVLPHAVRRLDIGGRDLTDYLAKLLREKGYSFSTsaeREIVRDIKEKL 163
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 245 CyvcpdivkefsrfdrepdrylkyasesitghsttidvgferflapeiffnpeiassdfltPLPELVDNVVQSSPIDVRK 324
Cdd:cd10169 164 C------------------------------------------------------------GLHELIYDSIMKCDIDLRK 183
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 325 GLYKNIVLSGGSTLFKNFGNRLQRDLKRIVDERIHrsemlsgaksggvdVNVISHKRQRNAVWFGGSLLAQTPEFGSYCH 404
Cdd:cd10169 184 ELYSNIVLSGGTTLFPGFAERLQKELSKLAPSSVK--------------VKVIAPPERKYSAWIGGSILASLSTFQQMWI 249

                ....*....
gi 19113810 405 TKADYEEYG 413
Cdd:cd10169 250 TKEEYEEHG 258
PTZ00466 PTZ00466
actin-like protein; Provisional
5-419 1.30e-79

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 250.63  E-value: 1.30e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810    5 NVPIIMDNGTGYSKLGYAGNDAPSYVFPTVIAtrsagassgpavssKPSY---MASKGSGhlsskratedlDFFIGNDAl 81
Cdd:PTZ00466  12 NQPIIIDNGTGYIKAGFAGEDVPNLVFPSYVG--------------RPKYkrvMAGAVEG-----------NIFVGNKA- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810   82 KKASAGYSLDYPIRHGQIENWDHMERFWQQsLFKYLRCEPEDHYFLLTEPPLNPPENRENTAEIMFESFNCAGLYIavqa 161
Cdd:PTZ00466  66 EEYRGLLKVTYPINHGIIENWNDMENIWIH-VYNSMKINSEEHPVLLTEAPLNPQKNKEKIAEVFFETFNVPALFI---- 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  162 VLALAASWTSSKVTdrslTGTVVDSGDGVTHIIPVAEGYVIGSSIKTMPLAGRDVTYFVQSLLRdRN----EPDSSLKTA 237
Cdd:PTZ00466 141 SIQAILSLYSCGKT----NGTVLDCGDGVCHCVSIYEGYSITNTITRTDVAGRDITTYLGYLLR-KNghlfNTSAEMEVV 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  238 ERIKEECCYVCPDIVKEFSRFDREPDRYlkyasESITGHSTTIDVGFERFLAPEIFFNPEIASSDFLTpLPELVDNVVQS 317
Cdd:PTZ00466 216 KNMKENCCYVSFNMNKEKNSSEKALTTL-----PYILPDGSQILIGSERYRAPEVLFNPSILGLEYLG-LSELIVTSITR 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  318 SPIDVRKGLYKNIVLSGGSTLFKNFGNRLQRDLKRIVDERIhrsemlsgaksggvDVNVISHKRQRNAVWFGGSLLAQTP 397
Cdd:PTZ00466 290 ADMDLRRTLYSHIVLSGGTTMFHGFGDRLLNEIRKFAPKDI--------------TIRISAPPERKFSTFIGGSILASLA 355
                        410       420
                 ....*....|....*....|..
gi 19113810  398 EFGSYCHTKADYEEYGASIARR 419
Cdd:PTZ00466 356 TFKKIWISKQEFDEYGSVILHR 377
PTZ00281 PTZ00281
actin; Provisional
8-419 2.95e-73

