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Conserved domains on  [gi|1919040695|ref|XP_036618067|]
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actin-related protein 6 [Trichosurus vulpecula]

Protein Classification

actin family protein( domain architecture ID 19020852)

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ASKHA_NBD_Arp6 cd10210
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ...
3-386 0e+00

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: 677.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695   3 TLVLDNGAYNAKIGYSHDS-VSVIPNCQFRSKTARLKTFTANQIDEIKDPSGLFYILPFQKGYLVNWDVQRQVWDYLFGK 81
Cdd:cd10210     1 TLVLDNGAYTIKAGFASDDpPRVIPNCIAKPKSERRRLFGDDQLDECKDLSGLFYRRPFERGYLVNWDLQRQIWDHLFGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  82 EMYQVDFVDTNIIITEPYFNFTSIQESMNEILFEEYQFQAVLRVNAGGLSAHRYFRDNP-----SELCCIIVDSGYSFTH 156
Cdd:cd10210    81 LLLNVDPSDTALVLTEPPFNPPSIQEAMDEIVFEEYGFQSLYRTTAAALSAFAYLADSEqssssSSQCCLVVDSGFSFTH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 157 IVPYCRSKKKKEAIIRINVGGKLLTNHLKEIISYRQLHVMDETHVINQVKEDVCYVSQDFYKDMDIAKLKGEENTVMVDY 236
Cdd:cd10210   161 IVPFFDGKPVKRAVRRIDVGGKLLTNYLKEIISYRQLNVMDETYLVNQIKEDLCFVSTDFYEDLEIAKKKGKENTIRRDY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 237 VLPDFSTIKKGFCKPREEMVlSGKYKSGEQILRLANERFAVPEILFNPSDIGIQEMGIPEAIVYSIQNLPEEMQPHFFKN 316
Cdd:cd10210   241 VLPDYTTSKRGYVRDPEEPN-RGKLKEDEQVLRLNNERFTVPELLFHPSDIGIQQAGIAEAIVQSINACPEELQPLLYAN 319
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 317 IVLTGGNTLFPGFRDRVYSEVRCLTPTDYDVSVVLPENPITYSWEGGKLISENDDFEDMVVTREDYEENG 386
Cdd:cd10210   320 IVLTGGNALFPGFRERLEAELRSLAPDDYDVNVTLPEDPITYAWEGGSLLAQSPEFEELAVTRAEYEEHG 389
 
Name Accession Description Interval E-value
ASKHA_NBD_Arp6 cd10210
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ...
3-386 0e+00

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: 677.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695   3 TLVLDNGAYNAKIGYSHDS-VSVIPNCQFRSKTARLKTFTANQIDEIKDPSGLFYILPFQKGYLVNWDVQRQVWDYLFGK 81
Cdd:cd10210     1 TLVLDNGAYTIKAGFASDDpPRVIPNCIAKPKSERRRLFGDDQLDECKDLSGLFYRRPFERGYLVNWDLQRQIWDHLFGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  82 EMYQVDFVDTNIIITEPYFNFTSIQESMNEILFEEYQFQAVLRVNAGGLSAHRYFRDNP-----SELCCIIVDSGYSFTH 156
Cdd:cd10210    81 LLLNVDPSDTALVLTEPPFNPPSIQEAMDEIVFEEYGFQSLYRTTAAALSAFAYLADSEqssssSSQCCLVVDSGFSFTH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 157 IVPYCRSKKKKEAIIRINVGGKLLTNHLKEIISYRQLHVMDETHVINQVKEDVCYVSQDFYKDMDIAKLKGEENTVMVDY 236
Cdd:cd10210   161 IVPFFDGKPVKRAVRRIDVGGKLLTNYLKEIISYRQLNVMDETYLVNQIKEDLCFVSTDFYEDLEIAKKKGKENTIRRDY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 237 VLPDFSTIKKGFCKPREEMVlSGKYKSGEQILRLANERFAVPEILFNPSDIGIQEMGIPEAIVYSIQNLPEEMQPHFFKN 316
Cdd:cd10210   241 VLPDYTTSKRGYVRDPEEPN-RGKLKEDEQVLRLNNERFTVPELLFHPSDIGIQQAGIAEAIVQSINACPEELQPLLYAN 319
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 317 IVLTGGNTLFPGFRDRVYSEVRCLTPTDYDVSVVLPENPITYSWEGGKLISENDDFEDMVVTREDYEENG 386
Cdd:cd10210   320 IVLTGGNALFPGFRERLEAELRSLAPDDYDVNVTLPEDPITYAWEGGSLLAQSPEFEELAVTRAEYEEHG 389
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
2-394 9.44e-110

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 326.52  E-value: 9.44e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695    2 ATLVLDNGAYNAKIGYS-HDS-VSVIPNCQFRSKTARLKTFTANQI---DEIKDPSG-LFYILPFQKGYLVNWDVQRQVW 75
Cdd:smart00268   2 PAIVIDNGSGTIKAGFAgEDFpQVVFPSIVGRPKDGKGMVGDAKDIfvgDEAQEKRGgLELKYPIENGIVENWDDMEKIW 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695   76 DYLFGKEMyQVDFVDTNIIITEPYFNFTSIQESMNEILFEEYQFQAVLRVNAGGLSAHRYfrdnpSELCCIIVDSGYSFT 155
Cdd:smart00268  82 DYTFFNEL-RVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYAS-----GRTTGLVIDSGDGVT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  156 HIVPYCRSKKKKEAIIRINVGGKLLTNHLKEIISYR--QLHVMDETHVINQVKEDVCYVSQDFYKDMDIAKLKGEENTVM 233
Cdd:smart00268 156 HVVPVVDGYVLPHAIKRIDIAGRDITDYLKELLSERgyQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLARESSESSKLE 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  234 VDYVLPDFSTIKKGfckpreemvlsgkyksgeqilrlaNERFAVPEILFNPSDIGIQEMGIPEAIVYSIQNLPEEMQPHF 313
Cdd:smart00268 236 KTYELPDGNTIKVG------------------------NERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDL 291
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  314 FKNIVLTGGNTLFPGFRDRVYSEVRCLTPTDYDVSVVLPENPITYSWEGGKLISENDDFEDMVVTREDYEENGHCICEEK 393
Cdd:smart00268 292 YENIVLSGGSTLIPGFGERLEKELKQLAPKKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERK 371

                   .
gi 1919040695  394 F 394
Cdd:smart00268 372 C 372
Actin pfam00022
Actin;
3-394 3.93e-85

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 264.94  E-value: 3.93e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695   3 TLVLDNGAYNAKIGYSHDSV--SVIPNCQFRSKTARLKTFTANQIDE--IKDPSGLFYILPFQKGYLVNWDVQRQVWDYL 78
Cdd:pfam00022   3 ALVIDNGSHTTRAGFAGEDApkAVIPSCVGKPRGTKVEAANKYYVGDeaLTYRPGMEVRSPVEDGIVVDWDAMEEIWEHV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  79 FGKEMyQVDFVDTNIIITEPYFNFTSIQESMNEILFEEYQFQAVLRVNAGGLSAHRYFRDnpselCCIIVDSGYSFTHIV 158
Cdd:pfam00022  83 LKEEL-QVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRT-----TGLVVDSGAGVTSVV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 159 PYCRSKKKKEAIIRINVGGKLLTNHLKEIISYRQL--------------------------------HVMDETHVINQVK 206
Cdd:pfam00022 157 PVHDGYVLQKAIRRSDLGGDFLTDYLRELLRSRNIeitprylikskkpgdpapavtkrelpdttysyKTYQERRVLEEIK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 207 EDVCYVSQDFYKDMDIAklkgeENTVMVDYVLPDFSTIKkgfckpreemvlsgkyksgeqilrLANERFAVPEILFNPSD 286
Cdd:pfam00022 237 ESVCYVSDDPFGDETTS-----SSIPTRVYELPDGSTII------------------------LGAERFRVPEILFNPSL 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 287 IGIQE--------MGIPEAIVYSIQNLPEEMQPHFFKNIVLTGGNTLFPGFRDRVYSEVRCLTPTDYDVSVVLPEN---P 355
Cdd:pfam00022 288 IGSESelpppqtaVGIPELIVDAINACDVDLRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVKIIAPGNtveR 367
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1919040695 356 ITYSWEGGKLISENDDFEDMVVTREDYEENGHCICEEKF 394
Cdd:pfam00022 368 RYSAWIGGSILASLGTFQQMWVSKQEYEEHGASVVERKC 406
PTZ00004 PTZ00004
actin-2; Provisional
4-386 2.16e-55

