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Conserved domains on  [gi|385861543|dbj|BAM14373|]
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actin, partial [Joenoides intermedia]

Protein Classification

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 ...
1-284 0e+00

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: 615.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543   1 HHTFYNELRVDPAEHPVLLTEAPMNPKANREKMIQLMFETFNVPSFYVGIQAVLSLYSSGRTTGIVFDAGDGVSHTVPIY 80
Cdd:cd10224   82 HHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIY 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  81 EGYSLPHAIMRLNLAGRDLTAWLQKILNERGYTFTTSAEREIVRDIKEKLAYVALDFDAEMQKAATTTDCNVSYTLPDGN 160
Cdd:cd10224  162 EGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDGQ 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 161 EIVIANERFRCPELLFKPAFNGFEFDGIDQTLFDSIMKCDIDVRKDLYANIVLSGGSTMFQGLPERIEKEITRLAPPTMK 240
Cdd:cd10224  242 VITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTMK 321
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 385861543 241 IKVVAPPERKYAVWIGGSILASLATFPQMVITHEEYNDAGPGIV 284
Cdd:cd10224  322 IKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIV 365
 
Name Accession Description Interval E-value
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
1-284 0e+00

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


Pssm-ID: 466823  Cd Length: 365  Bit Score: 615.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543   1 HHTFYNELRVDPAEHPVLLTEAPMNPKANREKMIQLMFETFNVPSFYVGIQAVLSLYSSGRTTGIVFDAGDGVSHTVPIY 80
Cdd:cd10224   82 HHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIY 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  81 EGYSLPHAIMRLNLAGRDLTAWLQKILNERGYTFTTSAEREIVRDIKEKLAYVALDFDAEMQKAATTTDCNVSYTLPDGN 160
Cdd:cd10224  162 EGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDGQ 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 161 EIVIANERFRCPELLFKPAFNGFEFDGIDQTLFDSIMKCDIDVRKDLYANIVLSGGSTMFQGLPERIEKEITRLAPPTMK 240
Cdd:cd10224  242 VITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTMK 321
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 385861543 241 IKVVAPPERKYAVWIGGSILASLATFPQMVITHEEYNDAGPGIV 284
Cdd:cd10224  322 IKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIV 365
PTZ00004 PTZ00004
actin-2; Provisional
1-289 1.58e-179

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 499.68  E-value: 1.58e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543   1 HHTFYNELRVDPAEHPVLLTEAPMNPKANREKMIQLMFETFNVPSFYVGIQAVLSLYSSGRTTGIVFDAGDGVSHTVPIY 80
Cdd:PTZ00004  88 HHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETHNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIY 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  81 EGYSLPHAIMRLNLAGRDLTAWLQKILNERGYTFTTSAEREIVRDIKEKLAYVALDFDAEMQKAATTTDCN-VSYTLPDG 159
Cdd:PTZ00004 168 EGYSLPHAIHRLDVAGRDLTEYMMKILHERGTTFTTTAEKEIVRDIKEKLCYIALDFDEEMGNSAGSSDKYeESYELPDG 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 160 NEIVIANERFRCPELLFKPAFNGFEF-DGIDQTLFDSIMKCDIDVRKDLYANIVLSGGSTMFQGLPERIEKEITRLAPPT 238
Cdd:PTZ00004 248 TIITVGSERFRCPEALFQPSLIGKEEpPGIHELTFQSINKCDIDIRKDLYGNIVLSGGTTMYRGLPERLTKELTTLAPST 327
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 385861543 239 MKIKVVAPPERKYAVWIGGSILASLATFPQMVITHEEYNDAGPGIVHRKCF 289
Cdd:PTZ00004 328 MKIKVVAPPERKYSVWIGGSILSSLPTFQQMWVTKEEYDESGPSIVHRKCF 378
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
1-289 1.22e-164

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 461.73  E-value: 1.22e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543     1 HHTFYNELRVDPAEHPVLLTEAPMNPKANREKMIQLMFETFNVPSFYVGIQAVLSLYSSGRTTGIVFDAGDGVSHTVPIY 80
Cdd:smart00268  82 DYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVPVV 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543    81 EGYSLPHAIMRLNLAGRDLTAWLQKILNERGYTFTTSAEREIVRDIKEKLAYVALDFDAEMQKAAT---TTDCNVSYTLP 157
Cdd:smart00268 162 DGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLAREsseSSKLEKTYELP 241
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543   158 DGNEIVIANERFRCPELLFKPAFNGFEFDGIDQTLFDSIMKCDIDVRKDLYANIVLSGGSTMFQGLPERIEKEITRLAPP 237
Cdd:smart00268 242 DGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELKQLAPK 321
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 385861543   238 TMKIKVVAPPERKYAVWIGGSILASLATFPQMVITHEEYNDAGPGIVHRKCF 289
Cdd:smart00268 322 KLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERKCF 373
Actin pfam00022
Actin;
1-289 1.15e-135

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 389.36  E-value: 1.15e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543    1 HHTFYNELRVDPAEHPVLLTEAPMNPKANREKMIQLMFETFNVPSFYVGIQAVLSLYSSGRTTGIVFDAGDGVSHTVPIY 80
Cdd:pfam00022  80 EHVLKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVPVH 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543   81 EGYSLPHAIMRLNLAGRDLTAWLQKILNER------------------------------GYTFTTSAEREIVRDIKEKL 130
Cdd:pfam00022 160 DGYVLQKAIRRSDLGGDFLTDYLRELLRSRnieitprylikskkpgdpapavtkrelpdtTYSYKTYQERRVLEEIKESV 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  131 AYVALDFdaEMQKAATTTDCNVSYTLPDGNEIVIANERFRCPELLFKPAFNGFE--------FDGIDQTLFDSIMKCDID 202
Cdd:pfam00022 240 CYVSDDP--FGDETTSSSIPTRVYELPDGSTIILGAERFRVPEILFNPSLIGSEselpppqtAVGIPELIVDAINACDVD 317
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  203 VRKDLYANIVLSGGSTMFQGLPERIEKEITRLAPPTMKIKVVAPP---ERKYAVWIGGSILASLATFPQMVITHEEYNDA 279
Cdd:pfam00022 318 LRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVKIIAPGntvERRYSAWIGGSILASLGTFQQMWVSKQEYEEH 397
                         330
                  ....*....|
gi 385861543  280 GPGIVHRKCF 289
Cdd:pfam00022 398 GASVVERKCK 407
COG5277 COG5277
Actin-related protein [Cytoskeleton];
2-276 7.26e-90

