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Conserved domains on  [gi|15227502|ref|NP_181739|]
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actin 9 [Arabidopsis thaliana]

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 ...
3-361 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: 696.42  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502   3 PIVCDKGHGMVQAGFAGDEAPKVVFPCVVGRPRD-----GLNPNESYVGEEGHANRDILTLKDPMEHGIVNNWDDMEKIW 77
Cdd:cd10224   2 ALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHqgvmvGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIW 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  78 HYTFYNELRVDPEEHPVLLTEAPYNPKANREKMTQIMFESFDVPAMYVSMQSVLYLYSSGRTTGVVLDLGERVSHTVPVY 157
Cdd:cd10224  82 HHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIY 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 158 EGYALPHGILRLDLGGRDLTDYLIEIMTERGYTYTTSAEREIVRDIKEKLCYVALDYEQEMEKTTKGWTIDKTYVLPDGQ 237
Cdd:cd10224 162 EGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDGQ 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 238 EITIEAERFMCPEVLFQPSVIGKESSGIHEATRNSILKCPVDTRRDMYGNILMTGGTTMLHGIKERMTKELNALVPSSMK 317
Cdd:cd10224 242 VITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTMK 321
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 15227502 318 VKVVVPPESECSVWIGGSILASLSTFHQMWITKDEYEEHGAAIV 361
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 ...
3-361 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: 696.42  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502   3 PIVCDKGHGMVQAGFAGDEAPKVVFPCVVGRPRD-----GLNPNESYVGEEGHANRDILTLKDPMEHGIVNNWDDMEKIW 77
Cdd:cd10224   2 ALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHqgvmvGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIW 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  78 HYTFYNELRVDPEEHPVLLTEAPYNPKANREKMTQIMFESFDVPAMYVSMQSVLYLYSSGRTTGVVLDLGERVSHTVPVY 157
Cdd:cd10224  82 HHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIY 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 158 EGYALPHGILRLDLGGRDLTDYLIEIMTERGYTYTTSAEREIVRDIKEKLCYVALDYEQEMEKTTKGWTIDKTYVLPDGQ 237
Cdd:cd10224 162 EGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDGQ 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 238 EITIEAERFMCPEVLFQPSVIGKESSGIHEATRNSILKCPVDTRRDMYGNILMTGGTTMLHGIKERMTKELNALVPSSMK 317
Cdd:cd10224 242 VITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTMK 321
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 15227502 318 VKVVVPPESECSVWIGGSILASLSTFHQMWITKDEYEEHGAAIV 361
Cdd:cd10224 322 IKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIV 365
PTZ00281 PTZ00281
actin; Provisional
1-365 0e+00

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 563.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502    1 MKPIVCDKGHGMVQAGFAGDEAPKVVFPCVVGRPRD-----GLNPNESYVGEEGHANRDILTLKDPMEHGIVNNWDDMEK 75
Cdd:PTZ00281   6 VQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHtgvmvGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502   76 IWHYTFYNELRVDPEEHPVLLTEAPYNPKANREKMTQIMFESFDVPAMYVSMQSVLYLYSSGRTTGVVLDLGERVSHTVP 155
Cdd:PTZ00281  86 IWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVSHTVP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  156 VYEGYALPHGILRLDLGGRDLTDYLIEIMTERGYTYTTSAEREIVRDIKEKLCYVALDYEQEMEKTTKGWTIDKTYVLPD 235
Cdd:PTZ00281 166 IYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEMQTAASSSALEKSYELPD 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  236 GQEITIEAERFMCPEVLFQPSVIGKESSGIHEATRNSILKCPVDTRRDMYGNILMTGGTTMLHGIKERMTKELNALVPSS 315
Cdd:PTZ00281 246 GQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELTALAPST 325
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 15227502  316 MKVKVVVPPESECSVWIGGSILASLSTFHQMWITKDEYEEHGAAIVHRKC 365
Cdd:PTZ00281 326 MKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIVHRKC 375
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
2-365 0e+00

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 562.26  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502      2 KPIVCDKGHGMVQAGFAGDEAPKVVFPCVVGRPRDG----LNPNESYVGEEGHANRDILTLKDPMEHGIVNNWDDMEKIW 77
Cdd:smart00268   2 PAIVIDNGSGTIKAGFAGEDFPQVVFPSIVGRPKDGkgmvGDAKDIFVGDEAQEKRGGLELKYPIENGIVENWDDMEKIW 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502     78 HYTFYNELRVDPEEHPVLLTEAPYNPKANREKMTQIMFESFDVPAMYVSMQSVLYLYSSGRTTGVVLDLGERVSHTVPVY 157
Cdd:smart00268  82 DYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVPVV 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502    158 EGYALPHGILRLDLGGRDLTDYLIEIMTERGYTYTTSAEREIVRDIKEKLCYVALDYEQEMEKTTKGWTID---KTYVLP 234
Cdd:smart00268 162 DGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLARESSESSkleKTYELP 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502    235 DGQEITIEAERFMCPEVLFQPSVIGKESSGIHEATRNSILKCPVDTRRDMYGNILMTGGTTMLHGIKERMTKELNALVPS 314
Cdd:smart00268 242 DGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELKQLAPK 321
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 15227502    315 SMKVKVVVPPESECSVWIGGSILASLSTFHQMWITKDEYEEHGAAIVHRKC 365
Cdd:smart00268 322 KLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERKC 372
Actin pfam00022
Actin;
3-365 5.18e-170

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 479.88  E-value: 5.18e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502     3 PIVCDKGHGMVQAGFAGDEAPKVVFPCVVGRPRD--GLNPNESYVGEEGHANRDILTLKDPMEHGIVNNWDDMEKIWHYT 80
Cdd:pfam00022   3 ALVIDNGSHTTRAGFAGEDAPKAVIPSCVGKPRGtkVEAANKYYVGDEALTYRPGMEVRSPVEDGIVVDWDAMEEIWEHV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502    81 FYNELRVDPEEHPVLLTEAPYNPKANREKMTQIMFESFDVPAMYVSMQSVLYLYSSGRTTGVVLDLGERVSHTVPVYEGY 160
Cdd:pfam00022  83 LKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVPVHDGY 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502   161 ALPHGILRLDLGGRDLTDYLIEIMTER------------------------------GYTYTTSAEREIVRDIKEKLCYV 210
Cdd:pfam00022 163 VLQKAIRRSDLGGDFLTDYLRELLRSRnieitprylikskkpgdpapavtkrelpdtTYSYKTYQERRVLEEIKESVCYV 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502   211 ALDyEQEMEkTTKGWTIDKTYVLPDGQEITIEAERFMCPEVLFQPSVIGKES--------SGIHEATRNSILKCPVDTRR 282
Cdd:pfam00022 243 SDD-PFGDE-TTSSSIPTRVYELPDGSTIILGAERFRVPEILFNPSLIGSESelpppqtaVGIPELIVDAINACDVDLRP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502   283 DMYGNILMTGGTTMLHGIKERMTKELNALVPSSMKVKVVVPPESEC---SVWIGGSILASLSTFHQMWITKDEYEEHGAA 359
Cdd:pfam00022 321 SLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVKIIAPGNTVErrySAWIGGSILASLGTFQQMWVSKQEYEEHGAS 400

                  ....*.
gi 15227502   360 IVHRKC 365
Cdd:pfam00022 401 VVERKC 406
COG5277 COG5277
Actin-related protein [Cytoskeleton];
3-356 6.85e-100