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 234.21  E-value: 2.95e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810    8 IIMDNGTGYSKLGYAGNDAPSYVFPTVIA-TRSAGASSGpavsskpsyMASKGSghlsskratedldfFIGNDALKKASA 86
Cdd:PTZ00281   9 LVIDNGSGMCKAGFAGDDAPRAVFPSIVGrPRHTGVMVG---------MGQKDS--------------YVGDEAQSKRGI 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810   87 gYSLDYPIRHGQIENWDHMERFWQQSLFKYLRCEPEDHYFLLTEPPLNPPENRENTAEIMFESFNCAGLYIAVQAVLALA 166
Cdd:PTZ00281  66 -LTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLY 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  167 ASWTSskvtdrslTGTVVDSGDGVTHIIPVAEGYVIGSSIKTMPLAGRDVTYFVQSLLRDRNEpdSSLKTAER-----IK 241
Cdd:PTZ00281 145 ASGRT--------TGIVMDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGY--SFTTTAEReivrdIK 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  242 EECCYVCPDIVKEFSrfDREPDRYLKYASESITGHSTTIdvGFERFLAPEIFFNPEIASSDfLTPLPELVDNVVQSSPID 321
Cdd:PTZ00281 215 EKLAYVALDFEAEMQ--TAASSSALEKSYELPDGQVITI--GNERFRCPEALFQPSFLGME-SAGIHETTYNSIMKCDVD 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  322 VRKGLYKNIVLSGGSTLFKNFGNRLQRDLKRIVDERIhrsemlsgaksggvDVNVISHKRQRNAVWFGGSLLAQTPEFGS 401
Cdd:PTZ00281 290 IRKDLYGNVVLSGGTTMFPGIADRMNKELTALAPSTM--------------KIKIIAPPERKYSVWIGGSILASLSTFQQ 355
                        410
                 ....*....|....*...
gi 19113810  402 YCHTKADYEEYGASIARR 419
Cdd:PTZ00281 356 MWISKEEYDESGPSIVHR 373
ASKHA_NBD_ACTL7 cd10214
nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ...
7-419 1.71e-68

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: 221.53  E-value: 1.71e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810   7 PIIMDNGTGYSKLGYAGNDAPSYVFPTVIATRsagassgpavsskpsYMASKGSGhlSSKRATedldfFIGnDALKKASA 86
Cdd:cd10214   5 AVIIDLGTGYCKAGFAGQPRPSYVISSTVGKP---------------PQESAKTG--DNRKET-----FVG-KELANVEP 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  87 GYSLDYPIRHGQIENWDHMERFWQQSLFKYLRCEPEDHYFLLTEPPLNPPENRENTAEIMFESFNCAGLYIavqaVLALA 166
Cdd:cd10214  62 PLKLVNPLRHGIVVDWDCVQDIWEYIFEKEMKILPEEHAVLVSDPPLSPTTNREKYAELMFETFSIPAMHI----AYQSR 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 167 ASWTSSKVTdrslTGTVVDSGDGVTHIIPVAEGYVIGSSIKTMPLAGRDVTYFVQSLLRDRNEP--DSSLKTAERIKEEC 244
Cdd:cd10214 138 LSLYSYGRT----SGLVVESGHGVSYVVPIHEGYNLPHITGRADYAGSDLTAYLMKLLNEAGNKftDDQLHIVEDIKKKC 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 245 CYVCPDIVKEFSRfdrePDRYLKYASESITGHstTIDVGFERFLAPEIFFNPEIASSdfLTP-LPELVDNVVQSSPIDVR 323
Cdd:cd10214 214 CYVALDFEEEMGL----PPQEYTVDYELPDGH--LITIGKERFRCPEMLFNPSLIGS--KQPgLHTLTMNSLNKCDANLK 285
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 324 KGLYKNIVLSGGSTLFKNFGNRLQRDLKRivderihrseMLSGaksggvDVNVISHKRQRN-AVWFGGSLLAQTPEFGSY 402
Cdd:cd10214 286 KDLAKNILLCGGSTMFDGFPDRFQKELSK----------LCPN------DNPIVAASPERKySVWTGGSILASLKSFQQL 349
                       410
                ....*....|....*..
gi 19113810 403 CHTKADYEEYGASIARR 419
Cdd:cd10214 350 WVRRREYEERGPFVIYR 366
ASKHA_NBD_Arp4_ACTL6-like cd13395
nucleotide-binding domain (NBD) of the actin-related protein 4 (Arp4)-like subfamily; The ...
8-413 2.26e-67