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 273.59  E-value: 7.26e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543   2 HTFYNELRVDPAEHP--VLLTEAPMNPKANREKMIQLMFETF---NVPSFYVGIQAVLSLYSSGRTTGIVFDAGDGVSHT 76
Cdd:COG5277  106 YTFAQFLVVDPEFHGflVVVALSALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPLAVAIAEKAVTCVVVEAGHGNSQV 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  77 VPIYEGySLPHAIMRLNLAGRDLTAWLQKILNERGYTFTTSAEReIVRDIKEKLAYVALDFDAEMQKAATTTD-CNVSYT 155
Cdd:COG5277  186 APISRG-PIREGLVALNRGGAEANAITREILKDRGYSDTAREEY-VVRVVKEALGLVPRDLAKAIQKAASNPDsFEAKVR 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 156 LPDGN-EIVIAN---ERFRCPELLFKPAFNGFEFD----------------------GIDQTLFDSIMKCDIDVRKDLYA 209
Cdd:COG5277  264 LPNPTvEIELGNyawERFLIGEILFNPNHEGFESYiqqgrlriedavigdvvlygemGLAEAIINSIMKCDVEIQDELYS 343
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 385861543 210 NIVLSGGSTMF---QGL-------PERIEKEITRLApPTMKIKVVAPPERKYAVWIGGSILASLATFPQM--VITHEEY 276
Cdd:COG5277  344 NIILSGGAFNWsvpPGLedvavdsVTRVQIELSELA-PELKVNVRLVSDPQYSVWKGAIIYGYALPFSVKwsWITKEGW 421
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
218-288 2.93e-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: 97.74  E-value: 2.93e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 385861543 218 TMFQGLPERIEKEITRLAPPTMKIKVVAPPERKYAVWIGGSILASLATFPQMVITHEEYNDAGPGIVHRKC 288
Cdd:NF040575  62 VNESGFYEKLKKSITEKAPKGALIGMTLDPKPESAAWRGAAMYAASEGFVEMAITKQEYDESGPSIVHRKC 132
 
Name Accession Description Interval E-value
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
1-284 0e+00

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


Pssm-ID: 466823  Cd Length: 365  Bit Score: 615.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543   1 HHTFYNELRVDPAEHPVLLTEAPMNPKANREKMIQLMFETFNVPSFYVGIQAVLSLYSSGRTTGIVFDAGDGVSHTVPIY 80
Cdd:cd10224   82 HHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIY 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  81 EGYSLPHAIMRLNLAGRDLTAWLQKILNERGYTFTTSAEREIVRDIKEKLAYVALDFDAEMQKAATTTDCNVSYTLPDGN 160
Cdd:cd10224  162 EGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDGQ 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 161 EIVIANERFRCPELLFKPAFNGFEFDGIDQTLFDSIMKCDIDVRKDLYANIVLSGGSTMFQGLPERIEKEITRLAPPTMK 240
Cdd:cd10224  242 VITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTMK 321
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 385861543 241 IKVVAPPERKYAVWIGGSILASLATFPQMVITHEEYNDAGPGIV 284
Cdd:cd10224  322 IKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIV 365
ASKHA_NBD_actin_Arp-T1-3 cd13397
nucleotide-binding domain (NBD) of actin, actin-related proteins T1-T3 (Arp-T1-3), and similar ...
1-280 0e+00

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


Pssm-ID: 466848 [Multi-domain]  Cd Length: 359  Bit Score: 536.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543   1 HHTFYNELRVDPAEHPVLLTEAPMNPKANREKMIQLMFETFNVPSFYVGIQAVLSLYSSGRTTGIVFDAGDGVSHTVPIY 80
Cdd:cd13397   82 HHTFENELRVKPEEHPVLLTEAPLNPKQNREKMAEIMFETFGVPAFYVAIQAVLSLYSSGRTTGLVLDSGDGVTHTVPIY 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  81 EGYSLPHAIMRLNLAGRDLTAWLQKILNERGYTFTTSAEREIVRDIKEKLAYVALDFDAEMQKaaTTTDCNVSYTLPDGN 160
Cdd:cd13397  162 EGYALPHAVQRLDLAGRDLTEYLMKLLKERGHSFTTTAEREIVRDIKEKLCYVALDYEEELKK--KSEELEKEYTLPDGQ 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 161 EIVIANERFRCPELLFKPAFNGFEFDGIDQTLFDSIMKCDIDVRKDLYANIVLSGGSTMFQGLPERIEKEITRLAPPTMK 240
Cdd:cd13397  240 VIKIGSERFRCPEALFRPSLIGREAPGIHKLVYNSIMKCDIDIRKDLYSNIVLSGGSTMFPGLPERLQKELEALAPSSTK 319
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 385861543 241 IKVVAPPERKYAVWIGGSILASLATFPQMVITHEEYNDAG 280
Cdd:cd13397  320 VKVIAPPERKYSVWIGGSILASLSTFKSMWITRAEYDEFG 359
PTZ00004 PTZ00004
actin-2; Provisional
1-289 1.58e-179