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 186.90  E-value: 2.16e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695   4 LVLDNGAYNAKIGYSHDSV--SVIPNCQFRSKTARLKTFTANQ----IDEIKDPSG-LFYILPFQKGYLVNWDVQRQVWD 76
Cdd:PTZ00004    9 AVVDNGSGMVKAGFAGDDAprCVFPSIVGRPKNPGIMVGMEEKdcyvGDEAQDKRGiLTLKYPIEHGIVTNWDDMEKIWH 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  77 YLFGKEMyQVDFVDTNIIITEPYFNFTSIQESMNEILFEEYQF-------QAVLRVNAGGLSAHryfrdnpselccIIVD 149
Cdd:PTZ00004   89 HTFYNEL-RVAPEEHPVLLTEAPLNPKANREKMTQIMFETHNVpamyvaiQAVLSLYASGRTTG------------IVLD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 150 SGYSFTHIVPYCRSKKKKEAIIRINVGGKLLTNHLKEIISYR--QLHVMDETHVINQVKEDVCYVSQDFykDMDIAKLKG 227
Cdd:PTZ00004  156 SGDGVSHTVPIYEGYSLPHAIHRLDVAGRDLTEYMMKILHERgtTFTTTAEKEIVRDIKEKLCYIALDF--DEEMGNSAG 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 228 EENTVMVDYVLPDFStikkgfckpreemvlsgkyksgeqILRLANERFAVPEILFNPSDIGIQE-MGIPEAIVYSIQNLP 306
Cdd:PTZ00004  234 SSDKYEESYELPDGT------------------------IITVGSERFRCPEALFQPSLIGKEEpPGIHELTFQSINKCD 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 307 EEMQPHFFKNIVLTGGNTLFPGFRDRVYSEVRCLTPTDYDVSVVLPENPITYSWEGGKLISENDDFEDMVVTREDYEENG 386
Cdd:PTZ00004  290 IDIRKDLYGNIVLSGGTTMYRGLPERLTKELTTLAPSTMKIKVVAPPERKYSVWIGGSILSSLPTFQQMWVTKEEYDESG 369
COG5277 COG5277
Actin-related protein [Cytoskeleton];
67-384 3.36e-28

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 114.50  E-value: 3.36e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  67 NWDVQRQVWDYLFGKEMY-QVDFVDTNIIITEPYFNFTSIQESMNEILFE---EYQFQAVLRVNAGGLSAHRYFRDNpse 142
Cdd:COG5277    96 AWRVLKELLRYTFAQFLVvDPEFHGFLVVVALSALAPDYMRERLFDIHFEvfsEEGAPAVTIIPQPLAVAIAEKAVT--- 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 143 lcCIIVDSGYSFTHIVPYCRSKKKkEAIIRINVGGKLLTNHLKEIIsyRQLHVMD---ETHVINQVKEDVCYVSQDFYKD 219
Cdd:COG5277   173 --CVVVEAGHGNSQVAPISRGPIR-EGLVALNRGGAEANAITREIL--KDRGYSDtarEEYVVRVVKEALGLVPRDLAKA 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 220 MDIAKlkGEENTVMVDYVLPDfstikkgfckPREEMVLsGKYksgeqilrlANERFAVPEILFNPSDIGIQ--------- 290
Cdd:COG5277   248 IQKAA--SNPDSFEAKVRLPN----------PTVEIEL-GNY---------AWERFLIGEILFNPNHEGFEsyiqqgrlr 305
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 291 -------------EMGIPEAIVYSIQNLPEEMQPHFFKNIVLTGGNTLF---PGFRD-------RVYSEVRCLTPTdYDV 347
Cdd:COG5277   306 iedavigdvvlygEMGLAEAIINSIMKCDVEIQDELYSNIILSGGAFNWsvpPGLEDvavdsvtRVQIELSELAPE-LKV 384
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1919040695 348 SVVLPENPITYSWEG----GKLISENDDFEDmvVTREDYEE 384
Cdd:COG5277   385 NVRLVSDPQYSVWKGaiiyGYALPFSVKWSW--ITKEGWYF 423
 
Name Accession Description Interval E-value
ASKHA_NBD_Arp6 cd10210
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ...
3-386 0e+00

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: 677.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695   3 TLVLDNGAYNAKIGYSHDS-VSVIPNCQFRSKTARLKTFTANQIDEIKDPSGLFYILPFQKGYLVNWDVQRQVWDYLFGK 81
Cdd:cd10210     1 TLVLDNGAYTIKAGFASDDpPRVIPNCIAKPKSERRRLFGDDQLDECKDLSGLFYRRPFERGYLVNWDLQRQIWDHLFGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  82 EMYQVDFVDTNIIITEPYFNFTSIQESMNEILFEEYQFQAVLRVNAGGLSAHRYFRDNP-----SELCCIIVDSGYSFTH 156
Cdd:cd10210    81 LLLNVDPSDTALVLTEPPFNPPSIQEAMDEIVFEEYGFQSLYRTTAAALSAFAYLADSEqssssSSQCCLVVDSGFSFTH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 157 IVPYCRSKKKKEAIIRINVGGKLLTNHLKEIISYRQLHVMDETHVINQVKEDVCYVSQDFYKDMDIAKLKGEENTVMVDY 236
Cdd:cd10210   161 IVPFFDGKPVKRAVRRIDVGGKLLTNYLKEIISYRQLNVMDETYLVNQIKEDLCFVSTDFYEDLEIAKKKGKENTIRRDY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 237 VLPDFSTIKKGFCKPREEMVlSGKYKSGEQILRLANERFAVPEILFNPSDIGIQEMGIPEAIVYSIQNLPEEMQPHFFKN 316
Cdd:cd10210   241 VLPDYTTSKRGYVRDPEEPN-RGKLKEDEQVLRLNNERFTVPELLFHPSDIGIQQAGIAEAIVQSINACPEELQPLLYAN 319
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 317 IVLTGGNTLFPGFRDRVYSEVRCLTPTDYDVSVVLPENPITYSWEGGKLISENDDFEDMVVTREDYEENG 386
Cdd:cd10210   320 IVLTGGNALFPGFRERLEAELRSLAPDDYDVNVTLPEDPITYAWEGGSLLAQSPEFEELAVTRAEYEEHG 389
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
2-394 9.44e-110