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: 220.13  E-value: 2.26e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810   8 IIMDNGTGYSKLGYAGNDAPSYVFPTVIATRSAGAssgpavsskpsyMASKGSGHLSSKRATedldFFIGNDALKKASAG 87
Cdd:cd13395   7 LVLDIGSYSTRAGYAGEDTPKAVFPSVVGVVTDDD------------DAEDYVGGSGEKKRK----YYIGTNSIGVPRPN 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  88 YSLDYPIRHGQIENWDHMERFWQQSLFKYLRCEPEDHYFLLTEPPLNPPENRENTAEIMFESFNCAGLYIAVQAVLalaa 167
Cdd:cd13395  71 MEVISPLKDGLIEDWDAFEKLWDHALKNRLRVDPSEHPLLLTEPSWNTRANREKLTELMFEKYNVPAFFLAKNAVL---- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 168 swtSSKVTDRSlTGTVVDSGDGVTHIIPVAEGYVIGSSIKTMPLAGRDVTYFVQSLLRDRN---EPDSSL--KTAERIKE 242
Cdd:cd13395 147 ---SAFANGRS-TALVVDSGATSTSVVPVHDGYVLQKAIVRSPLGGDFLTDQLLKLLESKNieiIPRYMIksKEPVEGGA 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 243 ECCYVC---PDIVKEFSRFDRE--------------PDRYLKYASESITGHS------TTIDVGFERFLAPEIFFNPEIA 299
Cdd:cd13395 223 PAKYTKkdlPNTTSSYHRYMVRrvlqdfkesvcqvsDSPFDESEAASIPTVSyelpdgYNIEFGAERFKIPELLFDPSLV 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 300 SSDF--------LTPLPELVDNVVQSSPIDVRKGLYKNIVLSGGSTLFKNFGNRLQRDLkrivderihrSEMLSGAksgg 371
Cdd:cd13395 303 KGIPappsegneLLGLPQLVYTSIGSCDVDIRPELYGNVVLTGGNSLLPGFTDRLNREL----------SEKAPGS---- 368
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*
gi 19113810 372 VDVNVIS---HKRQRNAVWFGGSLLAQTPEFGSYCHTKADYEEYG 413
Cdd:cd13395 369 LKLKILAsgnTVERRFSSWIGGSILASLGSFQQMWISKQEYEEHG 413
ASKHA_NBD_Arp6 cd10210
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ...
8-413 3.02e-58

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: 195.46  E-value: 3.02e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810   8 IIMDNGTGYSKLGYAGNDAPSyVFPTVIAtrsagassgpavsskpsymaskgsgHLSSKRATedldFFIGNDALK-KASA 86
Cdd:cd10210   2 LVLDNGAYTIKAGFASDDPPR-VIPNCIA-------------------------KPKSERRR----LFGDDQLDEcKDLS 51
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  87 GYSLDYPIRHGQIENWDHMERFWQQSLFK-YLRCEPEDHYFLLTEPPLNPPENRENTAEIMFESFNCAGLYIAVQAV--L 163
Cdd:cd10210  52 GLFYRRPFERGYLVNWDLQRQIWDHLFGKlLLNVDPSDTALVLTEPPFNPPSIQEAMDEIVFEEYGFQSLYRTTAAAlsA 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 164 ALAASWTSSKVTDRSLTGTVVDSGDGVTHIIPVAEGYVIGSSIKTMPLAGRDVTYFVQSLLrdrnepdsSLKT------- 236
Cdd:cd10210 132 FAYLADSEQSSSSSSQCCLVVDSGFSFTHIVPFFDGKPVKRAVRRIDVGGKLLTNYLKEII--------SYRQlnvmdet 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 237 --AERIKEECCYVCPDIVKE---------FSRFDRE---PD------RYLKYASESITGHST----TIDVGFERFLAPEI 292
Cdd:cd10210 204 ylVNQIKEDLCFVSTDFYEDleiakkkgkENTIRRDyvlPDyttskrGYVRDPEEPNRGKLKedeqVLRLNNERFTVPEL 283
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 293 FFNPeiasSD-FLTP--LPELVDNVVQSSPIDVRKGLYKNIVLSGGSTLFKNFGNRLQRDLKRIVderihrsemlsgakS 369
Cdd:cd10210 284 LFHP----SDiGIQQagIAEAIVQSINACPEELQPLLYANIVLTGGNALFPGFRERLEAELRSLA--------------P 345
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 19113810 370 GGVDVNVISHKRQRNAVWFGGSLLAQTPEFGSYCHTKADYEEYG 413
Cdd:cd10210 346 DDYDVNVTLPEDPITYAWEGGSLLAQSPEFEELAVTRAEYEEHG 389
PTZ00452 PTZ00452
actin; Provisional
8-419 8.22e-53