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 302.09  E-value: 6.85e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502   3 PIVCDKGHGMVQAG-FAGDEAPKVV-----FPCVVGRPR-----DGLNpNESYVGEE-----GHANRDILTLKDPMEHGI 66
Cdd:COG5277  10 VIGIDFGTSYVKYGpIALEEKPRVIqtrglFLRIVGESKllgpmEGLS-RGLVVGDEvskylSSVRDAIRNLKYPLRDGI 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  67 V-----NNWDDMEKIWHYTFYNELRVDPEEHP--VLLTEAPYNPKANREKMTQIMFESFD---VPAMYVSMQSVLYLYSS 136
Cdd:COG5277  89 VrrddeDAWRVLKELLRYTFAQFLVVDPEFHGflVVVALSALAPDYMRERLFDIHFEVFSeegAPAVTIIPQPLAVAIAE 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 137 GRTTGVVLDLGERVSHTVPVYEGyALPHGILRLDLGGRDLTDYLIEIMTERGYTYTTSAEReIVRDIKEKLCYVALDYEQ 216
Cdd:COG5277 169 KAVTCVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSDTAREEY-VVRVVKEALGLVPRDLAK 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 217 EMEKTTKGW-TIDKTYVLPDGQ-EITI---EAERFMCPEVLFQPSVIGKESS----------------------GIHEAT 269
Cdd:COG5277 247 AIQKAASNPdSFEAKVRLPNPTvEIELgnyAWERFLIGEILFNPNHEGFESYiqqgrlriedavigdvvlygemGLAEAI 326
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 270 RNSILKCPVDTRRDMYGNILMTGGTTML---HGIKE-------RMTKELNALVPsSMKVKVVVPPESECSVWIGGSILAS 339
Cdd:COG5277 327 INSIMKCDVEIQDELYSNIILSGGAFNWsvpPGLEDvavdsvtRVQIELSELAP-ELKVNVRLVSDPQYSVWKGAIIYGY 405
                       410
                ....*....|....*....
gi 15227502 340 LSTFHQMW--ITKDEYEEH 356
Cdd:COG5277 406 ALPFSVKWswITKEGWYFL 424
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
294-365 1.05e-23

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: 95.05  E-value: 1.05e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15227502  294 TTMLHGIKERMTKELNALVPSSMKVKVVVPPESECSVWIGGSILASLSTFHQMWITKDEYEEHGAAIVHRKC 365
Cdd:NF040575  61 RVNESGFYEKLKKSITEKAPKGALIGMTLDPKPESAAWRGAAMYAASEGFVEMAITKQEYDESGPSIVHRKC 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 ...
3-361 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: 696.42  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502   3 PIVCDKGHGMVQAGFAGDEAPKVVFPCVVGRPRD-----GLNPNESYVGEEGHANRDILTLKDPMEHGIVNNWDDMEKIW 77
Cdd:cd10224   2 ALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHqgvmvGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIW 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  78 HYTFYNELRVDPEEHPVLLTEAPYNPKANREKMTQIMFESFDVPAMYVSMQSVLYLYSSGRTTGVVLDLGERVSHTVPVY 157
Cdd:cd10224  82 HHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIY 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 158 EGYALPHGILRLDLGGRDLTDYLIEIMTERGYTYTTSAEREIVRDIKEKLCYVALDYEQEMEKTTKGWTIDKTYVLPDGQ 237
Cdd:cd10224 162 EGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDGQ 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 238 EITIEAERFMCPEVLFQPSVIGKESSGIHEATRNSILKCPVDTRRDMYGNILMTGGTTMLHGIKERMTKELNALVPSSMK 317
Cdd:cd10224 242 VITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTMK 321
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 15227502 318 VKVVVPPESECSVWIGGSILASLSTFHQMWITKDEYEEHGAAIV 361
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 ...
3-357 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: 632.30  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502   3 PIVCDKGHGMVQAGFAGDEAPKVVFPCVVGRPR-----DGLNPNESYVGEEGHANRDILTLKDPMEHGIVNNWDDMEKIW 77
Cdd:cd13397   2 AVVIDNGSGLIKAGFAGEDLPRAVFPSVVGRPKykavmLGAGQKEVYVGDEAQEKRGVLTLSYPIEHGIVTNWDDMEKIW 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  78 HYTFYNELRVDPEEHPVLLTEAPYNPKANREKMTQIMFESFDVPAMYVSMQSVLYLYSSGRTTGVVLDLGERVSHTVPVY 157
Cdd:cd13397  82 HHTFENELRVKPEEHPVLLTEAPLNPKQNREKMAEIMFETFGVPAFYVAIQAVLSLYSSGRTTGLVLDSGDGVTHTVPIY 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 158 EGYALPHGILRLDLGGRDLTDYLIEIMTERGYTYTTSAEREIVRDIKEKLCYVALDYEQEMEKttKGWTIDKTYVLPDGQ 237
Cdd:cd13397 162 EGYALPHAVQRLDLAGRDLTEYLMKLLKERGHSFTTTAEREIVRDIKEKLCYVALDYEEELKK--KSEELEKEYTLPDGQ 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 238 EITIEAERFMCPEVLFQPSVIGKESSGIHEATRNSILKCPVDTRRDMYGNILMTGGTTMLHGIKERMTKELNALVPSSMK 317
Cdd:cd13397 240 VIKIGSERFRCPEALFRPSLIGREAPGIHKLVYNSIMKCDIDIRKDLYSNIVLSGGSTMFPGLPERLQKELEALAPSSTK 319
                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 15227502 318 VKVVVPPESECSVWIGGSILASLSTFHQMWITKDEYEEHG 357
Cdd:cd13397 320 VKVIAPPERKYSVWIGGSILASLSTFKSMWITRAEYDEFG 359
PTZ00281 PTZ00281
actin; Provisional
1-365 0e+00

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 563.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502    1 MKPIVCDKGHGMVQAGFAGDEAPKVVFPCVVGRPRD-----GLNPNESYVGEEGHANRDILTLKDPMEHGIVNNWDDMEK 75
Cdd:PTZ00281   6 VQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHtgvmvGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502   76 IWHYTFYNELRVDPEEHPVLLTEAPYNPKANREKMTQIMFESFDVPAMYVSMQSVLYLYSSGRTTGVVLDLGERVSHTVP 155
Cdd:PTZ00281  86 IWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVSHTVP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  156 VYEGYALPHGILRLDLGGRDLTDYLIEIMTERGYTYTTSAEREIVRDIKEKLCYVALDYEQEMEKTTKGWTIDKTYVLPD 235
Cdd:PTZ00281 166 IYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEMQTAASSSALEKSYELPD 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  236 GQEITIEAERFMCPEVLFQPSVIGKESSGIHEATRNSILKCPVDTRRDMYGNILMTGGTTMLHGIKERMTKELNALVPSS 315
Cdd:PTZ00281 246 GQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELTALAPST 325
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 15227502  316 MKVKVVVPPESECSVWIGGSILASLSTFHQMWITKDEYEEHGAAIVHRKC 365
Cdd:PTZ00281 326 MKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIVHRKC 375
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
2-365 0e+00

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 562.26  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502      2 KPIVCDKGHGMVQAGFAGDEAPKVVFPCVVGRPRDG----LNPNESYVGEEGHANRDILTLKDPMEHGIVNNWDDMEKIW 77
Cdd:smart00268   2 PAIVIDNGSGTIKAGFAGEDFPQVVFPSIVGRPKDGkgmvGDAKDIFVGDEAQEKRGGLELKYPIENGIVENWDDMEKIW 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502     78 HYTFYNELRVDPEEHPVLLTEAPYNPKANREKMTQIMFESFDVPAMYVSMQSVLYLYSSGRTTGVVLDLGERVSHTVPVY 157
Cdd:smart00268  82 DYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVPVV 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502    158 EGYALPHGILRLDLGGRDLTDYLIEIMTERGYTYTTSAEREIVRDIKEKLCYVALDYEQEMEKTTKGWTID---KTYVLP 234
Cdd:smart00268 162 DGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLARESSESSkleKTYELP 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502    235 DGQEITIEAERFMCPEVLFQPSVIGKESSGIHEATRNSILKCPVDTRRDMYGNILMTGGTTMLHGIKERMTKELNALVPS 314
Cdd:smart00268 242 DGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELKQLAPK 321
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 15227502    315 SMKVKVVVPPESECSVWIGGSILASLSTFHQMWITKDEYEEHGAAIVHRKC 365
Cdd:smart00268 322 KLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERKC 372
PTZ00004 PTZ00004
actin-2; Provisional
4-365 0e+00