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 326.52  E-value: 9.44e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695    2 ATLVLDNGAYNAKIGYS-HDS-VSVIPNCQFRSKTARLKTFTANQI---DEIKDPSG-LFYILPFQKGYLVNWDVQRQVW 75
Cdd:smart00268   2 PAIVIDNGSGTIKAGFAgEDFpQVVFPSIVGRPKDGKGMVGDAKDIfvgDEAQEKRGgLELKYPIENGIVENWDDMEKIW 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695   76 DYLFGKEMyQVDFVDTNIIITEPYFNFTSIQESMNEILFEEYQFQAVLRVNAGGLSAHRYfrdnpSELCCIIVDSGYSFT 155
Cdd:smart00268  82 DYTFFNEL-RVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYAS-----GRTTGLVIDSGDGVT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  156 HIVPYCRSKKKKEAIIRINVGGKLLTNHLKEIISYR--QLHVMDETHVINQVKEDVCYVSQDFYKDMDIAKLKGEENTVM 233
Cdd:smart00268 156 HVVPVVDGYVLPHAIKRIDIAGRDITDYLKELLSERgyQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLARESSESSKLE 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  234 VDYVLPDFSTIKKGfckpreemvlsgkyksgeqilrlaNERFAVPEILFNPSDIGIQEMGIPEAIVYSIQNLPEEMQPHF 313
Cdd:smart00268 236 KTYELPDGNTIKVG------------------------NERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDL 291
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  314 FKNIVLTGGNTLFPGFRDRVYSEVRCLTPTDYDVSVVLPENPITYSWEGGKLISENDDFEDMVVTREDYEENGHCICEEK 393
Cdd:smart00268 292 YENIVLSGGSTLIPGFGERLEKELKQLAPKKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERK 371

                   .
gi 1919040695  394 F 394
Cdd:smart00268 372 C 372
Actin pfam00022
Actin;
3-394 3.93e-85

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 264.94  E-value: 3.93e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695   3 TLVLDNGAYNAKIGYSHDSV--SVIPNCQFRSKTARLKTFTANQIDE--IKDPSGLFYILPFQKGYLVNWDVQRQVWDYL 78
Cdd:pfam00022   3 ALVIDNGSHTTRAGFAGEDApkAVIPSCVGKPRGTKVEAANKYYVGDeaLTYRPGMEVRSPVEDGIVVDWDAMEEIWEHV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  79 FGKEMyQVDFVDTNIIITEPYFNFTSIQESMNEILFEEYQFQAVLRVNAGGLSAHRYFRDnpselCCIIVDSGYSFTHIV 158
Cdd:pfam00022  83 LKEEL-QVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRT-----TGLVVDSGAGVTSVV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 159 PYCRSKKKKEAIIRINVGGKLLTNHLKEIISYRQL--------------------------------HVMDETHVINQVK 206
Cdd:pfam00022 157 PVHDGYVLQKAIRRSDLGGDFLTDYLRELLRSRNIeitprylikskkpgdpapavtkrelpdttysyKTYQERRVLEEIK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 207 EDVCYVSQDFYKDMDIAklkgeENTVMVDYVLPDFSTIKkgfckpreemvlsgkyksgeqilrLANERFAVPEILFNPSD 286
Cdd:pfam00022 237 ESVCYVSDDPFGDETTS-----SSIPTRVYELPDGSTII------------------------LGAERFRVPEILFNPSL 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 287 IGIQE--------MGIPEAIVYSIQNLPEEMQPHFFKNIVLTGGNTLFPGFRDRVYSEVRCLTPTDYDVSVVLPEN---P 355
Cdd:pfam00022 288 IGSESelpppqtaVGIPELIVDAINACDVDLRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVKIIAPGNtveR 367
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1919040695 356 ITYSWEGGKLISENDDFEDMVVTREDYEENGHCICEEKF 394
Cdd:pfam00022 368 RYSAWIGGSILASLGTFQQMWVSKQEYEEHGASVVERKC 406
ASKHA_NBD_actin-like cd10169
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ...
4-386 3.58e-66

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: 210.81  E-value: 3.58e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695   4 LVLDNGAYNAKIGYSHDSVsviPNCQFRsktarlktftanqideikdpsglfyilpfqkgylvnWDVQRQVWDYLFGKEM 83
Cdd:cd10169     1 IVIDNGSGTIKAGFAGEDA---PRLIFP------------------------------------WDDMEKIWEHVFYNLL 41
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  84 yQVDFVDTNIIITEPYFNFTSIQESMNEILFEEYQFQAVLRVNAGGLSAHRYFRdnpseLCCIIVDSGYSFTHIVPYCRS 163
Cdd:cd10169    42 -RVDPEEHPVLLTEPPLNPKANREKLAEILFETFNVPSLYIANQAVLSLYASGR-----TTGLVVDSGEGVTHIVPVYEG 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 164 KKKKEAIIRINVGGKLLTNHLKEIISYR--QLHVMDETHVINQVKEDVCyvsqdfykdmdiaklkgeentvmvdyvlpdf 241
Cdd:cd10169   116 YVLPHAVRRLDIGGRDLTDYLAKLLREKgySFSTSAEREIVRDIKEKLC------------------------------- 164
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 242 stikkgfckpreemvlsgkyksgeqilrlanerfavpeilfnpsdigiqemGIPEAIVYSIQNLPEEMQPHFFKNIVLTG 321
Cdd:cd10169   165 ---------------------------------------------------GLHELIYDSIMKCDIDLRKELYSNIVLSG 193
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1919040695 322 GNTLFPGFRDRVYSEVRCLTPTDYDVSVVLPENPITYSWEGGKLISENDDFEDMVVTREDYEENG 386
Cdd:cd10169   194 GTTLFPGFAERLQKELSKLAPSSVKVKVIAPPERKYSAWIGGSILASLSTFQQMWITKEEYEEHG 258
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
4-394 5.26e-60

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: 198.54  E-value: 5.26e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695   4 LVLDNGAYNAKIGYSHDSvsvIPNCQFRSKTARLK------------TFTANQIDEIKdpsGLFYI-LPFQKGYLVNWDV 70
Cdd:cd10216     4 VVIDNGSGVIKAGFAGDD---IPKVVFPSYVGRPKhvrvmagalegdVFVGPKAEEHR---GLLKIrYPMEHGIVTDWND 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  71 QRQVWDYLFGKEMYQVDFVDTNIIITEPYFNFTSIQESMNEILFEEYQ-------FQAVLRVNAGGLSAHryfrdnpsel 143
Cdd:cd10216    78 MERIWQYVYSKLQLNTFSEEHPVLLTEAPLNPRKNREKAAEVFFETFNvpalfvsMQAVLSLYASGRTTG---------- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 144 ccIIVDSGYSFTHIVPYCRSKKKKEAIIRINVGGKLLTNHLKEIIsyRQ----LHVMDETHVINQVKEDVCYVSQDFYKD 219
Cdd:cd10216   148 --VVLDSGDGVTHAVPIYEGFALPHSIRRVDIAGRDVTEYLQLLL--RKsgynFHTSAEFEIVREIKEKACYVALNPQKE 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 220 mdiAKLKGEEnTVMVDYVLPDFSTIKkgfckpreemvlsgkyksgeqilrLANERFAVPEILFNPSDIGIQEMGIPEAIV 299
Cdd:cd10216   224 ---EKLEEEK-TEKAQYTLPDGSTIE------------------------IGPERFRAPEILFNPELIGLEYPGVHEVLV 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 300 YSIQNLPEEMQPHFFKNIVLTGGNTLFPGFRDRVYSEVRCLTPTDYDVSVVLPENPITYSWEGGKLISENDDFEDMVVTR 379
Cdd:cd10216   276 DSIQKSDLDLRKTLYSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDVKIRISAPPERLYSTWIGGSILASLSTFKKMWVSK 355
                         410
                  ....*....|....*
gi 1919040695 380 EDYEENGHCICEEKF 394
Cdd:cd10216   356 KEYEEDGARILHRKT 370
ASKHA_NBD_actin_Arp-T1-3 cd13397
nucleotide-binding domain (NBD) of actin, actin-related proteins T1-T3 (Arp-T1-3), and similar ...
2-386 1.35e-59

