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Conserved domains on  [gi|22122615|ref|NP_666219|]
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beta-centractin isoform b [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
9-375 0e+00

nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, also called centractin, actin-like protein, alpha-centractin, actin-RPV, or centrosome-associated actin homolog, may be a component of a multi-subunit centrosomal complex involved in microtubule-based vesicle motility. In yeast, actin-related protein is essential for viability and is associated with the centrosome. In vertebrates, Arp1 is a core component of the dynactin complex which assists cytoplasmic dynein by increasing its processivity and by regulation of its cargo binding. The dynactin complex is required for the spindle translocation late in anaphase and is involved in a cell wall synthesis checkpoint. ARP1 forms the backbone filament of the dynactin rod structure and serves as the scaffold for the remaining subunits. It is required for proper orientation of the mitotic spindle. Arp1 is the only actin-related protein known to form actin-like filaments. Human Arp1/centractin is encoded by the ACTR1A gene.


:

Pssm-ID: 466820 [Multi-domain]  Cd Length: 370  Bit Score: 815.24  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615   9 NQPVVIDNGSGVIKAGFAGDQIPKYCFPNYVGRPKHMRVMAGALEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMER 88
Cdd:cd10216   1 NQPVVIDNGSGVIKAGFAGDDIPKVVFPSYVGRPKHVRVMAGALEGDVFVGPKAEEHRGLLKIRYPMEHGIVTDWNDMER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  89 IWQYVYSKDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAV 168
Cdd:cd10216  81 IWQYVYSKLQLNTFSEEHPVLLTEAPLNPRKNREKAAEVFFETFNVPALFVSMQAVLSLYASGRTTGVVLDSGDGVTHAV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 169 PIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAEFEVVRTIKERACYLSINPQKDEALE---TEKVQYTLPD 245
Cdd:cd10216 161 PIYEGFALPHSIRRVDIAGRDVTEYLQLLLRKSGYNFHTSAEFEIVREIKEKACYVALNPQKEEKLEeekTEKAQYTLPD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 246 GSTLDVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKKLAPKD 325
Cdd:cd10216 241 GSTIEIGPERFRAPEILFNPELIGLEYPGVHEVLVDSIQKSDLDLRKTLYSNIVLSGGSTLFKGFGDRLLSEVKKLAPKD 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 22122615 326 VKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRKT 375
Cdd:cd10216 321 VKIRISAPPERLYSTWIGGSILASLSTFKKMWVSKKEYEEDGARILHRKT 370
 
Name Accession Description Interval E-value
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
9-375 0e+00

nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, also called centractin, actin-like protein, alpha-centractin, actin-RPV, or centrosome-associated actin homolog, may be a component of a multi-subunit centrosomal complex involved in microtubule-based vesicle motility. In yeast, actin-related protein is essential for viability and is associated with the centrosome. In vertebrates, Arp1 is a core component of the dynactin complex which assists cytoplasmic dynein by increasing its processivity and by regulation of its cargo binding. The dynactin complex is required for the spindle translocation late in anaphase and is involved in a cell wall synthesis checkpoint. ARP1 forms the backbone filament of the dynactin rod structure and serves as the scaffold for the remaining subunits. It is required for proper orientation of the mitotic spindle. Arp1 is the only actin-related protein known to form actin-like filaments. Human Arp1/centractin is encoded by the ACTR1A gene.


Pssm-ID: 466820 [Multi-domain]  Cd Length: 370  Bit Score: 815.24  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615   9 NQPVVIDNGSGVIKAGFAGDQIPKYCFPNYVGRPKHMRVMAGALEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMER 88
Cdd:cd10216   1 NQPVVIDNGSGVIKAGFAGDDIPKVVFPSYVGRPKHVRVMAGALEGDVFVGPKAEEHRGLLKIRYPMEHGIVTDWNDMER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  89 IWQYVYSKDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAV 168
Cdd:cd10216  81 IWQYVYSKLQLNTFSEEHPVLLTEAPLNPRKNREKAAEVFFETFNVPALFVSMQAVLSLYASGRTTGVVLDSGDGVTHAV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 169 PIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAEFEVVRTIKERACYLSINPQKDEALE---TEKVQYTLPD 245
Cdd:cd10216 161 PIYEGFALPHSIRRVDIAGRDVTEYLQLLLRKSGYNFHTSAEFEIVREIKEKACYVALNPQKEEKLEeekTEKAQYTLPD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 246 GSTLDVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKKLAPKD 325
Cdd:cd10216 241 GSTIEIGPERFRAPEILFNPELIGLEYPGVHEVLVDSIQKSDLDLRKTLYSNIVLSGGSTLFKGFGDRLLSEVKKLAPKD 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 22122615 326 VKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRKT 375
Cdd:cd10216 321 VKIRISAPPERLYSTWIGGSILASLSTFKKMWVSKKEYEEDGARILHRKT 370
PTZ00466 PTZ00466
actin-like protein; Provisional
5-376 0e+00

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 591.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615    5 DIIANQPVVIDNGSGVIKAGFAGDQIPKYCFPNYVGRPKHMRVMAGALEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWN 84
Cdd:PTZ00466   8 QLYSNQPIIIDNGTGYIKAGFAGEDVPNLVFPSYVGRPKYKRVMAGAVEGNIFVGNKAEEYRGLLKVTYPINHGIIENWN 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615   85 DMERIWQYVYSkdQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGV 164
Cdd:PTZ00466  88 DMENIWIHVYN--SMKINSEEHPVLLTEAPLNPQKNKEKIAEVFFETFNVPALFISIQAILSLYSCGKTNGTVLDCGDGV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  165 THAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAEFEVVRTIKERACYLSINPQKDEAlETEK----VQ 240
Cdd:PTZ00466 166 CHCVSIYEGYSITNTITRTDVAGRDITTYLGYLLRKNGHLFNTSAEMEVVKNMKENCCYVSFNMNKEKN-SSEKalttLP 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  241 YTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKK 320
Cdd:PTZ00466 245 YILPDGSQILIGSERYRAPEVLFNPSILGLEYLGLSELIVTSITRADMDLRRTLYSHIVLSGGTTMFHGFGDRLLNEIRK 324
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 22122615  321 LAPKDVKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRKTF 376
Cdd:PTZ00466 325 FAPKDITIRISAPPERKFSTFIGGSILASLATFKKIWISKQEFDEYGSVILHRKTF 380
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
9-376 0e+00

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 545.32  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615      9 NQPVVIDNGSGVIKAGFAGDQIPKYCFPNYVGRPKHMRVMAGaLEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMER 88
Cdd:smart00268   1 VPAIVIDNGSGTIKAGFAGEDFPQVVFPSIVGRPKDGKGMVG-DAKDIFVGDEAQEKRGGLELKYPIENGIVENWDDMEK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615     89 IWQYVYSKdQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAV 168
Cdd:smart00268  80 IWDYTFFN-ELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615    169 PIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAEFEVVRTIKERACYLSINPQKDEALE-------TEKVQY 241
Cdd:smart00268 159 PVVDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLAressessKLEKTY 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615    242 TLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKKL 321
Cdd:smart00268 239 ELPDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELKQL 318
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 22122615    322 APKDVKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRKTF 376
Cdd:smart00268 319 APKKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERKCF 373
Actin pfam00022
Actin;
9-376 0e+00

