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Conserved domains on  [gi|2321196102|gb|QTU91090|]
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beta-actin, partial [Lasiopodomys brandtii]

Protein Classification

acetate and sugar kinases/Hsc70/actin family protein( domain architecture ID 99298)

acetate and sugar kinases/Hsc70/actin (ASKHA) family protein catalyzes phosphoryl transfer from ATP to their respective substrates

CATH:  3.30.420.40
Gene Ontology:  GO:0000166
PubMed:  8800467|7781919
SCOP:  3000092

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ASKHA_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
 1-123 1.89e-107

ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.


The actual alignment was detected with superfamily member cd10224:

Pssm-ID: 483947  Cd Length: 365  Bit Score: 308.91  E-value: 1.89e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102   1 SYELPDGQVITIGNERFRAPEALFQPSFLGMESSGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEIT 80
Cdd:cd10224   234 SYELPDGQVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEIT 313

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2321196102  81 ALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQE 123
Cdd:cd10224   314 ALAPSTMKIKIVAPPERKYSVWIGGSILASLSTFQQMWISKQE 356
 
Name Accession Description Interval E-value
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
 1-123 1.89e-107

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: 308.91  E-value: 1.89e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102   1 SYELPDGQVITIGNERFRAPEALFQPSFLGMESSGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEIT 80
Cdd:cd10224   234 SYELPDGQVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEIT 313

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2321196102  81 ALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQE 123
Cdd:cd10224   314 ALAPSTMKIKIVAPPERKYSVWIGGSILASLSTFQQMWISKQE 356
PTZ00281 PTZ00281
actin; Provisional
 1-123 5.06e-84

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 250.00  E-value: 5.06e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102   1 SYELPDGQVITIGNERFRAPEALFQPSFLGMESSGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEIT 80
Cdd:PTZ00281  240 SYELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELT 319

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2321196102  81 ALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQE 123
Cdd:PTZ00281  320 ALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEE 362
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
 1-123 1.53e-72

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 220.59  E-value: 1.53e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102    1 SYELPDGQVITIGNERFRAPEALFQPSFLGMESSGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEIT 80
Cdd:smart00268 237 TYELPDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELK 316

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2321196102   81 ALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQE 123
Cdd:smart00268 317 QLAPKKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKE 359
Actin pfam00022
Actin;
1-123 3.55e-69

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 212.94  E-value: 3.55e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102   1 SYELPDGQVITIGNERFRAPEALFQPSFLGMES--------SGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIA 72
Cdd:pfam00022 260 VYELPDGSTIILGAERFRVPEILFNPSLIGSESelpppqtaVGIPELIVDAINACDVDLRPSLLANIVVTGGNSLFPGFT 339

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2321196102  73 DRMQKEITALAPSTMKIKIIAPP---ERKYSVWIGGSILASLSTFQQMWISKQE 123
Cdd:pfam00022 340 ERLEKELAQLAPPGVKVKIIAPGntvERRYSAWIGGSILASLGTFQQMWVSKQE 393
COG5277 COG5277
Actin-related protein [Cytoskeleton];
1-123 9.15e-42

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 142.24  E-value: 9.15e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102   1 SYELPDGQV-ITIGN---ERFRAPEALFQPSFLGMESS----------------------GIHETTFNSIMKCDVDIRKD 54
Cdd:COG5277   261 KVRLPNPTVeIELGNyawERFLIGEILFNPNHEGFESYiqqgrlriedavigdvvlygemGLAEAIINSIMKCDVEIQDE 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102  55 LYANTVLSGGTTMY---PGIAD-------RMQKEITALAPsTMKIKIIAPPERKYSVWIGGSILASLSTFQQMW--ISKQ 122
Cdd:COG5277   341 LYSNIILSGGAFNWsvpPGLEDvavdsvtRVQIELSELAP-ELKVNVRLVSDPQYSVWKGAIIYGYALPFSVKWswITKE 419


                  .
gi 2321196102 123 E 123
Cdd:COG5277   420 G 420
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
 65-123 9.43e-25

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: 91.19  E-value: 9.43e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2321196102  65 TTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQE 123
Cdd:NF040575   61 RVNESGFYEKLKKSITEKAPKGALIGMTLDPKPESAAWRGAAMYAASEGFVEMAITKQE 119
 
Name Accession Description Interval E-value
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
 1-123 1.89e-107

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: 308.91  E-value: 1.89e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102   1 SYELPDGQVITIGNERFRAPEALFQPSFLGMESSGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEIT 80
Cdd:cd10224   234 SYELPDGQVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEIT 313