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: 197.02  E-value: 1.35e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695   2 ATLVLDNGAYNAKIGYSHDSvsvIPNCQFRSKTARLKTFTANQIDEIKDpsglFYI--------------LPFQKGYLVN 67
Cdd:cd13397     1 PAVVIDNGSGLIKAGFAGED---LPRAVFPSVVGRPKYKAVMLGAGQKE----VYVgdeaqekrgvltlsYPIEHGIVTN 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  68 WDVQRQVWDYLFGKEMyQVDFVDTNIIITEPYFNFTSIQESMNEILFEEYQF-------QAVLRVNAGGLSAHryfrdnp 140
Cdd:cd13397    74 WDDMEKIWHHTFENEL-RVKPEEHPVLLTEAPLNPKQNREKMAEIMFETFGVpafyvaiQAVLSLYSSGRTTG------- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 141 selccIIVDSGYSFTHIVP----YCRSKkkkeAIIRINVGGKLLTNHLKEIISYRQLHVMD--ETHVINQVKEDVCYVSQ 214
Cdd:cd13397   146 -----LVLDSGDGVTHTVPiyegYALPH----AVQRLDLAGRDLTEYLMKLLKERGHSFTTtaEREIVRDIKEKLCYVAL 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 215 DFYKDMdiaklKGEENTVMVDYVLPDfstikkGfckpreemvlsgkyksgeQILRLANERFAVPEILFNPSDIGIQEMGI 294
Cdd:cd13397   217 DYEEEL-----KKKSEELEKEYTLPD------G------------------QVIKIGSERFRCPEALFRPSLIGREAPGI 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 295 PEAIVYSIQNLPEEMQPHFFKNIVLTGGNTLFPGFRDRVYSEVRCLTPTDYDVSVVLPENPItYS-WEGGKLISENDDFE 373
Cdd:cd13397   268 HKLVYNSIMKCDIDIRKDLYSNIVLSGGSTMFPGLPERLQKELEALAPSSTKVKVIAPPERK-YSvWIGGSILASLSTFK 346
                         410
                  ....*....|...
gi 1919040695 374 DMVVTREDYEENG 386
Cdd:cd13397   347 SMWITRAEYDEFG 359
PTZ00004 PTZ00004
actin-2; Provisional
4-386 2.16e-55

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 186.90  E-value: 2.16e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695   4 LVLDNGAYNAKIGYSHDSV--SVIPNCQFRSKTARLKTFTANQ----IDEIKDPSG-LFYILPFQKGYLVNWDVQRQVWD 76
Cdd:PTZ00004    9 AVVDNGSGMVKAGFAGDDAprCVFPSIVGRPKNPGIMVGMEEKdcyvGDEAQDKRGiLTLKYPIEHGIVTNWDDMEKIWH 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  77 YLFGKEMyQVDFVDTNIIITEPYFNFTSIQESMNEILFEEYQF-------QAVLRVNAGGLSAHryfrdnpselccIIVD 149
Cdd:PTZ00004   89 HTFYNEL-RVAPEEHPVLLTEAPLNPKANREKMTQIMFETHNVpamyvaiQAVLSLYASGRTTG------------IVLD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 150 SGYSFTHIVPYCRSKKKKEAIIRINVGGKLLTNHLKEIISYR--QLHVMDETHVINQVKEDVCYVSQDFykDMDIAKLKG 227
Cdd:PTZ00004  156 SGDGVSHTVPIYEGYSLPHAIHRLDVAGRDLTEYMMKILHERgtTFTTTAEKEIVRDIKEKLCYIALDF--DEEMGNSAG 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 228 EENTVMVDYVLPDFStikkgfckpreemvlsgkyksgeqILRLANERFAVPEILFNPSDIGIQE-MGIPEAIVYSIQNLP 306
Cdd:PTZ00004  234 SSDKYEESYELPDGT------------------------IITVGSERFRCPEALFQPSLIGKEEpPGIHELTFQSINKCD 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 307 EEMQPHFFKNIVLTGGNTLFPGFRDRVYSEVRCLTPTDYDVSVVLPENPITYSWEGGKLISENDDFEDMVVTREDYEENG 386
Cdd:PTZ00004  290 IDIRKDLYGNIVLSGGTTMYRGLPERLTKELTTLAPSTMKIKVVAPPERKYSVWIGGSILSSLPTFQQMWVTKEEYDESG 369
PTZ00281 PTZ00281
actin; Provisional
1-393 1.11e-48

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 169.11  E-value: 1.11e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695   1 MATLVLDNGAYNAKIGYSHDSV--SVIPNCQFRSKTARLKTFTANQI----DEIKDPSGLFYI-LPFQKGYLVNWDVQRQ 73
Cdd:PTZ00281    6 VQALVIDNGSGMCKAGFAGDDAprAVFPSIVGRPRHTGVMVGMGQKDsyvgDEAQSKRGILTLkYPIEHGIVTNWDDMEK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  74 VWDYLFGKEMyQVDFVDTNIIITEPYFNFTSIQESMNEILFEEYQ-------FQAVLRVNAGGLSAHryfrdnpselccI 146
Cdd:PTZ00281   86 IWHHTFYNEL-RVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNtpamyvaIQAVLSLYASGRTTG------------I 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 147 IVDSGYSFTHIVPYCRSKKKKEAIIRINVGGKLLTNHLKEIISYR--QLHVMDETHVINQVKEDVCYVSQDFYKDMDIAk 224
Cdd:PTZ00281  153 VMDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYMMKILTERgySFTTTAEREIVRDIKEKLAYVALDFEAEMQTA- 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 225 lkGEENTVMVDYVLPDfstikkgfckpreemvlsgkyksgEQILRLANERFAVPEILFNPSDIGIQEMGIPEAIVYSIQN 304
Cdd:PTZ00281  232 --ASSSALEKSYELPD------------------------GQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMK 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 305 LPEEMQPHFFKNIVLTGGNTLFPGFRDRVYSEVRCLTPTDYDVSVVLPENPITYSWEGGKLISENDDFEDMVVTREDYEE 384
Cdd:PTZ00281  286 CDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELTALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDE 365

                  ....*....
gi 1919040695 385 NGHCICEEK 393
Cdd:PTZ00281  366 SGPSIVHRK 374
ASKHA_NBD_Arp2 cd10220
nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, ...
3-340 1.50e-48

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: 168.90  E-value: 1.50e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695   3 TLVLDNGAYNAKIGYSHDSvsvIPNCQFRSKTAR--LKTFTANQIDEIKD------PSGLFYIL----PFQKGYLVNWDV 70
Cdd:cd10220     2 VVVCDNGTGFVKCGFAGSN---FPEHVFPSLVGRpiLRAEEKVGDIEIKDimvgdeASELRSMLevtyPMENGIVRNWDD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  71 QRQVWDYLFGKEMyQVDFVDTNIIITEPYFNFTSIQESMNEILFEEYQF-------QAVLRVNAGGLsahryfrdnpseL 143
Cdd:cd10220    79 MEHLWDYTFGEKL-KIDPRECKILLTEPPMNPTKNREKMVEVMFEKYGFagvyvaiQAVLTLYAQGL------------L 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 144 CCIIVDSGYSFTHIVPYCRSKKKKEAIIRINVGGKLLTNHLKEIISYRQL---HVMD-EThvINQVKEDVCYVSQDFYKD 219
Cdd:cd10220   146 TGVVVDSGDGVTHIVPVYEGFSLPHLTRRLDVAGRDITRYLIKLLLLRGYafnRTADfET--VREIKEKLCYVAYDIELE 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 220 MDIAklkgEENTVMV-DYVLPDFSTIKKGfckpreemvlsgkyksgeqilrlaNERFAVPEILFNPSDIGIQEMGIPEAI 298
Cdd:cd10220   224 QKLA----LETTVLVeSYTLPDGRVIKVG------------------------GERFEAPEALFQPHLIDVEGPGIAELL 275
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1919040695 299 VYSIQNLPEEMQPHFFKNIVLTGGNTLFPGFRDRVYSEVRCL 340
Cdd:cd10220   276 FNTIQAADIDTRPELYKHIVLSGGSTMYPGLPSRLEKEIKQL 317
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
3-387 2.47e-47