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 499.68  E-value: 1.58e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543   1 HHTFYNELRVDPAEHPVLLTEAPMNPKANREKMIQLMFETFNVPSFYVGIQAVLSLYSSGRTTGIVFDAGDGVSHTVPIY 80
Cdd:PTZ00004  88 HHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETHNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIY 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  81 EGYSLPHAIMRLNLAGRDLTAWLQKILNERGYTFTTSAEREIVRDIKEKLAYVALDFDAEMQKAATTTDCN-VSYTLPDG 159
Cdd:PTZ00004 168 EGYSLPHAIHRLDVAGRDLTEYMMKILHERGTTFTTTAEKEIVRDIKEKLCYIALDFDEEMGNSAGSSDKYeESYELPDG 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 160 NEIVIANERFRCPELLFKPAFNGFEF-DGIDQTLFDSIMKCDIDVRKDLYANIVLSGGSTMFQGLPERIEKEITRLAPPT 238
Cdd:PTZ00004 248 TIITVGSERFRCPEALFQPSLIGKEEpPGIHELTFQSINKCDIDIRKDLYGNIVLSGGTTMYRGLPERLTKELTTLAPST 327
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 385861543 239 MKIKVVAPPERKYAVWIGGSILASLATFPQMVITHEEYNDAGPGIVHRKCF 289
Cdd:PTZ00004 328 MKIKVVAPPERKYSVWIGGSILSSLPTFQQMWVTKEEYDESGPSIVHRKCF 378
PTZ00281 PTZ00281
actin; Provisional
1-289 2.16e-172

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 481.51  E-value: 2.16e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543   1 HHTFYNELRVDPAEHPVLLTEAPMNPKANREKMIQLMFETFNVPSFYVGIQAVLSLYSSGRTTGIVFDAGDGVSHTVPIY 80
Cdd:PTZ00281  88 HHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVSHTVPIY 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  81 EGYSLPHAIMRLNLAGRDLTAWLQKILNERGYTFTTSAEREIVRDIKEKLAYVALDFDAEMQKAATTTDCNVSYTLPDGN 160
Cdd:PTZ00281 168 EGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEMQTAASSSALEKSYELPDGQ 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 161 EIVIANERFRCPELLFKPAFNGFEFDGIDQTLFDSIMKCDIDVRKDLYANIVLSGGSTMFQGLPERIEKEITRLAPPTMK 240
Cdd:PTZ00281 248 VITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELTALAPSTMK 327
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 385861543 241 IKVVAPPERKYAVWIGGSILASLATFPQMVITHEEYNDAGPGIVHRKCF 289
Cdd:PTZ00281 328 IKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIVHRKCF 376
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
1-289 1.22e-164

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 461.73  E-value: 1.22e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543     1 HHTFYNELRVDPAEHPVLLTEAPMNPKANREKMIQLMFETFNVPSFYVGIQAVLSLYSSGRTTGIVFDAGDGVSHTVPIY 80
Cdd:smart00268  82 DYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVPVV 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543    81 EGYSLPHAIMRLNLAGRDLTAWLQKILNERGYTFTTSAEREIVRDIKEKLAYVALDFDAEMQKAAT---TTDCNVSYTLP 157
Cdd:smart00268 162 DGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLAREsseSSKLEKTYELP 241
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543   158 DGNEIVIANERFRCPELLFKPAFNGFEFDGIDQTLFDSIMKCDIDVRKDLYANIVLSGGSTMFQGLPERIEKEITRLAPP 237
Cdd:smart00268 242 DGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELKQLAPK 321
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 385861543   238 TMKIKVVAPPERKYAVWIGGSILASLATFPQMVITHEEYNDAGPGIVHRKCF 289
Cdd:smart00268 322 KLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERKCF 373
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
1-288 6.39e-161

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: 452.00  E-value: 6.39e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543   1 HHTFYNE-LRVDPAEHPVLLTEAPMNPKANREKMIQLMFETFNVPSFYVGIQAVLSLYSSGRTTGIVFDAGDGVSHTVPI 79
Cdd:cd10216   83 QYVYSKLqLNTFSEEHPVLLTEAPLNPRKNREKAAEVFFETFNVPALFVSMQAVLSLYASGRTTGVVLDSGDGVTHAVPI 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  80 YEGYSLPHAIMRLNLAGRDLTAWLQKILNERGYTFTTSAEREIVRDIKEKLAYVALDFDAEMQKAATTTDcNVSYTLPDG 159
Cdd:cd10216  163 YEGFALPHSIRRVDIAGRDVTEYLQLLLRKSGYNFHTSAEFEIVREIKEKACYVALNPQKEEKLEEEKTE-KAQYTLPDG 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 160 NEIVIANERFRCPELLFKPAFNGFEFDGIDQTLFDSIMKCDIDVRKDLYANIVLSGGSTMFQGLPERIEKEITRLAPPTM 239
Cdd:cd10216  242 STIEIGPERFRAPEILFNPELIGLEYPGVHEVLVDSIQKSDLDLRKTLYSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDV 321
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 385861543 240 KIKVVAPPERKYAVWIGGSILASLATFPQMVITHEEYNDAGPGIVHRKC 288
Cdd:cd10216  322 KIRISAPPERLYSTWIGGSILASLSTFKKMWVSKKEYEEDGARILHRKT 370
Actin pfam00022
Actin;
1-289 1.15e-135

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 389.36  E-value: 1.15e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543    1 HHTFYNELRVDPAEHPVLLTEAPMNPKANREKMIQLMFETFNVPSFYVGIQAVLSLYSSGRTTGIVFDAGDGVSHTVPIY 80
Cdd:pfam00022  80 EHVLKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVPVH 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543   81 EGYSLPHAIMRLNLAGRDLTAWLQKILNER------------------------------GYTFTTSAEREIVRDIKEKL 130
Cdd:pfam00022 160 DGYVLQKAIRRSDLGGDFLTDYLRELLRSRnieitprylikskkpgdpapavtkrelpdtTYSYKTYQERRVLEEIKESV 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  131 AYVALDFdaEMQKAATTTDCNVSYTLPDGNEIVIANERFRCPELLFKPAFNGFE--------FDGIDQTLFDSIMKCDID 202
Cdd:pfam00022 240 CYVSDDP--FGDETTSSSIPTRVYELPDGSTIILGAERFRVPEILFNPSLIGSEselpppqtAVGIPELIVDAINACDVD 317
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  203 VRKDLYANIVLSGGSTMFQGLPERIEKEITRLAPPTMKIKVVAPP---ERKYAVWIGGSILASLATFPQMVITHEEYNDA 279
Cdd:pfam00022 318 LRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVKIIAPGntvERRYSAWIGGSILASLGTFQQMWVSKQEYEEH 397
                         330
                  ....*....|
gi 385861543  280 GPGIVHRKCF 289
Cdd:pfam00022 398 GASVVERKCK 407
ASKHA_NBD_actin-like cd10169
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ...
1-280 1.10e-133