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 532.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615     9 NQPVVIDNGSGVIKAGFAGDQIPKYCFPNYVGRPKHMRVMAgalEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMER 88
Cdd:pfam00022   1 VSALVIDNGSHTTRAGFAGEDAPKAVIPSCVGKPRGTKVEA---ANKYYVGDEALTYRPGMEVRSPVEDGIVVDWDAMEE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615    89 IWQYVYsKDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAV 168
Cdd:pfam00022  78 IWEHVL-KEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615   169 PIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGAD------------------------------FHTSAEFEVVRTIK 218
Cdd:pfam00022 157 PVHDGYVLQKAIRRSDLGGDFLTDYLRELLRSRNIEitprylikskkpgdpapavtkrelpdttysYKTYQERRVLEEIK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615   219 ERACYLSINPQKDEALETE--KVQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESE--------GLHEVLAFAIHKSDM 288
Cdd:pfam00022 237 ESVCYVSDDPFGDETTSSSipTRVYELPDGSTIILGAERFRVPEILFNPSLIGSESElpppqtavGIPELIVDAINACDV 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615   289 DLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDVKIKISAPQ---ERLYSTWIGGSILASLDTFKKMWVSKKEYEE 365
Cdd:pfam00022 317 DLRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVKIIAPGntvERRYSAWIGGSILASLGTFQQMWVSKQEYEE 396
                         410
                  ....*....|.
gi 22122615   366 DGSRAIHRKTF 376
Cdd:pfam00022 397 HGASVVERKCK 407
COG5277 COG5277
Actin-related protein [Cytoskeleton];
9-365 6.47e-75

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 238.15  E-value: 6.47e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615   9 NQPVVIDNGSGVIKAG-FAGDQIPKYC-----FPNYVGRPKHMRVMAGaLEGDLFIGPKAEEH-----RGLLTIRYPMEH 77
Cdd:COG5277   8 KYVIGIDFGTSYVKYGpIALEEKPRVIqtrglFLRIVGESKLLGPMEG-LSRGLVVGDEVSKYlssvrDAIRNLKYPLRD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  78 GVVR-----DWNDMERIWQYVYSKdQLQTFSEEHP--VLLTEAPLNPSKNREKAAEVFFETF---NVPALFISMQAVLSL 147
Cdd:COG5277  87 GIVRrddedAWRVLKELLRYTFAQ-FLVVDPEFHGflVVVALSALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPLAVA 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 148 YATGRTTGVVLDSGDGVTHAVPIYEGfAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFhTSAEFEVVRTIKERACYL--- 224
Cdd:COG5277 166 IAEKAVTCVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSD-TAREEYVVRVVKEALGLVprd 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 225 ---SINPQKDEALETEKVqYTLPDGSTL----DVGPARFRAPELLFQPDLVGDESE----------------------GL 275
Cdd:COG5277 244 lakAIQKAASNPDSFEAK-VRLPNPTVEielgNYAWERFLIGEILFNPNHEGFESYiqqgrlriedavigdvvlygemGL 322
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 276 HEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLF---KGFGD-------RLLSEVKKLAPkDVKIKISAPQERLYSTWIGGS 345
Cdd:COG5277 323 AEAIINSIMKCDVEIQDELYSNIILSGGAFNWsvpPGLEDvavdsvtRVQIELSELAP-ELKVNVRLVSDPQYSVWKGAI 401
                       410       420
                ....*....|....*....|..
gi 22122615 346 ILASLDTFKKMW--VSKKEYEE 365
Cdd:COG5277 402 IYGYALPFSVKWswITKEGWYF 423
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
309-374 4.36e-16

syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in the plant pathogen Pseudomonas syringae and related species. This model was created, in part, to clarify that the family is real and distinct, rather than an artifact of eukaryotic contamination of bacterial genomic sequence data. As of the creation of this HMM, the family is uncharacterized.


Pssm-ID: 468549 [Multi-domain]  Cd Length: 132  Bit Score: 74.25  E-value: 4.36e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22122615  309 GFGDRLLSEVKKLAPKDVKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRK 374
Cdd:NF040575  66 GFYEKLKKSITEKAPKGALIGMTLDPKPESAAWRGAAMYAASEGFVEMAITKQEYDESGPSIVHRK 131
 
Name Accession Description Interval E-value
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
9-375 0e+00

nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, also called centractin, actin-like protein, alpha-centractin, actin-RPV, or centrosome-associated actin homolog, may be a component of a multi-subunit centrosomal complex involved in microtubule-based vesicle motility. In yeast, actin-related protein is essential for viability and is associated with the centrosome. In vertebrates, Arp1 is a core component of the dynactin complex which assists cytoplasmic dynein by increasing its processivity and by regulation of its cargo binding. The dynactin complex is required for the spindle translocation late in anaphase and is involved in a cell wall synthesis checkpoint. ARP1 forms the backbone filament of the dynactin rod structure and serves as the scaffold for the remaining subunits. It is required for proper orientation of the mitotic spindle. Arp1 is the only actin-related protein known to form actin-like filaments. Human Arp1/centractin is encoded by the ACTR1A gene.


Pssm-ID: 466820 [Multi-domain]  Cd Length: 370  Bit Score: 815.24  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615   9 NQPVVIDNGSGVIKAGFAGDQIPKYCFPNYVGRPKHMRVMAGALEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMER 88
Cdd:cd10216   1 NQPVVIDNGSGVIKAGFAGDDIPKVVFPSYVGRPKHVRVMAGALEGDVFVGPKAEEHRGLLKIRYPMEHGIVTDWNDMER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  89 IWQYVYSKDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAV 168
Cdd:cd10216  81 IWQYVYSKLQLNTFSEEHPVLLTEAPLNPRKNREKAAEVFFETFNVPALFVSMQAVLSLYASGRTTGVVLDSGDGVTHAV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 169 PIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAEFEVVRTIKERACYLSINPQKDEALE---TEKVQYTLPD 245
Cdd:cd10216 161 PIYEGFALPHSIRRVDIAGRDVTEYLQLLLRKSGYNFHTSAEFEIVREIKEKACYVALNPQKEEKLEeekTEKAQYTLPD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 246 GSTLDVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKKLAPKD 325
Cdd:cd10216 241 GSTIEIGPERFRAPEILFNPELIGLEYPGVHEVLVDSIQKSDLDLRKTLYSNIVLSGGSTLFKGFGDRLLSEVKKLAPKD 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 22122615 326 VKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRKT 375
Cdd:cd10216 321 VKIRISAPPERLYSTWIGGSILASLSTFKKMWVSKKEYEEDGARILHRKT 370
PTZ00466 PTZ00466
actin-like protein; Provisional
5-376 0e+00