actin; Provisional


Pssm-ID: 185631  Cd Length: 375  Bit Score: 181.11  E-value: 8.22e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810    8 IIMDNGTGYSKLGYAGNDAPSYVFPTVIATrsagassgpavsskpsymaskgSGHLSSKRATEDLDFFIGNDALKKASAg 87
Cdd:PTZ00452   8 VVIDNGSGYCKIGIAGDDAPTSCFPAIVGR----------------------SKQNDGIFSTFNKEYYVGEEAQAKRGV- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810   88 YSLDYPIRHGQIENWDHMERFWQQSLFKYLRCEPEDHYFLLTEPPLNPPENRENTAEIMFESFNCAGLYIAVQAVLALaa 167
Cdd:PTZ00452  65 LAIKEPIQNGIINSWDDIEIIWHHAFYNELCMSPEDQPVFMTDAPMNSKFNRERMTQIMFETFNTPCLYISNEAVLSL-- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  168 sWTSSKVtdrslTGTVVDSGDGVTHIIPVAEGYVIGSSIKTMPLAGRDVTYFVQSLLRD----RNEPDSSLkTAERIKEE 243
Cdd:PTZ00452 143 -YTSGKT-----IGLVVDSGEGVTHCVPVFEGHQIPQAITKINLAGRLCTDYLTQILQElgysLTEPHQRI-IVKNIKER 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  244 CCYVC--PDIVKEFSRFDREPDRYLKYASESItghsttIDVGFERFLAPEIFFNPEIASSDfLTPLPELVDNVVQSSPID 321
Cdd:PTZ00452 216 LCYTAldPQDEKRIYKESNSQDSPYKLPDGNI------LTIKSQKFRCSEILFQPKLIGLE-VAGIHHLAYSSIKKCDLD 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  322 VRKGLYKNIVLSGGSTLFKNFGNRLQRDLKRIVDERIhrsemlsgaksggvDVNVISHKRQRNAVWFGGS----LLAQTP 397
Cdd:PTZ00452 289 LRQELCRNIVLSGGTTLFPGIANRLSNELTNLVPSQL--------------KIQVAAPPDRRFSAWIGGSiqctLSTQQP 354
                        410       420
                 ....*....|....*....|..
gi 19113810  398 EFgsycHTKADYEEYGASIARR 419
Cdd:PTZ00452 355 QW----IKRQEYDEQGPSIVHR 372
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
7-414 7.97e-42

nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, also called actin-like protein 5, may act as a core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. It is involved in DNA double-strand break repair and UV-damage excision repair. Human Arp5 is encoded by the ACTR5 gene. Arabidopsis thaliana ARP5 (AtARp5) is a ubiquitously expressed nuclear protein involved in DNA repair and required for multicellular development of all organs. AtARp5 may be part of other chromatin remodeling machines in addition to INO80.


Pssm-ID: 466817 [Multi-domain]  Cd Length: 345  Bit Score: 150.80  E-value: 7.97e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810   7 PIIMDNGTGYSKLGYAGNDAPSYVFPTVIAtRSAGassgpavsskpsymaskgsghlsskRATEDLDFFIGNDALKKASA 86
Cdd:cd10211   1 PIVIDNGSYQCRAGWAGDKEPRLVFRNLVA-KPRD-------------------------RKKGITVTLVGNDILNDEAV 54
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  87 GYSLDYPIRHGQIENWDHMErfwqqSLFKYL-------RCEPEDHYFLLTEPPLNPPENRENTAEIMFE-------SFNC 152
Cdd:cd10211  55 RSHLRSPFDRNVVTNFDLQE-----QILDYIfshlginSEGSVDHPIVLTEALCNPNYSRQLMSELLFEcygvpsvAYGI 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 153 AGLYiavqavlalaaSWTSSKVTDRSLTGTVVDSGDGVTHIIPVAEGYVIGSSIKTMPLAGRDVTYFVQSLLrdrnepds 232
Cdd:cd10211 130 DSLF-----------SYYHNQPQGDPSDGLVISSGYSTTHVIPVLNGRLDLSQCKRINLGGFHATDYLQRLL-------- 190
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 233 SLK-----------TAERIKEECCYVCPDIVKEFSRFD-----REPDRYLKYAsesitghsttidVGferflapeiffnp 296
Cdd:cd10211 191 QLKypthpsaitlsRAEELVHEHCYVAEDYDEELKKWEdpeyyEENVRKIQLP------------FG------------- 245
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 297 eiassdfltpLPELVDNVVQSSPIDVRKGLYKNIVLSGGSTLFKNFGNRLQRDLKRIVDErihrsemlsgaksgGVDVNV 376
Cdd:cd10211 246 ----------LVETIEFVLKRYPAEQQDRLVQNVFLTGGNALFPGLKERLEKELRAIRPF--------------GSPFNV 301
                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 19113810 377 ishKRQRNAV---WFGGSLLAQTPEFGSYCHTKADYEEYGA 414
Cdd:cd10211 302 ---VRAKDPVldaWRGAAKWALDSTFEKVWITKQEYEEKGG 339
COG5277 COG5277
Actin-related protein [Cytoskeleton];
4-394 1.54e-38