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: 164.67  E-value: 2.47e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695   3 TLVLDNGAYNAKIGYSHDSVsviPNCQFRSKTARLK--------TFTANQIDEIkDPSGLFYILPFQKGYLVNWDVQRQV 74
Cdd:cd10211     1 PIVIDNGSYQCRAGWAGDKE---PRLVFRNLVAKPRdrkkgitvTLVGNDILND-EAVRSHLRSPFDRNVVTNFDLQEQI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  75 WDYLFGK-----EmyqvDFVDTNIIITEPYFNFTSIQESMNEILFEEYQFQAVlrvnAGGLSAHRYFRDNPSELC---CI 146
Cdd:cd10211    77 LDYIFSHlginsE----GSVDHPIVLTEALCNPNYSRQLMSELLFECYGVPSV----AYGIDSLFSYYHNQPQGDpsdGL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 147 IVDSGYSFTHIVPYCRSKKKKEAIIRINVGGKLLTNHLKEIISYR---QLHVMDeTHVINQVKEDVCYVSQDFykdmdia 223
Cdd:cd10211   149 VISSGYSTTHVIPVLNGRLDLSQCKRINLGGFHATDYLQRLLQLKyptHPSAIT-LSRAEELVHEHCYVAEDY------- 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 224 klkgeentvmvdyvlpdfstikkgfckpreemvlsgkyksGEQILRLANERFAvpeilfNPSDIGIQ-EMGIPEAIVYSI 302
Cdd:cd10211   221 ----------------------------------------DEELKKWEDPEYY------EENVRKIQlPFGLVETIEFVL 254
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 303 QNLPEEMQPHFFKNIVLTGGNTLFPGFRDRVYSEVRCLTPTDYDVSVVLPENPITYSWEGGKLISENDDFEDMVVTREDY 382
Cdd:cd10211   255 KRYPAEQQDRLVQNVFLTGGNALFPGLKERLEKELRAIRPFGSPFNVVRAKDPVLDAWRGAAKWALDSTFEKVWITKQEY 334

                  ....*
gi 1919040695 383 EENGH 387
Cdd:cd10211   335 EEKGG 339
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
2-389 2.91e-47

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: 165.23  E-value: 2.91e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695   2 ATLVLDNGAYNAKIGYSHDSV--SVIPNCQFRSKTARLKTFTANQI----DEIKDPSGLFYI-LPFQKGYLVNWDVQRQV 74
Cdd:cd10224     1 AALVVDNGSGMCKAGFAGDDAprAVFPSIVGRPRHQGVMVGMGQKDsyvgDEAQSKRGILTLkYPIEHGIVTNWDDMEKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  75 WDYLFGKEMyQVDFVDTNIIITEPYFNFTSIQESMNEILFEEY-------QFQAVLRVNAGGLSAHryfrdnpselccII 147
Cdd:cd10224    81 WHHTFYNEL-RVAPEEHPVLLTEAPLNPKANREKMTQIMFETFnvpamyvAIQAVLSLYASGRTTG------------IV 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 148 VDSGYSFTHIVPYCRSKKKKEAIIRINVGGKLLTNHLKEIISYR--QLHVMDETHVINQVKEDVCYVSQDFYKDMDIAKl 225
Cdd:cd10224   148 LDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERgySFTTTAEREIVRDIKEKLCYVALDFEQEMQTAA- 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 226 kgEENTVMVDYVLPDfstikkgfckpreemvlsgkyksgEQILRLANERFAVPEILFNPSDIGIQEMGIPEAIVYSIQNL 305
Cdd:cd10224   227 --SSSSLEKSYELPD------------------------GQVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKC 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 306 PEEMQPHFFKNIVLTGGNTLFPGFRDRVYSEVRCLTPTDYDVSVVLPENPiTYS-WEGGKLISENDDFEDMVVTREDYEE 384
Cdd:cd10224   281 DVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTMKIKIVAPPER-KYSvWIGGSILASLSTFQQMWISKQEYDE 359

                  ....*
gi 1919040695 385 NGHCI 389
Cdd:cd10224   360 SGPSI 364
ASKHA_NBD_ACTL7 cd10214
nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ...
5-386 4.80e-45

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: 159.13  E-value: 4.80e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695   5 VLDNGAYNAKIGY------SHdSVSVIPNCQFRsKTA-----RLKTFTANQIDEIKDPsgLFYILPFQKGYLVNWDVQRQ 73
Cdd:cd10214     7 IIDLGTGYCKAGFagqprpSY-VISSTVGKPPQ-ESAktgdnRKETFVGKELANVEPP--LKLVNPLRHGIVVDWDCVQD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  74 VWDYLFGKEMyQVDFVDTNIIITEPYFNFTSIQESMNEILFEEYQFQAVLRVNAGGLSAHRYFRDNPselccIIVDSGYS 153
Cdd:cd10214    83 IWEYIFEKEM-KILPEEHAVLVSDPPLSPTTNREKYAELMFETFSIPAMHIAYQSRLSLYSYGRTSG-----LVVESGHG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 154 FTHIVPYCRSKKKKEAIIRINVGGKLLTNHLKEIISYRQLHVMDET-HVINQVKEDVCYVSQDFYKDMdiaKLKGEENTV 232
Cdd:cd10214   157 VSYVVPIHEGYNLPHITGRADYAGSDLTAYLMKLLNEAGNKFTDDQlHIVEDIKKKCCYVALDFEEEM---GLPPQEYTV 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 233 mvDYVLPDFSTIKkgfckpreemvlsgkyksgeqilrLANERFAVPEILFNPSDIGIQEMGIPEAIVYSIQNLPEEMQPH 312
Cdd:cd10214   234 --DYELPDGHLIT------------------------IGKERFRCPEMLFNPSLIGSKQPGLHTLTMNSLNKCDANLKKD 287
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1919040695 313 FFKNIVLTGGNTLFPGFRDRVYSEVRCLTPTDYDVSVVLPENpiTYS-WEGGKLISENDDFEDMVVTREDYEENG 386
Cdd:cd10214   288 LAKNILLCGGSTMFDGFPDRFQKELSKLCPNDNPIVAASPER--KYSvWTGGSILASLKSFQQLWVRRREYEERG 360
ASKHA_NBD_Arp4_ACTL6-like cd13395
nucleotide-binding domain (NBD) of the actin-related protein 4 (Arp4)-like subfamily; The ...
4-386 6.30e-45