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 591.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615    5 DIIANQPVVIDNGSGVIKAGFAGDQIPKYCFPNYVGRPKHMRVMAGALEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWN 84
Cdd:PTZ00466   8 QLYSNQPIIIDNGTGYIKAGFAGEDVPNLVFPSYVGRPKYKRVMAGAVEGNIFVGNKAEEYRGLLKVTYPINHGIIENWN 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615   85 DMERIWQYVYSkdQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGV 164
Cdd:PTZ00466  88 DMENIWIHVYN--SMKINSEEHPVLLTEAPLNPQKNKEKIAEVFFETFNVPALFISIQAILSLYSCGKTNGTVLDCGDGV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  165 THAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAEFEVVRTIKERACYLSINPQKDEAlETEK----VQ 240
Cdd:PTZ00466 166 CHCVSIYEGYSITNTITRTDVAGRDITTYLGYLLRKNGHLFNTSAEMEVVKNMKENCCYVSFNMNKEKN-SSEKalttLP 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  241 YTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKK 320
Cdd:PTZ00466 245 YILPDGSQILIGSERYRAPEVLFNPSILGLEYLGLSELIVTSITRADMDLRRTLYSHIVLSGGTTMFHGFGDRLLNEIRK 324
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 22122615  321 LAPKDVKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRKTF 376
Cdd:PTZ00466 325 FAPKDITIRISAPPERKFSTFIGGSILASLATFKKIWISKQEFDEYGSVILHRKTF 380
ASKHA_NBD_actin_Arp-T1-3 cd13397
nucleotide-binding domain (NBD) of actin, actin-related proteins T1-T3 (Arp-T1-3), and similar ...
11-367 0e+00

nucleotide-binding domain (NBD) of actin, actin-related proteins T1-T3 (Arp-T1-3), and similar proteins; The family includes actin and human actin-related proteins T1, T2, and T3. Actin is a ubiquitous protein involved in the formation of filaments that are major components of the cytoskeleton. It is a highly dynamic structural protein network involved in processes such as cell contraction, cell motility, vesicle trafficking, intracellular organization, cytokinesis, endocytosis and apoptosis. Arp-T1, encoded by ACTRT1/ARPT1 gene expressed in testis, negatively regulates the Hedgehog (SHH) signaling, binds to the promoter of the SHH signaling mediator, GLI1, and inhibits its expression. Arp-T2 (also called actin-related protein M2; encoded by ACTRT2/ARPM2 gene expressed in testis and various other cell types) and Arp-T3 (also called actin-related protein M1; encoded by ACTRT3/ARPM1 gene expressed in all tested human tissues) play general roles in the organization of the cytoskeleton like other cytoplasmic actin-related proteins.


Pssm-ID: 466848 [Multi-domain]  Cd Length: 359  Bit Score: 578.37  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  11 PVVIDNGSGVIKAGFAGDQIPKYCFPNYVGRPKHMRVMAGALEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMERIW 90
Cdd:cd13397   2 AVVIDNGSGLIKAGFAGEDLPRAVFPSVVGRPKYKAVMLGAGQKEVYVGDEAQEKRGVLTLSYPIEHGIVTNWDDMEKIW 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  91 QYVYsKDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPI 170
Cdd:cd13397  82 HHTF-ENELRVKPEEHPVLLTEAPLNPKQNREKMAEIMFETFGVPAFYVAIQAVLSLYSSGRTTGLVLDSGDGVTHTVPI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 171 YEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAEFEVVRTIKERACYLSINPQKDEALETEKVQ--YTLPDGST 248
Cdd:cd13397 161 YEGYALPHAVQRLDLAGRDLTEYLMKLLKERGHSFTTTAEREIVRDIKEKLCYVALDYEEELKKKSEELEkeYTLPDGQV 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 249 LDVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDVKI 328
Cdd:cd13397 241 IKIGSERFRCPEALFRPSLIGREAPGIHKLVYNSIMKCDIDIRKDLYSNIVLSGGSTMFPGLPERLQKELEALAPSSTKV 320
                       330       340       350
                ....*....|....*....|....*....|....*....
gi 22122615 329 KISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDG 367
Cdd:cd13397 321 KVIAPPERKYSVWIGGSILASLSTFKSMWITRAEYDEFG 359
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
9-376 0e+00

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 545.32  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615      9 NQPVVIDNGSGVIKAGFAGDQIPKYCFPNYVGRPKHMRVMAGaLEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMER 88
Cdd:smart00268   1 VPAIVIDNGSGTIKAGFAGEDFPQVVFPSIVGRPKDGKGMVG-DAKDIFVGDEAQEKRGGLELKYPIENGIVENWDDMEK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615     89 IWQYVYSKdQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAV 168
Cdd:smart00268  80 IWDYTFFN-ELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615    169 PIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAEFEVVRTIKERACYLSINPQKDEALE-------TEKVQY 241
Cdd:smart00268 159 PVVDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLAressessKLEKTY 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615    242 TLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKKL 321
Cdd:smart00268 239 ELPDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELKQL 318
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 22122615    322 APKDVKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRKTF 376
Cdd:smart00268 319 APKKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERKCF 373
Actin pfam00022
Actin;
9-376 0e+00

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 532.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615     9 NQPVVIDNGSGVIKAGFAGDQIPKYCFPNYVGRPKHMRVMAgalEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMER 88
Cdd:pfam00022   1 VSALVIDNGSHTTRAGFAGEDAPKAVIPSCVGKPRGTKVEA---ANKYYVGDEALTYRPGMEVRSPVEDGIVVDWDAMEE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615    89 IWQYVYsKDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAV 168
Cdd:pfam00022  78 IWEHVL-KEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615   169 PIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGAD------------------------------FHTSAEFEVVRTIK 218
Cdd:pfam00022 157 PVHDGYVLQKAIRRSDLGGDFLTDYLRELLRSRNIEitprylikskkpgdpapavtkrelpdttysYKTYQERRVLEEIK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615   219 ERACYLSINPQKDEALETE--KVQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESE--------GLHEVLAFAIHKSDM 288
Cdd:pfam00022 237 ESVCYVSDDPFGDETTSSSipTRVYELPDGSTIILGAERFRVPEILFNPSLIGSESElpppqtavGIPELIVDAINACDV 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615   289 DLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDVKIKISAPQ---ERLYSTWIGGSILASLDTFKKMWVSKKEYEE 365
Cdd:pfam00022 317 DLRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVKIIAPGntvERRYSAWIGGSILASLGTFQQMWVSKQEYEE 396
                         410
                  ....*....|.
gi 22122615   366 DGSRAIHRKTF 376
Cdd:pfam00022 397 HGASVVERKCK 407
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
10-367 0e+00

nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein involved in the formation of filaments that are major components of the cytoskeleton. It is a highly dynamic structural protein network involved in processes such as cell contraction, cell motility, vesicle trafficking, intracellular organization, cytokinesis, endocytosis and apoptosis. Actin is a monomeric globular protein (G-actin) that reversibly polymerizes to form filaments (F-actin). Each actin protomer binds one molecule of ATP and either calcium or magnesium ions. At low salt concentrations, actin exists as a monomer, and as the salt concentration rises F-actin forms, with the consequent hydrolysis of ATP. F-actin assembly is in constant flux with G-actin association occurring at the barbed end (+) and its disassociation at the pointed end (-). Actin monomers that have been released from the pointed end can be reused, if the ADP is exchanged for ATP. F-actin filaments can assemble into higher order structures, for example branched F-actin, and stress fibers. Actin binding proteins regulate actin filament dynamics by a range of functions including actin severing, depolymerizing, capping, stabilizing and de novo actin polymerization. Actins interaction with myosin is the basis of muscular contraction and many aspects of cell motility. In vertebrates there are three main groups of actin isoforms, alpha, beta and gamma. The alpha actins found in muscle tissues are a major constituent of the contractile apparatus. The beta and gamma actins co-exist in most cell types as components of the cytoskeleton and as mediators of internal cell motility. In plants there are many isoforms which are probably involved in a variety of functions such as cytoplasmic streaming, cell shape determination, tip growth, graviperception, cell wall deposition, etc.


Pssm-ID: 466823  Cd Length: 365  Bit Score: 530.40  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  10 QPVVIDNGSGVIKAGFAGDQIPKYCFPNYVGRPKHMRVMAGALEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMERI 89
Cdd:cd10224   1 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  90 WQYVYSkDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVP 169
Cdd:cd10224  81 WHHTFY-NELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 170 IYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAEFEVVRTIKERACYLSINpqKDEALET-------EKvQYT 242
Cdd:cd10224 160 IYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALD--FEQEMQTaasssslEK-SYE 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 243 LPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKKLA 322
Cdd:cd10224 237 LPDGQVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALA 316
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 22122615 323 PKDVKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDG 367
Cdd:cd10224 317 PSTMKIKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESG 361
PTZ00004 PTZ00004
actin-2; Provisional
10-376 1.41e-168

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 475.41  E-value: 1.41e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615   10 QPVVIDNGSGVIKAGFAGDQIPKYCFPNYVGRPKHMRVMAGALEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMERI 89
Cdd:PTZ00004   7 NAAVVDNGSGMVKAGFAGDDAPRCVFPSIVGRPKNPGIMVGMEEKDCYVGDEAQDKRGILTLKYPIEHGIVTNWDDMEKI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615   90 WQYVYSkDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVP 169
Cdd:PTZ00004  87 WHHTFY-NELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETHNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  170 IYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAEFEVVRTIKERACYLSINPQK-----DEALETEKVQYTLP 244
Cdd:PTZ00004 166 IYEGYSLPHAIHRLDVAGRDLTEYMMKILHERGTTFTTTAEKEIVRDIKEKLCYIALDFDEemgnsAGSSDKYEESYELP 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  245 DGSTLDVGPARFRAPELLFQPDLVG-DESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKKLAP 323
Cdd:PTZ00004 246 DGTIITVGSERFRCPEALFQPSLIGkEEPPGIHELTFQSINKCDIDIRKDLYGNIVLSGGTTMYRGLPERLTKELTTLAP 325
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 22122615  324 KDVKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRKTF 376
Cdd:PTZ00004 326 STMKIKVVAPPERKYSVWIGGSILSSLPTFQQMWVTKEEYDESGPSIVHRKCF 378
PTZ00281 PTZ00281
actin; Provisional
1-376 2.91e-158

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 449.54  E-value: 2.91e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615    1 MESYDIianQPVVIDNGSGVIKAGFAGDQIPKYCFPNYVGRPKHMRVMAGALEGDLFIGPKAEEHRGLLTIRYPMEHGVV 80
Cdd:PTZ00281   1 MDGEDV---QALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615   81 RDWNDMERIWQYVYSkDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDS 160
Cdd:PTZ00281  78 TNWDDMEKIWHHTFY-NELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  161 GDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAEFEVVRTIKERACYLSINPQKD-------EA 233
Cdd:PTZ00281 157 GDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEmqtaassSA 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  234 LETekvQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFGDR 313
Cdd:PTZ00281 237 LEK---SYELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADR 313
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22122615  314 LLSEVKKLAPKDVKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRKTF 376
Cdd:PTZ00281 314 MNKELTALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIVHRKCF 376
ASKHA_NBD_Arp2 cd10220
nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, ...
10-371 1.24e-151

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: 432.76  E-value: 1.24e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  10 QPVVIDNGSGVIKAGFAGDQIPKYCFPNYVGRP---KHMRVMAGALEgDLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDM 86
Cdd:cd10220   1 KVVVCDNGTGFVKCGFAGSNFPEHVFPSLVGRPilrAEEKVGDIEIK-DIMVGDEASELRSMLEVTYPMENGIVRNWDDM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  87 ERIWQYVYsKDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTH 166
Cdd:cd10220  80 EHLWDYTF-GEKLKIDPRECKILLTEPPMNPTKNREKMVEVMFEKYGFAGVYVAIQAVLTLYAQGLLTGVVVDSGDGVTH 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 167 AVPIYEGFAMPHSIMRVDIAGRDVSRYL-RLLLRKeGADFHTSAEFEVVRTIKERACYLSINPQKDE--ALETEKV--QY 241
Cdd:cd10220 159 IVPVYEGFSLPHLTRRLDVAGRDITRYLiKLLLLR-GYAFNRTADFETVREIKEKLCYVAYDIELEQklALETTVLveSY 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 242 TLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKKL 321
Cdd:cd10220 238 TLPDGRVIKVGGERFEAPEALFQPHLIDVEGPGIAELLFNTIQAADIDTRPELYKHIVLSGGSTMYPGLPSRLEKEIKQL 317
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22122615 322 APKDV-----------KIKISAPQERLYSTWIGGSILASL----DTFkkmWVSKKEYEEDGSRAI 371
Cdd:cd10220 318 YLERVlkgdterlskfKIRIEDPPRRKHMVFLGGAVLADImkdkDEF---WITRQEYEEQGVRVL 379
ASKHA_NBD_actin-like cd10169
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ...
12-367 1.61e-134

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: 384.54  E-value: 1.61e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  12 VVIDNGSGVIKAGFAGDQIPKYCFPnyvgrpkhmrvmagalegdlfigpkaeehrglltirypmehgvvrdWNDMERIWQ 91
Cdd:cd10169   1 IVIDNGSGTIKAGFAGEDAPRLIFP----------------------------------------------WDDMEKIWE 34
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  92 YVYSKdQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIY 171
Cdd:cd10169  35 HVFYN-LLRVDPEEHPVLLTEPPLNPKANREKLAEILFETFNVPSLYIANQAVLSLYASGRTTGLVVDSGEGVTHIVPVY 113
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 172 EGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAEFEVVRTIKERACylsinpqkdealetekvqytlpdgstldv 251
Cdd:cd10169 114 EGYVLPHAVRRLDIGGRDLTDYLAKLLREKGYSFSTSAEREIVRDIKEKLC----------------------------- 164
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 252 gparfrapellfqpdlvgdeseGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDVKIKIS 331
Cdd:cd10169 165 ----------------------GLHELIYDSIMKCDIDLRKELYSNIVLSGGTTLFPGFAERLQKELSKLAPSSVKVKVI 222
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 22122615 332 APQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDG 367
Cdd:cd10169 223 APPERKYSAWIGGSILASLSTFQQMWITKEEYEEHG 258
ASKHA_NBD_ACTL7 cd10214
nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ...
11-374 7.07e-131