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: 378.76  E-value: 1.10e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543   1 HHTFYNELRVDPAEHPVLLTEAPMNPKANREKMIQLMFETFNVPSFYVGIQAVLSLYSSGRTTGIVFDAGDGVSHTVPIY 80
Cdd:cd10169   34 EHVFYNLLRVDPEEHPVLLTEPPLNPKANREKLAEILFETFNVPSLYIANQAVLSLYASGRTTGLVVDSGEGVTHIVPVY 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  81 EGYSLPHAIMRLNLAGRDLTAWLQKILNERGYTFTTSAEREIVRDIKEKLAyvaldfdaemqkaatttdcnvsytlpdgn 160
Cdd:cd10169  114 EGYVLPHAVRRLDIGGRDLTDYLAKLLREKGYSFSTSAEREIVRDIKEKLC----------------------------- 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 161 eivianerfrcpellfkpafngfefdGIDQTLFDSIMKCDIDVRKDLYANIVLSGGSTMFQGLPERIEKEITRLAPPTMK 240
Cdd:cd10169  165 --------------------------GLHELIYDSIMKCDIDLRKELYSNIVLSGGTTLFPGFAERLQKELSKLAPSSVK 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 385861543 241 IKVVAPPERKYAVWIGGSILASLATFPQMVITHEEYNDAG 280
Cdd:cd10169  219 VKVIAPPERKYSAWIGGSILASLSTFQQMWITKEEYEEHG 258
ASKHA_NBD_Arp2 cd10220
nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, ...
2-281 2.07e-131

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: 377.67  E-value: 2.07e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543   2 HTFYNELRVDPAEHPVLLTEAPMNPKANREKMIQLMFETFNVPSFYVGIQAVLSLYSSGRTTGIVFDAGDGVSHTVPIYE 81
Cdd:cd10220   85 YTFGEKLKIDPRECKILLTEPPMNPTKNREKMVEVMFEKYGFAGVYVAIQAVLTLYAQGLLTGVVVDSGDGVTHIVPVYE 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  82 GYSLPHAIMRLNLAGRDLTAWLQKILNERGYTFTTSAEREIVRDIKEKLAYVALDFDAEMQKAATTTDCNVSYTLPDGNE 161
Cdd:cd10220  165 GFSLPHLTRRLDVAGRDITRYLIKLLLLRGYAFNRTADFETVREIKEKLCYVAYDIELEQKLALETTVLVESYTLPDGRV 244
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 162 IVIANERFRCPELLFKPAFNGFEFDGIDQTLFDSIMKCDIDVRKDLYANIVLSGGSTMFQGLPERIEKEITRL------- 234
Cdd:cd10220  245 IKVGGERFEAPEALFQPHLIDVEGPGIAELLFNTIQAADIDTRPELYKHIVLSGGSTMYPGLPSRLEKEIKQLylervlk 324
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 385861543 235 ----APPTMKIKVVAPPERKYAVWIGGSILASL-ATFPQMVITHEEYNDAGP 281
Cdd:cd10220  325 gdteRLSKFKIRIEDPPRRKHMVFLGGAVLADImKDKDEFWITRQEYEEQGV 376
PTZ00466 PTZ00466
actin-like protein; Provisional
5-289 3.79e-125

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 361.95  E-value: 3.79e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543   5 YNELRVDPAEHPVLLTEAPMNPKANREKMIQLMFETFNVPSFYVGIQAVLSLYSSGRTTGIVFDAGDGVSHTVPIYEGYS 84
Cdd:PTZ00466  97 YNSMKINSEEHPVLLTEAPLNPQKNKEKIAEVFFETFNVPALFISIQAILSLYSCGKTNGTVLDCGDGVCHCVSIYEGYS 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  85 LPHAIMRLNLAGRDLTAWLQKILNERGYTFTTSAEREIVRDIKEKLAYVALDF---DAEMQKAATTtdcnVSYTLPDGNE 161
Cdd:PTZ00466 177 ITNTITRTDVAGRDITTYLGYLLRKNGHLFNTSAEMEVVKNMKENCCYVSFNMnkeKNSSEKALTT----LPYILPDGSQ 252
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 162 IVIANERFRCPELLFKPAFNGFEFDGIDQTLFDSIMKCDIDVRKDLYANIVLSGGSTMFQGLPERIEKEITRLAPPTMKI 241
Cdd:PTZ00466 253 ILIGSERYRAPEVLFNPSILGLEYLGLSELIVTSITRADMDLRRTLYSHIVLSGGTTMFHGFGDRLLNEIRKFAPKDITI 332
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 385861543 242 KVVAPPERKYAVWIGGSILASLATFPQMVITHEEYNDAGPGIVHRKCF 289
Cdd:PTZ00466 333 RISAPPERKFSTFIGGSILASLATFKKIWISKQEFDEYGSVILHRKTF 380
ASKHA_NBD_ACTL7 cd10214
nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ...
2-288 8.69e-122

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: 352.88  E-value: 8.69e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543   2 HTFYNELRVDPAEHPVLLTEAPMNPKANREKMIQLMFETFNVPSFYVGIQAVLSLYSSGRTTGIVFDAGDGVSHTVPIYE 81
Cdd:cd10214   86 YIFEKEMKILPEEHAVLVSDPPLSPTTNREKYAELMFETFSIPAMHIAYQSRLSLYSYGRTSGLVVESGHGVSYVVPIHE 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  82 GYSLPHAIMRLNLAGRDLTAWLQKILNERGYTFTTSaEREIVRDIKEKLAYVALDFDAEMqkAATTTDCNVSYTLPDGNE 161
Cdd:cd10214  166 GYNLPHITGRADYAGSDLTAYLMKLLNEAGNKFTDD-QLHIVEDIKKKCCYVALDFEEEM--GLPPQEYTVDYELPDGHL 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 162 IVIANERFRCPELLFKPAFNGFEFDGIDQTLFDSIMKCDIDVRKDLYANIVLSGGSTMFQGLPERIEKEITRLApPTMKI 241
Cdd:cd10214  243 ITIGKERFRCPEMLFNPSLIGSKQPGLHTLTMNSLNKCDANLKKDLAKNILLCGGSTMFDGFPDRFQKELSKLC-PNDNP 321
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 385861543 242 KVVAPPERKYAVWIGGSILASLATFPQMVITHEEYNDAGPGIVHRKC 288
Cdd:cd10214  322 IVAASPERKYSVWTGGSILASLKSFQQLWVRRREYEERGPFVIYRKC 368
PTZ00452 PTZ00452
actin; Provisional
1-289 2.01e-113