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: 160.04  E-value: 6.30e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695   4 LVLDNGAYNAKIGYSHDSV--SVIPNC--QFRSKTARLKTFTANQIDEIK---DPSGLFY-------ILPFQKGYLVNWD 69
Cdd:cd13395     7 LVLDIGSYSTRAGYAGEDTpkAVFPSVvgVVTDDDDAEDYVGGSGEKKRKyyiGTNSIGVprpnmevISPLKDGLIEDWD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  70 VQRQVWDYLFgKEMYQVDFVDTNIIITEPYFNFTSIQESMNEILFEEYQFQAVLRVNAGGLSA---HRYfrdnpselCCI 146
Cdd:cd13395    87 AFEKLWDHAL-KNRLRVDPSEHPLLLTEPSWNTRANREKLTELMFEKYNVPAFFLAKNAVLSAfanGRS--------TAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 147 IVDSGYSFTHIVP----YCRSKkkkeAIIRINVGGKLLTNHLK--------EII-------------------------- 188
Cdd:cd13395   158 VVDSGATSTSVVPvhdgYVLQK----AIVRSPLGGDFLTDQLLklleskniEIIprymikskepveggapakytkkdlpn 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 189 ---SYRQLHVMDethVINQVKEDVCYVSQDFYkDMDIAklkgeENTVMVDYVLPDFSTIKKGfckpreemvlsgkyksge 265
Cdd:cd13395   234 ttsSYHRYMVRR---VLQDFKESVCQVSDSPF-DESEA-----ASIPTVSYELPDGYNIEFG------------------ 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 266 qilrlaNERFAVPEILFNPSDI---------GIQEMGIPEAIVYSIQNLPEEMQPHFFKNIVLTGGNTLFPGFRDRVYSE 336
Cdd:cd13395   287 ------AERFKIPELLFDPSLVkgipappseGNELLGLPQLVYTSIGSCDVDIRPELYGNVVLTGGNSLLPGFTDRLNRE 360
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1919040695 337 VRCLTPTDYDVSVVLPENPI--TYS-WEGGKLISENDDFEDMVVTREDYEENG 386
Cdd:cd13395   361 LSEKAPGSLKLKILASGNTVerRFSsWIGGSILASLGSFQQMWISKQEYEEHG 413
PTZ00466 PTZ00466
actin-like protein; Provisional
4-393 9.12e-45

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 158.95  E-value: 9.12e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695   4 LVLDNGAYNAKIGYSHDSvsvIPNCQFRSKTARLK------------TFTANQIDEIKDPSGLFYilPFQKGYLVNWDVQ 71
Cdd:PTZ00466   15 IIIDNGTGYIKAGFAGED---VPNLVFPSYVGRPKykrvmagavegnIFVGNKAEEYRGLLKVTY--PINHGIIENWNDM 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  72 RQVWDYLFgKEMyQVDFVDTNIIITEPYFNFTSIQESMNEILFEEYQFQAVLRVNAGGLSAHRYFRDNPselccIIVDSG 151
Cdd:PTZ00466   90 ENIWIHVY-NSM-KINSEEHPVLLTEAPLNPQKNKEKIAEVFFETFNVPALFISIQAILSLYSCGKTNG-----TVLDCG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 152 YSFTHIVPYCRSKKKKEAIIRINVGGKLLTNHLKEIISyRQLHVMD---ETHVINQVKEDVCYVSQDFYKDmdiaKLKGE 228
Cdd:PTZ00466  163 DGVCHCVSIYEGYSITNTITRTDVAGRDITTYLGYLLR-KNGHLFNtsaEMEVVKNMKENCCYVSFNMNKE----KNSSE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 229 ENTVMVDYVLPDfstikkgfckpreemvlsgkyksGEQILrLANERFAVPEILFNPSDIGIQEMGIPEAIVYSIQNLPEE 308
Cdd:PTZ00466  238 KALTTLPYILPD-----------------------GSQIL-IGSERYRAPEVLFNPSILGLEYLGLSELIVTSITRADMD 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 309 MQPHFFKNIVLTGGNTLFPGFRDRVYSEVRCLTPTDYDVSVVLPENPITYSWEGGKLISENDDFEDMVVTREDYEENGHC 388
Cdd:PTZ00466  294 LRRTLYSHIVLSGGTTMFHGFGDRLLNEIRKFAPKDITIRISAPPERKFSTFIGGSILASLATFKKIWISKQEFDEYGSV 373

                  ....*
gi 1919040695 389 ICEEK 393
Cdd:PTZ00466  374 ILHRK 378
PTZ00452 PTZ00452
actin; Provisional
4-393 1.72e-37

actin; Provisional


Pssm-ID: 185631  Cd Length: 375  Bit Score: 139.50  E-value: 1.72e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695   4 LVLDNGAYNAKIGYSHDS--VSVIPNCQFRSKTARLKTFTANQI----DEIKDPSGLFYIL-PFQKGYLVNWDVQRQVWD 76
Cdd:PTZ00452    8 VVIDNGSGYCKIGIAGDDapTSCFPAIVGRSKQNDGIFSTFNKEyyvgEEAQAKRGVLAIKePIQNGIINSWDDIEIIWH 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  77 YLFGKEMYqVDFVDTNIIITEPYFNFTSIQESMNEILFEEYQFQAVLRVNAGGLSAHryfrdNPSELCCIIVDSGYSFTH 156
Cdd:PTZ00452   88 HAFYNELC-MSPEDQPVFMTDAPMNSKFNRERMTQIMFETFNTPCLYISNEAVLSLY-----TSGKTIGLVVDSGEGVTH 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 157 IVPYCRSKKKKEAIIRINVGGKLLTNHLKEIIsyRQL-HVMDETH---VINQVKEDVCYVSQDfykDMDIAKLKGEENTV 232
Cdd:PTZ00452  162 CVPVFEGHQIPQAITKINLAGRLCTDYLTQIL--QELgYSLTEPHqriIVKNIKERLCYTALD---PQDEKRIYKESNSQ 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 233 MVDYVLPDfstikkgfckpreemvlsgkyksgEQILRLANERFAVPEILFNPSDIGIQEMGIPEAIVYSIQNLPEEMQPH 312
Cdd:PTZ00452  237 DSPYKLPD------------------------GNILTIKSQKFRCSEILFQPKLIGLEVAGIHHLAYSSIKKCDLDLRQE 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 313 FFKNIVLTGGNTLFPGFRDRVYSEVRCLTPTDYDVSVVLPENPITYSWEGGKLISENDDFEDMVVTREDYEENGHCICEE 392
Cdd:PTZ00452  293 LCRNIVLSGGTTLFPGIANRLSNELTNLVPSQLKIQVAAPPDRRFSAWIGGSIQCTLSTQQPQWIKRQEYDEQGPSIVHR 372

                  .
gi 1919040695 393 K 393
Cdd:PTZ00452  373 K 373
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
4-386 6.81e-34

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: 129.05  E-value: 6.81e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695   4 LVLDNGAYNAKIGYSHDSVSviPNCQFRSKTARLKTFTANQIDEIKDPSglfyILPFQKGYLVNWDVQRQVWDYLFGKEM 83
Cdd:cd10209     1 VVIDAGSRLLKAGYAYPDRE--PSVVEPTRVTPAVEDGEESDTVVEGNT----VSPIRRGRIEDWDALEALLRYVFYTGL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  84 YQVDFVDTNIIITEPYFNFTSIQESMNEILFEEY-------QFQAVLRVNAGGlsahryfrdnpsELCCIIVDSGYSFTH 156
Cdd:cd10209    75 GWEEGNEGQVLIAEPLLTSKAERERLTQLMFETFnvsglyaSEQAVLSLYAVG------------RISGCVVDVGHGKID 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 157 IVPYCRSKKKKEAIIRINVGGKLLTNHLKEIISYRQLHVMDETHVINQVKEDVCYVSQDfykdmDIAKLKGEENTVMVDY 236
Cdd:cd10209   143 IAPVWEGAIQHNAVRRFEIGGRDLTELLAAELGKSNPKVKLDRSIVERLKEAVAWSADD-----EEAYEKKVLTCSPETY 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 237 VLPDfstikkgfckpreemvlsgkyksGEQIlRLANERFAVPEILFNPSDIGIQEMGIPEAIVYSIQNLPEEMQPHFFKN 316
Cdd:cd10209   218 TLPD-----------------------GRVI-SVGKERYCVGEALFRPSILGIEEYGIVEQLVRAVSTSPSENRRQLLEN 273
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1919040695 317 IVLTGGNTLFPGFRDRVYSEVRCLTPTDYDVSVV-----LPENPITYS-WEGGKLISENDDFEDMVVTREDYEENG 386
Cdd:cd10209   274 IVLCGGTSSVPGLEARLQKEIRLLSSPSSRPALVkppeyMPENTLRYSaWIGGAILAKVVFPQNQHVTKADYDETG 349
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
1-390 6.84e-32