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: 379.46  E-value: 7.07e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  11 PVVIDNGSGVIKAGFAGDQIPKYCFPNYVGRPKHMRVMAGALEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMERIW 90
Cdd:cd10214   5 AVIIDLGTGYCKAGFAGQPRPSYVISSTVGKPPQESAKTGDNRKETFVGKELANVEPPLKLVNPLRHGIVVDWDCVQDIW 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  91 QYVYSKDqLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPI 170
Cdd:cd10214  85 EYIFEKE-MKILPEEHAVLVSDPPLSPTTNREKYAELMFETFSIPAMHIAYQSRLSLYSYGRTSGLVVESGHGVSYVVPI 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 171 YEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFhTSAEFEVVRTIKERACYLSINPQKDEALETE--KVQYTLPDGST 248
Cdd:cd10214 164 HEGYNLPHITGRADYAGSDLTAYLMKLLNEAGNKF-TDDQLHIVEDIKKKCCYVALDFEEEMGLPPQeyTVDYELPDGHL 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 249 LDVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDVKI 328
Cdd:cd10214 243 ITIGKERFRCPEMLFNPSLIGSKQPGLHTLTMNSLNKCDANLKKDLAKNILLCGGSTMFDGFPDRFQKELSKLCPNDNPI 322
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 22122615 329 KISAPqERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRK 374
Cdd:cd10214 323 VAASP-ERKYSVWTGGSILASLKSFQQLWVRRREYEERGPFVIYRK 367
ASKHA_NBD_Arp4_ACTL6-like cd13395
nucleotide-binding domain (NBD) of the actin-related protein 4 (Arp4)-like subfamily; The ...
12-367 1.77e-127

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: 372.28  E-value: 1.77e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  12 VVIDNGSGVIKAGFAGDQIPKYCFPNYVG----RPKHMRVMAGALE-------GDLFIGPKAEEHRglltIRYPMEHGVV 80
Cdd:cd13395   7 LVLDIGSYSTRAGYAGEDTPKAVFPSVVGvvtdDDDAEDYVGGSGEkkrkyyiGTNSIGVPRPNME----VISPLKDGLI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  81 RDWNDMERIWQYVYsKDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDS 160
Cdd:cd13395  83 EDWDAFEKLWDHAL-KNRLRVDPSEHPLLLTEPSWNTRANREKLTELMFEKYNVPAFFLAKNAVLSAFANGRSTALVVDS 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 161 GDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGAD--------------------------------FHTS 208
Cdd:cd13395 162 GATSTSVVPVHDGYVLQKAIVRSPLGGDFLTDQLLKLLESKNIEiiprymikskepveggapakytkkdlpnttssYHRY 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 209 AEFEVVRTIKERACYLSINP-QKDEALETEKVQYTLPDGSTLDVGPARFRAPELLFQPDLV---------GDESEGLHEV 278
Cdd:cd13395 242 MVRRVLQDFKESVCQVSDSPfDESEAASIPTVSYELPDGYNIEFGAERFKIPELLFDPSLVkgipappseGNELLGLPQL 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 279 LAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDVKIKISAPQ---ERLYSTWIGGSILASLDTFKK 355
Cdd:cd13395 322 VYTSIGSCDVDIRPELYGNVVLTGGNSLLPGFTDRLNRELSEKAPGSLKLKILASGntvERRFSSWIGGSILASLGSFQQ 401
                       410
                ....*....|..
gi 22122615 356 MWVSKKEYEEDG 367
Cdd:cd13395 402 MWISKQEYEEHG 413
PTZ00452 PTZ00452
actin; Provisional
12-376 7.56e-121

actin; Provisional


Pssm-ID: 185631  Cd Length: 375  Bit Score: 354.45  E-value: 7.56e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615   12 VVIDNGSGVIKAGFAGDQIPKYCFPNYVGRPKHMRVMAGALEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMERIWQ 91
Cdd:PTZ00452   8 VVIDNGSGYCKIGIAGDDAPTSCFPAIVGRSKQNDGIFSTFNKEYYVGEEAQAKRGVLAIKEPIQNGIINSWDDIEIIWH 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615   92 YVYSkDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIY 171
Cdd:PTZ00452  88 HAFY-NELCMSPEDQPVFMTDAPMNSKFNRERMTQIMFETFNTPCLYISNEAVLSLYTSGKTIGLVVDSGEGVTHCVPVF 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  172 EGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAEFEVVRTIKERACYLSINPQKDEAL----ETEKVQYTLPDGS 247
Cdd:PTZ00452 167 EGHQIPQAITKINLAGRLCTDYLTQILQELGYSLTEPHQRIIVKNIKERLCYTALDPQDEKRIykesNSQDSPYKLPDGN 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  248 TLDVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDVK 327
Cdd:PTZ00452 247 ILTIKSQKFRCSEILFQPKLIGLEVAGIHHLAYSSIKKCDLDLRQELCRNIVLSGGTTLFPGIANRLSNELTNLVPSQLK 326
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 22122615  328 IKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRKTF 376
Cdd:PTZ00452 327 IQVAAPPDRRFSAWIGGSIQCTLSTQQPQWIKRQEYDEQGPSIVHRKCF 375
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
11-367 6.41e-111

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: 329.91  E-value: 6.41e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  11 PVVIDNGSGVIKAGFAGDQIPKYCFPNYVG-------RPKHMRVMAGALEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDW 83
Cdd:cd10221   1 AVVIDNGTGYTKMGYAGNTEPQFIIPTVIAikesakvGDGQRRSKKGIEDLDFYIGDEALANSPTYALKYPIRHGIVEDW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  84 NDMERIWQYVYSKdQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYA-------TGRT-TG 155
Cdd:cd10221  81 DLMERFWEQCIFK-YLRCEPEDHYFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQAVLALAAswtsrkvGERTlTG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 156 VVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAEFEVVRTIKERACYLSinpqKDEALE 235
Cdd:cd10221 160 TVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREEGIPPEDSLEVAKRIKERYCYVC----PDIVKE 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 236 TEK---------VQYTLPDGST-----LDVGPARFRAPELLFQPDLV-GDESEGLHEVLAFAIHKSDMDLRRTLFSNIVL 300
Cdd:cd10221 236 FAKydsdpakyiKQYTGINSVTgkpytVDVGYERFLAPEIFFNPEIAsSDFTTPLPEVVDQVIQSCPIDTRRGLYKNIVL 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 301 SGGSTLFKGFGDRLLSEVKKL------------------APKDVKIkISAPQERlYSTWIGGSILASLDTFKKMWVSKKE 362
Cdd:cd10221 316 SGGSTMFKDFGRRLQRDVKRIvdarlkaseelsggklkpKPIDVNV-ISHPMQR-YAVWFGGSMLASTPEFYTVCHTKAE 393