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 143.78  E-value: 1.54e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810   4 FNVPIIMDNGTGYSKLG-YAGNDAPSYVFPTVIATRSAGAS--SGPA-VSSKPSYMASKGSGHLSSKRatedldffignd 79
Cdd:COG5277   7 LKYVIGIDFGTSYVKYGpIALEEKPRVIQTRGLFLRIVGESklLGPMeGLSRGLVVGDEVSKYLSSVR------------ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  80 alkkaSAGYSLDYPIRHGQIE-----NWDHMERFWQQSLFKYLRCEPEDHYFL--LTEPPLNPPENRENTAEIMFESFNC 152
Cdd:COG5277  75 -----DAIRNLKYPLRDGIVRrddedAWRVLKELLRYTFAQFLVVDPEFHGFLvvVALSALAPDYMRERLFDIHFEVFSE 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 153 AGLYIAVQAVLALAASWTSSKVTdrsltGTVVDSGDGVTHIIPVAEGyVIGSSIKTMPLAGRDVTYFVQSLLRDRNEPDS 232
Cdd:COG5277 150 EGAPAVTIIPQPLAVAIAEKAVT-----CVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSDT 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 233 SL--KTAERIKEECCYVCPDIVKEFSRFDREPDRYLkyASESITGHSTTIDVG---FERFLAPEIFFNPE------IASS 301
Cdd:COG5277 224 AReeYVVRVVKEALGLVPRDLAKAIQKAASNPDSFE--AKVRLPNPTVEIELGnyaWERFLIGEILFNPNhegfesYIQQ 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 302 DFLTP---------------LPELVDNVVQSSPIDVRKGLYKNIVLSGGSTLFknfgnRLQRDLKRIVDERIHRSEMLSG 366
Cdd:COG5277 302 GRLRIedavigdvvlygemgLAEAIINSIMKCDVEIQDELYSNIILSGGAFNW-----SVPPGLEDVAVDSVTRVQIELS 376
                       410       420
                ....*....|....*....|....*...
gi 19113810 367 AKSGGVDVNVISHKRQRNAVWFGGSLLA 394
Cdd:COG5277 377 ELAPELKVNVRLVSDPQYSVWKGAIIYG 404
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
8-417 1.56e-38

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: 142.14  E-value: 1.56e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810   8 IIMDNGTGYSKLGYAGND-APSYVFPTViatrsagassgpavsskpsyMASKGSGHLSSKRATEDldffigndalkkasa 86
Cdd:cd10209   1 VVIDAGSRLLKAGYAYPDrEPSVVEPTR--------------------VTPAVEDGEESDTVVEG--------------- 45
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  87 gySLDYPIRHGQIENWDHMERFWQQSLfkYLRCEPEDHY---FLLTEPPLNPPENRENTAEIMFESFNCAGLYIAVQavl 163
Cdd:cd10209  46 --NTVSPIRRGRIEDWDALEALLRYVF--YTGLGWEEGNegqVLIAEPLLTSKAERERLTQLMFETFNVSGLYASEQ--- 118
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 164 alaaSWTSSKVTDRsLTGTVVDSGDGVTHIIPVAEGYVIGSSIKTMPLAGRDVTYFVQSLLRDRNEPDS-SLKTAERIKE 242
Cdd:cd10209 119 ----AVLSLYAVGR-ISGCVVDVGHGKIDIAPVWEGAIQHNAVRRFEIGGRDLTELLAAELGKSNPKVKlDRSIVERLKE 193
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 243 ECCYVCPDIVKEFSrfdrepdrylKYASESITGHS----TTIDVGFERFLAPEIFFNPEIASSDfLTPLPELVDNVVQSS 318
Cdd:cd10209 194 AVAWSADDEEAYEK----------KVLTCSPETYTlpdgRVISVGKERYCVGEALFRPSILGIE-EYGIVEQLVRAVSTS 262
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 319 PIDVRKGLYKNIVLSGGSTLFKNFGNRLQRDLkrivderihrsEMLSGAKSGGVDVNV---ISHKRQRNAVWFGGSLLAQ 395
Cdd:cd10209 263 PSENRRQLLENIVLCGGTSSVPGLEARLQKEI-----------RLLSSPSSRPALVKPpeyMPENTLRYSAWIGGAILAK 331
                       410       420
                ....*....|....*....|...
gi 19113810 396 TPeFGSYCH-TKADYEEYGASIA 417
Cdd:cd10209 332 VV-FPQNQHvTKADYDETGPSVV 353
ASKHA_NBD_Arp10 cd10207
nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins; ...
8-413 3.46e-34