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 560.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502    4 IVCDKGHGMVQAGFAGDEAPKVVFPCVVGRPRD-----GLNPNESYVGEEGHANRDILTLKDPMEHGIVNNWDDMEKIWH 78
Cdd:PTZ00004   9 AVVDNGSGMVKAGFAGDDAPRCVFPSIVGRPKNpgimvGMEEKDCYVGDEAQDKRGILTLKYPIEHGIVTNWDDMEKIWH 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502   79 YTFYNELRVDPEEHPVLLTEAPYNPKANREKMTQIMFESFDVPAMYVSMQSVLYLYSSGRTTGVVLDLGERVSHTVPVYE 158
Cdd:PTZ00004  89 HTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETHNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYE 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  159 GYALPHGILRLDLGGRDLTDYLIEIMTERGYTYTTSAEREIVRDIKEKLCYVALDYEQEMEKTTKGWTI-DKTYVLPDGQ 237
Cdd:PTZ00004 169 GYSLPHAIHRLDVAGRDLTEYMMKILHERGTTFTTTAEKEIVRDIKEKLCYIALDFDEEMGNSAGSSDKyEESYELPDGT 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  238 EITIEAERFMCPEVLFQPSVIGKESS-GIHEATRNSILKCPVDTRRDMYGNILMTGGTTMLHGIKERMTKELNALVPSSM 316
Cdd:PTZ00004 249 IITVGSERFRCPEALFQPSLIGKEEPpGIHELTFQSINKCDIDIRKDLYGNIVLSGGTTMYRGLPERLTKELTTLAPSTM 328
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 15227502  317 KVKVVVPPESECSVWIGGSILASLSTFHQMWITKDEYEEHGAAIVHRKC 365
Cdd:PTZ00004 329 KIKVVAPPERKYSVWIGGSILSSLPTFQQMWVTKEEYDESGPSIVHRKC 377
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
3-365 0e+00

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


Pssm-ID: 466820 [Multi-domain]  Cd Length: 370  Bit Score: 523.65  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502   3 PIVCDKGHGMVQAGFAGDEAPKVVFPCVVGRPR------DGLNPNeSYVGEEGHANRDILTLKDPMEHGIVNNWDDMEKI 76
Cdd:cd10216   3 PVVIDNGSGVIKAGFAGDDIPKVVFPSYVGRPKhvrvmaGALEGD-VFVGPKAEEHRGLLKIRYPMEHGIVTDWNDMERI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  77 WHYTFYNE-LRVDPEEHPVLLTEAPYNPKANREKMTQIMFESFDVPAMYVSMQSVLYLYSSGRTTGVVLDLGERVSHTVP 155
Cdd:cd10216  82 WQYVYSKLqLNTFSEEHPVLLTEAPLNPRKNREKAAEVFFETFNVPALFVSMQAVLSLYASGRTTGVVLDSGDGVTHAVP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 156 VYEGYALPHGILRLDLGGRDLTDYLIEIMTERGYTYTTSAEREIVRDIKEKLCYVALDyEQEMEKTTKGWTIDKTYVLPD 235
Cdd:cd10216 162 IYEGFALPHSIRRVDIAGRDVTEYLQLLLRKSGYNFHTSAEFEIVREIKEKACYVALN-PQKEEKLEEEKTEKAQYTLPD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 236 GQEITIEAERFMCPEVLFQPSVIGKESSGIHEATRNSILKCPVDTRRDMYGNILMTGGTTMLHGIKERMTKELNALVPSS 315
Cdd:cd10216 241 GSTIEIGPERFRAPEILFNPELIGLEYPGVHEVLVDSIQKSDLDLRKTLYSNIVLSGGSTLFKGFGDRLLSEVKKLAPKD 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 15227502 316 MKVKVVVPPESECSVWIGGSILASLSTFHQMWITKDEYEEHGAAIVHRKC 365
Cdd:cd10216 321 VKIRISAPPERLYSTWIGGSILASLSTFKKMWVSKKEYEEDGARILHRKT 370
Actin pfam00022
Actin;
3-365 5.18e-170

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 479.88  E-value: 5.18e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502     3 PIVCDKGHGMVQAGFAGDEAPKVVFPCVVGRPRD--GLNPNESYVGEEGHANRDILTLKDPMEHGIVNNWDDMEKIWHYT 80
Cdd:pfam00022   3 ALVIDNGSHTTRAGFAGEDAPKAVIPSCVGKPRGtkVEAANKYYVGDEALTYRPGMEVRSPVEDGIVVDWDAMEEIWEHV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502    81 FYNELRVDPEEHPVLLTEAPYNPKANREKMTQIMFESFDVPAMYVSMQSVLYLYSSGRTTGVVLDLGERVSHTVPVYEGY 160
Cdd:pfam00022  83 LKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVPVHDGY 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502   161 ALPHGILRLDLGGRDLTDYLIEIMTER------------------------------GYTYTTSAEREIVRDIKEKLCYV 210
Cdd:pfam00022 163 VLQKAIRRSDLGGDFLTDYLRELLRSRnieitprylikskkpgdpapavtkrelpdtTYSYKTYQERRVLEEIKESVCYV 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502   211 ALDyEQEMEkTTKGWTIDKTYVLPDGQEITIEAERFMCPEVLFQPSVIGKES--------SGIHEATRNSILKCPVDTRR 282
Cdd:pfam00022 243 SDD-PFGDE-TTSSSIPTRVYELPDGSTIILGAERFRVPEILFNPSLIGSESelpppqtaVGIPELIVDAINACDVDLRP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502   283 DMYGNILMTGGTTMLHGIKERMTKELNALVPSSMKVKVVVPPESEC---SVWIGGSILASLSTFHQMWITKDEYEEHGAA 359
Cdd:pfam00022 321 SLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVKIIAPGNTVErrySAWIGGSILASLGTFQQMWVSKQEYEEHGAS 400

                  ....*.
gi 15227502   360 IVHRKC 365
Cdd:pfam00022 401 VVERKC 406
ASKHA_NBD_Arp2 cd10220
nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, ...
2-358 5.30e-153

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: 435.84  E-value: 5.30e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502   2 KPIVCDKGHGMVQAGFAGDEAPKVVFPCVVGRP-------RDGLNPNESYVGEEGHANRDILTLKDPMEHGIVNNWDDME 74
Cdd:cd10220   1 KVVVCDNGTGFVKCGFAGSNFPEHVFPSLVGRPilraeekVGDIEIKDIMVGDEASELRSMLEVTYPMENGIVRNWDDME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  75 KIWHYTFYNELRVDPEEHPVLLTEAPYNPKANREKMTQIMFESFDVPAMYVSMQSVLYLYSSGRTTGVVLDLGERVSHTV 154
Cdd:cd10220  81 HLWDYTFGEKLKIDPRECKILLTEPPMNPTKNREKMVEVMFEKYGFAGVYVAIQAVLTLYAQGLLTGVVVDSGDGVTHIV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 155 PVYEGYALPHGILRLDLGGRDLTDYLIEIMTERGYTYTTSAEREIVRDIKEKLCYVALDYEQEM---EKTTkgwTIDKTY 231
Cdd:cd10220 161 PVYEGFSLPHLTRRLDVAGRDITRYLIKLLLLRGYAFNRTADFETVREIKEKLCYVAYDIELEQklaLETT---VLVESY 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 232 VLPDGQEITIEAERFMCPEVLFQPSVIGKESSGIHEATRNSILKCPVDTRRDMYGNILMTGGTTMLHGIKERMTKELNAL 311
Cdd:cd10220 238 TLPDGRVIKVGGERFEAPEALFQPHLIDVEGPGIAELLFNTIQAADIDTRPELYKHIVLSGGSTMYPGLPSRLEKEIKQL 317
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15227502 312 V-----------PSSMKVKVVVPPESECSVWIGGSILASLSTFH-QMWITKDEYEEHGA 358
Cdd:cd10220 318 YlervlkgdterLSKFKIRIEDPPRRKHMVFLGGAVLADIMKDKdEFWITRQEYEEQGV 376
PTZ00466 PTZ00466
actin-like protein; Provisional
2-364 2.30e-148