actin; Provisional


Pssm-ID: 185631  Cd Length: 375  Bit Score: 332.10  E-value: 2.01e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543   1 HHTFYNELRVDPAEHPVLLTEAPMNPKANREKMIQLMFETFNVPSFYVGIQAVLSLYSSGRTTGIVFDAGDGVSHTVPIY 80
Cdd:PTZ00452  87 HHAFYNELCMSPEDQPVFMTDAPMNSKFNRERMTQIMFETFNTPCLYISNEAVLSLYTSGKTIGLVVDSGEGVTHCVPVF 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  81 EGYSLPHAIMRLNLAGRDLTAWLQKILNERGYTFTTSAEREIVRDIKEKLAYVALDFDAEMQKAATTTDCNVSYTLPDGN 160
Cdd:PTZ00452 167 EGHQIPQAITKINLAGRLCTDYLTQILQELGYSLTEPHQRIIVKNIKERLCYTALDPQDEKRIYKESNSQDSPYKLPDGN 246
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 161 EIVIANERFRCPELLFKPAFNGFEFDGIDQTLFDSIMKCDIDVRKDLYANIVLSGGSTMFQGLPERIEKEITRLAPPTMK 240
Cdd:PTZ00452 247 ILTIKSQKFRCSEILFQPKLIGLEVAGIHHLAYSSIKKCDLDLRQELCRNIVLSGGTTLFPGIANRLSNELTNLVPSQLK 326
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 385861543 241 IKVVAPPERKYAVWIGGSILASLATFPQMVITHEEYNDAGPGIVHRKCF 289
Cdd:PTZ00452 327 IQVAAPPDRRFSAWIGGSIQCTLSTQQPQWIKRQEYDEQGPSIVHRKCF 375
ASKHA_NBD_Arp4_ACTL6-like cd13395
nucleotide-binding domain (NBD) of the actin-related protein 4 (Arp4)-like subfamily; The ...
1-280 5.52e-108

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: 319.13  E-value: 5.52e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543   1 HHTFYNELRVDPAEHPVLLTEAPMNPKANREKMIQLMFETFNVPSFYVGIQAVLSLYSSGRTTGIVFDAGDGVSHTVPIY 80
Cdd:cd13395   93 DHALKNRLRVDPSEHPLLLTEPSWNTRANREKLTELMFEKYNVPAFFLAKNAVLSAFANGRSTALVVDSGATSTSVVPVH 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  81 EGYSLPHAIMRLNLAGRDLTAWLQKILNERGYTF----------------------------TTS----AEREIVRDIKE 128
Cdd:cd13395  173 DGYVLQKAIVRSPLGGDFLTDQLLKLLESKNIEIiprymikskepveggapakytkkdlpntTSSyhryMVRRVLQDFKE 252
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 129 KLAYVALDFDAEmQKAATTTDcnVSYTLPDGNEIVIANERFRCPELLFKPAF---------NGFEFDGIDQTLFDSIMKC 199
Cdd:cd13395  253 SVCQVSDSPFDE-SEAASIPT--VSYELPDGYNIEFGAERFKIPELLFDPSLvkgipappsEGNELLGLPQLVYTSIGSC 329
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 200 DIDVRKDLYANIVLSGGSTMFQGLPERIEKEITRLAPPTMKIKVVAPP---ERKYAVWIGGSILASLATFPQMVITHEEY 276
Cdd:cd13395  330 DVDIRPELYGNVVLTGGNSLLPGFTDRLNRELSEKAPGSLKLKILASGntvERRFSSWIGGSILASLGSFQQMWISKQEY 409

                 ....
gi 385861543 277 NDAG 280
Cdd:cd13395  410 EEHG 413
COG5277 COG5277
Actin-related protein [Cytoskeleton];
2-276 7.26e-90

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 273.59  E-value: 7.26e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543   2 HTFYNELRVDPAEHP--VLLTEAPMNPKANREKMIQLMFETF---NVPSFYVGIQAVLSLYSSGRTTGIVFDAGDGVSHT 76
Cdd:COG5277  106 YTFAQFLVVDPEFHGflVVVALSALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPLAVAIAEKAVTCVVVEAGHGNSQV 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  77 VPIYEGySLPHAIMRLNLAGRDLTAWLQKILNERGYTFTTSAEReIVRDIKEKLAYVALDFDAEMQKAATTTD-CNVSYT 155
Cdd:COG5277  186 APISRG-PIREGLVALNRGGAEANAITREILKDRGYSDTAREEY-VVRVVKEALGLVPRDLAKAIQKAASNPDsFEAKVR 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 156 LPDGN-EIVIAN---ERFRCPELLFKPAFNGFEFD----------------------GIDQTLFDSIMKCDIDVRKDLYA 209
Cdd:COG5277  264 LPNPTvEIELGNyawERFLIGEILFNPNHEGFESYiqqgrlriedavigdvvlygemGLAEAIINSIMKCDVEIQDELYS 343
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 385861543 210 NIVLSGGSTMF---QGL-------PERIEKEITRLApPTMKIKVVAPPERKYAVWIGGSILASLATFPQM--VITHEEY 276
Cdd:COG5277  344 NIILSGGAFNWsvpPGLedvavdsVTRVQIELSELA-PELKVNVRLVSDPQYSVWKGAIIYGYALPFSVKwsWITKEGW 421
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
1-286 3.00e-85