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: 130.84  E-value: 3.46e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810   8 IIMDNGTGYSKLGYAGNDAPSYVFPTVIATRSAGassgpavssKPSYMASKGSGHlsskraTEDLDffignDALKkasag 87
Cdd:cd10207   1 VVLDIGSAYTKCGFAGESAPRCIIPSEVKLPGGK---------KVIRVVDQRSGN------EEELY-----EALK----- 55
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  88 ysldypirhgqienwdhmeRFWQQSLFKYLRCEPEDHYFLLTEPPLNPPENRENTAEIMFESFNCAGLyiavqavlalaa 167
Cdd:cd10207  56 -------------------EFLHELYFKHLLVNPKDRRVVVVESVLCPTPFRETLAKVLFKHFEVPSV------------ 104
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 168 SWTSSKVTdrSL------TGTVVDSGDGVTHIIPVAEGYVIGSSIKTMPLAGRDVTYFVQSLLRDRN------------- 228
Cdd:cd10207 105 LFAPSHLL--SLltlgirTALVVDCGYRETRVLPVYEGVPLLSAWQSTPLGGKALHKRLKKLLLEHAtvvtgdnkgqlls 182
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 229 EPDSSL--KTAERIKEECCYVCP-DIVKEFSRFDREPDRY--LKYASESITGHSTTID--VGFERFLAPEIFFNPEIass 301
Cdd:cd10207 183 SVDSLLseEVLEDIKVRACFVTSlERGKTLQSATEEGSTEepSPPPPVDYPLDGEKILivPGSIRESAEELLFEGDN--- 259
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 302 DFlTPLPELVDNVVQSSPIDVRKGLYKNIVLSGGSTLFKNFGNRLQRDLKRIVDERiHRSEMLSGAKSGGVDVNVISHkr 381
Cdd:cd10207 260 EE-KSLPTLILDSLLKCPIDVRKQLAENIVVIGGTSMLPGFKHRLLEELRALLRKP-KYFEELAPKTFRFHTPPSVFK-- 335
                       410       420       430
                ....*....|....*....|....*....|...
gi 19113810 382 qRNAV-WFGGSLLAQTPEFGSYCHTKADYEEYG 413
Cdd:cd10207 336 -PNYLaWLGGSIFGALESILGRSLSREAYLQTG 367
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
92-418 4.20e-29