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 423.97  E-value: 2.30e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502    2 KPIVCDKGHGMVQAGFAGDEAPKVVFPCVVGRPR-----DGLNPNESYVGEEGHANRDILTLKDPMEHGIVNNWDDMEKI 76
Cdd:PTZ00466  13 QPIIIDNGTGYIKAGFAGEDVPNLVFPSYVGRPKykrvmAGAVEGNIFVGNKAEEYRGLLKVTYPINHGIIENWNDMENI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502   77 WHYTfYNELRVDPEEHPVLLTEAPYNPKANREKMTQIMFESFDVPAMYVSMQSVLYLYSSGRTTGVVLDLGERVSHTVPV 156
Cdd:PTZ00466  93 WIHV-YNSMKINSEEHPVLLTEAPLNPQKNKEKIAEVFFETFNVPALFISIQAILSLYSCGKTNGTVLDCGDGVCHCVSI 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  157 YEGYALPHGILRLDLGGRDLTDYLIEIMTERGYTYTTSAEREIVRDIKEKLCYVALDYEQEMEKTTKGWTiDKTYVLPDG 236
Cdd:PTZ00466 172 YEGYSITNTITRTDVAGRDITTYLGYLLRKNGHLFNTSAEMEVVKNMKENCCYVSFNMNKEKNSSEKALT-TLPYILPDG 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  237 QEITIEAERFMCPEVLFQPSVIGKESSGIHEATRNSILKCPVDTRRDMYGNILMTGGTTMLHGIKERMTKELNALVPSSM 316
Cdd:PTZ00466 251 SQILIGSERYRAPEVLFNPSILGLEYLGLSELIVTSITRADMDLRRTLYSHIVLSGGTTMFHGFGDRLLNEIRKFAPKDI 330
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 15227502  317 KVKVVVPPESECSVWIGGSILASLSTFHQMWITKDEYEEHGAAIVHRK 364
Cdd:PTZ00466 331 TIRISAPPERKFSTFIGGSILASLATFKKIWISKQEFDEYGSVILHRK 378
ASKHA_NBD_ACTL7 cd10214
nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ...
2-365 1.59e-146

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: 418.75  E-value: 1.59e-146
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502   2 KPIVCDKGHGMVQAGFAGDEAPKVVFPCVVGRPRD-----GLNPNESYVGEEGHANRDILTLKDPMEHGIVNNWDDMEKI 76
Cdd:cd10214   4 KAVIIDLGTGYCKAGFAGQPRPSYVISSTVGKPPQesaktGDNRKETFVGKELANVEPPLKLVNPLRHGIVVDWDCVQDI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  77 WHYTFYNELRVDPEEHPVLLTEAPYNPKANREKMTQIMFESFDVPAMYVSMQSVLYLYSSGRTTGVVLDLGERVSHTVPV 156
Cdd:cd10214  84 WEYIFEKEMKILPEEHAVLVSDPPLSPTTNREKYAELMFETFSIPAMHIAYQSRLSLYSYGRTSGLVVESGHGVSYVVPI 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 157 YEGYALPHGILRLDLGGRDLTDYLIEIMTERGYTYTTSaEREIVRDIKEKLCYVALDYEQEMEKTTKGWTIDktYVLPDG 236
Cdd:cd10214 164 HEGYNLPHITGRADYAGSDLTAYLMKLLNEAGNKFTDD-QLHIVEDIKKKCCYVALDFEEEMGLPPQEYTVD--YELPDG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 237 QEITIEAERFMCPEVLFQPSVIGKESSGIHEATRNSILKCPVDTRRDMYGNILMTGGTTMLHGIKERMTKELNALVPSSM 316
Cdd:cd10214 241 HLITIGKERFRCPEMLFNPSLIGSKQPGLHTLTMNSLNKCDANLKKDLAKNILLCGGSTMFDGFPDRFQKELSKLCPNDN 320
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 15227502 317 KVkVVVPPESECSVWIGGSILASLSTFHQMWITKDEYEEHGAAIVHRKC 365
Cdd:cd10214 321 PI-VAASPERKYSVWTGGSILASLKSFQQLWVRRREYEERGPFVIYRKC 368
ASKHA_NBD_actin-like cd10169
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ...
4-357 1.18e-145

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: 412.27  E-value: 1.18e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502   4 IVCDKGHGMVQAGFAGDEAPKVVFPcvvgrprdglnpnesyvgeeghanrdiltlkdpmehgivnnWDDMEKIWHYTFYN 83
Cdd:cd10169   1 IVIDNGSGTIKAGFAGEDAPRLIFP-----------------------------------------WDDMEKIWEHVFYN 39
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  84 ELRVDPEEHPVLLTEAPYNPKANREKMTQIMFESFDVPAMYVSMQSVLYLYSSGRTTGVVLDLGERVSHTVPVYEGYALP 163
Cdd:cd10169  40 LLRVDPEEHPVLLTEPPLNPKANREKLAEILFETFNVPSLYIANQAVLSLYASGRTTGLVVDSGEGVTHIVPVYEGYVLP 119
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 164 HGILRLDLGGRDLTDYLIEIMTERGYTYTTSAEREIVRDIKEKLCyvaldyeqemekttkgwtidktyvlpdgqeitiea 243
Cdd:cd10169 120 HAVRRLDIGGRDLTDYLAKLLREKGYSFSTSAEREIVRDIKEKLC----------------------------------- 164
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 244 erfmcpevlfqpsvigkessGIHEATRNSILKCPVDTRRDMYGNILMTGGTTMLHGIKERMTKELNALVPSSMKVKVVVP 323
Cdd:cd10169 165 --------------------GLHELIYDSIMKCDIDLRKELYSNIVLSGGTTLFPGFAERLQKELSKLAPSSVKVKVIAP 224
                       330       340       350
                ....*....|....*....|....*....|....
gi 15227502 324 PESECSVWIGGSILASLSTFHQMWITKDEYEEHG 357
Cdd:cd10169 225 PERKYSAWIGGSILASLSTFQQMWITKEEYEEHG 258
PTZ00452 PTZ00452
actin; Provisional
4-365 1.08e-141