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 261.20  E-value: 3.00e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543   1 HHTFYNELRVDPAEHPVLLTEAPMNPKANREKMIQLMFETFNVPSFYVGIQAVLSLYSS----------GRTTGIVFDAG 70
Cdd:PTZ00280  89 EQCIFKYLRCEPEEHYFILTEPPMNPPENREYTAEIMFETFNVKGLYIAVQAVLALRASwtskkakelgGTLTGTVIDSG 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  71 DGVSHTVPIYEGYSLPHAIMRLNLAGRDLTAWLQKILNERGYTFTTSAEREIVRDIKEKLAYVALDFDAEMQK------A 144
Cdd:PTZ00280 169 DGVTHVIPVVDGYVIGSSIKHIPLAGRDITNFIQQMLRERGEPIPAEDILLLAQRIKEKYCYVAPDIAKEFEKydsdpkN 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 145 ATTTDCNVSYTLPDGNEIVIANERFRCPELLFKPAFNGFEFD-GIDQTLFDSIMKCDIDVRKDLYANIVLSGGSTMFQGL 223
Cdd:PTZ00280 249 HFKKYTAVNSVTKKPYTVDVGYERFLGPEMFFHPEIFSSEWTtPLPEVVDDAIQSCPIDCRRPLYKNIVLSGGSTMFKGF 328
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 385861543 224 PERIEKEITR----------------LAPPTMKIKVVAPPERKYAVWIGGSILASLATFPQMVITHEEYNDAGPGIVHR 286
Cdd:PTZ00280 329 DKRLQRDVRKrvdrrlkkaeelsggkLKPIPIDVNVVSHPRQRYAVWYGGSMLASSPEFEKVCHTKAEYDEYGPSICRY 407
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
1-284 2.87e-84

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: 258.27  E-value: 2.87e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543   1 HHTFYNELRVDPAEHPVLLTEAPMNPKANREKMIQLMFETFNVPSFYVGIQAVLSLYSSGRT--------TGIVFDAGDG 72
Cdd:cd10221   88 EQCIFKYLRCEPEDHYFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQAVLALAASWTSrkvgertlTGTVIDSGDG 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  73 VSHTVPIYEGYSLPHAIMRLNLAGRDLTAWLQKILNERGYTFTTSAEREIVRDIKEKLAYVALDFDAEMQKAAT------ 146
Cdd:cd10221  168 VTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREEGIPPEDSLEVAKRIKERYCYVCPDIVKEFAKYDSdpakyi 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 147 ------------TTDCNVSYtlpdgneivianERFRCPELLFKPAFNGFEF-DGIDQTLFDSIMKCDIDVRKDLYANIVL 213
Cdd:cd10221  248 kqytginsvtgkPYTVDVGY------------ERFLAPEIFFNPEIASSDFtTPLPEVVDQVIQSCPIDTRRGLYKNIVL 315
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 214 SGGSTMFQGLPERIEKEITR----------------LAPPTMKIKVVAPPERKYAVWIGGSILASLATFPQMVITHEEYN 277
Cdd:cd10221  316 SGGSTMFKDFGRRLQRDVKRivdarlkaseelsggkLKPKPIDVNVISHPMQRYAVWFGGSMLASTPEFYTVCHTKAEYE 395

                 ....*..
gi 385861543 278 DAGPGIV 284
Cdd:cd10221  396 EYGPSIC 402
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
2-285 9.04e-71

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: 222.26  E-value: 9.04e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543   2 HTFYNELRVDPA-EHPVLLTEAPMNPKANREKMIQLMFETFNVPSFYVGIQAVLSLYSSGRTTGIVFDAGDGVSHTVPIY 80
Cdd:cd10209   68 YVFYTGLGWEEGnEGQVLIAEPLLTSKAERERLTQLMFETFNVSGLYASEQAVLSLYAVGRISGCVVDVGHGKIDIAPVW 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  81 EGYSLPHAIMRLNLAGRDLTAWLQKILNERGYtfTTSAEREIVRDIKEKLAYVALDFDAEMQKAATTTDcnVSYTLPDGN 160
Cdd:cd10209  148 EGAIQHNAVRRFEIGGRDLTELLAAELGKSNP--KVKLDRSIVERLKEAVAWSADDEEAYEKKVLTCSP--ETYTLPDGR 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 161 EIVIANERFRCPELLFKPAFNGFEFDGIDQTLFDSIMKCDIDVRKDLYANIVLSGGSTMFQGLPERIEKEITRLAPPTMK 240
Cdd:cd10209  224 VISVGKERYCVGEALFRPSILGIEEYGIVEQLVRAVSTSPSENRRQLLENIVLCGGTSSVPGLEARLQKEIRLLSSPSSR 303
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 385861543 241 IKVVAPPE------RKYAVWIGGSILASlATFPQ-MVITHEEYNDAGPGIVH 285
Cdd:cd10209  304 PALVKPPEympentLRYSAWIGGAILAK-VVFPQnQHVTKADYDETGPSVVH 354
ASKHA_NBD_Arp6 cd10210
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ...
2-280 2.40e-64

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: 206.63  E-value: 2.40e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543   2 HTFYNE-LRVDPAEHPVLLTEAPMNPKANREKMIQLMFETFNVPSFYVGIQAVLSLY----------SSGRTTGIVFDAG 70
Cdd:cd10210   76 HLFGKLlLNVDPSDTALVLTEPPFNPPSIQEAMDEIVFEEYGFQSLYRTTAAALSAFayladseqssSSSSQCCLVVDSG 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  71 DGVSHTVPIYEGYSLPHAIMRLNLAGRDLTAWLQKI-----LNERGYTFttsaereIVRDIKEKLAYVALDFDAEMQKAA 145
Cdd:cd10210  156 FSFTHIVPFFDGKPVKRAVRRIDVGGKLLTNYLKEIisyrqLNVMDETY-------LVNQIKEDLCFVSTDFYEDLEIAK 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 146 TTTDCN---VSYTLPDGN-----------------------EIVIANERFRCPELLFKPAFNGFEFDGIDQTLFDSIMKC 199
Cdd:cd10210  229 KKGKENtirRDYVLPDYTtskrgyvrdpeepnrgklkedeqVLRLNNERFTVPELLFHPSDIGIQQAGIAEAIVQSINAC 308
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 200 DIDVRKDLYANIVLSGGSTMFQGLPERIEKEITRLAPPTMKIKVVAPPERKYAVWIGGSILASLATFPQMVITHEEYNDA 279
Cdd:cd10210  309 PEELQPLLYANIVLTGGNALFPGFRERLEAELRSLAPDDYDVNVTLPEDPITYAWEGGSLLAQSPEFEELAVTRAEYEEH 388