                ....*
gi 22122615 363 YEEDG 367
Cdd:cd10221 394 YEEYG 398
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
7-367 5.14e-105

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 315.13  E-value: 5.14e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615    7 IANQPVVIDNGSGVIKAGFAGDQIPKYCFPN-YVGRPKHMRVMA--GALEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDW 83
Cdd:PTZ00280   2 STLPVVVIDNGTGYTKMGYAGNTEPTYIIPTlIADNSKQSRRRSkkGFEDLDFYIGDEALAASKSYTLTYPMKHGIVEDW 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615   84 NDMERIWQYVYSKdQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYAT----------GRT 153
Cdd:PTZ00280  82 DLMEKFWEQCIFK-YLRCEPEEHYFILTEPPMNPPENREYTAEIMFETFNVKGLYIAVQAVLALRASwtskkakelgGTL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  154 TGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAEFEVVRTIKERACYLSINPQK--- 230
Cdd:PTZ00280 161 TGTVIDSGDGVTHVIPVVDGYVIGSSIKHIPLAGRDITNFIQQMLRERGEPIPAEDILLLAQRIKEKYCYVAPDIAKefe 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  231 --DEALETEKVQYTLPDGST-----LDVGPARFRAPELLFQPDLV-GDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSG 302
Cdd:PTZ00280 241 kyDSDPKNHFKKYTAVNSVTkkpytVDVGYERFLGPEMFFHPEIFsSEWTTPLPEVVDDAIQSCPIDCRRPLYKNIVLSG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  303 GSTLFKGFGDRLLSEVKKL------------------APKDVKIkISAPQERlYSTWIGGSILASLDTFKKMWVSKKEYE 364
Cdd:PTZ00280 321 GSTMFKGFDKRLQRDVRKRvdrrlkkaeelsggklkpIPIDVNV-VSHPRQR-YAVWYGGSMLASSPEFEKVCHTKAEYD 398

                 ...
gi 22122615  365 EDG 367
Cdd:PTZ00280 399 EYG 401
ASKHA_NBD_Arp6 cd10210
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ...
12-367 4.79e-89

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: 273.27  E-value: 4.79e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  12 VVIDNGSGVIKAGFAGDQIPKyCFPNYVGRPKHMRVMagalegdLFIGPKAEEHRGL--LTIRYPMEHGVVRDWnDMER- 88
Cdd:cd10210   2 LVLDNGAYTIKAGFASDDPPR-VIPNCIAKPKSERRR-------LFGDDQLDECKDLsgLFYRRPFERGYLVNW-DLQRq 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  89 IWQYVYSKDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYA----------TGRTTGVVL 158
Cdd:cd10210  73 IWDHLFGKLLLNVDPSDTALVLTEPPFNPPSIQEAMDEIVFEEYGFQSLYRTTAAALSAFAyladseqsssSSSQCCLVV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 159 DSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLrlllrKEGADFHT---SAEFEVVRTIKERACYLSIN-------P 228
Cdd:cd10210 153 DSGFSFTHIVPFFDGKPVKRAVRRIDVGGKLLTNYL-----KEIISYRQlnvMDETYLVNQIKEDLCFVSTDfyedleiA 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 229 QKDEALETEKVQYTLPDGST------LDVGPA-----------------RFRAPELLFQPDLVGDESEGLHEVLAFAIHK 285
Cdd:cd10210 228 KKKGKENTIRRDYVLPDYTTskrgyvRDPEEPnrgklkedeqvlrlnneRFTVPELLFHPSDIGIQQAGIAEAIVQSINA 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 286 SDMDLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDVKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEE 365
Cdd:cd10210 308 CPEELQPLLYANIVLTGGNALFPGFRERLEAELRSLAPDDYDVNVTLPEDPITYAWEGGSLLAQSPEFEELAVTRAEYEE 387

                ..
gi 22122615 366 DG 367
Cdd:cd10210 388 HG 389
COG5277 COG5277
Actin-related protein [Cytoskeleton];
9-365 6.47e-75

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 238.15  E-value: 6.47e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615   9 NQPVVIDNGSGVIKAG-FAGDQIPKYC-----FPNYVGRPKHMRVMAGaLEGDLFIGPKAEEH-----RGLLTIRYPMEH 77
Cdd:COG5277   8 KYVIGIDFGTSYVKYGpIALEEKPRVIqtrglFLRIVGESKLLGPMEG-LSRGLVVGDEVSKYlssvrDAIRNLKYPLRD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  78 GVVR-----DWNDMERIWQYVYSKdQLQTFSEEHP--VLLTEAPLNPSKNREKAAEVFFETF---NVPALFISMQAVLSL 147
Cdd:COG5277  87 GIVRrddedAWRVLKELLRYTFAQ-FLVVDPEFHGflVVVALSALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPLAVA 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 148 YATGRTTGVVLDSGDGVTHAVPIYEGfAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFhTSAEFEVVRTIKERACYL--- 224
Cdd:COG5277 166 IAEKAVTCVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSD-TAREEYVVRVVKEALGLVprd 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 225 ---SINPQKDEALETEKVqYTLPDGSTL----DVGPARFRAPELLFQPDLVGDESE----------------------GL 275
Cdd:COG5277 244 lakAIQKAASNPDSFEAK-VRLPNPTVEielgNYAWERFLIGEILFNPNHEGFESYiqqgrlriedavigdvvlygemGL 322
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 276 HEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLF---KGFGD-------RLLSEVKKLAPkDVKIKISAPQERLYSTWIGGS 345
Cdd:COG5277 323 AEAIINSIMKCDVEIQDELYSNIILSGGAFNWsvpPGLEDvavdsvtRVQIELSELAP-ELKVNVRLVSDPQYSVWKGAI 401
                       410       420
                ....*....|....*....|..
gi 22122615 346 ILASLDTFKKMW--VSKKEYEE 365
Cdd:COG5277 402 IYGYALPFSVKWswITKEGWYF 423
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
12-372 4.65e-67