actin; Provisional


Pssm-ID: 185631  Cd Length: 375  Bit Score: 406.83  E-value: 1.08e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502    4 IVCDKGHGMVQAGFAGDEAPKVVFPCVVGRPR-----DGLNPNESYVGEEGHANRDILTLKDPMEHGIVNNWDDMEKIWH 78
Cdd:PTZ00452   8 VVIDNGSGYCKIGIAGDDAPTSCFPAIVGRSKqndgiFSTFNKEYYVGEEAQAKRGVLAIKEPIQNGIINSWDDIEIIWH 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502   79 YTFYNELRVDPEEHPVLLTEAPYNPKANREKMTQIMFESFDVPAMYVSMQSVLYLYSSGRTTGVVLDLGERVSHTVPVYE 158
Cdd:PTZ00452  88 HAFYNELCMSPEDQPVFMTDAPMNSKFNRERMTQIMFETFNTPCLYISNEAVLSLYTSGKTIGLVVDSGEGVTHCVPVFE 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  159 GYALPHGILRLDLGGRDLTDYLIEIMTERGYTYTTSAEREIVRDIKEKLCYVALDYEQEMEKTTKGWTIDKTYVLPDGQE 238
Cdd:PTZ00452 168 GHQIPQAITKINLAGRLCTDYLTQILQELGYSLTEPHQRIIVKNIKERLCYTALDPQDEKRIYKESNSQDSPYKLPDGNI 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  239 ITIEAERFMCPEVLFQPSVIGKESSGIHEATRNSILKCPVDTRRDMYGNILMTGGTTMLHGIKERMTKELNALVPSSMKV 318
Cdd:PTZ00452 248 LTIKSQKFRCSEILFQPKLIGLEVAGIHHLAYSSIKKCDLDLRQELCRNIVLSGGTTLFPGIANRLSNELTNLVPSQLKI 327
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 15227502  319 KVVVPPESECSVWIGGSILASLSTFHQMWITKDEYEEHGAAIVHRKC 365
Cdd:PTZ00452 328 QVAAPPDRRFSAWIGGSIQCTLSTQQPQWIKRQEYDEQGPSIVHRKC 374
ASKHA_NBD_Arp4_ACTL6-like cd13395
nucleotide-binding domain (NBD) of the actin-related protein 4 (Arp4)-like subfamily; The ...
4-357 2.17e-130

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: 379.60  E-value: 2.17e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502   4 IVCDKGHGMVQAGFAGDEAPKVVFPCVVGRPRD-----------GLNPNESYVGEEG-HANRDILTLKDPMEHGIVNNWD 71
Cdd:cd13395   7 LVLDIGSYSTRAGYAGEDTPKAVFPSVVGVVTDdddaedyvggsGEKKRKYYIGTNSiGVPRPNMEVISPLKDGLIEDWD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  72 DMEKIWHYTFYNELRVDPEEHPVLLTEAPYNPKANREKMTQIMFESFDVPAMYVSMQSVLYLYSSGRTTGVVLDLGERVS 151
Cdd:cd13395  87 AFEKLWDHALKNRLRVDPSEHPLLLTEPSWNTRANREKLTELMFEKYNVPAFFLAKNAVLSAFANGRSTALVVDSGATST 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 152 HTVPVYEGYALPHGILRLDLGGRDLTDYLIEIMTERGYT----Y------------------------TTS----AEREI 199
Cdd:cd13395 167 SVVPVHDGYVLQKAIVRSPLGGDFLTDQLLKLLESKNIEiiprYmikskepveggapakytkkdlpntTSSyhryMVRRV 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 200 VRDIKEKLCYVA-LDYEQEMEKTTKGwtidKTYVLPDGQEITIEAERFMCPEVLFQPSVI---------GKESSGIHEAT 269
Cdd:cd13395 247 LQDFKESVCQVSdSPFDESEAASIPT----VSYELPDGYNIEFGAERFKIPELLFDPSLVkgipappseGNELLGLPQLV 322
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 270 RNSILKCPVDTRRDMYGNILMTGGTTMLHGIKERMTKELNALVPSSMKVKVVVPP---ESECSVWIGGSILASLSTFHQM 346
Cdd:cd13395 323 YTSIGSCDVDIRPELYGNVVLTGGNSLLPGFTDRLNRELSEKAPGSLKLKILASGntvERRFSSWIGGSILASLGSFQQM 402
                       410
                ....*....|.
gi 15227502 347 WITKDEYEEHG 357
Cdd:cd13395 403 WISKQEYEEHG 413
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
3-361 4.12e-101

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: 304.49  E-value: 4.12e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502   3 PIVCDKGHGMVQAGFAGDEAPKVVFPCVVG------------RPRDGLNPNESYVGEEGHANRDILTLKDPMEHGIVNNW 70
Cdd:cd10221   1 AVVIDNGTGYTKMGYAGNTEPQFIIPTVIAikesakvgdgqrRSKKGIEDLDFYIGDEALANSPTYALKYPIRHGIVEDW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  71 DDMEKIWHYTFYNELRVDPEEHPVLLTEAPYNPKANREKMTQIMFESFDVPAMYVSMQSVLYLYSSGRT--------TGV 142
Cdd:cd10221  81 DLMERFWEQCIFKYLRCEPEDHYFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQAVLALAASWTSrkvgertlTGT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 143 VLDLGERVSHTVPVYEGYALPHGILRLDLGGRDLTDYLIEIMTERGYTYTTSAEREIVRDIKEKLCYVALD-------YE 215
Cdd:cd10221 161 VIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREEGIPPEDSLEVAKRIKERYCYVCPDivkefakYD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 216 QEMEK-----------TTKGWTIDKTYvlpdgqeitieaERFMCPEVLFQPSVIGKE-SSGIHEATRNSILKCPVDTRRD 283
Cdd:cd10221 241 SDPAKyikqytginsvTGKPYTVDVGY------------ERFLAPEIFFNPEIASSDfTTPLPEVVDQVIQSCPIDTRRG 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 284 MYGNILMTGGTTMLHGIKERMTKELNALV----------------PSSMKVKVVVPPESECSVWIGGSILASLSTFHQMW 347
Cdd:cd10221 309 LYKNIVLSGGSTMFKDFGRRLQRDVKRIVdarlkaseelsggklkPKPIDVNVISHPMQRYAVWFGGSMLASTPEFYTVC 388
                       410
                ....*....|....
gi 15227502 348 ITKDEYEEHGAAIV 361
Cdd:cd10221 389 HTKAEYEEYGPSIC 402
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
1-366 5.92e-100

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 302.04  E-value: 5.92e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502    1 MKPIVCDKGHGMVQAGFAGDEAPKVVFPCVVG--------RPRDGLNPNESYVGEEGHANRDILTLKDPMEHGIVNNWDD 72
Cdd:PTZ00280   4 LPVVVIDNGTGYTKMGYAGNTEPTYIIPTLIAdnskqsrrRSKKGFEDLDFYIGDEALAASKSYTLTYPMKHGIVEDWDL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502   73 MEKIWHYTFYNELRVDPEEHPVLLTEAPYNPKANREKMTQIMFESFDVPAMYVSMQSVLYLYSS----------GRTTGV 142
Cdd:PTZ00280  84 MEKFWEQCIFKYLRCEPEEHYFILTEPPMNPPENREYTAEIMFETFNVKGLYIAVQAVLALRASwtskkakelgGTLTGT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  143 VLDLGERVSHTVPVYEGYALPHGILRLDLGGRDLTDYLIEIMTERGYTYTTSAEREIVRDIKEKLCYVALDYEQEMEK-- 220
Cdd:PTZ00280 164 VIDSGDGVTHVIPVVDGYVIGSSIKHIPLAGRDITNFIQQMLRERGEPIPAEDILLLAQRIKEKYCYVAPDIAKEFEKyd 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  221 ----------------TTKGWTIDKTYvlpdgqeitieaERFMCPEVLFQPSVI-GKESSGIHEATRNSILKCPVDTRRD 283
Cdd:PTZ00280 244 sdpknhfkkytavnsvTKKPYTVDVGY------------ERFLGPEMFFHPEIFsSEWTTPLPEVVDDAIQSCPIDCRRP 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  284 MYGNILMTGGTTMLHGIKERMTKELNALV----------------PSSMKVKVVVPPESECSVWIGGSILASLSTFHQMW 347
Cdd:PTZ00280 312 LYKNIVLSGGSTMFKGFDKRLQRDVRKRVdrrlkkaeelsggklkPIPIDVNVVSHPRQRYAVWYGGSMLASSPEFEKVC 391
                        410
                 ....*....|....*....
gi 15227502  348 ITKDEYEEHGAAIVHRKCV 366
Cdd:PTZ00280 392 HTKAEYDEYGPSICRYNNV 410
COG5277 COG5277
Actin-related protein [Cytoskeleton];
3-356 6.85e-100