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 124.84  E-value: 6.84e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695   1 MATLVLDNGAYNAKIGY------SHDSVSVIPNCQFRSKTARLKTFtaNQID-----EIKDPSG---LFYilPFQKGYLV 66
Cdd:PTZ00280    4 LPVVVIDNGTGYTKMGYagntepTYIIPTLIADNSKQSRRRSKKGF--EDLDfyigdEALAASKsytLTY--PMKHGIVE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  67 NWDVQRQVWDYLFGKEMyQVDFVDTNIIITEPYFNFTSIQESMNEILFEEYQ-------FQAVLRVNAGGLSAHRYFRDN 139
Cdd:PTZ00280   80 DWDLMEKFWEQCIFKYL-RCEPEEHYFILTEPPMNPPENREYTAEIMFETFNvkglyiaVQAVLALRASWTSKKAKELGG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 140 psELCCIIVDSGYSFTHIVPYCRSKKKKEAIIRINVGGKLLTNHLKEIISYRQLHV--MDETHVINQVKEDVCYVSQDFY 217
Cdd:PTZ00280  159 --TLTGTVIDSGDGVTHVIPVVDGYVIGSSIKHIPLAGRDITNFIQQMLRERGEPIpaEDILLLAQRIKEKYCYVAPDIA 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 218 KDMDIAKlkgeentvmvdyvlpdfSTIKKGFCKPREEMVLSGKYKSgeqiLRLANERFAVPEILFNPsDIGIQE--MGIP 295
Cdd:PTZ00280  237 KEFEKYD-----------------SDPKNHFKKYTAVNSVTKKPYT----VDVGYERFLGPEMFFHP-EIFSSEwtTPLP 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 296 EAIVYSIQNLPEEMQPHFFKNIVLTGGNTLFPGFRDRVYSEVRCLT----------------PTDYDVSVVlpENPIT-Y 358
Cdd:PTZ00280  295 EVVDDAIQSCPIDCRRPLYKNIVLSGGSTMFKGFDKRLQRDVRKRVdrrlkkaeelsggklkPIPIDVNVV--SHPRQrY 372
                         410       420       430
                  ....*....|....*....|....*....|...
gi 1919040695 359 S-WEGGKLISENDDFEDMVVTREDYEENGHCIC 390
Cdd:PTZ00280  373 AvWYGGSMLASSPEFEKVCHTKAEYDEYGPSIC 405
COG5277 COG5277
Actin-related protein [Cytoskeleton];
67-384 3.36e-28

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 114.50  E-value: 3.36e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  67 NWDVQRQVWDYLFGKEMY-QVDFVDTNIIITEPYFNFTSIQESMNEILFE---EYQFQAVLRVNAGGLSAHRYFRDNpse 142
Cdd:COG5277    96 AWRVLKELLRYTFAQFLVvDPEFHGFLVVVALSALAPDYMRERLFDIHFEvfsEEGAPAVTIIPQPLAVAIAEKAVT--- 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 143 lcCIIVDSGYSFTHIVPYCRSKKKkEAIIRINVGGKLLTNHLKEIIsyRQLHVMD---ETHVINQVKEDVCYVSQDFYKD 219
Cdd:COG5277   173 --CVVVEAGHGNSQVAPISRGPIR-EGLVALNRGGAEANAITREIL--KDRGYSDtarEEYVVRVVKEALGLVPRDLAKA 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 220 MDIAKlkGEENTVMVDYVLPDfstikkgfckPREEMVLsGKYksgeqilrlANERFAVPEILFNPSDIGIQ--------- 290
Cdd:COG5277   248 IQKAA--SNPDSFEAKVRLPN----------PTVEIEL-GNY---------AWERFLIGEILFNPNHEGFEsyiqqgrlr 305
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 291 -------------EMGIPEAIVYSIQNLPEEMQPHFFKNIVLTGGNTLF---PGFRD-------RVYSEVRCLTPTdYDV 347
Cdd:COG5277   306 iedavigdvvlygEMGLAEAIINSIMKCDVEIQDELYSNIILSGGAFNWsvpPGLEDvavdsvtRVQIELSELAPE-LKV 384
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1919040695 348 SVVLPENPITYSWEG----GKLISENDDFEDmvVTREDYEE 384
Cdd:COG5277   385 NVRLVSDPQYSVWKGaiiyGYALPFSVKWSW--ITKEGWYF 423
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
5-390 1.33e-24

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: 104.19  E-value: 1.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695   5 VLDNGAYNAKIGYSHDSVS--VIPNCQFRSKTARLKTFTANQIDEIKDpsgL-FYI--------------LPFQKGYLVN 67
Cdd:cd10221     3 VIDNGTGYTKMGYAGNTEPqfIIPTVIAIKESAKVGDGQRRSKKGIED---LdFYIgdealansptyalkYPIRHGIVED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  68 WDVQRQVWDYLFGKEMyQVDFVDTNIIITEPYFNFTSIQESMNEILFEEYQ-------FQAVLRVNAGGLSAHRYFRdnp 140
Cdd:cd10221    80 WDLMERFWEQCIFKYL-RCEPEDHYFLLTEPPLNPPENREYTAEIMFETFNvpglyiaVQAVLALAASWTSRKVGER--- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 141 sELCCIIVDSGYSFTHIVP----YCRSKkkkeAIIRINVGGKLLTNHLKEIISYRQLHVMDET--HVINQVKEDVCYVSQ 214
Cdd:cd10221   156 -TLTGTVIDSGDGVTHVIPvaegYVIGS----CIKHIPIAGRDITYFIQQLLREREEGIPPEDslEVAKRIKERYCYVCP 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 215 DFYK-----DMDIAK----------LKGEENTVMVDYvlpdfstikkgfckpreemvlsgkyksgeqilrlanERFAVPE 279
Cdd:cd10221   231 DIVKefakyDSDPAKyikqytginsVTGKPYTVDVGY------------------------------------ERFLAPE 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 280 ILFNP----SDIgiqEMGIPEAIVYSIQNLPEEMQPHFFKNIVLTGGNTLFPGFRDRVYSEVR----------------C 339
Cdd:cd10221   275 IFFNPeiasSDF---TTPLPEVVDQVIQSCPIDTRRGLYKNIVLSGGSTMFKDFGRRLQRDVKrivdarlkaseelsggK 351
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1919040695 340 LTPTDYDVSVVlpENPI-TYS-WEGGKLISENDDFEDMVVTREDYEENGHCIC 390
Cdd:cd10221   352 LKPKPIDVNVI--SHPMqRYAvWFGGSMLASTPEFYTVCHTKAEYEEYGPSIC 402
ASKHA_NBD_AtArp8-like cd13396
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and ...
146-394 2.54e-17