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: 215.72  E-value: 4.65e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  12 VVIDNGSGVIKAGFA-GDQIPKYCFPnyvgrpkhmRVMAGALEGDLFIGPKAEEhrglLTIRyPMEHGVVRDWNDMERIW 90
Cdd:cd10209   1 VVIDAGSRLLKAGYAyPDREPSVVEP---------TRVTPAVEDGEESDTVVEG----NTVS-PIRRGRIEDWDALEALL 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  91 QYVYSKDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPI 170
Cdd:cd10209  67 RYVFYTGLGWEEGNEGQVLIAEPLLTSKAERERLTQLMFETFNVSGLYASEQAVLSLYAVGRISGCVVDVGHGKIDIAPV 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 171 YEGfAMPHS-IMRVDIAGRDVSRYLRLLLRKEGAdfHTSAEFEVVRTIKERACYLSINPQKDEA--LETEKVQYTLPDGS 247
Cdd:cd10209 147 WEG-AIQHNaVRRFEIGGRDLTELLAAELGKSNP--KVKLDRSIVERLKEAVAWSADDEEAYEKkvLTCSPETYTLPDGR 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 248 TLDVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDVK 327
Cdd:cd10209 224 VISVGKERYCVGEALFRPSILGIEEYGIVEQLVRAVSTSPSENRRQLLENIVLCGGTSSVPGLEARLQKEIRLLSSPSSR 303
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 22122615 328 IKISAPQERL------YSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIH 372
Cdd:cd10209 304 PALVKPPEYMpentlrYSAWIGGAILAKVVFPQNQHVTKADYDETGPSVVH 354
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
11-367 1.28e-59

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: 196.25  E-value: 1.28e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  11 PVVIDNGSGVIKAGFAGDQIPKYCFPNYVGRPKHMRvmagALEGDLFIGPKAEEHRGL-LTIRYPMEHGVVRDWNDMERI 89
Cdd:cd10211   1 PIVIDNGSYQCRAGWAGDKEPRLVFRNLVAKPRDRK----KGITVTLVGNDILNDEAVrSHLRSPFDRNVVTNFDLQEQI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  90 WQYVYSKdqL---QTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRT----TGVVLDSGD 162
Cdd:cd10211  77 LDYIFSH--LginSEGSVDHPIVLTEALCNPNYSRQLMSELLFECYGVPSVAYGIDSLFSYYHNQPQgdpsDGLVISSGY 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 163 GVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYL-RLLLRKEgaDFHTSA-EFEVVRTIKERACYLSinPQKDEALEtekvq 240
Cdd:cd10211 155 STTHVIPVLNGRLDLSQCKRINLGGFHATDYLqRLLQLKY--PTHPSAiTLSRAEELVHEHCYVA--EDYDEELK----- 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 241 ytlpdgstldvgpaRFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKK 320
Cdd:cd10211 226 --------------KWEDPEYYEENVRKIQLPFGLVETIEFVLKRYPAEQQDRLVQNVFLTGGNALFPGLKERLEKELRA 291
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 22122615 321 LAPKDVKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDG 367
Cdd:cd10211 292 IRPFGSPFNVVRAKDPVLDAWRGAAKWALDSTFEKVWITKQEYEEKG 338
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
71-374 9.60e-50

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: 170.95  E-value: 9.60e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  71 IRYPMEHGVVRDWNDMERIWQYVYSK---DQLQTFseEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSL 147
Cdd:cd10208  35 IIWPIQDGRVVDWDALEALWRHILFSllsIPRPTN--NSPVLLSVPPSWSKSDLELLTQLFFERLNVPAFAILEAPLAAL 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 148 YATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGADFHTSAE------FEVVRTIKEra 221
Cdd:cd10208 113 YAAGATSGIVVDIGHEKTDITPIVDSQVVPHALVSIPIGGQDCTAHLAQLLKSDEPELKSQAEsgeeatLDLAEALKK-- 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 222 cylsinpqkDEALETEKVQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKS-DMDLRRTLFSNIVL 300
Cdd:cd10208 191 ---------SPICEVLSDGADLASGTEITVGKERFRACEPLFKPSSLRVDLLIAAIAGALVLNASdEPDKRPALWENIII 261
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 301 SGGSTLFKGFGDRLLSEVKKL-----------APKDVKI-KI----SAPQERLY--STWIGGSILASL---DTFKKMWVS 359
Cdd:cd10208 262 VGGGSRIRGLKEALLSELQQFhlisetsaspqQPRIIRLaKIpdyfPEWKKSGYeeAAFLGASIVAKLvfnDPSSKHYIS 341
                       330
                ....*....|....*
gi 22122615 360 KKEYEEDGSRAIHRK 374
Cdd:cd10208 342 KVDYNEKGPAAIHTK 356
ASKHA_NBD_Arp10 cd10207
nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins; ...
12-368 1.14e-47

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: 165.89  E-value: 1.14e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  12 VVIDNGSGVIKAGFAGDQIPKYCFPNYVGRPKhmrvMAGALEGDLFIGPKAEEHRGLLTirypmehgvvrdwndmeRIWQ 91
Cdd:cd10207   1 VVLDIGSAYTKCGFAGESAPRCIIPSEVKLPG----GKKVIRVVDQRSGNEEELYEALK-----------------EFLH 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  92 YVYSKdQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIY 171
Cdd:cd10207  60 ELYFK-HLLVNPKDRRVVVVESVLCPTPFRETLAKVLFKHFEVPSVLFAPSHLLSLLTLGIRTALVVDCGYRETRVLPVY 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 172 EGFAMPHSIMRVDIAGRDVSRYLRLLLRKEG------------ADFHTSAEFEVVRTIKERACYL-SINPQKDEALETEK 238
Cdd:cd10207 139 EGVPLLSAWQSTPLGGKALHKRLKKLLLEHAtvvtgdnkgqllSSVDSLLSEEVLEDIKVRACFVtSLERGKTLQSATEE 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 239 VQYTLP----------DGSTLDVGPARFRAP--ELLFQPDlvgDESEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTL 306
Cdd:cd10207 219 GSTEEPsppppvdyplDGEKILIVPGSIRESaeELLFEGD---NEEKSLPTLILDSLLKCPIDVRKQLAENIVVIGGTSM 295
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22122615 307 FKGFGDRLLSEVKKLAPKDV-KIKISAPQERLYST----------WIGGSILASLDTFKKMWVSKKEYEEDGS 368
Cdd:cd10207 296 LPGFKHRLLEELRALLRKPKyFEELAPKTFRFHTPpsvfkpnylaWLGGSIFGALESILGRSLSREAYLQTGR 368
ASKHA_NBD_AtArp8-like cd13396
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and ...
99-367 8.85e-38

nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and similar proteins; Arabidopsis thaliana ARP8, also called F-box protein ARP8, is an F-Box protein localized to the nucleolus. It is ubiquitously expressed in all organs and cell types and has a cell cycle-dependent subcellular pattern of distribution: it is localized to the nucleolus in interphase cells and dispersed in the cytoplasm in mitotic cells.