                 .
gi 385861543 280 G 280
Cdd:cd10210  389 G 389
ASKHA_NBD_Arp10 cd10207
nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins; ...
1-280 1.21e-45

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: 157.80  E-value: 1.21e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543   1 HHTFYNELRVDPAEHPVLLTEAPMNPKANREKMIQLMFETFNVPS--FYVGiqAVLSLYSSGRTTGIVFDAGDGVSHTVP 78
Cdd:cd10207   59 HELYFKHLLVNPKDRRVVVVESVLCPTPFRETLAKVLFKHFEVPSvlFAPS--HLLSLLTLGIRTALVVDCGYRETRVLP 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  79 IYEGYSLPHAIMRLNLAGRDLTAWLQKILNERGYTFTTSAER------------EIVRDIKEKLAYVA-LDFDAEMQKAA 145
Cdd:cd10207  137 VYEGVPLLSAWQSTPLGGKALHKRLKKLLLEHATVVTGDNKGqllssvdsllseEVLEDIKVRACFVTsLERGKTLQSAT 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 146 TTTDCN-------VSYTLPDGNEIVIANERFRCPELLFkpafngFEFDGIDQTL----FDSIMKCDIDVRKDLYANIVLS 214
Cdd:cd10207  217 EEGSTEepsppppVDYPLDGEKILIVPGSIRESAEELL------FEGDNEEKSLptliLDSLLKCPIDVRKQLAENIVVI 290
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 385861543 215 GGSTMFQGLPERIEKEIT----------RLAPPTMKIKVVAPP-ERKYAVWIGGSILASLATFPQMVITHEEYNDAG 280
Cdd:cd10207  291 GGTSMLPGFKHRLLEELRallrkpkyfeELAPKTFRFHTPPSVfKPNYLAWLGGSIFGALESILGRSLSREAYLQTG 367
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
2-282 4.94e-43

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


Pssm-ID: 466817 [Multi-domain]  Cd Length: 345  Bit Score: 150.03  E-value: 4.94e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543   2 HTFY-----NELRVDpaeHPVLLTEAPMNPKANREKMIQLMFETFNVPSFYVGIQAVLSLY----SSGRTTGIVFDAGDG 72
Cdd:cd10211   79 YIFShlginSEGSVD---HPIVLTEALCNPNYSRQLMSELLFECYGVPSVAYGIDSLFSYYhnqpQGDPSDGLVISSGYS 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  73 VSHTVPIYEGYSLPHAIMRLNLAGRDLTAWLQKILNERGYTFTTSAEREIVRDIKEKLAYVALDFDAEMQKAATTTDCnv 152
Cdd:cd10211  156 TTHVIPVLNGRLDLSQCKRINLGGFHATDYLQRLLQLKYPTHPSAITLSRAEELVHEHCYVAEDYDEELKKWEDPEYY-- 233
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 153 sytlpDGNEIVIanerfrcpELLFkpafngfefdGIDQTLFDSIMKCDIDVRKDLYANIVLSGGSTMFQGLPERIEKEIT 232
Cdd:cd10211  234 -----EENVRKI--------QLPF----------GLVETIEFVLKRYPAEQQDRLVQNVFLTGGNALFPGLKERLEKELR 290
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 385861543 233 RLAPPTMKIKVVAPPERKYAVWIGGSILASLATFPQMVITHEEYNDAGPG 282
Cdd:cd10211  291 AIRPFGSPFNVVRAKDPVLDAWRGAAKWALDSTFEKVWITKQEYEEKGGE 340
ASKHA_NBD_AtArp8-like cd13396
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and ...
3-280 6.87e-42

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: 146.92  E-value: 6.87e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543   3 TFYNELRVDPAEHPVLLTEaPM-------NPKANREKMIQLMFETF---NVPSFYVGIQAVLSLYSSGRTTGIVFDAGDG 72
Cdd:cd13396   47 TIMTRMQVKPSRQPVVVSL-PLchsddteSAAASRRQLRGTIFNVLfdmNVPAVCAVDQAVLALYAANRTSGIVVNIGFR 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  73 VSHTVPIYEGYSLPH-AIMRLNLAGRDLTAWLQKILNERGYTFTTSAereIVRDIKEKLAYVALDFDAEMQKaATTTDCN 151
Cdd:cd13396  126 VTTIVPVYRGRVMHDiGVEVVGQGALRLTGFLKELMQQNGIRFPSLY---TVRTIKEKLCYVAEDYEAELAK-DTQASCE 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 152 VSytlpDGNEIVIANERFRCPELLFKPAFNGFEFDGIDQTLFDSIMKCDIDVR---KDLYANIVLSGGSTMFQGLPERIE 228
Cdd:cd13396  202 VA----GEGWFTLSNERFKTGEILFQPGLGGMRAMGLHQAVALCMDHCALVHSqgdDGWFKTIVLSGGSACLPGLSERLE 277
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 385861543 229 KEITRLAPPTMK--IKVVAPPERKYAVWIGGSILASLATFPQ-MVITHEEYNDAG 280
Cdd:cd13396  278 RELRKLLPKSLSegIRIIPPPLGPDSAWQGAKLISNLSNFPDgWCITKKQFRNKP 332
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
1-287 5.74e-40