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 302.09  E-value: 6.85e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502   3 PIVCDKGHGMVQAG-FAGDEAPKVV-----FPCVVGRPR-----DGLNpNESYVGEE-----GHANRDILTLKDPMEHGI 66
Cdd:COG5277  10 VIGIDFGTSYVKYGpIALEEKPRVIqtrglFLRIVGESKllgpmEGLS-RGLVVGDEvskylSSVRDAIRNLKYPLRDGI 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  67 V-----NNWDDMEKIWHYTFYNELRVDPEEHP--VLLTEAPYNPKANREKMTQIMFESFD---VPAMYVSMQSVLYLYSS 136
Cdd:COG5277  89 VrrddeDAWRVLKELLRYTFAQFLVVDPEFHGflVVVALSALAPDYMRERLFDIHFEVFSeegAPAVTIIPQPLAVAIAE 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 137 GRTTGVVLDLGERVSHTVPVYEGyALPHGILRLDLGGRDLTDYLIEIMTERGYTYTTSAEReIVRDIKEKLCYVALDYEQ 216
Cdd:COG5277 169 KAVTCVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSDTAREEY-VVRVVKEALGLVPRDLAK 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 217 EMEKTTKGW-TIDKTYVLPDGQ-EITI---EAERFMCPEVLFQPSVIGKESS----------------------GIHEAT 269
Cdd:COG5277 247 AIQKAASNPdSFEAKVRLPNPTvEIELgnyAWERFLIGEILFNPNHEGFESYiqqgrlriedavigdvvlygemGLAEAI 326
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 270 RNSILKCPVDTRRDMYGNILMTGGTTML---HGIKE-------RMTKELNALVPsSMKVKVVVPPESECSVWIGGSILAS 339
Cdd:COG5277 327 INSIMKCDVEIQDELYSNIILSGGAFNWsvpPGLEDvavdsvtRVQIELSELAP-ELKVNVRLVSDPQYSVWKGAIIYGY 405
                       410
                ....*....|....*....
gi 15227502 340 LSTFHQMW--ITKDEYEEH 356
Cdd:COG5277 406 ALPFSVKWswITKEGWYFL 424
ASKHA_NBD_Arp6 cd10210
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ...
4-357 1.09e-96

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: 292.53  E-value: 1.09e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502   4 IVCDKGHGMVQAGFAGDEAPKVVfPCVVGRPRDGLNpneSYVGEEGHAN-RDI--LTLKDPMEHGIVNNWDDMEKIWHYT 80
Cdd:cd10210   2 LVLDNGAYTIKAGFASDDPPRVI-PNCIAKPKSERR---RLFGDDQLDEcKDLsgLFYRRPFERGYLVNWDLQRQIWDHL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  81 FYNE-LRVDPEEHPVLLTEAPYNPKANREKMTQIMFESFDVPAMYVSMQSVL----YLYSSGRTTG------VVLDLGER 149
Cdd:cd10210  78 FGKLlLNVDPSDTALVLTEPPFNPPSIQEAMDEIVFEEYGFQSLYRTTAAALsafaYLADSEQSSSsssqccLVVDSGFS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 150 VSHTVPVYEGYALPHGILRLDLGGRDLTDYLIEIMTERGY-----TYttsaereIVRDIKEKLCYVALDYEQEMEKT--- 221
Cdd:cd10210 158 FTHIVPFFDGKPVKRAVRRIDVGGKLLTNYLKEIISYRQLnvmdeTY-------LVNQIKEDLCFVSTDFYEDLEIAkkk 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 222 TKGWTIDKTYVLPDG-----------------------QEITIEAERFMCPEVLFQPSVIGKESSGIHEATRNSILKCPV 278
Cdd:cd10210 231 GKENTIRRDYVLPDYttskrgyvrdpeepnrgklkedeQVLRLNNERFTVPELLFHPSDIGIQQAGIAEAIVQSINACPE 310
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15227502 279 DTRRDMYGNILMTGGTTMLHGIKERMTKELNALVPSSMKVKVVVPPESECSVWIGGSILASLSTFHQMWITKDEYEEHG 357
Cdd:cd10210 311 ELQPLLYANIVLTGGNALFPGFRERLEAELRSLAPDDYDVNVTLPEDPITYAWEGGSLLAQSPEFEELAVTRAEYEEHG 389
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
4-362 1.92e-78

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: 244.61  E-value: 1.92e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502   4 IVCDKGHGMVQAGFA-GDEAPKVVFPCVVgrprdglNPNESYVGEEGHANRDILTlkDPMEHGIVNNWDDMEKIWHYTFY 82
Cdd:cd10209   1 VVIDAGSRLLKAGYAyPDREPSVVEPTRV-------TPAVEDGEESDTVVEGNTV--SPIRRGRIEDWDALEALLRYVFY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  83 NELR-VDPEEHPVLLTEAPYNPKANREKMTQIMFESFDVPAMYVSMQSVLYLYSSGRTTGVVLDLGERVSHTVPVYEGYA 161
Cdd:cd10209  72 TGLGwEEGNEGQVLIAEPLLTSKAERERLTQLMFETFNVSGLYASEQAVLSLYAVGRISGCVVDVGHGKIDIAPVWEGAI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 162 LPHGILRLDLGGRDLTDYLIEIMTERGYTytTSAEREIVRDIKEKlCYVALDYEQEMEKTTKGWTiDKTYVLPDGQEITI 241
Cdd:cd10209 152 QHNAVRRFEIGGRDLTELLAAELGKSNPK--VKLDRSIVERLKEA-VAWSADDEEAYEKKVLTCS-PETYTLPDGRVISV 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 242 EAERFMCPEVLFQPSVIGKESSGIHEATRNSILKCPVDTRRDMYGNILMTGGTTMLHGIKERMTKELNALVPSSMKVKVV 321
Cdd:cd10209 228 GKERYCVGEALFRPSILGIEEYGIVEQLVRAVSTSPSENRRQLLENIVLCGGTSSVPGLEARLQKEIRLLSSPSSRPALV 307
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 15227502 322 VPPE------SECSVWIGGSILASLSTFHQMWITKDEYEEHGAAIVH 362
Cdd:cd10209 308 KPPEympentLRYSAWIGGAILAKVVFPQNQHVTKADYDETGPSVVH 354
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
3-358 7.62e-70

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: 222.45  E-value: 7.62e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502   3 PIVCDKGHGMVQAGFAGDEAPKVVFPCVVGRPRDG-LNPNESYVGEEghANRDIL---TLKDPMEHGIVNNWDDMEKIWH 78
Cdd:cd10211   1 PIVIDNGSYQCRAGWAGDKEPRLVFRNLVAKPRDRkKGITVTLVGND--ILNDEAvrsHLRSPFDRNVVTNFDLQEQILD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  79 YTFyNELRVDPE---EHPVLLTEAPYNPKANREKMTQIMFESFDVPAMYVSMQSVLYLY----SSGRTTGVVLDLGERVS 151
Cdd:cd10211  79 YIF-SHLGINSEgsvDHPIVLTEALCNPNYSRQLMSELLFECYGVPSVAYGIDSLFSYYhnqpQGDPSDGLVISSGYSTT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 152 HTVPVYEGYALPHGILRLDLGGRDLTDYLIEIMTERGYTYTTSAEREIVRDIKEKLCYVALDYEQEMEKttkgwtidkty 231
Cdd:cd10211 158 HVIPVLNGRLDLSQCKRINLGGFHATDYLQRLLQLKYPTHPSAITLSRAEELVHEHCYVAEDYDEELKK----------- 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 232 vlpdgqeitieaerFMCPEVLFQPSVIGKESSGIHEATRNSILKCPVDTRRDMYGNILMTGGTTMLHGIKERMTKELNAL 311
Cdd:cd10211 227 --------------WEDPEYYEENVRKIQLPFGLVETIEFVLKRYPAEQQDRLVQNVFLTGGNALFPGLKERLEKELRAI 292
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 15227502 312 VPSSMKVKVVVPPESECSVWIGGSILASLSTFHQMWITKDEYEEHGA 358
Cdd:cd10211 293 RPFGSPFNVVRAKDPVLDAWRGAAKWALDSTFEKVWITKQEYEEKGG 339
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
61-364 5.88e-51