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: 116.64  E-value: 4.20e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  92 YPIRHGQIENWDHMERFWQQSLFKYL--RCEPEDHYFLLTEPPLNPPENRENTAEIMFESFNCAGLYIavqavlalaasw 169
Cdd:cd10208  37 WPIQDGRVVDWDALEALWRHILFSLLsiPRPTNNSPVLLSVPPSWSKSDLELLTQLFFERLNVPAFAI------------ 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 170 tsskvTDRSL---------TGTVVDSGDGVTHIIPVAEGYVIGSSIKTMPLAGRDVTYFVQSLLRDRNEPDSSLKT---- 236
Cdd:cd10208 105 -----LEAPLaalyaagatSGIVVDIGHEKTDITPIVDSQVVPHALVSIPIGGQDCTAHLAQLLKSDEPELKSQAEsgee 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 237 -----AERIKEEccyvcpDIVkEFSRFDREPDrylkyasesitgHSTTIDVGFERFLAPEIFFNPEIASSDFLTPLPELV 311
Cdd:cd10208 180 atldlAEALKKS------PIC-EVLSDGADLA------------SGTEITVGKERFRACEPLFKPSSLRVDLLIAAIAGA 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 312 DNVVQSSPIDVRKGLYKNIVLSGGSTLFKNFGNRLQRDLKrivdERIHRSEMLSGA-------------------KSGGV 372
Cdd:cd10208 241 LVLNASDEPDKRPALWENIIIVGGGSRIRGLKEALLSELQ----QFHLISETSASPqqpriirlakipdyfpewkKSGYE 316
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 19113810 373 DvnvishkrqrnAVWFGGSLLAQT--PEFGSYCH-TKADYEEYGASIAR 418
Cdd:cd10208 317 E-----------AAFLGASIVAKLvfNDPSSKHYiSKVDYNEKGPAAIH 354
ASKHA_NBD_Arp8-like cd10206
nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The ...
73-395 1.85e-16

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: 80.75  E-value: 1.85e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  73 DFFIGNDALK-KASAGYSLDYPIRHGQIeNW-----------DHMERFWQQSLFKYLRCEPED--HYF-LLTEPPL-NPP 136
Cdd:cd10206 121 DFLVGEEALRlPPSEEYNLHWPIRRGRL-NVhsdggsltavlDDLEDIWSHALEEKLEIPRKDlkNYRaVLVIPDLfDRR 199
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 137 ENREnTAEIMFES--FNCAGLYiavqavlalaaswtsskvtDRSL---------TGTVVDSGDGVTHIIPVAEGYVIGSS 205
Cdd:cd10206 200 HVKE-LVDLLLRRlgFSSVFVH-------------------QESVcatfgaglsSACVVDIGAQKTSVACVEDGLSIPNS 259
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 206 IKTMPLAGRDVTYFVQSLLRDRNEP--DSSLKT------AERIKEECCYVCPDI--VKEFSRFDREPDR-YLKYAsesit 274
Cdd:cd10206 260 RIRLPYGGDDITRCFLWLLRRSGFPyrECNLNSpldfllLERLKETYCTLDQDDigVQLHEFYVREPGQpTLKYQ----- 334
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 275 ghsttidvgferflapeifFNpeiassdfLTPlpeLVDNVVQS----SPIDVRKGLYKNIVLSGGSTLFKNFGNRLQrdl 350
Cdd:cd10206 335 -------------------FK--------LLP---LDEAIVQSilscASDELKRKMYSSILLVGGGAKIPGLAEALE--- 381
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 19113810 351 krivdERIHRSemLSGAKSGGVDVNVISHKRQ---RNAVWFGGSLLAQ 395
Cdd:cd10206 382 -----DRLLIK--IPSLFEAVETVEVLPPPKDmdpSLLAWKGGAVLAC 422
ASKHA_NBD_AtArp8-like cd13396
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and ...
177-406 1.30e-14

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: 74.50  E-value: 1.30e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 177 RSLTGTVVDSGDGVTHIIPVAEGYVIGS-SIKTMPLAGRDVTYFVQSLLRDRNEPDSSLKTAERIKEECCYVCPDIVKEF 255
Cdd:cd13396 113 NRTSGIVVNIGFRVTTIVPVYRGRVMHDiGVEVVGQGALRLTGFLKELMQQNGIRFPSLYTVRTIKEKLCYVAEDYEAEL 192
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 256 SRfDREpdrylkyASESITGHSTTIdVGFERFLAPEIFFNPEIASSDFLTpLPELVDNVVQSSPIDVRKG---LYKNIVL 332
Cdd:cd13396 193 AK-DTQ-------ASCEVAGEGWFT-LSNERFKTGEILFQPGLGGMRAMG-LHQAVALCMDHCALVHSQGddgWFKTIVL 262
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19113810 333 SGGSTLFKNFGNRLQRDLKRIVDerihrSEMLSGaksggvdVNVISHKRQRNAVWFGGSLLAQTPEF-GSYCHTK 406
Cdd:cd13396 263 SGGSACLPGLSERLERELRKLLP-----KSLSEG-------IRIIPPPLGPDSAWQGAKLISNLSNFpDGWCITK 325
ASKHA_NBD_MamK cd24009
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ...
73-360 6.14e-05