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2321196102  81 ALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQE 123
Cdd:cd10224   314 ALAPSTMKIKIVAPPERKYSVWIGGSILASLSTFQQMWISKQE 356
ASKHA_NBD_actin_Arp-T1-3 cd13397
nucleotide-binding domain (NBD) of actin, actin-related proteins T1-T3 (Arp-T1-3), and similar ...
 1-123 1.96e-87

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: 257.89  E-value: 1.96e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102   1 SYELPDGQVITIGNERFRAPEALFQPSFLGMESSGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEIT 80
Cdd:cd13397   232 EYTLPDGQVIKIGSERFRCPEALFRPSLIGREAPGIHKLVYNSIMKCDIDIRKDLYSNIVLSGGSTMFPGLPERLQKELE 311

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2321196102  81 ALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQE 123
Cdd:cd13397   312 ALAPSSTKVKVIAPPERKYSVWIGGSILASLSTFKSMWITRAE 354
PTZ00281 PTZ00281
actin; Provisional
 1-123 5.06e-84

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 250.00  E-value: 5.06e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102   1 SYELPDGQVITIGNERFRAPEALFQPSFLGMESSGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEIT 80
Cdd:PTZ00281  240 SYELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELT 319

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2321196102  81 ALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQE 123
Cdd:PTZ00281  320 ALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEE 362
PTZ00004 PTZ00004
actin-2; Provisional
 1-123 1.05e-75

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 228.89  E-value: 1.05e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102   1 SYELPDGQVITIGNERFRAPEALFQPSFLGMESS-GIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEI 79
Cdd:PTZ00004  241 SYELPDGTIITVGSERFRCPEALFQPSLIGKEEPpGIHELTFQSINKCDIDIRKDLYGNIVLSGGTTMYRGLPERLTKEL 320

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2321196102  80 TALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQE 123
Cdd:PTZ00004  321 TTLAPSTMKIKVVAPPERKYSVWIGGSILSSLPTFQQMWVTKEE 364
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
 1-123 1.53e-72

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 220.59  E-value: 1.53e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102    1 SYELPDGQVITIGNERFRAPEALFQPSFLGMESSGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEIT 80
Cdd:smart00268 237 TYELPDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELK 316

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2321196102   81 ALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQE 123
Cdd:smart00268 317 QLAPKKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKE 359
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
 1-123 1.16e-71

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: 218.18  E-value: 1.16e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102   1 SYELPDGQVITIGNERFRAPEALFQPSFLGMESSGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEIT 80
Cdd:cd10216   235 QYTLPDGSTIEIGPERFRAPEILFNPELIGLEYPGVHEVLVDSIQKSDLDLRKTLYSNIVLSGGSTLFKGFGDRLLSEVK 314

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2321196102  81 ALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQE 123
Cdd:cd10216   315 KLAPKDVKIRISAPPERLYSTWIGGSILASLSTFKKMWVSKKE 357
Actin pfam00022
Actin;
1-123 3.55e-69

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 212.94  E-value: 3.55e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102   1 SYELPDGQVITIGNERFRAPEALFQPSFLGMES--------SGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIA 72
Cdd:pfam00022 260 VYELPDGSTIILGAERFRVPEILFNPSLIGSESelpppqtaVGIPELIVDAINACDVDLRPSLLANIVVTGGNSLFPGFT 339

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2321196102  73 DRMQKEITALAPSTMKIKIIAPP---ERKYSVWIGGSILASLSTFQQMWISKQE 123
Cdd:pfam00022 340 ERLEKELAQLAPPGVKVKIIAPGntvERRYSAWIGGSILASLGTFQQMWVSKQE 393
ASKHA_NBD_Arp4_ACTL6-like cd13395
nucleotide-binding domain (NBD) of the actin-related protein 4 (Arp4)-like subfamily; The ...
 1-123 9.48e-67