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: 173.65  E-value: 5.88e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  61 PMEHGIVNNWDDMEKIWHYTFYNELRVDPE--EHPVLLTEAPYNPKANREKMTQIMFESFDVPAMYVSMQSVLYLYSSGR 138
Cdd:cd10208  38 PIQDGRVVDWDALEALWRHILFSLLSIPRPtnNSPVLLSVPPSWSKSDLELLTQLFFERLNVPAFAILEAPLAALYAAGA 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 139 TTGVVLDLGERVSHTVPVYEGYALPHGILRLDLGGRDLTDYLIEIMTERGYTYTTSAE------REIVRDIKE-KLCYVA 211
Cdd:cd10208 118 TSGIVVDIGHEKTDITPIVDSQVVPHALVSIPIGGQDCTAHLAQLLKSDEPELKSQAEsgeeatLDLAEALKKsPICEVL 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 212 LDYEQemekttkgwtidktyvLPDGQEITIEAERFMCPEVLFQPSVIGKESSGIHEA-TRNSILKCPVDTRRDMYGNILM 290
Cdd:cd10208 198 SDGAD----------------LASGTEITVGKERFRACEPLFKPSSLRVDLLIAAIAgALVLNASDEPDKRPALWENIII 261
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 291 TGGTTMLHGIKERMTKELNALVPSSMKVKVVVPPES------------------ECSVWIGGSILASLSTFH---QMWIT 349
Cdd:cd10208 262 VGGGSRIRGLKEALLSELQQFHLISETSASPQQPRIirlakipdyfpewkksgyEEAAFLGASIVAKLVFNDpssKHYIS 341
                       330
                ....*....|....*
gi 15227502 350 KDEYEEHGAAIVHRK 364
Cdd:cd10208 342 KVDYNEKGPAAIHTK 356
ASKHA_NBD_AtArp8-like cd13396
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and ...
79-353 4.64e-47

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: 162.71  E-value: 4.64e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  79 YTFYNELRVDPEEHPVLLTEaPY-------NPKANREKMTQIMFES-FD--VPAMYVSMQSVLYLYSSGRTTGVVLDLGE 148
Cdd:cd13396  46 FTIMTRMQVKPSRQPVVVSL-PLchsddteSAAASRRQLRGTIFNVlFDmnVPAVCAVDQAVLALYAANRTSGIVVNIGF 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 149 RVSHTVPVYEGYALPH-GILRLDLGGRDLTDYLIEIMTERGYTYTTSAereIVRDIKEKLCYVALDYEQEMEKTTKGwti 227
Cdd:cd13396 125 RVTTIVPVYRGRVMHDiGVEVVGQGALRLTGFLKELMQQNGIRFPSLY---TVRTIKEKLCYVAEDYEAELAKDTQA--- 198
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 228 dktyVLPDGQE--ITIEAERFMCPEVLFQPSVIGKESSGIHEATRNSILKCPVD---TRRDMYGNILMTGGTTMLHGIKE 302
Cdd:cd13396 199 ----SCEVAGEgwFTLSNERFKTGEILFQPGLGGMRAMGLHQAVALCMDHCALVhsqGDDGWFKTIVLSGGSACLPGLSE 274
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 15227502 303 RMTKELNALVPSSMK--VKVVVPPESECSVWIGGSILASLSTFHQMW-ITKDEY 353
Cdd:cd13396 275 RLERELRKLLPKSLSegIRIIPPPLGPDSAWQGAKLISNLSNFPDGWcITKKQF 328
ASKHA_NBD_Arp10 cd10207
nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins; ...
4-357 1.38e-46

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: 162.81  E-value: 1.38e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502   4 IVCDKGHGMVQAGFAGDEAPKVVFPCVVGRPRDGLnpnESYVGEEGHANRDILTLKdpmehgivnnwddMEKIWHYTFYN 83
Cdd:cd10207   1 VVLDIGSAYTKCGFAGESAPRCIIPSEVKLPGGKK---VIRVVDQRSGNEEELYEA-------------LKEFLHELYFK 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  84 ELRVDPEEHPVLLTEAPYNPKANREKMTQIMFESFDVPAmyVSMQS--VLYLYSSGRTTGVVLDLGERVSHTVPVYEGYA 161
Cdd:cd10207  65 HLLVNPKDRRVVVVESVLCPTPFRETLAKVLFKHFEVPS--VLFAPshLLSLLTLGIRTALVVDCGYRETRVLPVYEGVP 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 162 LPHGILRLDLGGRDLTDYLIEIMTERGYTYTTSAER------------EIVRDIKEKLCYVA-LDYEQEMEKTTKGWTI- 227
Cdd:cd10207 143 LLSAWQSTPLGGKALHKRLKKLLLEHATVVTGDNKGqllssvdsllseEVLEDIKVRACFVTsLERGKTLQSATEEGSTe 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 228 ------DKTYVLPDGQEITIEAERFMCPEVLFQPSVIGKESsgIHEATRNSILKCPVDTRRDMYGNILMTGGTTMLHGIK 301
Cdd:cd10207 223 epspppPVDYPLDGEKILIVPGSIRESAEELLFEGDNEEKS--LPTLILDSLLKCPIDVRKQLAENIVVIGGTSMLPGFK 300
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15227502 302 ERMTKELNALV--------PSSMKVKVVVPPE---SECSVWIGGSILASLSTFHQMWITKDEYEEHG 357
Cdd:cd10207 301 HRLLEELRALLrkpkyfeeLAPKTFRFHTPPSvfkPNYLAWLGGSIFGALESILGRSLSREAYLQTG 367
ASKHA_NBD_Arp8-like cd10206
nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The ...
71-360 1.63e-32

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: 126.20  E-value: 1.63e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  71 DDMEKIWHYTFYNELRVDPEEHP----VLLTEAPYNpKANREKMTQIMFESFDVPAMYVSMQSVLYLYSSGRTTGVVLDL 146
Cdd:cd10206 162 DDLEDIWSHALEEKLEIPRKDLKnyraVLVIPDLFD-RRHVKELVDLLLRRLGFSSVFVHQESVCATFGAGLSSACVVDI 240
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 147 GERVSHTVPVYEGYALPHGILRLDLGGRDLTDYLIEIMTERGYTYT-----TSAEREIVRDIKEKLCYVALDyeqemekt 221
Cdd:cd10206 241 GAQKTSVACVEDGLSIPNSRIRLPYGGDDITRCFLWLLRRSGFPYRecnlnSPLDFLLLERLKETYCTLDQD-------- 312
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 222 tkgwtidktyvlPDGQEITIEAERFMC-PEVLFQPSVIGkessgIHEATRNSILKCP-VDTRRDMYGNILMTGGTTMLHG 299
Cdd:cd10206 313 ------------DIGVQLHEFYVREPGqPTLKYQFKLLP-----LDEAIVQSILSCAsDELKRKMYSSILLVGGGAKIPG 375
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15227502 300 IKERMTKELNALVPSSMK----VKVVVPPE---SECSVWIGGSILASLSTFHQMWITKDEYEEHGAAI 360
Cdd:cd10206 376 LAEALEDRLLIKIPSLFEavetVEVLPPPKdmdPSLLAWKGGAVLACLDSAQELWITRKEWQRLGVRA 443
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
294-365 1.05e-23

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: 95.05  E-value: 1.05e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15227502  294 TTMLHGIKERMTKELNALVPSSMKVKVVVPPESECSVWIGGSILASLSTFHQMWITKDEYEEHGAAIVHRKC 365
Cdd:NF040575  61 RVNESGFYEKLKKSITEKAPKGALIGMTLDPKPESAAWRGAAMYAASEGFVEMAITKQEYDESGPSIVHRKC 132
ASKHA_NBD_ScArp7-like cd10212
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and ...
2-354 4.70e-22