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: 142.45  E-value: 5.74e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543   1 HHTFYNELRVDPA--EHPVLLTEAPMNPKANREKMIQLMFETFNVPSFYVGIQAVLSLYSSGRTTGIVFDAGDGVSHTVP 78
Cdd:cd10208   55 RHILFSLLSIPRPtnNSPVLLSVPPSWSKSDLELLTQLFFERLNVPAFAILEAPLAALYAAGATSGIVVDIGHEKTDITP 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  79 IYEGYSLPHAIMRLNLAGRDLTAWLQKILNERGYTFTTSAE--REIVRDIKEKLAYVALdFDAEMQKAAtttdcnvsytL 156
Cdd:cd10208  135 IVDSQVVPHALVSIPIGGQDCTAHLAQLLKSDEPELKSQAEsgEEATLDLAEALKKSPI-CEVLSDGAD----------L 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 157 PDGNEIVIANERFRCPELLFKPAFNgfEFDGIDQTLFDSIMK---CDIDVRKDLYANIVLSGGSTMFQGLPERIEKEI-T 232
Cdd:cd10208  204 ASGTEITVGKERFRACEPLFKPSSL--RVDLLIAAIAGALVLnasDEPDKRPALWENIIIVGGGSRIRGLKEALLSELqQ 281
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 385861543 233 RLAPPTMKIKVVAP------------PERK-----YAVWIGGSILASLAtFP----QMVITHEEYNDAGPGIVHRK 287
Cdd:cd10208  282 FHLISETSASPQQPriirlakipdyfPEWKksgyeEAAFLGASIVAKLV-FNdpssKHYISKVDYNEKGPAAIHTK 356
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
218-288 2.93e-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: 97.74  E-value: 2.93e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 385861543 218 TMFQGLPERIEKEITRLAPPTMKIKVVAPPERKYAVWIGGSILASLATFPQMVITHEEYNDAGPGIVHRKC 288
Cdd:NF040575  62 VNESGFYEKLKKSITEKAPKGALIGMTLDPKPESAAWRGAAMYAASEGFVEMAITKQEYDESGPSIVHRKC 132
ASKHA_NBD_Arp8-like cd10206
nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The ...
31-281 1.12e-21

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: 93.84  E-value: 1.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  31 EKMIQLMFETFNVPSFYVGIQAVLSLYSSGRTTGIVFDAGDGVSHTVPIYEGYSLPHAIMRLNLAGRDLTAWLQKILNER 110
Cdd:cd10206  202 KELVDLLLRRLGFSSVFVHQESVCATFGAGLSSACVVDIGAQKTSVACVEDGLSIPNSRIRLPYGGDDITRCFLWLLRRS 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 111 G--YTF---TTSAEREIVRDIKEKlaYVALDFDaemqkaatttDCNVSytlpdgneIVIANERFRC-PELLFKpafngFE 184
Cdd:cd10206  282 GfpYREcnlNSPLDFLLLERLKET--YCTLDQD----------DIGVQ--------LHEFYVREPGqPTLKYQ-----FK 336
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 185 FDGIDQTLFDSIMKC-DIDVRKDLYANIVLSGGSTMFQGLPERIEKEITRLAPPTMK----IKVVAPPERKYA---VWIG 256
Cdd:cd10206  337 LLPLDEAIVQSILSCaSDELKRKMYSSILLVGGGAKIPGLAEALEDRLLIKIPSLFEavetVEVLPPPKDMDPsllAWKG 416
                        250       260
                 ....*....|....*....|....*
gi 385861543 257 GSILASLATFPQMVITHEEYNDAGP 281
Cdd:cd10206  417 GAVLACLDSAQELWITRKEWQRLGV 441
ASKHA_NBD_ScArp7-like cd10212
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and ...
2-266 1.09e-13

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: 70.52  E-value: 1.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543   2 HTFYNELRVDPAEHPVLLTEAPMNPKANR---EKMIQLMFETFNVPSFYVGIQAVLSLYSSGRTTGIVFDAGDGVSHTVP 78
Cdd:cd10212   87 YLYDTQLKVSPEELPLVITMPATNGKPDMailERYYELAFDKLNVPVFQIVIEPLAIALSMGKSSAFVIDIGASGCNVTP 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  79 IYEGYSLPHAIMRLNLAGRDL-----------------------------------TAWLQKILNergyTFTTSAER--- 120
Cdd:cd10212  167 IIDGIVVKNAVVRSKFGGDFLdfqvherlaplikeendmenmadeqkrstdvwyeaSTWIQQFKS----TMLQVSEKdlf 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 121 EIVRDIKEKlayvaLDFDAEMQKAATTTDCNVSYTLPDG--NEIVIANERF-----------------RCPELLFKPAFN 181
Cdd:cd10212  243 ELERYYKEQ-----ADIYAKQQEQLKQMDQQLQYTALTGspNNPLVQKKNFlfkplnktltldlkecyQFAEYLFKPQLI 317
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543 182 GFEF---DGIDQTLFDSIMKCDIDVRKDLYANIVLSGGSTMFQGLPERIEKEITrLAPPTMKIKVVAPP---ERKYAVWI 255
Cdd:cd10212  318 SDKFspeDGLGPLMAKSVKKAPEQVYSLLLTNVIITGSTSLIEGMEQRIIKELS-IRFPQYKLTTFANQvmmDRKIQGWL 396
                        330
                 ....*....|.
gi 385861543 256 GGSILASLATF 266
Cdd:cd10212  397 GALTMANLPSW 407
ASKHA_NBD_MamK cd24009
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ...
92-230 5.87e-05

nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called magnetosome cytoskeleton protein MamK, is a protein with ATPase activity which forms dynamic cytoplasmic filaments (probably with paralog MamK-like) that may organize magnetosomes into long chains running parallel to the long axis of the cell. Turnover of MamK filaments is probably promoted by MamK-like (e.g.. MamJ and/or LimJ), which provides a monomer pool. MamK forms twisted filaments in the presence of ATP or GTP. It serves to close gaps between magnetosomes in the chain. Interaction with MCP10 is involved in controlling the response to magnetic fields, possibly by controlling flagellar rotation. The MamK family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466859 [Multi-domain]  Cd Length: 328  Bit Score: 43.74  E-value: 5.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861543  92 LNLAGRDLTAWLQKILNER--GYTFTtsaeREIVRDIKEKLAYValdfdaemqkaaTTTDCNVSYTLP-DGN--EIVIAN 166
Cdd:cd24009  175 LPKAGDYIDEELVDLIKERypEVQLT----LNMARRWKEKYGFV------------GDASEPVKVELPvDGKpvTYDITE 238
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 385861543 167 E-RFRCPELLfkpafngfefDGIDQTLFDSIMKCDIDVRKDLYANIVLSGGSTMFQGLPERIEKE 230
Cdd:cd24009  239 ElRIACESLV----------PDIVEGIKKLIASFDPEFQEELRNNIVLAGGGSRIRGLDTYIEKA 293
 
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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