Pssm-ID: 466847  Cd Length: 332  Bit Score: 138.45  E-value: 8.85e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  99 LQTFSEEHPVLLTEaPLNPSKNREKAA-----------EVFFEtFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHA 167
Cdd:cd13396  52 MQVKPSRQPVVVSL-PLCHSDDTESAAasrrqlrgtifNVLFD-MNVPAVCAVDQAVLALYAANRTSGIVVNIGFRVTTI 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 168 VPIYEGFAMpHSI--MRVDIAGRDVSRYLRLLLRKEGADFHTsaeFEVVRTIKERACYLSINPQKDEALETEKVQYTLPD 245
Cdd:cd13396 130 VPVYRGRVM-HDIgvEVVGQGALRLTGFLKELMQQNGIRFPS---LYTVRTIKEKLCYVAEDYEAELAKDTQASCEVAGE 205
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 246 GSTLdVGPARFRAPELLFQPDLVGDESEGLHEVLAFAIHKSDMDLR---RTLFSNIVLSGGSTLFKGFGDRLLSEVKKLA 322
Cdd:cd13396 206 GWFT-LSNERFKTGEILFQPGLGGMRAMGLHQAVALCMDHCALVHSqgdDGWFKTIVLSGGSACLPGLSERLERELRKLL 284
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 22122615 323 PKDVK--IKISAPQERLYSTWIGGSILASLDTFKKMW-VSKKEYEEDG 367
Cdd:cd13396 285 PKSLSegIRIIPPPLGPDSAWQGAKLISNLSNFPDGWcITKKQFRNKP 332
ASKHA_NBD_Arp8-like cd10206
nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The ...
70-371 2.94e-29

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


Pssm-ID: 466812 [Multi-domain]  Cd Length: 447  Bit Score: 117.34  E-value: 2.94e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  70 TIRYPMEHGV------------VRDwnDMERIWQYVYSKD---QLQTFSEEHPVLLTeaplnPSK-NREKAAE---VFFE 130
Cdd:cd10206 138 NLHWPIRRGRlnvhsdggsltaVLD--DLEDIWSHALEEKleiPRKDLKNYRAVLVI-----PDLfDRRHVKElvdLLLR 210
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 131 TFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKegADFH---- 206
Cdd:cd10206 211 RLGFSSVFVHQESVCATFGAGLSSACVVDIGAQKTSVACVEDGLSIPNSRIRLPYGGDDITRCFLWLLRR--SGFPyrec 288
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 207 ---TSAEFEVVRTIKERACYLS---INPQKDEALETEKVQytlpdgstldvgparfraPELLFQPDLVgdeseGLHEvla 280
Cdd:cd10206 289 nlnSPLDFLLLERLKETYCTLDqddIGVQLHEFYVREPGQ------------------PTLKYQFKLL-----PLDE--- 342
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 281 fAIHKS-----DMDLRRTLFSNIVLSGGSTLFKGFG----DRLLSEVKKL--APKDVKIkISAPQER--LYSTWIGGSIL 347
Cdd:cd10206 343 -AIVQSilscaSDELKRKMYSSILLVGGGAKIPGLAealeDRLLIKIPSLfeAVETVEV-LPPPKDMdpSLLAWKGGAVL 420
                       330       340
                ....*....|....*....|....
gi 22122615 348 ASLDTFKKMWVSKKEYEEDGSRAI 371
Cdd:cd10206 421 ACLDSAQELWITRKEWQRLGVRAL 444
ASKHA_NBD_ScArp7-like cd10212
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and ...
12-364 1.15e-23

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: 101.33  E-value: 1.15e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  12 VVIDNGSGVIKAGFAGDQIPKYCFPN-YVGRPKHMRVMAGALEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMERIW 90
Cdd:cd10212   6 VVIHNGSHRTVAGFSNVELPQCIIPSsYIKRTDEGGEAEFIFGTYNMIDAAAEKRNGDEVYTLVDSQGLPYNWDALEMQW 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  91 QYVYSKdQLQTFSEEHPVLLTEAPLNPSKNR---EKAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHA 167
Cdd:cd10212  86 RYLYDT-QLKVSPEELPLVITMPATNGKPDMailERYYELAFDKLNVPVFQIVIEPLAIALSMGKSSAFVIDIGASGCNV 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 168 VPIYEGFAMPHSIMRVDIAGR--DVSRYLRLL-LRKEGADFHTSAE-------------------------------FEV 213
Cdd:cd10212 165 TPIIDGIVVKNAVVRSKFGGDflDFQVHERLApLIKEENDMENMADeqkrstdvwyeastwiqqfkstmlqvsekdlFEL 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 214 VRTIKERAcylSINPQKDEALET--EKVQYTLPDGS--------------------TLDVGPArFRAPELLFQPDLVGDE 271
Cdd:cd10212 245 ERYYKEQA---DIYAKQQEQLKQmdQQLQYTALTGSpnnplvqkknflfkplnktlTLDLKEC-YQFAEYLFKPQLISDK 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 272 ---SEGLHEVLAFAIHKSDMDLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKKLAPKdVKIKISAPQ---ERLYSTWIGGS 345
Cdd:cd10212 321 fspEDGLGPLMAKSVKKAPEQVYSLLLTNVIITGSTSLIEGMEQRIIKELSIRFPQ-YKLTTFANQvmmDRKIQGWLGAL 399
                       410       420
                ....*....|....*....|
gi 22122615 346 ILASLDTFK-KMWVSKKEYE 364
Cdd:cd10212 400 TMANLPSWSlGKWYSKEDYE 419
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
309-374 4.36e-16

syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in the plant pathogen Pseudomonas syringae and related species. This model was created, in part, to clarify that the family is real and distinct, rather than an artifact of eukaryotic contamination of bacterial genomic sequence data. As of the creation of this HMM, the family is uncharacterized.


Pssm-ID: 468549 [Multi-domain]  Cd Length: 132  Bit Score: 74.25  E-value: 4.36e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22122615  309 GFGDRLLSEVKKLAPKDVKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRK 374
Cdd:NF040575  66 GFYEKLKKSITEKAPKGALIGMTLDPKPESAAWRGAAMYAASEGFVEMAITKQEYDESGPSIVHRK 131
ASKHA_NBD_MamK cd24009
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ...
32-314 1.92e-11

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: 64.54  E-value: 1.92e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615  32 KYCFPNYVGRPKHMrVMAGALEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDW--NDMEriwqyvYSKDQLQtfseeHPVL 109
Cdd:cd24009  22 RFSFRSVVGYPKDI-IARKLLGKEVLFGDEALENRLALDLRRPLEDGVIKEGddRDLE------AARELLQ-----HLIE 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 110 LTEAPLN---------PS----KNREKAAEVFFETFN----VPALFismqAVlsLYATGRTTG-VVLDSGDGVTHAVPIY 171
Cdd:cd24009  90 LALPGPDdeiyavigvPArasaENKQALLEIARELVDgvmvVSEPF----AV--AYGLDRLDNsLIVDIGAGTTDLCRMK 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122615 172 EGFAMPHSIMRVDIAGRDVSRYLRLLLRKEgadfHTSAEF--EVVRTIKERACYLSINPqkdealetEKVQYTLP-DGS- 247
Cdd:cd24009 164 GTIPTEEDQITLPKAGDYIDEELVDLIKER----YPEVQLtlNMARRWKEKYGFVGDAS--------EPVKVELPvDGKp 231
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22122615 248 -TLDVGPARFRAPELLFqPDLVgdesEGLHEVLAfaihKSDMDLRRTLFSNIVLSGGSTLFKGFGDRL 314
Cdd:cd24009 232 vTYDITEELRIACESLV-PDIV----EGIKKLIA----SFDPEFQEELRNNIVLAGGGSRIRGLDTYI 290
 
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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