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: 96.71  E-value: 4.70e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502   2 KPIVCDKGHGMVQAGFAGDEAPKVVFPCVVGRPRDGLNPNESYVGE--------EGHANRDILTLKDpmEHGIVNNWDDM 73
Cdd:cd10212   4 KCVVIHNGSHRTVAGFSNVELPQCIIPSSYIKRTDEGGEAEFIFGTynmidaaaEKRNGDEVYTLVD--SQGLPYNWDAL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  74 EKIWHYTFYNELRVDPEEHPVLLTEAPYNPKANR---EKMTQIMFESFDVPAMYVSMQSVLYLYSSGRTTGVVLDLGERV 150
Cdd:cd10212  82 EMQWRYLYDTQLKVSPEELPLVITMPATNGKPDMailERYYELAFDKLNVPVFQIVIEPLAIALSMGKSSAFVIDIGASG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 151 SHTVPVYEGYALPHGILRLDLGGrDLTDYLI--------------EIM-------TERGYTYTTSAER------------ 197
Cdd:cd10212 162 CNVTPIIDGIVVKNAVVRSKFGG-DFLDFQVherlaplikeendmENMadeqkrsTDVWYEASTWIQQfkstmlqvsekd 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 198 --EIVRDIKEKLCYVALDYEQ--EMEKTTKGWTI----------DKTYVL-PDGQEITIE-AERFMCPEVLFQPSVIGKE 261
Cdd:cd10212 241 lfELERYYKEQADIYAKQQEQlkQMDQQLQYTALtgspnnplvqKKNFLFkPLNKTLTLDlKECYQFAEYLFKPQLISDK 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 262 SS---GIHEATRNSILKCPVDTRRDMYGNILMTGGTTMLHGIKERMTKELNALVP----SSMKVKVVVppESECSVWIGG 334
Cdd:cd10212 321 FSpedGLGPLMAKSVKKAPEQVYSLLLTNVIITGSTSLIEGMEQRIIKELSIRFPqyklTTFANQVMM--DRKIQGWLGA 398
                       410       420
                ....*....|....*....|.
gi 15227502 335 SILASLSTFH-QMWITKDEYE 354
Cdd:cd10212 399 LTMANLPSWSlGKWYSKEDYE 419
ASKHA_NBD_MamK cd24009
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ...
11-308 7.88e-05

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


Pssm-ID: 466859 [Multi-domain]  Cd Length: 328  Bit Score: 44.12  E-value: 7.88e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  11 GMVQAGFAGDEAPKVVFPCVVGRPRD--GLNP-NESYV-GEEGHANRDILTLKDPMEHGIVNNWD--DMEKIWHYT--FY 82
Cdd:cd24009   9 GTSRSAVVTSRGKRFSFRSVVGYPKDiiARKLlGKEVLfGDEALENRLALDLRRPLEDGVIKEGDdrDLEAARELLqhLI 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502  83 NELRVDPEEHPVLLTEAPYNP-KANREKMTQIMFESFDvPAMYVSmQSVLYLYSSGRTTG-VVLDLGE------RVSHTV 154
Cdd:cd24009  89 ELALPGPDDEIYAVIGVPARAsAENKQALLEIARELVD-GVMVVS-EPFAVAYGLDRLDNsLIVDIGAgttdlcRMKGTI 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227502 155 PvyegyaLPHGILRLDLGGRDLTDYLIEIMTERgytYT-TSAEREIVRDIKEKLCYVALDYEQEMEKTTKgwtidktyvl 233
Cdd:cd24009 167 P------TEEDQITLPKAGDYIDEELVDLIKER---YPeVQLTLNMARRWKEKYGFVGDASEPVKVELPV---------- 227
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15227502 234 pDGQEITI---EAERFMCPEVLfqPSVIgkessgihEATRNSILKCPVDTRRDMYGNILMTGGTTMLHGIKERMTKEL 308
Cdd:cd24009 228 -DGKPVTYditEELRIACESLV--PDIV--------EGIKKLIASFDPEFQEELRNNIVLAGGGSRIRGLDTYIEKAL 294
ASKHA_NBD_MreB-like cd10225
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ...
263-337 1.86e-04

nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and similar proteins; MreB proteins are bacterial actin homologs that may play a role in cell shape determination by positioning the cell wall synthetic machinery. MreB has also been implicated in chromosome segregation; specifically, MreB is thought to bind to and segregate the replication origin of bacterial chromosomes. The family includes three MreB isoforms, MreB (also called actin-like MreB protein or rod shape-determining protein MreB), Mbl (also called actin-like Mbl protein or rod shape-determining protein Mbl) and MreBH (also called actin-like MreBH protein or rod shape-determining protein MreBH), in cell morphogenesis of Bacillus subtilis. All isoforms can support rod-shaped cell growth normal conditions. They form membrane-associated dynamic filaments that are essential for cell shape determination. They act by regulating cell wall synthesis and cell elongation, and thus cell shape. The feedback loops between cell geometry and their localizations may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature. Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on their polymerization. They organize peptidoglycan synthesis in the lateral cell wall. MreB, Mbl and MreBH can form a complex. The MreB-like 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: 466824 [Multi-domain]  Cd Length: 317  Bit Score: 42.85  E-value: 1.86e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15227502 263 SGIHEATRNSILKCPVDTRRDMYGN-ILMTGGTTMLHGIKERMTKELnalvpssmKVKVVVPPESECSVWIG-GSIL 337
Cdd:cd10225 249 NAIVEAVRSTLERTPPELAADIVDRgIVLTGGGALLRGLDELLREET--------GLPVHVADDPLTCVAKGaGKAL 317
MreB COG1077
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ...
288-351 5.05e-03

Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 440695 [Multi-domain]  Cd Length: 339  Bit Score: 38.52  E-value: 5.05e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15227502 288 ILMTGGTTMLHGIKERMTKELnalvpssmKVKVVVPPESECSVWIG-GSILASLSTFHQMWITKD 351
Cdd:COG1077 283 IVLTGGGALLRGLDKLLSEET--------GLPVHVAEDPLTCVARGtGKALENLDLLRRVLISSD 339
ASKHA_NBD_BcrAD_BadFG_HgdC_HadI cd24036
nucleotide-binding domain (NBD) of the BcrAD/BadFG and HgdC/HadI family; The BcrAD/BadFG and ...
264-337 9.64e-03

nucleotide-binding domain (NBD) of the BcrAD/BadFG and HgdC/HadI family; The BcrAD/BadFG and HgdC/HadI family includes BcrA/BadF/BzdQ and BcrD/BadG/BzdP proteins which are subunits of benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also contains some dehydratase activators, such as Acidaminococcus fermentans (R)-2-hydroxyglutaryl-CoA dehydratase activating ATPase (HgdC), Clostridioides difficile 2-hydroxyisocaproyl-CoA dehydratase activator (HadI), Clostridium sporogenes (R)-phenyllactate dehydratase activator (FldI), and Anaerotignum propionicum activator of lactoyl-CoA dehydratase (LcdC). Uncharacterized proteins, such as Escherichia coli protein YjiL and Methanocaldococcus jannaschii protein MJ0800, are also included in this family.


Pssm-ID: 466886 [Multi-domain]  Cd Length: 250  Bit Score: 37.13  E-value: 9.64e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15227502 264 GIHEATRNSILKcpVDTRRDMYGNILMTGGTTMLHGIKERMTKELNalvpssmkVKVVVPPESECSVWIGGSIL 337
Cdd:cd24036 187 GIHNSIAKRVAA--LAKRVGVEDPVVLTGGVAKNPGVVKALEEKLG--------VEVIVPPNPQLVGALGAALL 250
 
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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