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: 44.89  E-value: 6.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810  73 DFFIGNDALKKASAGySLDYPIRHGQIENWD----HMERFWQQSLFKYLRCEPEDH-YFLLTEPPLNPPENRENTAEIMF 147
Cdd:cd24009  44 EVLFGDEALENRLAL-DLRRPLEDGVIKEGDdrdlEAARELLQHLIELALPGPDDEiYAVIGVPARASAENKQALLEIAR 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 148 ESFN---------CAGLYIavqavlalaaswtsskvtdRSLTGT-VVDSGDGVTHI------IPVAEGYVigssikTMPL 211
Cdd:cd24009 123 ELVDgvmvvsepfAVAYGL-------------------DRLDNSlIVDIGAGTTDLcrmkgtIPTEEDQI------TLPK 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 212 AGRDVTYFVQSLLRDRNePDS--SLKTAERIKEECCYVCPD---IVKEFSrfdrepdrylkyasesITGHSTTIDVGfer 286
Cdd:cd24009 178 AGDYIDEELVDLIKERY-PEVqlTLNMARRWKEKYGFVGDAsepVKVELP----------------VDGKPVTYDIT--- 237
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113810 287 flaPEIffnpEIASSDFLTPLPELVDNVVQSSPIDVRKGLYKNIVLSGGSTLFKNFGNRLQRDLKRIVDERIHR 360
Cdd:cd24009 238 ---EEL----RIACESLVPDIVEGIKKLIASFDPEFQEELRNNIVLAGGGSRIRGLDTYIEKALKEYGGGKVTC 304
ASKHA_NBD_ScArp7-like cd10212
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and ...
101-410 3.33e-03

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: 39.70  E-value: 3.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 101 NWDHMERFWQQSLFKYLRCEPEDHYFLLTEPPLNPPENR---ENTAEIMFESFNCAGLYIAVQAVLALAASWTSSKVtdr 177
Cdd:cd10212  77 NWDALEMQWRYLYDTQLKVSPEELPLVITMPATNGKPDMailERYYELAFDKLNVPVFQIVIEPLAIALSMGKSSAF--- 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 178 sltgtVVDSGDGVTHIIPVAEGYVIGSSIKTMPLAGRDVTYFVQS----LLRDRNEPDSSLKTAER-------------- 239
Cdd:cd10212 154 -----VIDIGASGCNVTPIIDGIVVKNAVVRSKFGGDFLDFQVHErlapLIKEENDMENMADEQKRstdvwyeastwiqq 228
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 240 IKEECCYVCPDIVKEFSRFDREP--------------DRYLKYAseSITG------------------HSTTIDVGfERF 287
Cdd:cd10212 229 FKSTMLQVSEKDLFELERYYKEQadiyakqqeqlkqmDQQLQYT--ALTGspnnplvqkknflfkplnKTLTLDLK-ECY 305
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113810 288 LAPEIFFNPEIASSDFlTP---LPELVDNVVQSSPIDVRKGLYKNIVLSGGSTLFKNFGNRLQRDLKRivdeRIHRSEML 364
Cdd:cd10212 306 QFAEYLFKPQLISDKF-SPedgLGPLMAKSVKKAPEQVYSLLLTNVIITGSTSLIEGMEQRIIKELSI----RFPQYKLT 380
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 19113810 365 SGAKSGGVDVNVIShkrqrnavWFGGSLLAQTPEF--GSYcHTKADYE 410
Cdd:cd10212 381 TFANQVMMDRKIQG--------WLGALTMANLPSWslGKW-YSKEDYE 419
ASKHA_NBD_PilM-like cd24004
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ...
177-243 6.30e-03

nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes type IV pilus inner membrane component PilM, cell division protein FtsA, and ethanolamine utilization protein EutJ. PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity. Members in PilM-like family belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466854 [Multi-domain]  Cd Length: 282  Bit Score: 38.43  E-value: 6.30e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19113810 177 RSLTGTVVDSGDGVTHIIPVAEGYVIGSSikTMPLAGRDVTYFV-QSLLrdrnepdSSLKTAERIKEE 243
Cdd:cd24004 112 RDLNIALVDIGAGTTDIALIRNGGIEAYR--MVPLGGDDFTKAIaEGFL-------ISFEEAEKIKRT 170
 
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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