nucleotide-binding domain (NBD) of the actin-related protein 4 (Arp4)-like subfamily; The Arp4-like subfamily includes Arp4, also called actin-like protein 4, from fungi and plants. Saccharomyces cerevisiae Arp4 acts synergistically with Arp8 to depolymerize F-actin; it binds ATP, but unlike conventional actin, does not form filaments. It is a component of the NuA4 histone acetyltransferase complex, the chromatin-remodeling INO80 complex and the SWR1 chromatin remodeling complex. Arabidopsis thaliana Arp4 is involved in several developmental processes including organization of plant organs, flowering time, anther development, flower senescence and fertility, probably by regulating the chromatin structure. This family also includes human homologs of yeast and plant, which are actin-like protein 6A (encoded by the ACTL6A gene; also known as ArpNbeta, 53 kDa BRG1-associated factor A/BRG1-associated factor 53A/BAF35A, and INO80 complex subunit K/INO80K) and actin-like protein 6B (encoded by the ACTL6B gene; also known as ArpNalpha, 53 kDa BRG1-associated factor B/BRG1-associated factor 53B/BAF35B). ACTL6A and ACTL6B are involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). They are components of numerous complexes with chromatin remodeling and histone acetyltransferase activity. ACTL6A is also a putative core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. Schizosaccharomyces pombe actin-related protein 42 (Arp42) is also included in this family. It is also a component of SWI/SNF and RSC complexes.


Pssm-ID: 466846 [Multi-domain]  Cd Length: 413  Bit Score: 206.65  E-value: 9.48e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102   1 SYELPDGQVITIGNERFRAPEALFQPSFL---------GMESSGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGI 71
Cdd:cd13395   274 SYELPDGYNIEFGAERFKIPELLFDPSLVkgipappseGNELLGLPQLVYTSIGSCDVDIRPELYGNVVLTGGNSLLPGF 353

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2321196102  72 ADRMQKEITALAPSTMKIKIIAPP---ERKYSVWIGGSILASLSTFQQMWISKQE 123
Cdd:cd13395   354 TDRLNRELSEKAPGSLKLKILASGntvERRFSSWIGGSILASLGSFQQMWISKQE 408
PTZ00466 PTZ00466
actin-like protein; Provisional
 2-123 4.75e-57

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 180.91  E-value: 4.75e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102   2 YELPDGQVITIGNERFRAPEALFQPSFLGMESSGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITA 81
Cdd:PTZ00466  245 YILPDGSQILIGSERYRAPEVLFNPSILGLEYLGLSELIVTSITRADMDLRRTLYSHIVLSGGTTMFHGFGDRLLNEIRK 324

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2321196102  82 LAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQE 123
Cdd:PTZ00466  325 FAPKDITIRISAPPERKFSTFIGGSILASLATFKKIWISKQE 366
ASKHA_NBD_ACTL7 cd10214
nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ...
 2-123 1.06e-54

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: 174.53  E-value: 1.06e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102   2 YELPDGQVITIGNERFRAPEALFQPSFLGMESSGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITA 81
Cdd:cd10214   235 YELPDGHLITIGKERFRCPEMLFNPSLIGSKQPGLHTLTMNSLNKCDANLKKDLAKNILLCGGSTMFDGFPDRFQKELSK 314

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2321196102  82 LAPSTMKIkIIAPPERKYSVWIGGSILASLSTFQQMWISKQE 123
Cdd:cd10214   315 LCPNDNPI-VAASPERKYSVWTGGSILASLKSFQQLWVRRRE 355
ASKHA_NBD_Arp2 cd10220
nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, ...
 1-123 1.88e-54

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: 174.29  E-value: 1.88e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102   1 SYELPDGQVITIGNERFRAPEALFQPSFLGMESSGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEIT 80
Cdd:cd10220   236 SYTLPDGRVIKVGGERFEAPEALFQPHLIDVEGPGIAELLFNTIQAADIDTRPELYKHIVLSGGSTMYPGLPSRLEKEIK 315

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2321196102  81 AL-----------APSTMKIKIIAPPERKYSVWIGGSILASLSTFQ-QMWISKQE 123
Cdd:cd10220   316 QLylervlkgdteRLSKFKIRIEDPPRRKHMVFLGGAVLADIMKDKdEFWITRQE 370
ASKHA_NBD_actin-like cd10169
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ...
 34-123 6.49e-53

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: 166.90  E-value: 6.49e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102  34 SGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLST 113
Cdd:cd10169   164 CGLHELIYDSIMKCDIDLRKELYSNIVLSGGTTLFPGFAERLQKELSKLAPSSVKVKVIAPPERKYSAWIGGSILASLST 243

                          90
                  ....*....|
gi 2321196102 114 FQQMWISKQE 123
Cdd:cd10169   244 FQQMWITKEE 253
PTZ00452 PTZ00452
actin; Provisional
 2-123 3.92e-49

actin; Provisional


Pssm-ID: 185631  Cd Length: 375  Bit Score: 160.31  E-value: 3.92e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102   2 YELPDGQVITIGNERFRAPEALFQPSFLGMESSGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITA 81
Cdd:PTZ00452  240 YKLPDGNILTIKSQKFRCSEILFQPKLIGLEVAGIHHLAYSSIKKCDLDLRQELCRNIVLSGGTTLFPGIANRLSNELTN 319