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: 82.21  E-value: 2.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 146 IIVDSGYSFTHIVPYCRSKKKKE-AIIRINVGGKLLTNHLKEIISYRQLHvMDETHVINQVKEDVCYVSQDFYKDmdiaK 224
Cdd:cd13396   118 IVVNIGFRVTTIVPVYRGRVMHDiGVEVVGQGALRLTGFLKELMQQNGIR-FPSLYTVRTIKEKLCYVAEDYEAE----L 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 225 LKGEENTVMVDyvlpdfstikkgfckpreemvlsgkyksGEQILRLANERFAVPEILFNPSDIGIQEMGIPEAIVYSIQ- 303
Cdd:cd13396   193 AKDTQASCEVA----------------------------GEGWFTLSNERFKTGEILFQPGLGGMRAMGLHQAVALCMDh 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 304 --NLPEEMQPHFFKNIVLTGGNTLFPGFRDRVYSEVRCLTPTDY--DVSVVLPENPITYSWEGGKLISENDDFEDmvvtr 379
Cdd:cd13396   245 caLVHSQGDDGWFKTIVLSGGSACLPGLSERLERELRKLLPKSLseGIRIIPPPLGPDSAWQGAKLISNLSNFPD----- 319
                         250
                  ....*....|....*
gi 1919040695 380 edyeenGHCICEEKF 394
Cdd:cd13396   320 ------GWCITKKQF 328
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
57-386 3.36e-16

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: 79.27  E-value: 3.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  57 ILPFQKGYLVNWDVQRQVWDYLFGKEM-YQVDFVDTNIIITEPYfNFT-SIQESMNEILFEEYQFQAVLRVNAG-----G 129
Cdd:cd10208    36 IWPIQDGRVVDWDALEALWRHILFSLLsIPRPTNNSPVLLSVPP-SWSkSDLELLTQLFFERLNVPAFAILEAPlaalyA 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 130 LSAhryfrdnpseLCCIIVDSGYSFTHIVPYCRSKKKKEAIIRINVGGKLLTNHLKEIISyrqlhvmDETHVINQVKEDV 209
Cdd:cd10208   115 AGA----------TSGIVVDIGHEKTDITPIVDSQVVPHALVSIPIGGQDCTAHLAQLLK-------SDEPELKSQAESG 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 210 CYVSQDFykdmdIAKLKGEEntvmVDYVLPDfstikkgfckpreemvlSGKYKSGEQIlRLANERFAVPEILFNPSDIGI 289
Cdd:cd10208   178 EEATLDL-----AEALKKSP----ICEVLSD-----------------GADLASGTEI-TVGKERFRACEPLFKPSSLRV 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 290 QEMGIPEAIVYSIQNLPE-EMQPHFFKNIVLTGGNTLFPGFRDRVYSE--VRCL----TPTDYDVSVV----LPEnpitY 358
Cdd:cd10208   231 DLLIAAIAGALVLNASDEpDKRPALWENIIIVGGGSRIRGLKEALLSElqQFHLisetSASPQQPRIIrlakIPD----Y 306
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1919040695 359 --SWE----------GGKLISE---NDDFEDMVVTREDYEENG 386
Cdd:cd10208   307 fpEWKksgyeeaaflGASIVAKlvfNDPSSKHYISKVDYNEKG 349
ASKHA_NBD_Arp10 cd10207
nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins; ...
78-387 9.52e-16

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: 78.06  E-value: 9.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  78 LFGKEMyQVDFVDTNIIITEPYFNFTSIQESMNEILFEEYQFQAVLRVnagglsahryfrdnPSELCC---------IIV 148
Cdd:cd10207    61 LYFKHL-LVNPKDRRVVVVESVLCPTPFRETLAKVLFKHFEVPSVLFA--------------PSHLLSlltlgirtaLVV 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 149 DSGYSFTHIVPYCRSKKKKEAIIRINVGGKLLTNHLK-EIISYRQLHVMDETHVINQVKED-------------VCYVSq 214
Cdd:cd10207   126 DCGYRETRVLPVYEGVPLLSAWQSTPLGGKALHKRLKkLLLEHATVVTGDNKGQLLSSVDSllseevledikvrACFVT- 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 215 dfykDMDIAKlKGEENTVMVDYVLPDFStikKGFCKPReemvlsgkykSGEQILRLANE-RFAVPEILFNPSDigiQEMG 293
Cdd:cd10207   205 ----SLERGK-TLQSATEEGSTEEPSPP---PPVDYPL----------DGEKILIVPGSiRESAEELLFEGDN---EEKS 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 294 IPEAIVYSIQNLPEEMQPHFFKNIVLTGGNTLFPGFRDRVYSEVR-CLTPTDY------------DVSVVLPENPItySW 360
Cdd:cd10207   264 LPTLILDSLLKCPIDVRKQLAENIVVIGGTSMLPGFKHRLLEELRaLLRKPKYfeelapktfrfhTPPSVFKPNYL--AW 341
                         330       340
                  ....*....|....*....|....*..
gi 1919040695 361 EGGKLISENDDFEDMVVTREDYEENGH 387
Cdd:cd10207   342 LGGSIFGALESILGRSLSREAYLQTGR 368
ASKHA_NBD_ScArp7-like cd10212
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and ...
4-342 8.35e-08

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: 53.95  E-value: 8.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695   4 LVLDNGAYNAKIGYSHDSVS--VIPNCQFRSK----TARLKTFTANQIDEI--KDPSGLFYILPFQKGYLVNWDVQRQVW 75
Cdd:cd10212     6 VVIHNGSHRTVAGFSNVELPqcIIPSSYIKRTdeggEAEFIFGTYNMIDAAaeKRNGDEVYTLVDSQGLPYNWDALEMQW 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695  76 DYLFGKEMyQVDFVDTNIIITEPYFNF---TSIQESMNEILFEEYQ---FQAVLRVNAGGLSAHRYfrdnpselCCIIVD 149
Cdd:cd10212    86 RYLYDTQL-KVSPEELPLVITMPATNGkpdMAILERYYELAFDKLNvpvFQIVIEPLAIALSMGKS--------SAFVID 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 150 SGYSFTHIVPYCRSKKKKEAIIRINVGGKLLTNHLKEIIS----------------YRQLHVMDETHV-INQVKEDVCYV 212
Cdd:cd10212   157 IGASGCNVTPIIDGIVVKNAVVRSKFGGDFLDFQVHERLAplikeendmenmadeqKRSTDVWYEASTwIQQFKSTMLQV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 213 SQD-------FYKDMDIAKLKGEENTVMVDYVLpDFSTIKKgfcKPREEMVLSGK--YKSGEQILRL-ANERFAVPEILF 282
Cdd:cd10212   237 SEKdlfelerYYKEQADIYAKQQEQLKQMDQQL-QYTALTG---SPNNPLVQKKNflFKPLNKTLTLdLKECYQFAEYLF 312
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1919040695 283 NP---SDIGIQEMGIPEAIVYSIQNLPEEMQPHFFKNIVLTGGNTLFPGFRDRVYSEVRCLTP 342
Cdd:cd10212   313 KPqliSDKFSPEDGLGPLMAKSVKKAPEQVYSLLLTNVIITGSTSLIEGMEQRIIKELSIRFP 375
ASKHA_NBD_Arp8-like cd10206
nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The ...
282-386 1.03e-07

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: 53.78  E-value: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919040695 282 FNPSDIGIQE-------------------MGIPEAIVYSIQNLP-EEMQPHFFKNIVLTGGNTLFPGFR----DRVYSEV 337
Cdd:cd10206   309 LDQDDIGVQLhefyvrepgqptlkyqfklLPLDEAIVQSILSCAsDELKRKMYSSILLVGGGAKIPGLAealeDRLLIKI 388
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1919040695 338 RCLTPTDYDVSVVLP---ENPITYSWEGGKLISENDDFEDMVVTREDYEENG 386
Cdd:cd10206   389 PSLFEAVETVEVLPPpkdMDPSLLAWKGGAVLACLDSAQELWITRKEWQRLG 440
 
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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