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2321196102  82 LAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQE 123
Cdd:PTZ00452  320 LVPSQLKIQVAAPPDRRFSAWIGGSIQCTLSTQQPQWIKRQE 361
COG5277 COG5277
Actin-related protein [Cytoskeleton];
1-123 9.15e-42

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 142.24  E-value: 9.15e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102   1 SYELPDGQV-ITIGN---ERFRAPEALFQPSFLGMESS----------------------GIHETTFNSIMKCDVDIRKD 54
Cdd:COG5277   261 KVRLPNPTVeIELGNyawERFLIGEILFNPNHEGFESYiqqgrlriedavigdvvlygemGLAEAIINSIMKCDVEIQDE 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102  55 LYANTVLSGGTTMY---PGIAD-------RMQKEITALAPsTMKIKIIAPPERKYSVWIGGSILASLSTFQQMW--ISKQ 122
Cdd:COG5277   341 LYSNIILSGGAFNWsvpPGLEDvavdsvtRVQIELSELAP-ELKVNVRLVSDPQYSVWKGAIIYGYALPFSVKWswITKE 419


                  .
gi 2321196102 123 E 123
Cdd:COG5277   420 G 420
ASKHA_NBD_Arp6 cd10210
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ...
 5-123 4.36e-37

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: 129.21  E-value: 4.36e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102   5 PDGQVITIGNERFRAPEALFQPSFLGMESSGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAP 84
Cdd:cd10210   266 EDEQVLRLNNERFTVPELLFHPSDIGIQQAGIAEAIVQSINACPEELQPLLYANIVLTGGNALFPGFRERLEAELRSLAP 345

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2321196102  85 STMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQE 123
Cdd:cd10210   346 DDYDVNVTLPEDPITYAWEGGSLLAQSPEFEELAVTRAE 384
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
 1-123 7.00e-32

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: 114.79  E-value: 7.00e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102   1 SYELPDGQVITIGNERFRAPEALFQPSFLGMESSGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEIT 80
Cdd:cd10209   216 TYTLPDGRVISVGKERYCVGEALFRPSILGIEEYGIVEQLVRAVSTSPSENRRQLLENIVLCGGTSSVPGLEARLQKEIR 295

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2321196102  81 ALAPSTMKIKIIAPPE------RKYSVWIGGSILASLSTFQQMWISKQE 123
Cdd:cd10209   296 LLSSPSSRPALVKPPEympentLRYSAWIGGAILAKVVFPQNQHVTKAD 344
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
 10-123 1.53e-27

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 104.43  E-value: 1.53e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102  10 ITIGNERFRAPEALFQPSFLGME-SSGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITA------- 81
Cdd:PTZ00280  266 VDVGYERFLGPEMFFHPEIFSSEwTTPLPEVVDDAIQSCPIDCRRPLYKNIVLSGGSTMFKGFDKRLQRDVRKrvdrrlk 345

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2321196102  82 ---------LAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQE 123
Cdd:PTZ00280  346 kaeelsggkLKPIPIDVNVVSHPRQRYAVWYGGSMLASSPEFEKVCHTKAE 396
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
 65-123 9.43e-25

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: 91.19  E-value: 9.43e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2321196102  65 TTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQE 123
Cdd:NF040575   61 RVNESGFYEKLKKSITEKAPKGALIGMTLDPKPESAAWRGAAMYAASEGFVEMAITKQE 119
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
 10-123 2.39e-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: 95.33  E-value: 2.39e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102  10 ITIGNERFRAPEALFQPSFLGME-SSGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITA------- 81
Cdd:cd10221   263 VDVGYERFLAPEIFFNPEIASSDfTTPLPEVVDQVIQSCPIDTRRGLYKNIVLSGGSTMFKDFGRRLQRDVKRivdarlk 342

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2321196102  82 ---------LAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQE 123
Cdd:cd10221   343 aseelsggkLKPKPIDVNVISHPMQRYAVWFGGSMLASTPEFYTVCHTKAE 393
ASKHA_NBD_AtArp8-like cd13396
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and ...
 11-123 2.07e-21

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: 86.83  E-value: 2.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102  11 TIGNERFRAPEALFQPSFLGMESSGIHETTFNSIMKCDVDIR---KDLYANTVLSGGTTMYPGIADRMQKEITALAPSTM 87
Cdd:cd13396   209 TLSNERFKTGEILFQPGLGGMRAMGLHQAVALCMDHCALVHSqgdDGWFKTIVLSGGSACLPGLSERLERELRKLLPKSL 288

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2321196102  88 K--IKIIAPPERKYSVWIGGSILASLSTFQQMW-ISKQE 123
Cdd:cd13396   289 SegIRIIPPPLGPDSAWQGAKLISNLSNFPDGWcITKKQ 327
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
 3-123 1.02e-14

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: 68.49  E-value: 1.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102   3 ELPDGQVITIGNERFRAPEALFQPSFLGM----ESSGIHETTFNSimkCDVDIRKDLYANTVLSGGTTMYPGIADRMQKE 78
Cdd:cd10208   202 DLASGTEITVGKERFRACEPLFKPSSLRVdlliAAIAGALVLNAS---DEPDKRPALWENIIIVGGGSRIRGLKEALLSE 278

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2321196102  79 ITAL-----------APSTMKIKIIaP---PERK-----YSVWIGGSILASLsTF----QQMWISKQE 123
Cdd:cd10208   279 LQQFhlisetsaspqQPRIIRLAKI-PdyfPEWKksgyeEAAFLGASIVAKL-VFndpsSKHYISKVD 344
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
 35-123 7.92e-14

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: 66.06  E-value: 7.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102  35 GIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTF 114
Cdd:cd10211   245 GLVETIEFVLKRYPAEQQDRLVQNVFLTGGNALFPGLKERLEKELRAIRPFGSPFNVVRAKDPVLDAWRGAAKWALDSTF 324


                  ....*....
gi 2321196102 115 QQMWISKQE 123
Cdd:cd10211   325 EKVWITKQE 333
ASKHA_NBD_Arp10 cd10207
nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins; ...
 1-123 1.30e-13

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: 65.35  E-value: 1.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102   1 SYELPDGQVITIGNERFRAPEALFqpsFLGMES-SGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEI 79
Cdd:cd10207   231 DYPLDGEKILIVPGSIRESAEELL---FEGDNEeKSLPTLILDSLLKCPIDVRKQLAENIVVIGGTSMLPGFKHRLLEEL 307

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2321196102  80 TA----------LAPSTMKI---KIIAPPErkYSVWIGGSILASLSTFQQMWISKQE 123
Cdd:cd10207   308 RAllrkpkyfeeLAPKTFRFhtpPSVFKPN--YLAWLGGSIFGALESILGRSLSREA 362
ASKHA_NBD_Arp8-like cd10206
nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The ...
 35-123 9.86e-13

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: 63.03  E-value: 9.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102  35 GIHETTFNSIMKC-DVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMK----IKIIAPPERK---YSVWIGGS 106
Cdd:cd10206   339 PLDEAIVQSILSCaSDELKRKMYSSILLVGGGAKIPGLAEALEDRLLIKIPSLFEavetVEVLPPPKDMdpsLLAWKGGA 418

                          90
                  ....*....|....*..
gi 2321196102 107 ILASLSTFQQMWISKQE 123
Cdd:cd10206   419 VLACLDSAQELWITRKE 435
ASKHA_NBD_ScArp7-like cd10212
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and ...
 15-123 3.57e-04

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: 38.55  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102  15 ERFRAPEALFQPSFLGMESS---GIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAP----STM 87
Cdd:cd10212   303 ECYQFAEYLFKPQLISDKFSpedGLGPLMAKSVKKAPEQVYSLLLTNVIITGSTSLIEGMEQRIIKELSIRFPqyklTTF 382

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2321196102  88 KIKIIAppERKYSVWIGGSILASLSTFQ-QMWISKQE 123
Cdd:cd10212   383 ANQVMM--DRKIQGWLGALTMANLPSWSlGKWYSKED 417
ASKHA_ATPase-like cd00012
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
 6-104 3.86e-03

ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.


Pssm-ID: 466786 [Multi-domain]  Cd Length: 135  Bit Score: 34.75  E-value: 3.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321196102   6 DGQVITIGNERFRAPEALFQPSFLGMESSGIHETTfnSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEItalaPS 85
Cdd:cd00012    41 QTNAATFALFTGPPVRIVNEAVAAAIGALLTLGPE--GLLVVDLGGGTDISANVVLVGGGARNNGLAKRLKELL----LF 114

                          90
                  ....*....|....*....
gi 2321196102  86 TMKIKIIAPPERKYSVWIG 104
Cdd:cd00012   115 RGGLKVVKAVDPDEAVALG 133
 
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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